PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
15513323-4	2004	RESULTS: Pretreatment plasminogen activator inhibitor 1 (PAI-1) levels correlated negatively to SHBG and antithrombin III (AT III) negatively to total and free cortisol.	Hydrocortisone	160-168	serpin family C member 1	Homo sapiens	105-121
15513323-4	2004	RESULTS: Pretreatment plasminogen activator inhibitor 1 (PAI-1) levels correlated negatively to SHBG and antithrombin III (AT III) negatively to total and free cortisol.	Hydrocortisone	160-168	serpin family C member 1	Homo sapiens	123-129
14519763-5	2003	We have demonstrated the feasibility of this new approach to rapidly assemble antithrombin III-binding classical and non-classical anticoagulant polysaccharide structures for the first time.	Polysaccharides	145-159	serpin family C member 1	Homo sapiens	78-94
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
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.	Sodium Dodecyl Sulfate	187-190	serpin family C member 1	Homo sapiens	340-352
12907439-0	2003	Heparin-induced substrate behavior of antithrombin Cambridge II.	Heparin	0-7	serpin family C member 1	Homo sapiens	38-50
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
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.	Sodium Dodecyl Sulfate	98-120	serpin family C member 1	Homo sapiens	0-12
12907439-5	2003	The stoichiometries were not affected by pentasaccharides, indicating that the inhibitory mechanism of antithrombin Cambridge II is perturbed only in the presence of a bridging glycosaminoglycan.	Glycosaminoglycans	177-194	serpin family C member 1	Homo sapiens	103-115
14652650-9	2003	Concomitant incubation with pentasaccharide abolished this effect of antithrombin.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	69-81
14679575-1	2003	The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods.	polyacrylamide	156-170	serpin family C member 1	Homo sapiens	46-62
14679575-1	2003	The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods.	polyacrylamide	156-170	serpin family C member 1	Homo sapiens	64-69
14679575-1	2003	The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods.	2-Isopropoxyethanol	207-210	serpin family C member 1	Homo sapiens	46-62
14679575-1	2003	The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods.	2-Isopropoxyethanol	207-210	serpin family C member 1	Homo sapiens	64-69
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
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
14679575-5	2003	The main isoforms of ATIII-alpha and ATIII-beta exhibit pI values of 5.18 and 5.32, respectively, both values determined in the presence of high concentrations of urea.	Urea	163-167	serpin family C member 1	Homo sapiens	21-26
14679575-5	2003	The main isoforms of ATIII-alpha and ATIII-beta exhibit pI values of 5.18 and 5.32, respectively, both values determined in the presence of high concentrations of urea.	Urea	163-167	serpin family C member 1	Homo sapiens	37-42
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
14719183-3	2003	To gain insight into structure-activity relationships, we investigated the interaction of a homogeneous series of sulfated polysaccharides, derived from controlled desulfation of a supersulfated low-molecular-weight heparin (LMWH) with the target enzymes human antithrombin (AT) and thrombin (T).	Polysaccharides	123-138	serpin family C member 1	Homo sapiens	261-273
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
14650860-5	2003	Inhibition of factor Xa via antithrombin (AT) by fondaparinux has been studied extensively.	Fondaparinux	49-61	serpin family C member 1	Homo sapiens	28-40
14575696-0	2003	Platelet factor 4 neutralizes heparan sulfate-enhanced antithrombin inactivation of factor Xa by preventing interaction(s) of enzyme with polysaccharide.	Heparitin Sulfate	30-45	serpin family C member 1	Homo sapiens	55-67
14575696-0	2003	Platelet factor 4 neutralizes heparan sulfate-enhanced antithrombin inactivation of factor Xa by preventing interaction(s) of enzyme with polysaccharide.	Polysaccharides	138-152	serpin family C member 1	Homo sapiens	55-67
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
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
14528313-0	2003	Enzymatic synthesis of antithrombin III-binding heparan sulfate pentasaccharide.	heparan sulfate pentasaccharide	48-79	serpin family C member 1	Homo sapiens	23-39
14528313-4	2003	We rapidly and efficiently assembled the antithrombin III-binding pentasaccharide in just 6 steps, in contrast to the approximately 60 steps needed for its chemical synthesis, with an overall yield at least twofold greater and a completion time at least 100 times faster than for the chemical process.	pentasaccharide	66-81	serpin family C member 1	Homo sapiens	41-57
15199446-4	2003	Larger clinical studies are needed to confirm the safety and efficacy of LMWH as an antithrombin for the treatment across the spectrum of ACS.	Heparin, Low-Molecular-Weight	73-77	serpin family C member 1	Homo sapiens	84-96
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
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
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
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
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
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
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
13679071-1	2003	Antithrombin (AT) circulates in two isoforms, alpha- (90-95%) and beta-AT (5-10%).	methylphenyl carbinol	46-52	serpin family C member 1	Homo sapiens	0-12
13679071-1	2003	Antithrombin (AT) circulates in two isoforms, alpha- (90-95%) and beta-AT (5-10%).	beta-at	66-73	serpin family C member 1	Homo sapiens	0-12
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
12920045-2	2003	To explore how glycosaminoglycan changes could influence the thrombogenicity of atherosclerotic lesions, water-transfer reactions were examined during activation of antithrombin by CS.	Chondroitin Sulfates	181-183	serpin family C member 1	Homo sapiens	165-177
12920045-5	2003	Oversulfated CS functionally bound antithrombin with a dissociation constant of 3.3+/-1.9 micromol/L.	Chondroitin Sulfates	13-15	serpin family C member 1	Homo sapiens	35-47
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
14502551-6	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
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
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
12860985-2	2003	In contrast, alpha1-proteinase inhibitor (alpha1PI) Pittsburgh (P1 Met --> Arg natural variant) inhibits thrombin 17 times faster than pentasaccharide heparin-activated antithrombin.	pentasaccharide	138-153	serpin family C member 1	Homo sapiens	172-184
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
12832413-0	2003	Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide.	pentasaccharide	97-112	serpin family C member 1	Homo sapiens	54-66
12832413-3	2003	This result demonstrates that antithrombin is the predominant inhibitor of f.IXa in plasma, and that the activity of antithrombin is promoted by pentasaccharide.	pentasaccharide	145-160	serpin family C member 1	Homo sapiens	117-129
12832413-4	2003	Kinetic experiments reveal that pentasaccharide increases the rates of antithrombin-mediated inhibition of both f.IXa and f.Xa by 2 orders of magnitude.	pentasaccharide	32-47	serpin family C member 1	Homo sapiens	71-83
12832413-5	2003	These findings indicate that pentasaccharide-induced conformational changes in antithrombin enhance its capacity to inhibit both f.IXa and f.Xa.	pentasaccharide	29-44	serpin family C member 1	Homo sapiens	79-91
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
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
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
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.	pentasaccharide	105-120	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	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
12837765-7	2003	A fraction of these fragments contains the specific pentasaccharide sequence required for high affinity binding to antithrombin implicated with anticoagulant activity.	pentasaccharide	52-67	serpin family C member 1	Homo sapiens	115-127
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
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.	Disaccharides	94-106	serpin family C member 1	Homo sapiens	178-190
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.	Polysaccharides	134-148	serpin family C member 1	Homo sapiens	178-190
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.	Oligosaccharides	199-215	serpin family C member 1	Homo sapiens	178-190
12837765-12	2003	These findings strongly suggest that the intracellular processing of the heparin proteoglycan polysaccharide chains is catalyzed by heparanase, which primarily cleaves target structures distinct from the antithrombin-binding sequence.	Polysaccharides	94-108	serpin family C member 1	Homo sapiens	204-216
12939144-0	2003	Introduction of a mutation in the shutter region of antithrombin (Phe77 --> Leu) increases affinity for heparin and decreases thermal stability.	Leucine	79-82	serpin family C member 1	Homo sapiens	52-64
14607764-3	2003	It is a pentasaccharide mimicking the site where heparin binds to antithrombin III (1).	pentasaccharide	8-23	serpin family C member 1	Homo sapiens	66-82
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
12939144-0	2003	Introduction of a mutation in the shutter region of antithrombin (Phe77 --> Leu) increases affinity for heparin and decreases thermal stability.	Heparin	107-114	serpin family C member 1	Homo sapiens	52-64
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.	IC 831423	138-161	serpin family C member 1	Homo sapiens	62-74
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.	Arginine	137-145	serpin family C member 1	Homo sapiens	101-113
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.	Arginine	137-145	serpin family C member 1	Homo sapiens	195-207
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
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
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
12941037-2	2003	The aim of this work was to study the inhibition of clot-bound FXa and clot-bound thrombin by SanOrg123781A, a synthetic hexadecasaccharide that enhances the inhibition of thrombin and FXa by antithrombin (AT).	hexadecasaccharide	121-139	serpin family C member 1	Homo sapiens	192-204
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).	Heparitin Sulfate	28-43	serpin family C member 1	Homo sapiens	135-147
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).	Dermatan Sulfate	65-81	serpin family C member 1	Homo sapiens	135-147
12556442-0	2003	Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation.	Phenylalanine	17-31	serpin family C member 1	Homo sapiens	0-16
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
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
12556442-5	2003	Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide.	Phenylalanine	51-54	serpin family C member 1	Homo sapiens	153-158
12556442-5	2003	Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide.	Lysine	63-66	serpin family C member 1	Homo sapiens	153-158
12556442-5	2003	Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide.	pentasaccharide	174-189	serpin family C member 1	Homo sapiens	153-158
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.	Phenylalanine	42-45	serpin family C member 1	Homo sapiens	172-184
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.	Phenylalanine	54-57	serpin family C member 1	Homo sapiens	172-184
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
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
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
12845799-0	2003	[Synthesis and antithrombin activity of phosphoalanine-containing peptides].	phosphoalanine	40-54	serpin family C member 1	Homo sapiens	15-27
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
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.	pentasaccharide	74-89	serpin family C member 1	Homo sapiens	165-177
12871355-4	2003	We also calculated the molar concentration of A-domain with 12 sugar units at its non-reducing end, i.e. the structure that carries antithrombin activity (C-domain).	Sugars	63-68	serpin family C member 1	Homo sapiens	132-144
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 (>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
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 (>15 000) are less active, probably through interaction with non-antithrombin plasma proteins.	Heparin, Low-Molecular-Weight	171-175	serpin family C member 1	Homo sapiens	13-25
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
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
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
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
14760212-2	2003	Two subcutaneously injected synthetic pentasaccharide anticoagulants, fondaparinux and idraparinux, employ the minimal chain length required to bind to antithrombin and confer a conformational change, increasing its ability to catalyze inactivation of activated factor X (Xa).	pentasaccharide	38-53	serpin family C member 1	Homo sapiens	152-164
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
12873131-1	2003	Antithrombin is activated as an inhibitor of the coagulation proteases through its specific interaction with a heparin pentasaccharide.	IC 831423	111-134	serpin family C member 1	Homo sapiens	0-12
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
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.	pentasaccharide	115-130	serpin family C member 1	Homo sapiens	52-64
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
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
12873131-6	2003	Here we present the structure of an intermediate pentasaccharide-bound conformation of antithrombin which has undergone all of the conformational changes associated with activation except loop expulsion and helix D elongation.	pentasaccharide	49-64	serpin family C member 1	Homo sapiens	87-99
12873131-7	2003	We conclude that the basis of the high-affinity state is not improved interaction with the pentasaccharide but a lowering of the global free energy due to conformational changes elsewhere in antithrombin.	pentasaccharide	91-106	serpin family C member 1	Homo sapiens	191-203
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
12846563-0	2003	Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites.	Calcium	12-19	serpin family C member 1	Homo sapiens	46-58
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
12846563-2	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.	Calcium	386-393	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).	IC 831423	126-149	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).	IC 831423	126-149	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).	Calcium	210-217	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).	Calcium	210-217	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	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).	Calcium	306-313	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	245-252	serpin family C member 1	Homo sapiens	90-102
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.	p6-p3	15-20	serpin family C member 1	Homo sapiens	48-60
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.	Arginine	162-165	serpin family C member 1	Homo sapiens	48-60
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
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
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
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
12783932-10	2003	Several blood biomarkers showed dose-response relationships with tamoxifen, including decreased insulin-like growth factor-I, increased sex hormone-binding globulin, and decreased low-density lipoprotein-cholesterol, ultrasensitive C-reactive protein, fibrinogen, and antithrombin-III levels.	Tamoxifen	65-74	serpin family C member 1	Homo sapiens	268-284
12841884-9	2003	CONCLUSIONS: The results of this prospective study show for the first time that raloxifene use is associated with a significant reduction in plasma antithrombin activity.	Raloxifene Hydrochloride	80-90	serpin family C member 1	Homo sapiens	148-160
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
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
12865952-5	2003	Antithrombin binds to endothelial glycosaminoglycans and then significantly increases anticoagulant activity.	Glycosaminoglycans	34-52	serpin family C member 1	Homo sapiens	0-12
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
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
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.	2-(4-Amino-N-ethylanilino)ethanol	196-199	serpin family C member 1	Homo sapiens	24-31
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
12578831-2	2003	Exposure of this histidine in antithrombin, which has a partially opened sheet, allows polymerization and peptide insertion to occur at pH 6 or less when His-334 will be predictably protonated with disruption of the H-bond network.	Histidine	17-26	serpin family C member 1	Homo sapiens	30-42
12754837-2	2003	Polymeric systems with antithrombin activity and LCST were prepared via a reaction of amino groups of hirudin with phthalimide groups of the copolymers.	phthalimide	115-126	serpin family C member 1	Homo sapiens	23-35
12754837-4	2003	The antithrombin activity of polymeric systems obtained by hirudin immobilization on copolymer carriers was inversely related to the content of the copolymer, amounting to 6% of the activity of native hirudin.	copolymer	85-94	serpin family C member 1	Homo sapiens	4-16
12754837-4	2003	The antithrombin activity of polymeric systems obtained by hirudin immobilization on copolymer carriers was inversely related to the content of the copolymer, amounting to 6% of the activity of native hirudin.	copolymer	148-157	serpin family C member 1	Homo sapiens	4-16
12578831-2	2003	Exposure of this histidine in antithrombin, which has a partially opened sheet, allows polymerization and peptide insertion to occur at pH 6 or less when His-334 will be predictably protonated with disruption of the H-bond network.	Histidine	154-157	serpin family C member 1	Homo sapiens	30-42
12578831-3	2003	Similarly, thermal stability of antithrombin is pH-dependent with a single unfolding transition at pH 6, but there is no such transition when His-334 is buried by a fully closed A-sheet in heparin-complexed antithrombin or in alpha(1)-antitrypsin.	Histidine	142-145	serpin family C member 1	Homo sapiens	32-44
12578831-4	2003	Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH.	Histidine	15-18	serpin family C member 1	Homo sapiens	157-169
12578831-4	2003	Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH.	Serine	52-58	serpin family C member 1	Homo sapiens	157-169
12578831-4	2003	Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH.	Alanine	62-69	serpin family C member 1	Homo sapiens	157-169
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.	galactopyranosyl-1-4-paragloboside	12-14	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.	galactopyranosyl-1-4-paragloboside	12-14	serpin family C member 1	Homo sapiens	57-69
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.	Arginine	15-23	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.	Arginine	15-23	serpin family C member 1	Homo sapiens	57-69
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
12591924-2	2003	Sequencing of the antithrombin genes of the patient revealed that one of the two alleles was abnormal due to an in-frame deletion of the codon for the P1 arginine residue.	Arginine	154-162	serpin family C member 1	Homo sapiens	18-30
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
12591924-3	2003	The abnormal antithrombin was separated from the normal inhibitor by complexing the latter with thrombin followed by heparin-agarose affinity chromatography.	Sepharose	125-132	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.	Heparitin Sulfate	148-163	serpin family C member 1	Homo sapiens	109-121
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
12480701-0	2003	Antithrombin reduces ischemia/reperfusion-induced renal injury in rats by inhibiting leukocyte activation through promotion of prostacyclin production.	Epoprostenol	127-139	serpin family C member 1	Homo sapiens	0-12
12689824-2	2003	An affinity capillary electrophoresis method has been developed to evidence the complex formation and to determine the binding properties between an anticoagulant polysaccharide of marine origin, fucoidan, and a potential target protein, antithrombin.	Polysaccharides	163-177	serpin family C member 1	Homo sapiens	238-250
12689824-5	2003	The effective mobility data of the protein were processed according to classical linearization treatments to obtain the binding constant for the polysaccharide/antithrombin complex.	Polysaccharides	145-159	serpin family C member 1	Homo sapiens	160-172
12689824-6	2003	The results indicate that fucoidan binds to antithrombin in a 1:1 stoichiometry and with an affinity depending on the molecular weight of the polysaccharide.	Polysaccharides	142-156	serpin family C member 1	Homo sapiens	44-56
12871411-5	2003	The CVBETWEEN was significantly higher for antithrombin and protein S for samples with low levels similar to heterozygous deficiencies.	cvbetween	4-13	serpin family C member 1	Homo sapiens	43-55
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.	Diclofenac	285-295	serpin family C member 1	Homo sapiens	67-83
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
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.	thiotriasoline	306-320	serpin family C member 1	Homo sapiens	67-83
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.	prednizolon	370-381	serpin family C member 1	Homo sapiens	67-83
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
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.	thiotriasoline	392-406	serpin family C member 1	Homo sapiens	67-83
12623072-0	2003	N-linked oligosaccharide processing, but not association with calnexin/calreticulin is highly correlated with endoplasmic reticulum-associated degradation of antithrombin Glu313-deleted mutant.	n-linked oligosaccharide	0-24	serpin family C member 1	Homo sapiens	158-170
12623072-7	2003	These results indicate that, besides proteasome inhibitors, inhibitors of ER mannosidase I and protein synthesis suppress ERAD of the antithrombin deltaGlu mutant at different stages, and processing of N-linked oligosaccharides highly correlated with the efficiency of ERAD.	n-linked oligosaccharides	202-227	serpin family C member 1	Homo sapiens	134-146
12633766-3	2003	Results Using D-BUT-CHT-lys-pNA as a plasmin-specific substrate, we show that incubation of plasma with fructose, glyceraldehyde or MG but not glucose decreases plasminogen activity reaching more than 40% in 16 h. A parallel dose-dependent decrease in heparin activation of AT III by up to a 50% was demonstrated using SAR-PRO-ARG-pNA as a specific thrombin substrate.	Fructose	104-112	serpin family C member 1	Homo sapiens	274-280
12633766-3	2003	Results Using D-BUT-CHT-lys-pNA as a plasmin-specific substrate, we show that incubation of plasma with fructose, glyceraldehyde or MG but not glucose decreases plasminogen activity reaching more than 40% in 16 h. A parallel dose-dependent decrease in heparin activation of AT III by up to a 50% was demonstrated using SAR-PRO-ARG-pNA as a specific thrombin substrate.	Glyceraldehyde	114-128	serpin family C member 1	Homo sapiens	274-280
12633766-3	2003	Results Using D-BUT-CHT-lys-pNA as a plasmin-specific substrate, we show that incubation of plasma with fructose, glyceraldehyde or MG but not glucose decreases plasminogen activity reaching more than 40% in 16 h. A parallel dose-dependent decrease in heparin activation of AT III by up to a 50% was demonstrated using SAR-PRO-ARG-pNA as a specific thrombin substrate.	Magnesium	132-134	serpin family C member 1	Homo sapiens	274-280
12639557-0	2003	Exploring new non-sugar sulfated molecules as activators of antithrombin.	Sugars	18-23	serpin family C member 1	Homo sapiens	60-72
12639557-1	2003	New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa.	Sugars	8-13	serpin family C member 1	Homo sapiens	163-175
12639557-1	2003	New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa.	epicatechin sulfate	93-116	serpin family C member 1	Homo sapiens	163-175
12639557-1	2003	New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa.	epicatechin sulfate	118-121	serpin family C member 1	Homo sapiens	163-175
12639557-2	2003	For the activators studied, the equilibrium dissociation constant (K(D)) of the interaction with plasma antithrombin varies nearly 53-fold, with the highest affinity of 1.8 microM observed for morin sulfate, while the acceleration in factor Xa inhibition varies 2.6-fold.	NSC676013	193-206	serpin family C member 1	Homo sapiens	104-116
12768169-7	2003	The most important mechanism responsible of the anti-inflammatory properties of AT is the binding to the glycosaminoglycans of the endothelial cells and the consequent release of prostacyclin.	Glycosaminoglycans	105-123	serpin family C member 1	Homo sapiens	80-82
12768169-7	2003	The most important mechanism responsible of the anti-inflammatory properties of AT is the binding to the glycosaminoglycans of the endothelial cells and the consequent release of prostacyclin.	Epoprostenol	179-191	serpin family C member 1	Homo sapiens	80-82
12651125-0	2003	Separation between the alpha and beta forms of human antithrombin by hydroxyapatite high-performance liquid chromatography.	Durapatite	69-83	serpin family C member 1	Homo sapiens	53-65
12651125-2	2003	The predominant form of AT in plasma is ATalpha, which contains four glycosylated asparagine residues, and the minor form is ATbeta, which lacks the Asn-135 glycosylation.	Asparagine	82-92	serpin family C member 1	Homo sapiens	24-26
12651125-5	2003	Two analyzed commercial AT products both contained about 2% ATbeta.	atbeta	60-66	serpin family C member 1	Homo sapiens	24-26
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
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
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
12581643-3	2003	Activation of antithrombin is brought about by a conformational change initiated upon binding heparin or heparan sulphate.	Heparitin Sulfate	105-121	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
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
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).	pentasaccharide	100-115	serpin family C member 1	Homo sapiens	79-91
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).	pentasaccharide	100-115	serpin family C member 1	Homo sapiens	79-91
12581643-8	2003	The new structures have a remarkable degree of ordered carbohydrate and include parts of the antithrombin chain not modeled before.	Carbohydrates	55-67	serpin family C member 1	Homo sapiens	93-105
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
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
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
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
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.	Carbohydrates	250-262	serpin family C member 1	Homo sapiens	79-91
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.	Carbohydrates	250-262	serpin family C member 1	Homo sapiens	102-114
12627673-3	2003	Antithrombin drugs such as argatroban and hirudin are already approved for alternative management of heparin-compromised patients.	argatroban	27-37	serpin family C member 1	Homo sapiens	0-12
12627673-15	2003	In addition, binding oligosaccharides are conjugated with antithrombin agents to mimic the anti-Xa/anti-IIa activities of heparin.	Oligosaccharides	21-37	serpin family C member 1	Homo sapiens	58-70
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
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
12535860-2	2003	Here, we report that treatment of coronary artery patients with 100 mg/day of aspirin does not attenuate thrombin generation, but reduces free thrombin by favouring the formation of thrombin/antithrombin (TAT) complexes.	Aspirin	78-85	serpin family C member 1	Homo sapiens	191-203
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
12492585-6	2003	Among tamoxifen-treated women, antithrombin and protein S, but not protein C or APC ratio were reduced.	Tamoxifen	6-15	serpin family C member 1	Homo sapiens	31-43
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
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
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
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
12765778-5	2003	The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide.	pentasaccharide	90-105	serpin family C member 1	Homo sapiens	60-72
12765778-5	2003	The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide.	Glucosamine	152-163	serpin family C member 1	Homo sapiens	60-72
12765778-5	2003	The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide.	Sugars	185-190	serpin family C member 1	Homo sapiens	60-72
12765778-5	2003	The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide.	Sulfates	143-150	serpin family C member 1	Homo sapiens	60-72
12765778-5	2003	The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide.	Polysaccharides	249-263	serpin family C member 1	Homo sapiens	60-72
12765779-1	2003	We have synthesized three new antithrombin activating pentasaccharides displaying various sulfation patterns on the reducing end unit (H).	pentasaccharides	54-70	serpin family C member 1	Homo sapiens	30-42
14587291-7	2003	Sequential crystallographic structures now provide clear depictions of the way antithrombin is activated on binding to the heparans of the microcirculation, and how evolution has utilized this mobile mechanism for subtle variations in activity.	heparans	123-131	serpin family C member 1	Homo sapiens	79-91
12492585-7	2003	Sequential antithrombin concentrations with tamoxifen were 114% and 104% (P = 0.001 compared with placebo).	Tamoxifen	44-53	serpin family C member 1	Homo sapiens	11-23
14556453-1	2003	In the early eighties, following breakthroughs in oligosaccharide chemistry, we achieved the total chemical synthesis of pentasaccharides related to the antithrombin-binding domain in heparin.	Oligosaccharides	50-65	serpin family C member 1	Homo sapiens	153-165
14556453-1	2003	In the early eighties, following breakthroughs in oligosaccharide chemistry, we achieved the total chemical synthesis of pentasaccharides related to the antithrombin-binding domain in heparin.	pentasaccharides	121-137	serpin family C member 1	Homo sapiens	153-165
14556453-3	2003	In a further step, we have designed and synthesised oligosaccharides (pentadeca--to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain.	Oligosaccharides	52-68	serpin family C member 1	Homo sapiens	118-130
14556453-3	2003	In a further step, we have designed and synthesised oligosaccharides (pentadeca--to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain.	pentadeca--to eicosasaccharides	70-101	serpin family C member 1	Homo sapiens	118-130
14556454-3	2003	We determined the molar concentration of material (HAM) containing the antithrombin (AT) binding pentasaccharide (A-domain), the specific catalytic activity in thrombin- and factor Xa inactivation and the capacity to inhibit thrombin generation (TG).	pentasaccharide	97-112	serpin family C member 1	Homo sapiens	71-83
14515016-7	2003	After 1200 s of clotting, purified antithrombin III (22 microM) reduced PCF by 74%.	PHENYL CHLOROFORMATE	72-75	serpin family C member 1	Homo sapiens	35-51
12891293-3	2003	AIM: To study changes of parameters of fibrinolysis during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin.	Ticlopidine	77-88	serpin family C member 1	Homo sapiens	150-162
12891293-3	2003	AIM: To study changes of parameters of fibrinolysis during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin.	Clopidogrel	93-104	serpin family C member 1	Homo sapiens	150-162
14593356-4	2003	AIM: To study changes of markers of coagulation and platelet activation during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin.	Ticlopidine	97-108	serpin family C member 1	Homo sapiens	170-182
14593356-4	2003	AIM: To study changes of markers of coagulation and platelet activation during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin.	Clopidogrel	113-124	serpin family C member 1	Homo sapiens	170-182
14593356-15	2003	Both ticlopidine and clopidogrel used in regimes with loading doses in NSTEACS patients treated with aspirin and antithrombin prevented acute phase elevation of vWF.	Ticlopidine	5-16	serpin family C member 1	Homo sapiens	113-125
14593356-15	2003	Both ticlopidine and clopidogrel used in regimes with loading doses in NSTEACS patients treated with aspirin and antithrombin prevented acute phase elevation of vWF.	Clopidogrel	21-32	serpin family C member 1	Homo sapiens	113-125
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
12492585-10	2003	Reductions of antithrombin and protein S, but not protein C or APC resistance, might relate to the increased risk of venous thrombosis associated with tamoxifen treatment.	Tamoxifen	151-160	serpin family C member 1	Homo sapiens	14-26
12679126-1	2003	Fondaparinux (Arixtra) is the first of a new class of selective indirect antithrombin-dependent factor Xa inhibitors, which inhibits thrombin generation.	Fondaparinux	0-12	serpin family C member 1	Homo sapiens	73-85
12876681-9	2003	The strategy allows the fast identification of methionine- and methionine-sulfoxide-containing peptides even in complex tryptic digests, as demonstrated here for the glycoprotein antithrombin.	Methionine	47-57	serpin family C member 1	Homo sapiens	179-191
12876681-9	2003	The strategy allows the fast identification of methionine- and methionine-sulfoxide-containing peptides even in complex tryptic digests, as demonstrated here for the glycoprotein antithrombin.	Methionine	63-73	serpin family C member 1	Homo sapiens	179-191
12876681-9	2003	The strategy allows the fast identification of methionine- and methionine-sulfoxide-containing peptides even in complex tryptic digests, as demonstrated here for the glycoprotein antithrombin.	sulfoxide	74-83	serpin family C member 1	Homo sapiens	179-191
12679126-1	2003	Fondaparinux (Arixtra) is the first of a new class of selective indirect antithrombin-dependent factor Xa inhibitors, which inhibits thrombin generation.	Fondaparinux	14-21	serpin family C member 1	Homo sapiens	73-85
12433487-6	2002	Our results indicate that a 2-sulfated, 3-linked alpha-L-galactan, but not an alpha-L-fucan, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II.	sulfated	30-38	serpin family C member 1	Homo sapiens	136-148
15013282-0	2003	Antithrombin activity of lepirudin adsorbed to silicone (polydimethylsiloxane) tubing.	Silicones	47-55	serpin family C member 1	Homo sapiens	0-12
15013282-0	2003	Antithrombin activity of lepirudin adsorbed to silicone (polydimethylsiloxane) tubing.	baysilon	57-77	serpin family C member 1	Homo sapiens	0-12
12441904-8	2002	Anti-inflammatory properties of AT independent of coagulation involve direct interactions with cells leading to the release of, for instance, prostacyclin.	Epoprostenol	142-154	serpin family C member 1	Homo sapiens	32-34
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
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.	(2S)-2-(4-(((3S)-1-acetimidoyl-3-pyrrolidinyl)oxy)phenyl)-3-(7-amidino-2-naphtyl)propanoic acid	57-65	serpin family C member 1	Homo sapiens	165-177
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
12397068-5	2002	Similarly, antithrombin inactivated FIXa derivatives with a similar second-order association rate constant (k(2)) in both the absence and presence of pentasaccharide.	pentasaccharide	150-165	serpin family C member 1	Homo sapiens	11-23
12433487-6	2002	Our results indicate that a 2-sulfated, 3-linked alpha-L-galactan, but not an alpha-L-fucan, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II.	3-linked alpha-l-galactan	40-65	serpin family C member 1	Homo sapiens	136-148
12433488-3	2002	1D 1H NMR showed two-thirds of the N-acetyl groups were lost on periodate cleavage, suggesting cleavage had occurred at the glucopyranosyluronic acid (GlcpA) and idopyranosyluronic acid (IdopA) residues located within and adjacent to the antithrombin III (ATIII) binding site.	metaperiodate	64-73	serpin family C member 1	Homo sapiens	238-254
12433488-3	2002	1D 1H NMR showed two-thirds of the N-acetyl groups were lost on periodate cleavage, suggesting cleavage had occurred at the glucopyranosyluronic acid (GlcpA) and idopyranosyluronic acid (IdopA) residues located within and adjacent to the antithrombin III (ATIII) binding site.	metaperiodate	64-73	serpin family C member 1	Homo sapiens	256-261
12433488-5	2002	The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue.	glcpa	4-9	serpin family C member 1	Homo sapiens	30-35
12433488-5	2002	The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue.	n-sulfo	85-92	serpin family C member 1	Homo sapiens	30-35
12433488-5	2002	The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue.	3, 6-o-sulfo glycopyranosylamine	94-126	serpin family C member 1	Homo sapiens	30-35
12433488-5	2002	The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue.	glcpns3s6s	128-138	serpin family C member 1	Homo sapiens	30-35
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
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
12501872-7	2002	RESULTS: Fondaparinux is a synthetic pentasaccharide that selectively binds to antithrombin III, inducing a conformational change that increases anti-factor Xa activity.	pentasaccharide	37-52	serpin family C member 1	Homo sapiens	79-95
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
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
12369826-1	2002	The anticoagulant polysaccharide heparin binds and activates the plasma proteinase inhibitor antithrombin through a pentasaccharide sequence.	polysaccharide heparin	18-40	serpin family C member 1	Homo sapiens	93-105
12369826-1	2002	The anticoagulant polysaccharide heparin binds and activates the plasma proteinase inhibitor antithrombin through a pentasaccharide sequence.	pentasaccharide	116-131	serpin family C member 1	Homo sapiens	93-105
12369826-5	2002	However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114.	Arginine	70-73	serpin family C member 1	Homo sapiens	151-163
12369826-5	2002	However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114.	pentasaccharide	196-211	serpin family C member 1	Homo sapiens	151-163
12369826-5	2002	However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114.	Lysine	223-226	serpin family C member 1	Homo sapiens	151-163
12369826-10	2002	This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor.	Arginine	54-57	serpin family C member 1	Homo sapiens	93-105
12369826-10	2002	This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor.	Arginine	181-184	serpin family C member 1	Homo sapiens	93-105
12369826-10	2002	This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor.	pentasaccharide	212-227	serpin family C member 1	Homo sapiens	93-105
12359224-6	2002	Dimethylsphingosine also inhibited leukocyte chemotaxis toward antithrombin, indicating that similar mechanisms may be involved upon syndecan-4 ligation.	dimethylsphingosine	0-19	serpin family C member 1	Homo sapiens	63-75
12138164-2	2002	The 3-O-sulfated glucosamine residue contributes to two important biological functions of HS: binding to antithrombin and thereby carrying anticoagulant activity, and binding to herpes simplex viral envelope glycoprotein D to serve as an entry receptor for herpes simplex virus 1.	Glucosamine	17-28	serpin family C member 1	Homo sapiens	105-117
12368161-10	2002	Plasma TpP levels correlated significantly with other DIC parameters including platelet count, fibrinogen, antithrombin and TAT, and correlated weakly with D-dimer.	tpp	7-10	serpin family C member 1	Homo sapiens	107-119
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
12244069-3	2002	Our results indicate that a 2-O-sulfated, 3-linked alpha-L-galactan, but not a alpha-L-fucan with a similar molecular size, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II.	2-o-sulfated	28-40	serpin family C member 1	Homo sapiens	167-179
12244069-3	2002	Our results indicate that a 2-O-sulfated, 3-linked alpha-L-galactan, but not a alpha-L-fucan with a similar molecular size, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II.	3-linked alpha-l-galactan	42-67	serpin family C member 1	Homo sapiens	167-179
12244069-5	2002	The occurrence of 2,4-di-O-sulfated units is an amplifying motif for 3-linked alpha-fucan-enhanced thrombin inhibition by antithrombin.	2,4-di-o	18-26	serpin family C member 1	Homo sapiens	122-134
12244069-5	2002	The occurrence of 2,4-di-O-sulfated units is an amplifying motif for 3-linked alpha-fucan-enhanced thrombin inhibition by antithrombin.	sulfated	27-35	serpin family C member 1	Homo sapiens	122-134
12244069-6	2002	If we replace antithrombin by heparin cofactor II, then the major structural requirement for the activity becomes single 4-O-sulfated fucose units.	4-o-sulfated fucose	121-140	serpin family C member 1	Homo sapiens	14-26
12425373-2	2002	This pentasaccharide selectively and specifically inhibits coagulation factor Xa, and requires antithrombin as co-factor It is entirely synthetic, in contrast to conventional heparin and low molecular heparins which are derived from animal tissues.	pentasaccharide	5-20	serpin family C member 1	Homo sapiens	95-107
12238925-1	2002	Recently, we designed (-)-epicatechin sulfate (ECS), the first small nonsaccharide molecule, as an activator of antithrombin for the accelerated inhibition of factor Xa, a key proteinase of the coagulation cascade (Gunnarsson, G. T.; Desai, U. R. J. Med.	epicatechin sulfate	22-45	serpin family C member 1	Homo sapiens	112-124
12238925-1	2002	Recently, we designed (-)-epicatechin sulfate (ECS), the first small nonsaccharide molecule, as an activator of antithrombin for the accelerated inhibition of factor Xa, a key proteinase of the coagulation cascade (Gunnarsson, G. T.; Desai, U. R. J. Med.	epicatechin sulfate	47-50	serpin family C member 1	Homo sapiens	112-124
12238925-1	2002	Recently, we designed (-)-epicatechin sulfate (ECS), the first small nonsaccharide molecule, as an activator of antithrombin for the accelerated inhibition of factor Xa, a key proteinase of the coagulation cascade (Gunnarsson, G. T.; Desai, U. R. J. Med.	nonsaccharide	69-82	serpin family C member 1	Homo sapiens	112-124
12238925-6	2002	(+)-Catechin sulfate (CS), a chiral stereoisomer of ECS, bound plasma antithrombin with a 3-fold higher affinity (K(D) = 3.5 microM) and a 2-fold higher second-order rate constant for factor Xa inhibition (k(ACT) = 6750 M(-1) s(-1)).	catechin sulfate	0-20	serpin family C member 1	Homo sapiens	70-82
12238925-6	2002	(+)-Catechin sulfate (CS), a chiral stereoisomer of ECS, bound plasma antithrombin with a 3-fold higher affinity (K(D) = 3.5 microM) and a 2-fold higher second-order rate constant for factor Xa inhibition (k(ACT) = 6750 M(-1) s(-1)).	catechin sulfate	22-24	serpin family C member 1	Homo sapiens	70-82
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.	silyl-heparins	26-40	serpin family C member 1	Homo sapiens	161-177
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.	pentasaccharide	55-70	serpin family C member 1	Homo sapiens	34-46
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
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
12009311-2	2002	Antithrombin III (ATIII) was purified from ostrich plasma by heparin-Sepharose and Super Q-650S chromatography.	Sepharose	69-78	serpin family C member 1	Homo sapiens	18-23
13679662-1	2002	Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III.	Dermatan Sulfate	0-17	serpin family C member 1	Homo sapiens	151-167
13679662-1	2002	Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III.	Dermatan Sulfate	19-21	serpin family C member 1	Homo sapiens	151-167
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
12353072-1	2002	We investigated the effect of various oligosaccharides (OS) on the inhibition of factor IXa by antithrombin (AT) in a purified system.	Oligosaccharides	38-54	serpin family C member 1	Homo sapiens	95-107
12353072-1	2002	We investigated the effect of various oligosaccharides (OS) on the inhibition of factor IXa by antithrombin (AT) in a purified system.	Oligosaccharides	56-58	serpin family C member 1	Homo sapiens	95-107
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
12353073-1	2002	Here we report the finding of a new natural antithrombin mutation that confirms the critical contribution of lysine 114 to the binding of the core heparin pentasaccharide, with the replacement of lysine 114 by glutamate causing a complete loss in affinity.	Lysine	109-115	serpin family C member 1	Homo sapiens	44-56
12353073-1	2002	Here we report the finding of a new natural antithrombin mutation that confirms the critical contribution of lysine 114 to the binding of the core heparin pentasaccharide, with the replacement of lysine 114 by glutamate causing a complete loss in affinity.	IC 831423	147-170	serpin family C member 1	Homo sapiens	44-56
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.	Sodium Dodecyl Sulfate	18-21	serpin family C member 1	Homo sapiens	187-199
12353073-4	2002	Normal antithrombin binds to the high affinity heparin pentasaccharide with a Kd of 1nM, as detected by a 45% change in intrinsic fluorescence, resulting in a 230-fold increase in rate of factor Xa inhibition.	IC 831423	47-70	serpin family C member 1	Homo sapiens	7-19
12145015-6	2002	CONCLUSION: Percentage enrichment at 3 d (but not at 6 h) can be used to evaluate vitamin A body stores in humans.	Vitamin A	82-91	serpin family C member 1	Homo sapiens	34-40
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
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.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	84-96
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
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
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.	Heparitin Sulfate	64-79	serpin family C member 1	Homo sapiens	84-96
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
12244482-0	2002	Effects of calcium ions on the interactions between antithrombin and factor Xa mediated by variously sulfated, semisynthetic low-molecular-weight heparins.	Calcium	11-18	serpin family C member 1	Homo sapiens	52-64
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
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
12413592-1	2002	Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans.	Glycosaminoglycans	235-253	serpin family C member 1	Homo sapiens	0-12
12413592-1	2002	Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans.	Glycosaminoglycans	235-253	serpin family C member 1	Homo sapiens	14-19
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
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
12121115-9	2002	Finally, the current methodology was applied to the characterization of the biologically important ATIII binding pentasaccharide and its precursors, which differ from each other by sulfation pattern and/or degree of sulfation.	pentasaccharide	113-128	serpin family C member 1	Homo sapiens	99-104
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).	argatroban	103-113	serpin family C member 1	Homo sapiens	69-81
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
12361208-4	2002	These observations provide evidence that the direct antithrombin inhibitors, lepirudin and argatroban, can improve DIC.	argatroban	91-101	serpin family C member 1	Homo sapiens	52-64
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
27264755-2	2002	It is a synthetic pentasaccharide mimicking the site of heparin that binds to antithrombin III (AT).	pentasaccharide	18-33	serpin family C member 1	Homo sapiens	78-94
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
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
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.	pentasaccharide	305-320	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
12161073-3	2002	One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex.	Lysine	13-16	serpin family C member 1	Homo sapiens	37-49
12161073-3	2002	One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex.	Trisaccharides	92-105	serpin family C member 1	Homo sapiens	37-49
12161073-3	2002	One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex.	pentasaccharide	113-128	serpin family C member 1	Homo sapiens	37-49
12161073-4	2002	Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established.	Lysine	20-23	serpin family C member 1	Homo sapiens	203-215
12161073-4	2002	Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established.	Arginine	32-35	serpin family C member 1	Homo sapiens	203-215
12161073-4	2002	Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established.	Lysine	61-64	serpin family C member 1	Homo sapiens	203-215
12161073-4	2002	Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established.	pentasaccharide	231-246	serpin family C member 1	Homo sapiens	203-215
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.	Trisaccharides	74-87	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	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
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
12004255-7	2002	Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces.	pentasaccharides	31-47	serpin family C member 1	Homo sapiens	0-12
12010802-8	2002	The observation that chemically modified AT III that lacks heparin-binding capacity had no effect on NF-kappaB activation supports the current understanding that the inhibitory potency of AT III depends on the interaction of AT III with heparinlike cell surface glycosaminoglycans.	Glycosaminoglycans	262-280	serpin family C member 1	Homo sapiens	188-194
12010802-8	2002	The observation that chemically modified AT III that lacks heparin-binding capacity had no effect on NF-kappaB activation supports the current understanding that the inhibitory potency of AT III depends on the interaction of AT III with heparinlike cell surface glycosaminoglycans.	Glycosaminoglycans	262-280	serpin family C member 1	Homo sapiens	188-194
12010802-9	2002	This hypothesis was underscored by the finding that the AT III beta-isoform, known to have higher affinity for glycosaminoglycans, is more effective in preventing NF-kappaB transactivation than alpha-AT III.	Glycosaminoglycans	111-129	serpin family C member 1	Homo sapiens	56-62
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
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.	pentasaccharide	73-88	serpin family C member 1	Homo sapiens	48-60
12022882-6	2002	The reactivities of Arg(143) and Lys(147) mutants were improved approximately 2-fold with antithrombin in the absence but not in the presence of heparin cofactors.	Arginine	20-23	serpin family C member 1	Homo sapiens	90-102
12022882-6	2002	The reactivities of Arg(143) and Lys(147) mutants were improved approximately 2-fold with antithrombin in the absence but not in the presence of heparin cofactors.	Lysine	33-36	serpin family C member 1	Homo sapiens	90-102
12022882-7	2002	On the other hand, the pentasaccharide-catalyzed reactivity of antithrombin with the Arg(150) mutant was impaired by an order of magnitude.	pentasaccharide	23-38	serpin family C member 1	Homo sapiens	63-75
12022882-7	2002	On the other hand, the pentasaccharide-catalyzed reactivity of antithrombin with the Arg(150) mutant was impaired by an order of magnitude.	Arginine	85-88	serpin family C member 1	Homo sapiens	63-75
12022882-8	2002	These results suggest that Arg(150) of the autolysis loop may specifically interact with the activated conformation of antithrombin.	Arginine	27-30	serpin family C member 1	Homo sapiens	119-131
11971909-0	2002	Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition.	Arginine	18-26	serpin family C member 1	Homo sapiens	97-113
11971909-0	2002	Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition.	Glutamic Acid	59-72	serpin family C member 1	Homo sapiens	97-113
11971909-1	2002	The mechanism for heparin activation of antithrombin III has been postulated to involve disruption of interactions between its reactive loop P1 residue and Glu(255) on the underlying protein surface.	Glutamic Acid	156-159	serpin family C member 1	Homo sapiens	40-56
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
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
12004255-7	2002	Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces.	Glycosaminoglycans	70-88	serpin family C member 1	Homo sapiens	0-12
12004255-10	2002	In addition, antithrombin exerts anti-inflammatory properties by both prostacyclin-dependent and prostacyclin-independent actions; heparin interferes with these anti-inflammatory properties.	Epoprostenol	70-82	serpin family C member 1	Homo sapiens	13-25
12004255-10	2002	In addition, antithrombin exerts anti-inflammatory properties by both prostacyclin-dependent and prostacyclin-independent actions; heparin interferes with these anti-inflammatory properties.	Epoprostenol	97-109	serpin family C member 1	Homo sapiens	13-25
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
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
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
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
11870603-4	2002	Elevation of expression level by selection for increased drug resistance in Chinese hamster ovary cells stably expressing ATIII resulted in formation of disulfide-bonded aggregates of ATIII.	Disulfides	153-162	serpin family C member 1	Homo sapiens	122-127
11870603-4	2002	Elevation of expression level by selection for increased drug resistance in Chinese hamster ovary cells stably expressing ATIII resulted in formation of disulfide-bonded aggregates of ATIII.	Disulfides	153-162	serpin family C member 1	Homo sapiens	184-189
11870603-8	2002	However, the amount of ATIII-synthesized per L-glutamine consumed did not seem to increase steadily with expression level for ATIII, indicating that secretion of ATIII may be limited by the capacity of the cell to utilize L-glutamine.	Glutamine	45-56	serpin family C member 1	Homo sapiens	23-28
11939772-0	2002	Importance of lysine 125 for heparin binding and activation of antithrombin.	Lysine	14-20	serpin family C member 1	Homo sapiens	63-75
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
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.	Polysaccharides	27-41	serpin family C member 1	Homo sapiens	106-118
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
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.	pentasaccharide	194-209	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.	pentasaccharide	194-209	serpin family C member 1	Homo sapiens	175-187
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.	pentasaccharide	194-209	serpin family C member 1	Homo sapiens	175-187
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
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
11939772-3	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.	pentasaccharide	119-134	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
11895775-13	2002	Some antibodies reacted strongly with the pentasaccharide, which interacts with antithrombin III.	pentasaccharide	42-57	serpin family C member 1	Homo sapiens	80-96
11934350-2	2002	Fondaparinux is a synthetic polysaccharide that selectively binds to antithrombin, the primary endogenous regulator of blood coagulation.	Polysaccharides	28-42	serpin family C member 1	Homo sapiens	69-81
11881992-7	2002	HINT suggested a comparable antithrombin-binding geometry and interaction profile for ECS and trisaccharide DEF.	Trisaccharides	94-107	serpin family C member 1	Homo sapiens	28-40
11854268-0	2002	Molecular determinants of the mechanism underlying acceleration of the interaction between antithrombin and factor Xa by heparin pentasaccharide.	IC 831423	121-144	serpin family C member 1	Homo sapiens	91-103
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.	pentasaccharide	11-26	serpin family C member 1	Homo sapiens	101-113
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
11854268-4	2002	Thus, synthetic H5 accelerates the interaction between antithrombin and fXa 100-fold as compared with only 2-fold versus thrombin.	h5	16-18	serpin family C member 1	Homo sapiens	55-67
11854268-8	2002	The x-ray crystal structure of fXa reveals that Gln(61) forms part of the S1" and S3" pocket, suggesting that the P" region of the reactive center loop of antithrombin is crucial for mediating the acceleration in the rate of inhibition of fXa by H5-activated antithrombin.	Glutamine	48-51	serpin family C member 1	Homo sapiens	155-167
11854268-8	2002	The x-ray crystal structure of fXa reveals that Gln(61) forms part of the S1" and S3" pocket, suggesting that the P" region of the reactive center loop of antithrombin is crucial for mediating the acceleration in the rate of inhibition of fXa by H5-activated antithrombin.	Glutamine	48-51	serpin family C member 1	Homo sapiens	259-271
11951068-8	2002	In the patient group (with AT III and/or PC and/or PS decrease) statistically significant reduction of kaolin-kephalin time in comparison with controls was observed (a<0.	kaolin-kephalin	103-118	serpin family C member 1	Homo sapiens	27-33
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
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.	polyanionic polysaccharide	188-214	serpin family C member 1	Homo sapiens	29-41
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
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.	pentasaccharide	2-17	serpin family C member 1	Homo sapiens	54-66
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
11741963-4	2002	To investigate the role of helix D elongation in the allosteric activation of antithrombin, we substituted a proline residue for Lys(133).	Proline	109-116	serpin family C member 1	Homo sapiens	78-90
11741963-4	2002	To investigate the role of helix D elongation in the allosteric activation of antithrombin, we substituted a proline residue for Lys(133).	Lysine	129-132	serpin family C member 1	Homo sapiens	78-90
11846379-6	2002	Similar experiments with alpha(1)-proteinase inhibitor and antithrombin, two inhibitory serpins that exhibit reactive center loop insertion, show a decrease in ANS fluorescence on cleavage with porcine pancreatic elastase and thrombin, respectively.	1-anilino-8-naphthalenesulfonate	160-163	serpin family C member 1	Homo sapiens	59-71
12532174-3	2002	Its structure is the copy of the heparin pentasaccharide sequence, the shortest chain required for antithrombin inhibition of activated factor X without antithrombin action.	IC 831423	33-56	serpin family C member 1	Homo sapiens	99-111
12532174-3	2002	Its structure is the copy of the heparin pentasaccharide sequence, the shortest chain required for antithrombin inhibition of activated factor X without antithrombin action.	IC 831423	33-56	serpin family C member 1	Homo sapiens	153-165
11866668-2	2002	It is a chemically synthetic pentasaccharide mimicking the site of heparin that binds to antithrombin III (AT).	pentasaccharide	29-44	serpin family C member 1	Homo sapiens	89-105
12096932-5	2002	A small, preliminary clinical trial has suggested that antithrombin therapy with intravenously administered argatroban may be useful in treatment of ICH.	argatroban	108-118	serpin family C member 1	Homo sapiens	55-67
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
12091056-1	2002	Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a specific pentasaccharide sequence.	pentasaccharide	86-101	serpin family C member 1	Homo sapiens	0-12
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
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
11806943-7	2002	Analytical characterization of water-permeable volumes in x-ray-derived bound and free antithrombin structures were correlated with the volumes measured in solution.	Water	31-36	serpin family C member 1	Homo sapiens	87-99
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
11812067-12	2002	These findings regarding enoxaparin add to the data to be considered by clinicians when selecting an antithrombin for the acute phase of management of unstable angina/non-ST elevation myocardial infarction.	Enoxaparin	25-35	serpin family C member 1	Homo sapiens	101-113
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
11831754-5	2002	The buffer, 25 mM Tris-HCl pH 8.0; the eluting agent, 2 M (NH4)2SO4; and 100% expansion of settled bed were determined to be the optimum conditions for the purification of antithrombin by ion-exchange expanded bed chromatography.	Tris hydrochloride	18-26	serpin family C member 1	Homo sapiens	172-184
11831754-5	2002	The buffer, 25 mM Tris-HCl pH 8.0; the eluting agent, 2 M (NH4)2SO4; and 100% expansion of settled bed were determined to be the optimum conditions for the purification of antithrombin by ion-exchange expanded bed chromatography.	Ammonium Sulfate	58-67	serpin family C member 1	Homo sapiens	172-184
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)).	pentasaccharide	108-123	serpin family C member 1	Homo sapiens	7-19
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
12168569-4	2002	Antithrombin III stimulates prostacyclin generation in endothelial cells by interacting with heparan sulfate of endothelial cells and inhibits cytokine and tissue factor production in endothelial cells and monocytes.	Epoprostenol	28-40	serpin family C member 1	Homo sapiens	0-16
12168569-4	2002	Antithrombin III stimulates prostacyclin generation in endothelial cells by interacting with heparan sulfate of endothelial cells and inhibits cytokine and tissue factor production in endothelial cells and monocytes.	Heparitin Sulfate	93-108	serpin family C member 1	Homo sapiens	0-16
11919156-5	2002	We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding.	3-o, 6-o	36-44	serpin family C member 1	Homo sapiens	100-116
11919156-5	2002	We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding.	3-o, 6-o	36-44	serpin family C member 1	Homo sapiens	118-124
11919156-5	2002	We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding.	Oligosaccharides	80-95	serpin family C member 1	Homo sapiens	100-116
11919156-5	2002	We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding.	Oligosaccharides	80-95	serpin family C member 1	Homo sapiens	118-124
11919156-6	2002	We regenerated the binding sites for AT-III on completely desulfated N-resulfated heparin and revealed the critical modification enzymes.	Nitrogen	69-70	serpin family C member 1	Homo sapiens	37-43
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
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
12383040-4	2002	OBJECTIVE: To investigate the in vitro binding of fondaparinux sodium to purified antithrombin III (ATIII) and other plasma proteins.	Fondaparinux	50-69	serpin family C member 1	Homo sapiens	82-98
12383040-4	2002	OBJECTIVE: To investigate the in vitro binding of fondaparinux sodium to purified antithrombin III (ATIII) and other plasma proteins.	Fondaparinux	50-69	serpin family C member 1	Homo sapiens	100-105
12383040-5	2002	METHODS: Fondaparinux sodium was incubated with human plasma, antithrombin-depleted plasma or purified human plasma proteins, including antithrombin, alpha1-acid glycoprotein, serum albumin and immunoglobulin.	Fondaparinux	9-28	serpin family C member 1	Homo sapiens	62-74
12383040-5	2002	METHODS: Fondaparinux sodium was incubated with human plasma, antithrombin-depleted plasma or purified human plasma proteins, including antithrombin, alpha1-acid glycoprotein, serum albumin and immunoglobulin.	Fondaparinux	9-28	serpin family C member 1	Homo sapiens	136-148
12383040-7	2002	RESULTS: At steady state, fondaparinux sodium at therapeutic concentrations [i.e. those attainable in the prevention (0.14 to 0.50 mg/L) and treatment (up to approximately 2 mg/L) of VTE] was extensively bound (>97%) to plasma proteins and specifically bound (>94%) to purified ATIII.	Fondaparinux	26-45	serpin family C member 1	Homo sapiens	284-289
12811008-0	2002	Development of argatroban as an anticoagulant and antithrombin agent in Japan.	argatroban	15-25	serpin family C member 1	Homo sapiens	50-62
11801740-10	2002	Effects of antithrombin were abolished by pretreating cells with heparinase-1, chondroitinase, sodium chlorate and anti-syndecan-4 antibodies.	sodium chlorate	95-110	serpin family C member 1	Homo sapiens	11-23
11801740-12	2002	In the presence of pentasaccharide, antithrombin lost its effect on cells.	pentasaccharide	19-34	serpin family C member 1	Homo sapiens	36-48
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
12494145-5	2002	Multifactorial regression analysis showed that gender was independently (of age, duration of hypertension, smoking, body mass index, and total cholesterol level) related to only antithrombin III and protein C levels.	Cholesterol	143-154	serpin family C member 1	Homo sapiens	178-194
12811008-2	2002	In patients with chronic arterial occlusion, argatroban increased the skin temperature, reduced the size of skin ulcers, and decreased the thrombin-antithrombin complex.	argatroban	45-55	serpin family C member 1	Homo sapiens	148-160
12811013-1	2002	Argatroban was the very first antithrombin agent that was approved for clinical use.	argatroban	0-10	serpin family C member 1	Homo sapiens	30-42
12811013-3	2002	Unlike other antithrombin drugs, argatroban is a reversible antithrombin agent.	argatroban	33-43	serpin family C member 1	Homo sapiens	13-25
12811013-3	2002	Unlike other antithrombin drugs, argatroban is a reversible antithrombin agent.	argatroban	33-43	serpin family C member 1	Homo sapiens	60-72
12811013-6	2002	At a comparable ACT (300 s), argatroban produces much stronger inhibition of thrombin generation as measured by F(1.2) and thrombin-antithrombin complex generation.	argatroban	29-39	serpin family C member 1	Homo sapiens	132-144
12811013-8	2002	The pharmacological profile of argatroban is unique as this antithrombin drug not only inhibits thrombogenesis but also modulates cellular functions.	argatroban	31-41	serpin family C member 1	Homo sapiens	60-72
11755953-3	2001	We have estimated the concentration of circulating thrombin-antithrombin (TAT) complex in patients subjected to transperitoneal nephrectomy and randomized into controls and who received 40-mg enoxaparin 12 h before and 12 h after the operation and then once daily for 7 days.	Enoxaparin	192-202	serpin family C member 1	Homo sapiens	60-72
11677228-1	2001	Measurement of water transfer during antithrombin activation by heparin.	Water	15-20	serpin family C member 1	Homo sapiens	37-49
11677228-1	2001	Measurement of water transfer during antithrombin activation by heparin.	Heparin	64-71	serpin family C member 1	Homo sapiens	37-49
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
11677228-4	2001	We investigated water-transfer reactions during the activation process to explore the possibility that functional interaction between antithrombin and sulfated glycosaminoglycans can be regulated by osmotic potentials.	Water	16-21	serpin family C member 1	Homo sapiens	134-146
11677228-6	2001	Osmotic stress was induced with chemically inert probes that are geometrically excluded from the water-permeable spaces of antithrombin and from intermolecular spaces formed during the association reaction.	Water	97-102	serpin family C member 1	Homo sapiens	123-135
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
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
11677228-11	2001	Analytical characterization of water-permeable volumes in x-ray-derived bound and free antithrombin structures revealed complex surfaces with smaller hydration volumes in the bound relative to the free conformation.	Water	31-36	serpin family C member 1	Homo sapiens	87-99
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
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
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
11798464-7	2001	To date, we cannot provide a mechanism to explain the AT III-promoted modulation of TNF-alpha and IL-1beta generation in VSMC.	vsmc	121-125	serpin family C member 1	Homo sapiens	54-60
11567021-0	2001	Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding.	Lysine	0-6	serpin family C member 1	Homo sapiens	14-26
11567021-0	2001	Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding.	IC 831423	85-108	serpin family C member 1	Homo sapiens	14-26
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
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.	pentasaccharide	251-266	serpin family C member 1	Homo sapiens	57-69
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.	pentasaccharide	251-266	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
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
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%.	pentasaccharide	131-146	serpin family C member 1	Homo sapiens	98-110
11567021-4	2001	The mutation minimally affected the initial, weak binding of the two-step mechanism of pentasaccharide binding to antithrombin but appreciably (>40-fold) decreased the forward rate constant of the conformational change in the second step and greatly (>1000-fold) increased the reverse rate constant of this step.	pentasaccharide	87-102	serpin family C member 1	Homo sapiens	114-126
11567021-8	2001	However, its major effect, also larger than that of these two residues, is in maintaining antithrombin in the activated state by interactions that most likely involve the reducing end disaccharide unit.	Disaccharides	184-196	serpin family C member 1	Homo sapiens	90-102
11728442-4	2001	The serpin antithrombin III (ATIII) and the thrombin inhibitor hirudin both inhibited nuclear factor (NF)-kappaB activation by LPS and Lipid A.	Lipid A	135-142	serpin family C member 1	Homo sapiens	11-27
11728442-4	2001	The serpin antithrombin III (ATIII) and the thrombin inhibitor hirudin both inhibited nuclear factor (NF)-kappaB activation by LPS and Lipid A.	Lipid A	135-142	serpin family C member 1	Homo sapiens	29-34
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.	Iduronic Acid	37-52	serpin family C member 1	Homo sapiens	154-166
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.	Iduronic Acid	57-72	serpin family C member 1	Homo sapiens	121-133
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
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.	Iduronic Acid	83-98	serpin family C member 1	Homo sapiens	120-132
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
11794963-2	2001	The new anticoagulants are as follows: saccharide structures such as danaparoid and the pentasaccharide of antithrombin binding, and direct thrombin inhibitors, such as recombinating hirudines (desirudine, lepirudine), bivalirudine, melagatran.... Other molecular targets are possible, both at platelet and blood clotting levels but, for the moment, the dilemma remains and reinforcement of antithrombotic activity goes hand in hand with a greater decrease in the defensive mechanisms against bleeding.	pentasaccharide	88-103	serpin family C member 1	Homo sapiens	107-119
11722589-3	2001	We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI).	Tritium	22-26	serpin family C member 1	Homo sapiens	174-190
11722589-3	2001	We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI).	Estradiol	57-66	serpin family C member 1	Homo sapiens	174-190
11722589-3	2001	We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI).	Progesterone	68-80	serpin family C member 1	Homo sapiens	174-190
11722589-3	2001	We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI).	Testosterone	82-94	serpin family C member 1	Homo sapiens	174-190
11722589-3	2001	We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI).	Hydrocortisone	96-104	serpin family C member 1	Homo sapiens	174-190
11722589-3	2001	We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI).	Aldosterone	106-117	serpin family C member 1	Homo sapiens	174-190
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<.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
11583572-0	2001	Conformation of heparin pentasaccharide bound to antithrombin III.	IC 831423	16-39	serpin family C member 1	Homo sapiens	49-65
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
12004145-8	2001	Activity of AT III and protein C within 72 hours after introduction of steroids increased without any marked alterations in the clinical and biochemical course of the nephrotic syndrome.	Steroids	71-79	serpin family C member 1	Homo sapiens	12-18
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
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, Low-Molecular-Weight	127-139	serpin family C member 1	Homo sapiens	265-277
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
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
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
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
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.	Sodium Dodecyl Sulfate	32-35	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.	Sodium Dodecyl Sulfate	32-35	serpin family C member 1	Homo sapiens	74-79
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.	Sodium Dodecyl Sulfate	32-35	serpin family C member 1	Homo sapiens	151-156
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.	Sodium Dodecyl Sulfate	32-35	serpin family C member 1	Homo sapiens	151-156
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
11549250-3	2001	In vitro effects of antithrombin on human neutrophil migration in modified Boyden chambers were abolished by pretreating cells with heparinase-1, chondroitinase, sodium chlorate, and anti-syndecan-4 antibodies.	sodium chlorate	162-177	serpin family C member 1	Homo sapiens	20-32
11549250-5	2001	In the presence of pentasaccharide, antithrombin lost its activity on the cells.	pentasaccharide	19-34	serpin family C member 1	Homo sapiens	36-48
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
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
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.	pgma-i	115-121	serpin family C member 1	Homo sapiens	165-181
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
11748680-10	2001	All the three heparin-PGMA beads were exploited for the separation of antithrombin III from human plasma.	pgma	22-26	serpin family C member 1	Homo sapiens	70-86
11669429-14	2001	A predictable drop of AT III (24.2%) occurred with saline dilution, while AT III levels in the AT III/Saline group were similar to the undiluted control.	Sodium Chloride	51-57	serpin family C member 1	Homo sapiens	22-28
11669429-14	2001	A predictable drop of AT III (24.2%) occurred with saline dilution, while AT III levels in the AT III/Saline group were similar to the undiluted control.	Sodium Chloride	102-108	serpin family C member 1	Homo sapiens	74-80
11669429-14	2001	A predictable drop of AT III (24.2%) occurred with saline dilution, while AT III levels in the AT III/Saline group were similar to the undiluted control.	Sodium Chloride	102-108	serpin family C member 1	Homo sapiens	74-80
11575948-3	2001	Atherospermidine and squamolone exhibited cytotoxicity against hepatocarcinoma cancer cell lines (Hep G(2) and 2,2,15), and the activity of some of the alkaloids in an antithrombin assay is also discussed.	atherospermidine	0-16	serpin family C member 1	Homo sapiens	168-180
11575948-3	2001	Atherospermidine and squamolone exhibited cytotoxicity against hepatocarcinoma cancer cell lines (Hep G(2) and 2,2,15), and the activity of some of the alkaloids in an antithrombin assay is also discussed.	squamolone	21-31	serpin family C member 1	Homo sapiens	168-180
11778099-5	2001	The pentasaccharide binds specifically to antithrombin III (ATIII) thus potentiating its inhibitory activity on factor Xa.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	42-58
11778099-5	2001	The pentasaccharide binds specifically to antithrombin III (ATIII) thus potentiating its inhibitory activity on factor Xa.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	60-65
11479487-6	2001	RESULTS: The more recently developed synthetic pentasaccharide Org31540/SR90107A provides potent antithrombotic activity through selective inhibition of Factor Xa by high-affinity binding to antithrombin III.	pentasaccharide	47-62	serpin family C member 1	Homo sapiens	191-207
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
11522012-7	2001	The release of these proteins from cells within the necrotic core of a tumour or from cells killed during chemotherapy may abrogate the heparan sulphate/antithrombin system and possibly contribute to the idiopathic thromboembolism often associated with cancer (Trousseau"s syndrome).	Heparitin Sulfate	136-152	serpin family C member 1	Homo sapiens	153-165
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
11487039-9	2001	The efficacy and safety of pentasaccharide (the smallest antithrombin binding sequence of heparin) in the treatment and prevention of venous thromboembolic disorders is currently under investigation.	pentasaccharide	27-42	serpin family C member 1	Homo sapiens	57-69
11487041-8	2001	Antithrombin has been shown in vitro to increase prostacyclin responses and activated protein C has been shown to inhibit a variety of cellular responses including endotoxin induced calcium fluxes in monocytes and the nuclear translocation of NFKB, a key step in the generation of the inflammatory response.	Calcium	182-189	serpin family C member 1	Homo sapiens	0-12
11389017-4	2001	The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond.	Arginine	179-182	serpin family C member 1	Homo sapiens	75-91
11389017-4	2001	The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond.	Arginine	179-182	serpin family C member 1	Homo sapiens	133-149
11521878-4	2001	Micellar electrokinetic chromatography was used to analytically separate these AT III variants, which differ in their affinity to the polysaccharide heparin.	Polysaccharides	134-148	serpin family C member 1	Homo sapiens	79-85
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
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
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
11380262-2	2001	Heparin has been proposed to conformationally activate the serpin, antithrombin, by making the reactive center loop P1 arginine residue accessible to proteinases.	Arginine	119-127	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.	Arginine	71-79	serpin family C member 1	Homo sapiens	83-95
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
11380262-4	2001	As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)).	Arginine	32-40	serpin family C member 1	Homo sapiens	120-132
11380262-4	2001	As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)).	Tryptophan	44-54	serpin family C member 1	Homo sapiens	120-132
11380262-4	2001	As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)).	Histidine	56-65	serpin family C member 1	Homo sapiens	120-132
11380262-4	2001	As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)).	Leucine	67-74	serpin family C member 1	Homo sapiens	120-132
11380262-4	2001	As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)).	Methionine	80-90	serpin family C member 1	Homo sapiens	120-132
11380262-6	2001	Mutation of the P1 arginine greatly reduced k(assoc) for antithrombin inhibition of thrombin and factor Xa from 40- to 5000-fold, but heparin normally accelerated the reactions of the variant antithrombins with these enzymes to make them reasonably efficient inhibitors (k(assoc) = 10(3)-10(4) M(-1) s(-1)).	Arginine	19-27	serpin family C member 1	Homo sapiens	57-69
11380262-10	2001	Together, these findings suggest that the P1 arginine residue is similarly accessible to proteinases in both native and heparin-activated states of the serpin and contributes similarly to the specificity of antithrombin for thrombin and factor Xa in the two serpin conformational states.	Arginine	45-53	serpin family C member 1	Homo sapiens	207-219
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
11278943-5	2001	The kinetics of inhibition of factor Xa (FXa) by antithrombin (AT) and AT-heparin were measured by monitoring activation of II(S525C)-fluorescein and the hydrolysis of the chromogenic substrate S2222 in the presence of AT.	Fluorescein	134-145	serpin family C member 1	Homo sapiens	49-61
11389017-4	2001	The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond.	Serine	188-191	serpin family C member 1	Homo sapiens	75-91
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
11278930-4	2001	Evaluation of 12 such antithrombin variants showed that the thrombin specificity of the serpin allosterically activated by a heparin pentasaccharide could be enhanced as much as 55-fold by changing P3, P2, and P2" residues to a consensus thrombin recognition sequence.	IC 831423	125-148	serpin family C member 1	Homo sapiens	22-34
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
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
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
11350186-6	2001	Short-term low-dose oral mannose supplementation improved her transferrin IEF pattern and normalized her antithrombin III activity, further substantiating the beneficial effect of mannose in CDG-Ib.	Mannose	25-32	serpin family C member 1	Homo sapiens	105-121
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
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
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, Low-Molecular-Weight	66-70	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, Low-Molecular-Weight	66-70	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.	Enoxaparin	73-83	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.	Dalteparin	85-92	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.	ardeparin	97-106	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.	ardeparin	97-106	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
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
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
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
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
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
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
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
11337927-2	2001	The purpose of this study is to elucidate efficacy and safety of a combined approach using a bolus injection of low dose of mutant tissue plasminogen activator (mt-PA) with heparin and aspirin to ensure definite antithrombin and antiplatelet efficacy, followed by back-up percutaneous transluminal coronary angioplasty(PTCA).	mt-pa	161-166	serpin family C member 1	Homo sapiens	212-224
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
11337927-2	2001	The purpose of this study is to elucidate efficacy and safety of a combined approach using a bolus injection of low dose of mutant tissue plasminogen activator (mt-PA) with heparin and aspirin to ensure definite antithrombin and antiplatelet efficacy, followed by back-up percutaneous transluminal coronary angioplasty(PTCA).	Aspirin	185-192	serpin family C member 1	Homo sapiens	212-224
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
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
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
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
11260565-6	2001	RESULTS: We found that high-dose methotrexate administration adversely affected both the coagulation system (prolonged prothrombin time and activated partial thromboplastin time and decreased fibrinogen levels) and coagulation inhibitors (decreased protein C, protein S, antithrombin III) on day 1 after chemotherapy compared to the baseline values.	Methotrexate	33-45	serpin family C member 1	Homo sapiens	271-287
11134031-2	2001	Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold.	Heparin, Low-Molecular-Weight	34-38	serpin family C member 1	Homo sapiens	66-78
11134031-2	2001	Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold.	la-lmwh	80-87	serpin family C member 1	Homo sapiens	66-78
11134031-2	2001	Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold.	Heparin, Low-Molecular-Weight	83-87	serpin family C member 1	Homo sapiens	66-78
11323006-1	2001	In the presence of glycosaminoglycans, thrombin is rapidly inactivated by two natural inhibitors secreted from liver: antithrombin (AT) is presumed to be the principal thrombin inhibitor in circulating blood, while for heparin cofactor II (HCII), a role outside circulation has been proposed.	Glycosaminoglycans	19-37	serpin family C member 1	Homo sapiens	118-130
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
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
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
11304663-10	2001	In children treated with prednisone alone, a marked increase in plasma AT-III (by 76%, P < 0.001) and alpha 2-A (36%, P < 0.019) activity, and a significant decrease of the plasma fibrinogen concentration (6.07 +/- 1.66 vs. 3.17 +/- 1.64 g/L, P < 0.001), and APTT (45.1 +/- 7.6 vs. 33.8 +/- 4.4 s, P < 0.001) were found.	Prednisone	25-35	serpin family C member 1	Homo sapiens	71-77
11304663-11	2001	Prednisone plus EACA therapy resulted in a significant increase in plasma AT-III activity (by 53%, P < 0.003), whereas plasma fibrinogen concentration and APTT remained unchanged.	Prednisone	0-10	serpin family C member 1	Homo sapiens	74-80
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
11159540-4	2001	Preincubation in vitro of neutrophils with Kybernin P or immune-adsorbed AT III significantly deactivated migration toward fMet-Leu-Phe, or interleukin-8 (IL-8), in a concentration-dependent manner.	Leucine	128-131	serpin family C member 1	Homo sapiens	73-79
11159540-4	2001	Preincubation in vitro of neutrophils with Kybernin P or immune-adsorbed AT III significantly deactivated migration toward fMet-Leu-Phe, or interleukin-8 (IL-8), in a concentration-dependent manner.	Phenylalanine	132-135	serpin family C member 1	Homo sapiens	73-79
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
11159540-8	2001	Mechanisms of intracellular signaling differed; the deactivation of IL-8-induced chemotaxis resulted from tyrphostin-sensitive interactions of AT III-signaling with the IL-8 signal transduction pathway, whereas AT III-induced chemotaxis involved protein kinase C and phosphodiesterases.	Tyrphostins	106-116	serpin family C member 1	Homo sapiens	143-149
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
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
11162400-6	2001	Antithrombin was eluted at about 13 min, and L-AT, at 30 min, corresponding to about 4.2 and 1.6 mol/L sodium chloride, respectively.	Sodium Chloride	103-118	serpin family C member 1	Homo sapiens	0-12
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
14728009-1	2001	Enoxaparin (enoxaparin sodium) is a low-molecular-weight heparin that binds to and increases the activity of antithrombin III.	Enoxaparin	0-10	serpin family C member 1	Homo sapiens	109-125
14728009-1	2001	Enoxaparin (enoxaparin sodium) is a low-molecular-weight heparin that binds to and increases the activity of antithrombin III.	Enoxaparin	12-29	serpin family C member 1	Homo sapiens	109-125
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
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
11133602-13	2001	In adult patients, preoperative AT activity depended predominantly on preoperative heparin treatment: 62% of the patients with an AT activity <80% were pretreated with heparin.	Heparin	83-90	serpin family C member 1	Homo sapiens	32-34
11133602-13	2001	In adult patients, preoperative AT activity depended predominantly on preoperative heparin treatment: 62% of the patients with an AT activity <80% were pretreated with heparin.	Heparin	171-178	serpin family C member 1	Homo sapiens	32-34
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
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
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
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
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
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.	pentasaccharide	12-27	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.	pentasaccharide	12-27	serpin family C member 1	Homo sapiens	83-88
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.	PENTA	29-36	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.	PENTA	29-36	serpin family C member 1	Homo sapiens	83-88
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
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
11133602-16	2001	In Group A patients with decreased AT activity, 18% demonstrated an inadequate ACT response-defined as ACT <400 s-to the first bolus injection of heparin.	Heparin	149-156	serpin family C member 1	Homo sapiens	35-37
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
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
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.	reviparin	12-21	serpin family C member 1	Homo sapiens	150-162
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.	reviparin	23-39	serpin family C member 1	Homo sapiens	150-162
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, Low-Molecular-Weight	76-80	serpin family C member 1	Homo sapiens	150-162
11099716-5	2000	Percent activity of AT-III was significantly decreased in CEI patients for 3 weeks compared to this activity in controls, LI and ATI (P<0.001).	4-Amino-2,2,5,5-tetramethyl-3-imidazoli-ne-1-yloxyl free radical	129-132	serpin family C member 1	Homo sapiens	20-26
11734954-1	2001	The aim of this study was to assess in vivo patency of seven commonly used non-ferromagnetic plain stents as regards demonstration of the contained lumen at 3D gadolinium-enhanced MRA in a 0.5-T MR environment.	Gadolinium	160-170	serpin family C member 1	Homo sapiens	154-159
11853380-3	2001	The APTT was prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III.	pu-hep	26-32	serpin family C member 1	Homo sapiens	83-99
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
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
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
11124600-7	2000	Serum anti-Xa activity is better than activated partial thromboplastin time and antithrombin in assessing the optimal dose of LMWH.	Heparin, Low-Molecular-Weight	126-130	serpin family C member 1	Homo sapiens	80-92
11154130-0	2000	Antithrombin niigata: a novel missense mutation (Thr194-Ile) of the antithrombin gene results in type I deficiency.	niigata	13-20	serpin family C member 1	Homo sapiens	0-12
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
11154130-0	2000	Antithrombin niigata: a novel missense mutation (Thr194-Ile) of the antithrombin gene results in type I deficiency.	niigata	13-20	serpin family C member 1	Homo sapiens	68-80
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
10973949-9	2000	Antithrombin binds to Xa-calcium with a approximately 4-fold faster rate, to sodium-Xa with a approximately 24-fold faster rate and to sodium-Xa-calcium with a approximately 28-fold faster rate.	sodium-xa	77-86	serpin family C member 1	Homo sapiens	0-12
10973949-9	2000	Antithrombin binds to Xa-calcium with a approximately 4-fold faster rate, to sodium-Xa with a approximately 24-fold faster rate and to sodium-Xa-calcium with a approximately 28-fold faster rate.	sodium-xa-calcium	135-152	serpin family C member 1	Homo sapiens	0-12
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
11065253-2	2000	In our previous study, the antithrombin drug argatroban t ameliorated the neurological exacerbations in a BD patient with antiphospholipid antibody syndrome.	argatroban	45-55	serpin family C member 1	Homo sapiens	27-39
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
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.	Calcium	84-91	serpin family C member 1	Homo sapiens	173-185
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
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%.	Nadroparin	150-161	serpin family C member 1	Homo sapiens	197-203
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.	Calcium	0-7	serpin family C member 1	Homo sapiens	42-54
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
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.	Calcium	0-7	serpin family C member 1	Homo sapiens	127-139
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
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.	Calcium	248-255	serpin family C member 1	Homo sapiens	49-61
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.	Calcium	270-277	serpin family C member 1	Homo sapiens	49-61
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.	gamma-Linolenic Acid	300-303	serpin family C member 1	Homo sapiens	49-61
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
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.	gdfxa	156-161	serpin family C member 1	Homo sapiens	101-113
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.	Calcium	241-248	serpin family C member 1	Homo sapiens	101-113
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).	Carbohydrates	123-133	serpin family C member 1	Homo sapiens	65-77
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
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
11009624-5	2000	Similar saturation kinetics were observed for the inhibition of GDFXa by the antithrombin-heparin complex, except that Ca(2+) was not required for the effect.	gdfxa	64-69	serpin family C member 1	Homo sapiens	77-89
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
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
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
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
11006120-0	2000	Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III.	Heparitin Sulfate	26-41	serpin family C member 1	Homo sapiens	85-101
11006120-2	2000	Surface plasmon resonance spectroscopy showed a low affinity interaction with antithrombin III (ATIII) when it was flowed over a surface containing heparan sulfate.	Heparitin Sulfate	148-163	serpin family C member 1	Homo sapiens	78-94
11006120-2	2000	Surface plasmon resonance spectroscopy showed a low affinity interaction with antithrombin III (ATIII) when it was flowed over a surface containing heparan sulfate.	Heparitin Sulfate	148-163	serpin family C member 1	Homo sapiens	96-101
11006120-3	2000	ATIII bound tightly with high affinity when the same surface was enzymatically modified to using 3-O-sulfotransferase isoform 1 (3-OST-1) in the presence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS).	Phosphoadenosine Phosphosulfate	157-194	serpin family C member 1	Homo sapiens	0-5
11006120-3	2000	ATIII bound tightly with high affinity when the same surface was enzymatically modified to using 3-O-sulfotransferase isoform 1 (3-OST-1) in the presence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS).	Phosphoadenosine Phosphosulfate	196-200	serpin family C member 1	Homo sapiens	0-5
11006120-4	2000	The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII.	Heparitin Sulfate	34-49	serpin family C member 1	Homo sapiens	220-225
11006120-4	2000	The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII.	3-o-sulfo	89-98	serpin family C member 1	Homo sapiens	220-225
11006120-4	2000	The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII.	Glycosaminoglycans	115-132	serpin family C member 1	Homo sapiens	220-225
11006120-4	2000	The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII.	pentasaccharide	159-174	serpin family C member 1	Homo sapiens	220-225
10974350-3	2000	The interaction of plasminogen was significantly (>90%) inhibited by lysine, indicating the involvement of kringles in binding antithrombin III.	Lysine	72-78	serpin family C member 1	Homo sapiens	130-146
10974350-6	2000	Using carboxypeptidase B digestion, the plasminogen-binding site of antithrombin III was localized to the carboxy-terminus lysine of the anticoagulant protein.	Lysine	123-129	serpin family C member 1	Homo sapiens	68-84
10974350-7	2000	Tissue plasminogen activator also interacted with antithrombin III in a time- and concentration-dependent manner and its binding was also significantly (>90%) inhibited by lysine.	Lysine	175-181	serpin family C member 1	Homo sapiens	50-66
10984531-0	2000	Sequencing of 3-O sulfate containing heparin decasaccharides with a partial antithrombin III binding site.	3-o sulfate	14-25	serpin family C member 1	Homo sapiens	76-92
10984531-0	2000	Sequencing of 3-O sulfate containing heparin decasaccharides with a partial antithrombin III binding site.	heparin decasaccharides	37-60	serpin family C member 1	Homo sapiens	76-92
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	IC 831423	29-52	serpin family C member 1	Homo sapiens	0-6
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	IC 831423	29-52	serpin family C member 1	Homo sapiens	161-167
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	3-o sulfate	85-96	serpin family C member 1	Homo sapiens	0-6
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	3-o sulfate	85-96	serpin family C member 1	Homo sapiens	161-167
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	6-o	114-117	serpin family C member 1	Homo sapiens	0-6
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	6-o	114-117	serpin family C member 1	Homo sapiens	161-167
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	Glucosamine	127-138	serpin family C member 1	Homo sapiens	0-6
10984531-3	2000	AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade.	Glucosamine	127-138	serpin family C member 1	Homo sapiens	161-167
10966821-1	2000	The mechanism of activation of antithrombin by heparin.	Heparin	47-54	serpin family C member 1	Homo sapiens	31-43
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
10966821-4	2000	Here we compare the structures of the circulating inactive form of antithrombin with the activated structure in complex with heparin pentasaccharide.	IC 831423	125-148	serpin family C member 1	Homo sapiens	67-79
11776053-3	2000	The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system.	Glycosaminoglycans	30-33	serpin family C member 1	Homo sapiens	4-16
11776053-3	2000	The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system.	Glycosaminoglycans	30-33	serpin family C member 1	Homo sapiens	172-184
11776053-16	2000	GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin.	Glycosaminoglycans	0-3	serpin family C member 1	Homo sapiens	83-95
11776053-16	2000	GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin.	Dermatan Sulfate	19-35	serpin family C member 1	Homo sapiens	83-95
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
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
10992803-8	2000	In the ArT patient group, there was 1 patient (5.88%) with AT III, 3 (17.64%) with PC deficiency, 1 (5.88%) with PS deficiency and no APC resistant patients, while there was one (2.08%) with PC deficiency and one (2.08%) with APC resistance in the control group (49 persons, mean age 41 years).	art	7-10	serpin family C member 1	Homo sapiens	59-65
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.	pentasaccharide	97-112	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.	pentasaccharide	34-49	serpin family C member 1	Homo sapiens	102-114
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.	pentasaccharide	70-85	serpin family C member 1	Homo sapiens	36-48
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
10913257-3	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.	pentasaccharide	240-255	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
10899490-9	2000	Tibolone showed a stronger reduction of factor VII activity; less reduction of AT-III, protein C activity, and protein S activity; stronger increase of the activated partial thromboplastin time, plasminogen and plasminogen-antiplasminogen complexes; and less increase of D-Dimer than ccHRT.	tibolone	0-8	serpin family C member 1	Homo sapiens	79-85
11060763-6	2000	There are two general classes of FXa inhibitors in development, of which SR90107A/ORG31540, an antithrombin-III-dependent pentasaccharide and DX-9065a, a small molecule direct FXa inhibitor, have published clinical data.	PENTA	73-81	serpin family C member 1	Homo sapiens	95-111
11127851-3	2000	The treatment decision involves continuation or discontinuation of vitamin K antagonists in patients with a first spontaneous or secondary venous thromboembolism and an antithrombin, protein C or S deficiency.	Vitamin K	67-76	serpin family C member 1	Homo sapiens	169-181
11060763-6	2000	There are two general classes of FXa inhibitors in development, of which SR90107A/ORG31540, an antithrombin-III-dependent pentasaccharide and DX-9065a, a small molecule direct FXa inhibitor, have published clinical data.	pentasaccharide	122-137	serpin family C member 1	Homo sapiens	95-111
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.	Fluorescein	86-97	serpin family C member 1	Homo sapiens	52-64
10764763-0	2000	Role of arginine 129 in heparin binding and activation of antithrombin.	Arginine	8-16	serpin family C member 1	Homo sapiens	58-70
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.	Arginine	20-23	serpin family C member 1	Homo sapiens	44-56
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
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.	Histidine	192-195	serpin family C member 1	Homo sapiens	44-56
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.	Glutamine	199-202	serpin family C member 1	Homo sapiens	44-56
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.	pentasaccharide	36-51	serpin family C member 1	Homo sapiens	16-28
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
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
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
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.	Arginine	44-47	serpin family C member 1	Homo sapiens	106-118
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
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.	Arginine	177-180	serpin family C member 1	Homo sapiens	106-118
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.	IC 831423	243-266	serpin family C member 1	Homo sapiens	106-118
10872794-7	2000	Based on its known anticoagulative function in endothelial cells and effects on the production of prostacyclin, it is reasonable to speculate that antithrombin III present in aqueous humor might influence the physiology of the trabecular and uveoscleral meshwork and thereby regulate intraocular pressure.	Epoprostenol	98-110	serpin family C member 1	Homo sapiens	147-163
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.	Fluorescein	103-114	serpin family C member 1	Homo sapiens	52-64
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
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
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
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
10822073-11	2000	While neither drug had any effect on the percutaneous transluminal coronary angioplasty-induced inflammatory response, argatroban may more effectively inhibit the generated thrombin and prevent antithrombin consumption during and after percutaneous transluminal coronary angioplasty.	argatroban	119-129	serpin family C member 1	Homo sapiens	194-206
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
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
10904927-4	2000	This process also occurs in other members of the serine proteinase inhibitor (serpin) superfamily, antithrombin, C1-inhibitor and alpha 1-antichymotrypsin, in association with thrombosis, angioedema and chronic obstructive pulmonary disease, respectively, and we have recently shown that it underlies a novel inclusion body dementia.	Serine	49-55	serpin family C member 1	Homo sapiens	99-111
10850803-7	2000	Substitutions of the lysine at equivalent positions in two other inhibitory serpins, human alpha1-antichymotrypsin and human antithrombin III, also increased stability and decreased inhibitory activity toward alpha-chymotrypsin and thrombin, respectively.	Lysine	21-27	serpin family C member 1	Homo sapiens	125-141
10766996-4	2000	The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N).	Glycosaminoglycans	126-129	serpin family C member 1	Homo sapiens	62-65
10766996-4	2000	The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N).	Glutamic Acid	134-137	serpin family C member 1	Homo sapiens	62-65
10766996-4	2000	The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N).	Lysine	234-237	serpin family C member 1	Homo sapiens	62-65
10766996-4	2000	The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N).	Asparagine	251-254	serpin family C member 1	Homo sapiens	62-65
10810875-4	2000	Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes.	Epoprostenol	24-36	serpin family C member 1	Homo sapiens	0-12
10810875-4	2000	Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes.	Heparitin Sulfate	91-106	serpin family C member 1	Homo sapiens	0-12
10810875-4	2000	Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes.	Epoprostenol	142-154	serpin family C member 1	Homo sapiens	0-12
10898273-7	2000	These data suggest that (a) in patients with diabetes, antiplatelet therapy with sarpogrelate hydrochloride is a useful antithrombin therapy because it suppresses the production of intrinsic coagulants by activated platelets; and (b) sarpogrelate hydrochloride decreases endothelial cell damage via adhesion molecules.	sarpogrelate hydrochloride	81-107	serpin family C member 1	Homo sapiens	120-132
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
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
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
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
10722716-0	2000	The effect of a reducing-end extension on pentasaccharide binding by antithrombin.	pentasaccharide	42-57	serpin family C member 1	Homo sapiens	69-81
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
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.	pentasaccharide	42-57	serpin family C member 1	Homo sapiens	0-12
10722716-7	2000	This conclusion supports the likely presence of a range of sequences that can bind to and activate antithrombin in the natural heparan sulfates that line the vascular endothelium.	Heparitin Sulfate	127-143	serpin family C member 1	Homo sapiens	99-111
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
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
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
11014724-5	2000	It remains to be seen whether the new antithrombin agents reduce the rate of periprocedural complications if used in combination with aspirin and new antiplatelet therapies.	Aspirin	134-141	serpin family C member 1	Homo sapiens	38-50
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
10712595-0	2000	Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human beta-antithrombin.	Carbohydrates	35-47	serpin family C member 1	Homo sapiens	7-19
10712595-3	2000	Due to a single nucleotide replacement, Asn135 of the antithrombin in higher vertebrates is substituted by Asp in the salmon homolog.	Aspartic Acid	107-110	serpin family C member 1	Homo sapiens	54-66
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.	Nitrogen	28-29	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.	Nitrogen	28-29	serpin family C member 1	Homo sapiens	357-369
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.	Carbohydrates	97-109	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	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
10712595-6	2000	Furthermore, the invariant third-position Ser137 at this glycosylation site of mammalian and chicken antithrombins is substituted by Thr in the salmon, a replacement that has been shown to induce full glycosylation in human antithrombin.	Threonine	133-136	serpin family C member 1	Homo sapiens	101-113
10712595-8	2000	Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid.	Oligosaccharides	50-65	serpin family C member 1	Homo sapiens	7-19
10712595-8	2000	Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid.	N-Acetylneuraminic Acid	89-100	serpin family C member 1	Homo sapiens	7-19
10712595-8	2000	Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid.	Galactose	133-142	serpin family C member 1	Homo sapiens	7-19
10712595-8	2000	Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	179-185	serpin family C member 1	Homo sapiens	7-19
10712595-8	2000	Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid.	N-Acetylneuraminic Acid	236-247	serpin family C member 1	Homo sapiens	7-19
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
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.	Aspartic Acid	4-7	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.	Glutamic Acid	13-16	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	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
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
10652320-5	2000	Antithrombin inactivated FXa derivatives with a similar second-order association rate constant (k(2)) in both the absence and presence of pentasaccharide.	pentasaccharide	138-153	serpin family C member 1	Homo sapiens	0-12
11096650-7	2000	On the other hand, available data suggest that serious bleeding should not be problematic despite difficulties measuring that antithrombin effect among patients receiving LMWH, even when it is combined with potent platelet inhibitor therapy.	Heparin, Low-Molecular-Weight	171-175	serpin family C member 1	Homo sapiens	126-138
10660568-0	2000	Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa.	Serine	0-6	serpin family C member 1	Homo sapiens	53-65
10660568-0	2000	Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa.	Glutamic Acid	24-33	serpin family C member 1	Homo sapiens	53-65
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
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
10660568-7	2000	This is comparable to that of antithrombin activated by high affinity heparin pentasaccharide.	IC 831423	70-93	serpin family C member 1	Homo sapiens	30-42
10644732-1	2000	The binding of pentasaccharide heparin to antithrombin induces a conformational change that is transmitted to the reactive center loop and increases the rate of inhibition of factor Xa by approximately 300-fold.	pentasaccharide heparin	15-38	serpin family C member 1	Homo sapiens	42-54
11011802-21	2000	The FDA has approved a recombinant hirudin (Refludan) and a synthetic antithrombin agent, argatroban (Novastan), for this indication.	argatroban	90-100	serpin family C member 1	Homo sapiens	70-82
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
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
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
10574918-10	1999	We generated a carboxyl-terminal histidine-tagged recombinant antithrombin III to study the tag on another serpin.	Histidine	33-42	serpin family C member 1	Homo sapiens	62-78
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
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
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
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
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
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
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
10569284-7	1999	These values are lower than those reported for low-molecular-weight heparins and are consistent with the requirement of an antithrombin III pentasaccharide binding site for anti-factor Xa activity.	pentasaccharide	140-155	serpin family C member 1	Homo sapiens	123-139
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
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.	argatroban	82-92	serpin family C member 1	Homo sapiens	43-55
11094330-4	1999	The anticoagulant activity of this polysaccharide is mediated by both antithrombin and heparin cofactor II; it has antithrombotic activity when targeted at the intrinsic coagulation pathway.	Polysaccharides	35-49	serpin family C member 1	Homo sapiens	70-82
10502216-3	1999	Efegatran is a new direct antithrombin, which in experimental animals has been shown to enhance thrombolysis, reduce rate of reocclusion, and limit infarct size.	efegatran	0-9	serpin family C member 1	Homo sapiens	26-38
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 --> Pro mutation.	Glycine	21-28	serpin family C member 1	Homo sapiens	32-44
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 --> Pro mutation.	Heparin	79-86	serpin family C member 1	Homo sapiens	32-44
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 --> Pro mutation.	Glycine	161-164	serpin family C member 1	Homo sapiens	32-44
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.	IC 831423	20-43	serpin family C member 1	Homo sapiens	66-78
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
10497166-2	1999	To test whether the factor Xa specificity of allosterically activated antithrombin is encoded in the serpin reactive center loop, we mutated the factor Xa-preferred P2 Gly to the thrombin-preferred P2 Pro.	Glycine	168-171	serpin family C member 1	Homo sapiens	70-82
10497166-3	1999	Kinetic studies revealed that the mutation maximally enhanced the reactivity of antithrombin with thrombin 15-fold and decreased its reactivity toward factor Xa 2-fold when the serpin was activated by heparin pentasaccharide, thereby transforming antithrombin into an allosterically activated inhibitor of both factor Xa and thrombin.	IC 831423	201-224	serpin family C member 1	Homo sapiens	80-92
10497166-3	1999	Kinetic studies revealed that the mutation maximally enhanced the reactivity of antithrombin with thrombin 15-fold and decreased its reactivity toward factor Xa 2-fold when the serpin was activated by heparin pentasaccharide, thereby transforming antithrombin into an allosterically activated inhibitor of both factor Xa and thrombin.	IC 831423	201-224	serpin family C member 1	Homo sapiens	247-259
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.	Glycine	197-200	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.	Glycine	197-200	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.	Glycine	197-200	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	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
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
10656170-10	1999	Small fibrinogen (t0, t2, t6, t8), PAI-1 (t6) and AT III (t0-t8) increases were observed after gemfibrozil, while simvastatin did not significantly modify these parameters.	Gemfibrozil	95-106	serpin family C member 1	Homo sapiens	50-56
11212344-8	1999	Heparan sulfate thus binds and regulates the activity of growth factors, cytokines, superoxide dismutase and antithrombin, which contribute to aberrant cell proliferation, migration and matrix production, scavenging of reactive oxygen radicals and thrombosis.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	109-121
11212344-8	1999	Heparan sulfate thus binds and regulates the activity of growth factors, cytokines, superoxide dismutase and antithrombin, which contribute to aberrant cell proliferation, migration and matrix production, scavenging of reactive oxygen radicals and thrombosis.	reactive oxygen radicals	219-243	serpin family C member 1	Homo sapiens	109-121
10844407-5	1999	Serum 17beta-oestradiol exhibited a direct correlation with endogenous thrombin potential extrinsic pathway (R = 0.42, p = 0.01) and prothrombin fragments 1 and 2 (R = 0.37, p = 0.03) and an inverse correlation with antithrombin III (R = -0.36, p = 0.03) and alpha(2)-antiplasmin (R = -0.45, p = 0.005).	Estradiol	6-23	serpin family C member 1	Homo sapiens	216-232
10585151-6	1999	Heparin resistance was defined as at least one activated clotting time < 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 < 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
10530936-3	1999	Conjugates VI and VIII show a remarkable increase in antithrombin activity compared to the structurally related conjugates with persulfated TBDs (i.e. compounds IV and V), whereas compound VII displays a diminished activity.	H-D-Ser(tBu)-OH	140-144	serpin family C member 1	Homo sapiens	53-65
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
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
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
10688418-0	1999	Clinical laboratory monitoring of a synthetic antithrombin agent, argatroban, using high performance liquid chromatography and functional methods.	argatroban	66-76	serpin family C member 1	Homo sapiens	46-58
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
10499652-7	1999	The total heparin dosage was less in group GA than in groups A and C. Purified AT-III administration is recommended in heparin pretreated patients; the addition of gabexate mesilate to this protocol decreases the heparin requirement and increases the AT-III preservation.	Gabexate	164-181	serpin family C member 1	Homo sapiens	251-257
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
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
10726036-4	1999	Argatroban represents the first clinically approved antithrombin agent, which was made available in Japan several years ago.	argatroban	0-10	serpin family C member 1	Homo sapiens	52-64
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.	pentasaccharide	138-153	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.	pentasaccharide	138-153	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
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.	pentasaccharide	153-168	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.	pentasaccharide	153-168	serpin family C member 1	Homo sapiens	169-181
10433728-10	1999	These results are in agreement with a previously proposed model, in which an initial low-affinity binding of the nonreducing-end trisaccharide of the heparin pentasaccharide induces the antithrombin conformational change.	Trisaccharides	129-142	serpin family C member 1	Homo sapiens	186-198
10433728-10	1999	These results are in agreement with a previously proposed model, in which an initial low-affinity binding of the nonreducing-end trisaccharide of the heparin pentasaccharide induces the antithrombin conformational change.	IC 831423	150-173	serpin family C member 1	Homo sapiens	186-198
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
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
10192656-8	1999	Levels of antithrombin decreased during treatment with oestradiol, whereas no changes were seen in levels of fibrinogen, von Willebrand factor, prothrombin fragment 1+2, protein S, protein C or resistance to activated protein C. In conclusion, oestrogen replacement therapy in postmenopausal women with NIDDM improved the fibrinolytic activity, while only clinically insignificant alterations in the clotting system were seen.	Estradiol	55-65	serpin family C member 1	Homo sapiens	10-22
10441134-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin.	Disulfides	8-17	serpin family C member 1	Homo sapiens	111-123
10215897-0	1999	Structure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts.	heparin-derived tetrasaccharide	13-44	serpin family C member 1	Homo sapiens	77-89
10215897-1	1999	A complex of the synthetic tetrasaccharide AGA*IM [GlcN, 6-SO3-alpha(1-4)-GlcA-beta(1-4)-GlcN,3, 6-SO3-alpha(1-4)-IdoA-alphaOMe] and the plasma protein antithrombin has been studied by NMR spectroscopy.	tetrasaccharide	27-42	serpin family C member 1	Homo sapiens	152-164
10215897-1	1999	A complex of the synthetic tetrasaccharide AGA*IM [GlcN, 6-SO3-alpha(1-4)-GlcA-beta(1-4)-GlcN,3, 6-SO3-alpha(1-4)-IdoA-alphaOMe] and the plasma protein antithrombin has been studied by NMR spectroscopy.	polyethylene glycol-glutaminase-asparaginase	43-46	serpin family C member 1	Homo sapiens	152-164
10215897-3	1999	Considerable changes were observed at both 20 : 1 and 10 : 1 ratios (AGA*IM : antithrombin) in 1H as well as 13C chemical shifts.	Hydrogen	95-97	serpin family C member 1	Homo sapiens	78-90
10215897-11	1999	All monitored NMR variables, 1H and 13C chemical shifts, 1JC-H couplings and transferred NOEs, indicated that the changes in conformation at the glycosidic linkage GlcN, 6-SO3-alpha(1-4)-GlcA were induced by the presence of antithrombin and suggested that the receptor selected a conformer different from that in the free state.	Glucosamine	164-168	serpin family C member 1	Homo sapiens	224-236
10215897-11	1999	All monitored NMR variables, 1H and 13C chemical shifts, 1JC-H couplings and transferred NOEs, indicated that the changes in conformation at the glycosidic linkage GlcN, 6-SO3-alpha(1-4)-GlcA were induced by the presence of antithrombin and suggested that the receptor selected a conformer different from that in the free state.	6-so3-alpha(1-4)-glca	170-191	serpin family C member 1	Homo sapiens	224-236
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
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.	Oligosaccharides	55-71	serpin family C member 1	Homo sapiens	77-89
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.	tetrasaccharide	257-272	serpin family C member 1	Homo sapiens	77-89
10466207-1	1999	Three hexasaccharides, having from low to very high affinity for antithrombin, were synthesised from disaccharide building block precursors.	hexasaccharides	6-21	serpin family C member 1	Homo sapiens	65-77
10466207-1	1999	Three hexasaccharides, having from low to very high affinity for antithrombin, were synthesised from disaccharide building block precursors.	Disaccharides	101-113	serpin family C member 1	Homo sapiens	65-77
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
10466208-4	1999	These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide.	pentadeca-	114-124	serpin family C member 1	Homo sapiens	66-78
10466208-4	1999	These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide.	hexadecasaccharide	130-148	serpin family C member 1	Homo sapiens	66-78
10328304-1	1999	Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained.	pentadeca-, heptadeca- and nonadecasaccharides	10-56	serpin family C member 1	Homo sapiens	72-88
10328304-1	1999	Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained.	pentadeca-, heptadeca- and nonadecasaccharides	10-56	serpin family C member 1	Homo sapiens	90-96
10328304-1	1999	Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained.	pentasaccharide	106-121	serpin family C member 1	Homo sapiens	72-88
10328304-1	1999	Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained.	pentasaccharide	106-121	serpin family C member 1	Homo sapiens	90-96
10328304-2	1999	The pentadecasaccharide is the shortest oligosaccharide able to catalyse thrombin inhibition by AT III.	pentadecasaccharide	4-23	serpin family C member 1	Homo sapiens	96-102
10328304-2	1999	The pentadecasaccharide is the shortest oligosaccharide able to catalyse thrombin inhibition by AT III.	Oligosaccharides	40-55	serpin family C member 1	Homo sapiens	96-102
10187813-0	1999	Oxidation of methionine residues in antithrombin.	Methionine	13-23	serpin family C member 1	Homo sapiens	36-48
10510546-7	1999	sE-selectin levels in GDM correlated inversely with ATIII activity (r = -0.905, p = 0.0028).	se-selectin	0-11	serpin family C member 1	Homo sapiens	52-57
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
10401691-6	1999	Several carbohydrate-deficient isoforms were found in transferrin (four), alpha1-antitrypsin (three), antithrombin (two) and thyroxine-binding globulin (four).	Carbohydrates	8-20	serpin family C member 1	Homo sapiens	102-114
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
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
10037709-3	1999	Protection from inhibition by antithrombin and heparin cofactor II requires ligation of both exosites 1 and 2 because minimal protection is seen when exosite 1 variants (gamma-thrombin and thrombin Quick 1) or an exosite 2 variant (Arg93 --> Ala, Arg97 --> Ala, and Arg101 --> Ala thrombin) is substituted for thrombin.	Alanine	245-248	serpin family C member 1	Homo sapiens	30-42
10037709-3	1999	Protection from inhibition by antithrombin and heparin cofactor II requires ligation of both exosites 1 and 2 because minimal protection is seen when exosite 1 variants (gamma-thrombin and thrombin Quick 1) or an exosite 2 variant (Arg93 --> Ala, Arg97 --> Ala, and Arg101 --> Ala thrombin) is substituted for thrombin.	Alanine	263-266	serpin family C member 1	Homo sapiens	30-42
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
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).	Tritium	1-3	serpin family C member 1	Homo sapiens	53-69
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
10375387-0	1999	Heparin induced thrombocytopenia: diagnosis and contemporary antithrombin management.	Heparin	0-7	serpin family C member 1	Homo sapiens	61-73
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).	Oligosaccharides	50-65	serpin family C member 1	Homo sapiens	162-174
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).	pentasaccharides	109-125	serpin family C member 1	Homo sapiens	162-174
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
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
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
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.	Oligosaccharides	98-114	serpin family C member 1	Homo sapiens	62-74
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.	Oligosaccharides	98-114	serpin family C member 1	Homo sapiens	164-176
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.	pentadeca- to eicosasaccharides	116-147	serpin family C member 1	Homo sapiens	62-74
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.	pentadeca- to eicosasaccharides	116-147	serpin family C member 1	Homo sapiens	164-176
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
9929104-8	1999	Included in this analysis is a linkage analysis of a trinucleotide repeat in intron 5 of the AT gene of the various family members, which also confirmed maternity and paternity.	trinucleotide	53-66	serpin family C member 1	Homo sapiens	93-95
10063994-2	1999	a sulfated pentasaccharide, which enhances specifically antithrombin III mediated inactivation of factor-Xa, in a clinical setting known to promote arterial thrombosis, i.e. coronary angioplasty.	pentasaccharide	11-26	serpin family C member 1	Homo sapiens	56-72
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
12080632-1	1999	OBJECTIVES: To partly elucidate the relationship between homocysteine(Hcy) and thrombosis, we observed Hcy"s effects on platelet aggregation and antithrombin activity of heparin cofactor in vitro.	Homocysteine	103-106	serpin family C member 1	Homo sapiens	145-157
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.	Dextrans	22-29	serpin family C member 1	Homo sapiens	109-121
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
10914239-1	1999	Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate.	danaparoid	0-17	serpin family C member 1	Homo sapiens	24-36
10914239-1	1999	Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate.	Glycosaminoglycans	51-69	serpin family C member 1	Homo sapiens	24-36
10914239-1	1999	Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate.	Heparitin Sulfate	71-86	serpin family C member 1	Homo sapiens	24-36
10914239-1	1999	Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate.	Dermatan Sulfate	88-104	serpin family C member 1	Homo sapiens	24-36
10914239-1	1999	Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate.	Chondroitin Sulfates	109-128	serpin family C member 1	Homo sapiens	24-36
10914239-2	1999	Similar to heparin, danaparoid operates by activating antithrombin 3, but does not contain heparin or heparin fragments, and is therefore antigenically distinct.	danaparoid	20-30	serpin family C member 1	Homo sapiens	54-66
10226408-2	1999	We used an antithrombin agent, argatroban, as an alternative anticoagulant in left heart bypass with the Bio-Medicus centrifugal pump in 7 of 9 recent patients who underwent aortic repair using left heart bypass.	argatroban	31-41	serpin family C member 1	Homo sapiens	11-23
9988693-4	1999	The neoepitope encompasses the motif DAFHK, located in native antithrombin on strand 4 of beta-sheet A, which becomes strand 5 of beta-sheet A in the RCL-cleaved and latent conformers.	dafhk	37-42	serpin family C member 1	Homo sapiens	62-74
10064272-0	1999	Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity.	Aspartic Acid	17-20	serpin family C member 1	Homo sapiens	101-113
10064272-0	1999	Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity.	Serine	21-24	serpin family C member 1	Homo sapiens	101-113
10064272-0	1999	Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity.	Phenylalanine	25-28	serpin family C member 1	Homo sapiens	101-113
10064272-0	1999	Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity.	hirutonin	60-69	serpin family C member 1	Homo sapiens	101-113
9950667-4	1999	METHODS AND RESULTS: Vasoflux is prepared by depolymerization of heparin, restricting molecular size to between 3000 and 8000 Da, and reducing antithrombin affinity by periodate oxidation.	metaperiodate	168-177	serpin family C member 1	Homo sapiens	143-155
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
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
10026234-10	1999	These findings suggest that antithrombin, probably in association with heparin or heparan sulfate, is internalized by renal proximal epithelial cells.	Heparitin Sulfate	82-97	serpin family C member 1	Homo sapiens	28-40
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
9882436-0	1999	Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III.	Disulfides	8-17	serpin family C member 1	Homo sapiens	116-132
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
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
10050080-8	1999	Furthermore, antiplatelet therapy with cilostazol for diabetic patients may be useful as antithrombin therapy including antiplatelet therapy, since it suppresses the production of intrinsic coagulants produced by platelet activation.	Cilostazol	39-49	serpin family C member 1	Homo sapiens	89-101
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.	Warfarin	127-135	serpin family C member 1	Homo sapiens	40-52
9930564-2	1999	Organic synthetic benzamidine derivatives were initially developed as direct antithrombin agents.	benzamidine	18-29	serpin family C member 1	Homo sapiens	77-89
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
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.	Heparitin Sulfate	101-117	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.	Heparitin Sulfate	101-117	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.	Heparitin Sulfate	101-117	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.	Heparitin Sulfate	101-117	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	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
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
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
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
10537578-8	1998	However, significant reduction in CTD (p = 0.05) was seen in the aminocaproic acid patients who were treated with ATIII pre-CPB or within the first 20 minutes of CPB.	Aminocaproic Acid	65-82	serpin family C member 1	Homo sapiens	114-119
10537578-8	1998	However, significant reduction in CTD (p = 0.05) was seen in the aminocaproic acid patients who were treated with ATIII pre-CPB or within the first 20 minutes of CPB.	cpb	124-127	serpin family C member 1	Homo sapiens	114-119
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.	Heparitin Sulfate	108-123	serpin family C member 1	Homo sapiens	53-69
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
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.	Heparitin Sulfate	190-205	serpin family C member 1	Homo sapiens	53-69
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
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
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
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
9794814-5	1998	An antithrombin to papain inactivation stoichiometry of approximately 3 indicated extensive cleavage of the inhibitor concurrent with enzyme inactivation, a behaviour verified by SDS/PAGE.	Sodium Dodecyl Sulfate	179-182	serpin family C member 1	Homo sapiens	3-15
9794814-7	1998	The papain band in SDS/PAGE progressively disappeared on reaction of the enzyme with increasing amounts of antithrombin, but no band representing a stable antithrombin-papain complex appeared.	Sodium Dodecyl Sulfate	19-22	serpin family C member 1	Homo sapiens	107-119
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
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
9758732-7	1998	Methylprednisolone treatment effectively inhibited the increases in TNF-alpha and IL-6 and the decreases in AT-III and albumin, but did not inhibit the increases in PMN-elastase and TAT levels.	Methylprednisolone	0-18	serpin family C member 1	Homo sapiens	108-114
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Threonine	0-9	serpin family C member 1	Homo sapiens	119-131
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Threonine	0-9	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Threonine	0-9	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Threonine	0-9	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Lysine	108-114	serpin family C member 1	Homo sapiens	119-131
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Lysine	108-114	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Lysine	108-114	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Lysine	108-114	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Methionine	322-332	serpin family C member 1	Homo sapiens	119-131
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Methionine	322-332	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Methionine	322-332	serpin family C member 1	Homo sapiens	175-187
9763552-2	1998	Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease.	Methionine	322-332	serpin family C member 1	Homo sapiens	175-187
9763552-3	1998	Isolated antithrombin Wibble had a decreased thermal stability (Tm 56.2, normal 57.6 degreesC) but was fully stabilized by the heparin pentasaccharide (Tm 71.8, normal 71.0 degreesC), indicating that the prime abnormality is a laxity in the transition of the main sheet of the molecule from the 5- to 6-stranded form, as was confirmed by the ready conversion of antithrombin Wibble to the 6-stranded latent form on incubation.	IC 831423	127-150	serpin family C member 1	Homo sapiens	9-21
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
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
9771845-6	1998	Allografts with depleted tubular antithrombin at transplantation (n=20) had significantly greater plasma creatinine concentrations at posttransplant days 3 (P < 0.001) and 5 (P < 0.03) than allografts with normal tubular antithrombin (n=21).	Creatinine	105-115	serpin family C member 1	Homo sapiens	33-45
9737884-1	1998	The anticoagulant activation of the serpin antithrombin by heparin pentasaccharide DEFGH was previously shown to involve trisaccharide DEF first binding and inducing activation of the serpin, followed by disaccharide GH binding and stabilizing the activated state [Petitou et al.	pentasaccharide	67-82	serpin family C member 1	Homo sapiens	43-55
9737884-1	1998	The anticoagulant activation of the serpin antithrombin by heparin pentasaccharide DEFGH was previously shown to involve trisaccharide DEF first binding and inducing activation of the serpin, followed by disaccharide GH binding and stabilizing the activated state [Petitou et al.	Trisaccharides	121-134	serpin family C member 1	Homo sapiens	43-55
9737884-1	1998	The anticoagulant activation of the serpin antithrombin by heparin pentasaccharide DEFGH was previously shown to involve trisaccharide DEF first binding and inducing activation of the serpin, followed by disaccharide GH binding and stabilizing the activated state [Petitou et al.	Disaccharides	204-216	serpin family C member 1	Homo sapiens	43-55
9737884-7	1998	Perturbation of the conformational equilibrium of iduronate residue G through replacement of the nonessential 3-OH of this residue with -H resulted in parallel decreases in the fraction of residue G in the skew boat conformer (from 64 to 24%) and in the association constant for pentasaccharide binding to antithrombin [(2.6 +/- 0.3)-fold], consistent with selective binding of the skew boat conformer to the serpin.	Iduronic Acid	50-59	serpin family C member 1	Homo sapiens	306-318
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	Salts	4-8	serpin family C member 1	Homo sapiens	78-90
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	pentasaccharide	91-106	serpin family C member 1	Homo sapiens	78-90
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	pentasaccharide	91-106	serpin family C member 1	Homo sapiens	299-311
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	pentasaccharide	183-198	serpin family C member 1	Homo sapiens	78-90
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	pentasaccharide	183-198	serpin family C member 1	Homo sapiens	299-311
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	Hydrogen	235-243	serpin family C member 1	Homo sapiens	78-90
9737884-9	1998	The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin.	3-o-sulfate	282-293	serpin family C member 1	Homo sapiens	78-90
9737884-10	1998	All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications.	pentasaccharides	12-28	serpin family C member 1	Homo sapiens	62-74
9737884-10	1998	All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications.	pentasaccharides	12-28	serpin family C member 1	Homo sapiens	216-228
9737884-10	1998	All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications.	pentasaccharide	12-27	serpin family C member 1	Homo sapiens	62-74
9737884-10	1998	All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications.	pentasaccharide	12-27	serpin family C member 1	Homo sapiens	216-228
9737884-11	1998	Rapid kinetic studies were consistent with the altered affinities of the variant pentasaccharides resulting mostly from perturbed interactions of the reducing-end GH disaccharide with the activated antithrombin conformation and minimally to an altered binding of the nonreducing-end DEF trisaccharide to the native serpin conformation.	pentasaccharides	81-97	serpin family C member 1	Homo sapiens	198-210
9737884-11	1998	Rapid kinetic studies were consistent with the altered affinities of the variant pentasaccharides resulting mostly from perturbed interactions of the reducing-end GH disaccharide with the activated antithrombin conformation and minimally to an altered binding of the nonreducing-end DEF trisaccharide to the native serpin conformation.	Disaccharides	166-178	serpin family C member 1	Homo sapiens	198-210
9737884-12	1998	Together, these results support a model in which the conformational flexibility of the G residue facilitates conversion to the skew boat conformer and thereby allows charged groups of the GH disaccharide to bind and stabilize the activated antithrombin conformation that is induced by the DEF trisaccharide.	gh disaccharide	188-203	serpin family C member 1	Homo sapiens	240-252
9737884-12	1998	Together, these results support a model in which the conformational flexibility of the G residue facilitates conversion to the skew boat conformer and thereby allows charged groups of the GH disaccharide to bind and stabilize the activated antithrombin conformation that is induced by the DEF trisaccharide.	Trisaccharides	293-306	serpin family C member 1	Homo sapiens	240-252
9737475-2	1998	The favorable pharmacologic properties of LMWHs include a binding affinity for antithrombin III, anti-factor IIa activity, excellent bioavailability, minimal protein binding, predictable anticoagulant response, and clinical tolerance by patients.	Heparin, Low-Molecular-Weight	42-47	serpin family C member 1	Homo sapiens	79-91
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
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.	Polysaccharides	131-146	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	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
9748565-3	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, Low-Molecular-Weight	255-259	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.	fucoidan	265-273	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
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, Low-Molecular-Weight	118-122	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, Low-Molecular-Weight	118-122	serpin family C member 1	Homo sapiens	190-202
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
9722560-2	1998	We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans.	Tryptophan	61-64	serpin family C member 1	Homo sapiens	29-41
9722560-2	1998	We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans.	Phenylalanine	72-75	serpin family C member 1	Homo sapiens	29-41
9722560-2	1998	We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans.	Tryptophan	175-186	serpin family C member 1	Homo sapiens	29-41
9722560-3	1998	The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307.	Tryptophan	79-82	serpin family C member 1	Homo sapiens	44-56
9722560-3	1998	The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307.	Tryptophan	95-98	serpin family C member 1	Homo sapiens	44-56
9722560-3	1998	The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307.	Tryptophan	95-98	serpin family C member 1	Homo sapiens	44-56
9722560-3	1998	The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307.	Tryptophan	95-98	serpin family C member 1	Homo sapiens	44-56
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.	Tryptophan	0-3	serpin family C member 1	Homo sapiens	100-112
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.	Tryptophan	11-14	serpin family C member 1	Homo sapiens	100-112
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.	Tryptophan	56-67	serpin family C member 1	Homo sapiens	81-93
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.	Tryptophan	155-158	serpin family C member 1	Homo sapiens	81-93
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.	Tryptophan	167-170	serpin family C member 1	Homo sapiens	81-93
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
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.	c-pentasaccharide	65-82	serpin family C member 1	Homo sapiens	107-123
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.	c-pentasaccharide	65-82	serpin family C member 1	Homo sapiens	125-131
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
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
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.	Oxygen	220-226	serpin family C member 1	Homo sapiens	125-131
9805364-0	1998	Chemical structure of antithrombin-active Rhamnan sulfate from Monostrom nitidum.	rhamnan sulfate	42-57	serpin family C member 1	Homo sapiens	22-34
9805364-2	1998	The polysaccharide, which is regarded as a homopolysaccharide, was 6-fold more antithrombin-active than the heparin standard.	Polysaccharides	4-18	serpin family C member 1	Homo sapiens	79-91
9805364-2	1998	The polysaccharide, which is regarded as a homopolysaccharide, was 6-fold more antithrombin-active than the heparin standard.	homopolysaccharide	43-61	serpin family C member 1	Homo sapiens	79-91
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
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
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
9748634-5	1998	PAI-1-ovalbumin, PAI-1-antithrombin III and PAI-1-P13 (Val-->Glu) revealed specific activities of 86+/-15%, 77+/-11%, and 100+/-30% respectively, towards t-PA and similar inhibitory properties towards u-PA.	Valine	55-58	serpin family C member 1	Homo sapiens	23-39
9730869-4	1998	Our results showed that stretch induced glycosaminoglycan production with increased antithrombin activity due to an increase in the concentration of active chondroitin sulfate.	Chondroitin Sulfates	156-175	serpin family C member 1	Homo sapiens	84-96
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
9804516-2	1998	The purpose of this study was to bind covalently a basecoat protein (canine serum albumin [CSAJ) and a potent antithrombin agent (recombinant hirudin [rHir]) to 4 mm inner diameter poly(carbonate urea) urethane grafts with reactive carboxylic acid groups (cPU).	poly(carbonate urea) urethane	181-210	serpin family C member 1	Homo sapiens	110-122
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
9805364-3	1998	The antithrombin activity was decreased, by desulfation, although the non-active product still retained 8% of the sulfate ester.	sulfate ester	114-127	serpin family C member 1	Homo sapiens	4-16
9758732-9	1998	CONCLUSIONS: These results suggest that methylprednisolone pretreatment attenuates the decrease in AT-III by reducing IL-6 production postoperatively.	Methylprednisolone	40-58	serpin family C member 1	Homo sapiens	99-105
9765662-11	1998	ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin.	Heparin	10-17	serpin family C member 1	Homo sapiens	93-109
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<0.0001) and of free and endothelial-bound TFPI.	Heparin	12-15	serpin family C member 1	Homo sapiens	138-150
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
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, Low-Molecular-Weight	35-39	serpin family C member 1	Homo sapiens	43-55
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, Low-Molecular-Weight	115-119	serpin family C member 1	Homo sapiens	43-55
9675160-6	1998	Hydration fingerprints of antithrombin (that is, water-permeable pockets) are analyzed to determine their location, volume, and size of access pores, using alpha shape-based methods from computational geometry.	Water	49-54	serpin family C member 1	Homo sapiens	26-38
9675160-11	1998	This study demonstrates that conformational changes of antithrombin, including loop insertion, are linked to water transfer from antithrombin to bulk solution.	Water	109-114	serpin family C member 1	Homo sapiens	55-67
9675160-11	1998	This study demonstrates that conformational changes of antithrombin, including loop insertion, are linked to water transfer from antithrombin to bulk solution.	Water	109-114	serpin family C member 1	Homo sapiens	129-141
9684790-4	1998	The second order rate constant of the inactivation of FXIa by antithrombin was increased up to 6-fold by LMWH, whereas LMWdxs had no effect.	Heparin, Low-Molecular-Weight	105-109	serpin family C member 1	Homo sapiens	62-74
9684790-7	1998	LMWH at maximal therapeutic plasma levels enhanced the contribution of antithrombin to the inactivation of FXIa in plasma up to 5-fold.	Heparin, Low-Molecular-Weight	0-4	serpin family C member 1	Homo sapiens	71-83
9684790-9	1998	Furthermore, LMWH but not LMWdxs slightly enhanced FXIa inhibition by antithrombin.	Heparin, Low-Molecular-Weight	13-17	serpin family C member 1	Homo sapiens	70-82
9702317-0	1998	Covalent linkage of recombinant hirudin to a novel ionic poly(carbonate) urethane polymer with protein binding sites: determination of surface antithrombin activity.	poly(carbonate) urethane	57-81	serpin family C member 1	Homo sapiens	143-155
9702317-3	1998	The purpose of this study was to covalently immobilize the potent, specific antithrombin agent recombinant hirudin (rHir) onto a novel polyurethane polymer synthesized with carboxylic acid groups which served as protein attachment sites.	polyurethane polymer	135-155	serpin family C member 1	Homo sapiens	76-88
9702317-12	1998	Thus, these results demonstrate that rHir can be covalently bound to this novel polyurethane surface and still maintain potent antithrombin activity.	Polyurethanes	80-92	serpin family C member 1	Homo sapiens	127-139
9784873-0	1998	Synthesis of a 3-deoxy-L-iduronic acid containing heparin pentasaccharide to probe the conformation of the antithrombin III binding sequence.	3-deoxy-l-iduronic acid	15-38	serpin family C member 1	Homo sapiens	107-123
9784873-0	1998	Synthesis of a 3-deoxy-L-iduronic acid containing heparin pentasaccharide to probe the conformation of the antithrombin III binding sequence.	IC 831423	50-73	serpin family C member 1	Homo sapiens	107-123
9784873-2	1998	1H NMR studies demonstrated that, as anticipated, such a modification induces a shift of the conformational equilibrium toward 1C4 (contribution to the conformational equilibrium rises from 37% to 65%) and a substantial decrease of the affinity for antithrombin III (Kd 0.154 microM versus 0.050 microM).	Hydrogen	0-2	serpin family C member 1	Homo sapiens	249-265
9724163-0	1998	Coagulation protein function V: diminution of antithrombin III function by acetaldehyde.	Acetaldehyde	75-87	serpin family C member 1	Homo sapiens	46-62
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	153-165	serpin family C member 1	Homo sapiens	30-46
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	153-165	serpin family C member 1	Homo sapiens	48-53
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	167-170	serpin family C member 1	Homo sapiens	30-46
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	167-170	serpin family C member 1	Homo sapiens	48-53
9724163-4	1998	Clotting times of 20.9+/-1.0, 32.3+/-1.0, and 45.3+/-1.6 sec were obtained with 447, 89.4, and 17.9 mM AcH-ATIII mixtures, respectively.	Acetaldehyde	103-106	serpin family C member 1	Homo sapiens	107-112
9724163-5	1998	These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant.	Guanidine	60-72	serpin family C member 1	Homo sapiens	45-50
9724163-5	1998	These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant.	aminos	74-80	serpin family C member 1	Homo sapiens	45-50
9724163-5	1998	These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant.	Acetaldehyde	134-137	serpin family C member 1	Homo sapiens	45-50
9721974-8	1998	AT III supplementation prevented the continuous increase in sICAM-1 plasma concentration observed in control patients and led to a significant fall in soluble sE-selectin and CRP concentration (p < or = .01).	se-selectin	159-170	serpin family C member 1	Homo sapiens	0-6
9692954-11	1998	Homology modeling of PEDF based on the X-ray crystal structures of antithrombin III and ovalbumin shows a region at the center of beta-sheet A-strands 2 and 3- and helix F that has a basic electrostatic surface potential and is densely populated with lysines exposed to the surface (K134, K137, K189, K191, H212, and K214) that are available to interact with various glycosaminoglycans/polyanions.	Lysine	251-258	serpin family C member 1	Homo sapiens	67-83
9692954-11	1998	Homology modeling of PEDF based on the X-ray crystal structures of antithrombin III and ovalbumin shows a region at the center of beta-sheet A-strands 2 and 3- and helix F that has a basic electrostatic surface potential and is densely populated with lysines exposed to the surface (K134, K137, K189, K191, H212, and K214) that are available to interact with various glycosaminoglycans/polyanions.	Glycosaminoglycans	367-385	serpin family C member 1	Homo sapiens	67-83
9642241-0	1998	Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism.	Calcium	0-7	serpin family C member 1	Homo sapiens	42-54
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
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
9713170-1	1998	We investigated the effect of cell surface glycosaminoglycans (GAGs) on the inactivation of factor VIIa-tissue factor activity by antithrombin III (ATIII) on a human bladder carcinoma (J82) cell line and an ovarian carcinoma (OC-2008) cell line, two tumor cell lines which constitutively synthesize and express high levels of cell surface tissue factor.	Glycosaminoglycans	43-61	serpin family C member 1	Homo sapiens	148-153
9713170-6	1998	In addition, we demonstrated that the ability of ATIII to inactivate factor VIIa-tissue factor activity was markedly reduced following treatment of cells with calcium ionophore (A23187).	Calcium	159-166	serpin family C member 1	Homo sapiens	49-54
9713170-6	1998	In addition, we demonstrated that the ability of ATIII to inactivate factor VIIa-tissue factor activity was markedly reduced following treatment of cells with calcium ionophore (A23187).	Calcimycin	178-184	serpin family C member 1	Homo sapiens	49-54
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).	Dextrans	167-174	serpin family C member 1	Homo sapiens	124-136
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
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
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.	phyllophoran	107-119	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.	phyllophoran	107-119	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.	furcellaran	124-135	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.	furcellaran	124-135	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-cellulose	252-269	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-cellulose	252-269	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
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.	Sepharose	282-291	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.	Sepharose	282-291	serpin family C member 1	Homo sapiens	58-64
9662467-7	1998	This preventive effect of antithrombin is mediated by the promotion of endothelial release of prostacyclin, an inhibitor of leukocyte activation.	Epoprostenol	94-106	serpin family C member 1	Homo sapiens	26-38
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
9662467-8	1998	An interaction between antithrombin and heparin-like glycosaminoglycans on the endothelial cell surface appears to be important for this effect.	Glycosaminoglycans	53-71	serpin family C member 1	Homo sapiens	23-35
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
9662467-9	1998	Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans.	Glycosaminoglycans	127-145	serpin family C member 1	Homo sapiens	45-57
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
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
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
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
9516447-1	1998	Role of individual residues of the pentasaccharide activating sequence in the recognition of native and activated states of antithrombin.	pentasaccharide	35-50	serpin family C member 1	Homo sapiens	124-136
9516447-2	1998	To determine the role of individual saccharide residues of a specific heparin pentasaccharide, denoted DEFGH, in the allosteric activation of the serpin, antithrombin, we studied the effect of deleting pentasaccharide residues on this activation.	IC 831423	70-93	serpin family C member 1	Homo sapiens	154-166
9516447-2	1998	To determine the role of individual saccharide residues of a specific heparin pentasaccharide, denoted DEFGH, in the allosteric activation of the serpin, antithrombin, we studied the effect of deleting pentasaccharide residues on this activation.	pentasaccharide	78-93	serpin family C member 1	Homo sapiens	154-166
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.	Disaccharides	68-80	serpin family C member 1	Homo sapiens	168-180
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.	pentasaccharide	67-82	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	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
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
9622211-8	1998	At therapeutic subcutaneous doses, Bemiparin exerted an anti-FXa effect through TFPI during the first 2 h, through both ATIII and TFPI during the following 8 h (range 2-10 h) and through ATIII during the last 8 h (range 10-18 h).	bemiparin	35-44	serpin family C member 1	Homo sapiens	120-125
9622211-8	1998	At therapeutic subcutaneous doses, Bemiparin exerted an anti-FXa effect through TFPI during the first 2 h, through both ATIII and TFPI during the following 8 h (range 2-10 h) and through ATIII during the last 8 h (range 10-18 h).	bemiparin	35-44	serpin family C member 1	Homo sapiens	187-192
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
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
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.	pentasaccharide	2-17	serpin family C member 1	Homo sapiens	65-77
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.	ps	19-21	serpin family C member 1	Homo sapiens	65-77
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
9493570-1	1998	Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution.	Trichloroacetic Acid	167-170	serpin family C member 1	Homo sapiens	55-67
9493570-1	1998	Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution.	Alanine	188-195	serpin family C member 1	Homo sapiens	55-67
9493570-1	1998	Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution.	Serine	199-205	serpin family C member 1	Homo sapiens	55-67
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
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
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
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.	Serine	48-54	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.	Cysteine	173-181	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	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.	Cysteine	26-34	serpin family C member 1	Homo sapiens	72-84
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.	Fluorescein	55-66	serpin family C member 1	Homo sapiens	72-84
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
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
9514616-2	1998	GAG-UTM accelerates protein C activation by thrombin and also thrombin inhibition by antithrombin III (ATIII) in the buffer system.	gag-utm	0-7	serpin family C member 1	Homo sapiens	85-101
9514616-2	1998	GAG-UTM accelerates protein C activation by thrombin and also thrombin inhibition by antithrombin III (ATIII) in the buffer system.	gag-utm	0-7	serpin family C member 1	Homo sapiens	103-108
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
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.	IC 831423	59-82	serpin family C member 1	Homo sapiens	12-24
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
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.	pentasaccharide	17-32	serpin family C member 1	Homo sapiens	45-57
10806853-6	1998	Simple linear regression analysis revealed a negative correlation between antithrombin III activity and fast blood glucose.	Glucose	115-122	serpin family C member 1	Homo sapiens	74-90
18370504-0	1998	Omega-3 Ethyl Ester Concentrate Decreases Total Apolipoprotein CIII and Increases Antithrombin III in Postmyocardial Infarction Patients.	omega-3 ethyl ester	0-19	serpin family C member 1	Homo sapiens	82-98
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
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).	phenylalanyl-prolyl-arginine methyl chloride	153-171	serpin family C member 1	Homo sapiens	66-82
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).	Dinoprostone	226-230	serpin family C member 1	Homo sapiens	66-82
9587911-0	1998	[Coefficient of linear correlation between levels of fibrinogen, antithrombin III, thrombin-antithrombin complex and lipid fractions in women exposed chronically to carbon disulfide].	Carbon Disulfide	165-181	serpin family C member 1	Homo sapiens	65-81
9587911-0	1998	[Coefficient of linear correlation between levels of fibrinogen, antithrombin III, thrombin-antithrombin complex and lipid fractions in women exposed chronically to carbon disulfide].	Carbon Disulfide	165-181	serpin family C member 1	Homo sapiens	65-77
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
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
9515777-7	1998	Interaction of AT III with heparin-like glycosaminoglycans (GAGs) on the endothelial cell surface appears to be important for this effect.	Glycosaminoglycans	40-58	serpin family C member 1	Homo sapiens	15-21
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
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
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
9405673-0	1997	The anticoagulant activation of antithrombin by heparin.	Heparin	48-55	serpin family C member 1	Homo sapiens	32-44
9405673-1	1997	Antithrombin, a plasma serpin, is relatively inactive as an inhibitor of the coagulation proteases until it binds to the heparan side chains that line the microvasculature.	heparan	121-128	serpin family C member 1	Homo sapiens	0-12
9405673-3	1997	The accompanying conformational change of antithrombin is revealed in a 2.9-A structure of a dimer of latent and active antithrombins, each in complex with the high-affinity pentasaccharide.	pentasaccharide	174-189	serpin family C member 1	Homo sapiens	42-54
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
9499673-7	1997	Low-dose or very low-dose warfarin were subsequently demonstrated to be effective in patients with morbid obesity and decreased antithrombin III functional and antigenic levels, in patients with indwelling catheters, in patients undergoing gynecological surgery, as well as in patients with stage IV breast cancer.	Warfarin	26-34	serpin family C member 1	Homo sapiens	128-144
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
9405673-6	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.	heparans	125-133	serpin family C member 1	Homo sapiens	105-117
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
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
9361342-13	1997	AT III prevented the continuous rise in total serum bilirubin concentration observed in control patients and diminished the frequency of artificial renal support therapy (p < .05).	Bilirubin	52-61	serpin family C member 1	Homo sapiens	0-6
9342999-9	1997	Therefore, our results challenge current practice of prescribing lifelong warfarin therapy after a first or second episode of venous thromboembolism in patients with antithrombin or protein C or S deficiency.	Warfarin	74-82	serpin family C member 1	Homo sapiens	166-178
9374919-12	1997	The lack of a parallel increase of TAT with F1 + 2, in the presence of normal levels of antithrombin III (ATIII), indirectly suggests an impairment of the heparan sulphate-ATIII system which would favour thrombin generation.	Heparitin Sulfate	155-171	serpin family C member 1	Homo sapiens	172-177
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
9395268-3	1997	Addition of LNA to porcine aortic endothelial cells reduced 125I-labeled antithrombin III binding to the cell surface heparan sulfate in a dose- and time-dependent fashion.	Iodine-125	60-64	serpin family C member 1	Homo sapiens	73-89
9395268-3	1997	Addition of LNA to porcine aortic endothelial cells reduced 125I-labeled antithrombin III binding to the cell surface heparan sulfate in a dose- and time-dependent fashion.	Heparitin Sulfate	118-133	serpin family C member 1	Homo sapiens	73-89
9395268-4	1997	Significant inhibition was observed with 1 mM LNA, and the maximal suppression (-50% of control) occurred at 10 mM LNA after 12 h. L-NAME (1 mM) and L-NMMA (1 mM) also significantly inhibited the antithrombin III binding.	NG-Nitroarginine Methyl Ester	131-137	serpin family C member 1	Homo sapiens	196-212
9395268-4	1997	Significant inhibition was observed with 1 mM LNA, and the maximal suppression (-50% of control) occurred at 10 mM LNA after 12 h. L-NAME (1 mM) and L-NMMA (1 mM) also significantly inhibited the antithrombin III binding.	omega-N-Methylarginine	149-155	serpin family C member 1	Homo sapiens	196-212
9395268-5	1997	The iron chelator desferrioxamine significantly prevented the reduction of antithrombin III binding to LNA-treated cells.	Iron	4-8	serpin family C member 1	Homo sapiens	75-91
9395268-5	1997	The iron chelator desferrioxamine significantly prevented the reduction of antithrombin III binding to LNA-treated cells.	Deferoxamine	18-33	serpin family C member 1	Homo sapiens	75-91
9336303-2	1997	The aim of this work was to compare the extent of prothrombinase inhibition produced by two factor Xa inhibitors: the antithrombin III-dependent synthetic pentasaccharide (SR 90107/Org 31540) and DX-9065A, a direct factor Xa inhibitor.	pentasaccharide	155-170	serpin family C member 1	Homo sapiens	118-134
9309844-7	1997	Homocysteine inhibits the expression of thrombomodulin, the thrombin cofactor responsible for protein C activation, and inhibits antithrombin-III binding.	Homocysteine	0-12	serpin family C member 1	Homo sapiens	129-145
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
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.	argatroban	51-61	serpin family C member 1	Homo sapiens	4-16
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
9342556-17	1997	Although toremifene decreases antithrombin III levels slightly, the incidence of thromboembolic complications is low.	Toremifene	9-19	serpin family C member 1	Homo sapiens	30-46
9335355-6	1997	One of them, HAH, contained the specific antithrombin binding sequence and the other one, NAH, had a low affinity for antithrombin and had no anticoagulant activity.	sodium bisulfide	90-93	serpin family C member 1	Homo sapiens	118-130
9335355-7	1997	Our data demonstrate that in contrast to PU, PU-NAH and PU-HAH are strong mediators of factor XIa and factor IXa formation in normal and antithrombin-deficient plasma.	pu-nah	45-51	serpin family C member 1	Homo sapiens	137-149
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
9335355-7	1997	Our data demonstrate that in contrast to PU, PU-NAH and PU-HAH are strong mediators of factor XIa and factor IXa formation in normal and antithrombin-deficient plasma.	1-(N-(2-hydroxy-5-azidobenzoyl)-2-aminoethyl)-4-(N-hydroxysuccinimidyl)succinate	59-62	serpin family C member 1	Homo sapiens	137-149
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
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
10322873-9	1997	After the infusion of TTMP the levels of PAdT, PagT, VIII:C, dWF and Fg were decreased significantly, while TXB2, 6-keto-PGF1 alpha, AT-III:a and AT-III:Ag remained unchanged.	tetramethylpyrazine	22-26	serpin family C member 1	Homo sapiens	146-152
9306621-5	1997	Following danazol administration, marked and sustained increases were noted in Free Protein S, Antithrombin, and Protein C. Platelet CD62 (P-selectin) positivity which was elevated before therapy, decreased to assay threshold limits within five weeks.	Danazol	10-17	serpin family C member 1	Homo sapiens	95-107
9306621-6	1997	Both Prothrombin Fragment 1.2 and thrombin-antithrombin complexes were elevated post danazol therapy indicating continued clearance of generated thrombin.	Danazol	85-92	serpin family C member 1	Homo sapiens	43-55
9242619-4	1997	Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex.	Arginine	35-38	serpin family C member 1	Homo sapiens	48-60
9247347-3	1997	APTT was significantly prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III.	pu-hep	36-42	serpin family C member 1	Homo sapiens	93-109
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.	Arginine	54-62	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
9242619-2	1997	Recent crystallographic structures reveal the structural changes that occur when antithrombin is activated by the heparin pentasaccharide, with the exception of the final changes, which take place at the reactive center itself.	IC 831423	114-137	serpin family C member 1	Homo sapiens	81-93
9242619-3	1997	Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible.	Arginine	43-46	serpin family C member 1	Homo sapiens	56-68
9242619-3	1997	Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible.	Arginine	43-46	serpin family C member 1	Homo sapiens	261-273
9242619-3	1997	Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible.	IC 831423	164-187	serpin family C member 1	Homo sapiens	56-68
9242619-3	1997	Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible.	Arginine	326-329	serpin family C member 1	Homo sapiens	56-68
9242619-4	1997	Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex.	Arginine	35-38	serpin family C member 1	Homo sapiens	238-250
9242619-4	1997	Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex.	IC 831423	107-130	serpin family C member 1	Homo sapiens	48-60
9242619-4	1997	Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex.	IC 831423	107-130	serpin family C member 1	Homo sapiens	238-250
9242619-4	1997	Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex.	pentasaccharide	115-130	serpin family C member 1	Homo sapiens	48-60
9242619-5	1997	The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1 Arg.	Arginine	165-168	serpin family C member 1	Homo sapiens	38-50
9242619-5	1997	The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1 Arg.	Arginine	298-301	serpin family C member 1	Homo sapiens	38-50
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
9184748-6	1997	ATIII could be bound to the surface modified with alb-hep conjugate but not to a polystyrene surface modified with albumin.	alb-hep	50-57	serpin family C member 1	Homo sapiens	0-5
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
9235938-6	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.	Lysine	34-37	serpin family C member 1	Homo sapiens	140-145
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.	Arginine	42-45	serpin family C member 1	Homo sapiens	140-145
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.	Arginine	50-53	serpin family C member 1	Homo sapiens	140-145
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.	Arginine	50-53	serpin family C member 1	Homo sapiens	140-145
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.	Lysine	66-69	serpin family C member 1	Homo sapiens	140-145
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.	Arginine	50-53	serpin family C member 1	Homo sapiens	140-145
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.	Arginine	50-53	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
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
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
9233715-5	1997	The presence of adenosine triphosphate, however, predicts a significantly better metabolic capacity to eliminate bilirubin, to synthesize fibrinogen and antithrombin III, and to maintain a better prothrombin time after transplantation.	Adenosine Triphosphate	16-38	serpin family C member 1	Homo sapiens	153-169
9377090-9	1997	These results are in keeping with the observation that 2-O-sulfated pentasaccharides display a similar affinity for antithrombin III as their 2-N-sulfated counterparts.	hippuric acid	55-58	serpin family C member 1	Homo sapiens	116-132
9377090-9	1997	These results are in keeping with the observation that 2-O-sulfated pentasaccharides display a similar affinity for antithrombin III as their 2-N-sulfated counterparts.	sulfated	59-67	serpin family C member 1	Homo sapiens	116-132
9377090-9	1997	These results are in keeping with the observation that 2-O-sulfated pentasaccharides display a similar affinity for antithrombin III as their 2-N-sulfated counterparts.	pentasaccharides	68-84	serpin family C member 1	Homo sapiens	116-132
9368910-10	1997	Magnesium infusion was associated with a significant elevation in ADP (+19.3%); ristocetin (+13.6%); and collagen-induced platelet aggregation (+14.2%); an increase in plasma antithrombin-III (+10.3%) and thromboxane (+49.4%) when compared to pre-infusion levels.	Magnesium	0-9	serpin family C member 1	Homo sapiens	175-191
9253806-6	1997	The results showed that at lower concentration of the OSXP, the complexation of 125I-thrombin with heparin cofactor-II(HC-II) was enhanced, while at higher concentration of the compound, the complexation with both antithrombin-III(AT-III) and HC-II was enhanced.	osxp	54-58	serpin family C member 1	Homo sapiens	214-230
9253806-6	1997	The results showed that at lower concentration of the OSXP, the complexation of 125I-thrombin with heparin cofactor-II(HC-II) was enhanced, while at higher concentration of the compound, the complexation with both antithrombin-III(AT-III) and HC-II was enhanced.	osxp	54-58	serpin family C member 1	Homo sapiens	231-237
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.	Oligosaccharides	4-19	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.	Oligosaccharides	4-19	serpin family C member 1	Homo sapiens	80-92
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.	Asparagine	34-37	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.	Asparagine	34-37	serpin family C member 1	Homo sapiens	80-92
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.	Carbohydrates	41-53	serpin family C member 1	Homo sapiens	17-29
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.	Asparagine	68-71	serpin family C member 1	Homo sapiens	17-29
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
9184148-2	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.	IC 831423	147-170	serpin family C member 1	Homo sapiens	126-138
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.	IC 831423	147-170	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
9184148-3	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.	pentasaccharide	114-129	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.	Oligosaccharides	4-19	serpin family C member 1	Homo sapiens	117-129
9184148-4	1997	The oligosaccharide at Asn-135 thus at most moderately interferes with the initial, weak binding of heparin to alpha-antithrombin.	asn-135	23-30	serpin family C member 1	Homo sapiens	117-129
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
9184148-5	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.	pentasaccharide	84-99	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.	pentasaccharide	84-99	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.	Carbohydrates	4-16	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.	Asparagine	31-34	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	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.	asn-135 oligosaccharide	56-79	serpin family C member 1	Homo sapiens	89-101
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
9348117-0	1997	Mechanisms of antithrombin polymerisation and heparin activation probed by the insertion of synthetic reactive loop peptides.	Peptides	116-124	serpin family C member 1	Homo sapiens	14-26
9348117-1	1997	Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation.	Peptides	68-76	serpin family C member 1	Homo sapiens	14-26
9348117-1	1997	Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation.	Peptides	68-76	serpin family C member 1	Homo sapiens	136-148
9348117-1	1997	Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation.	Peptides	105-113	serpin family C member 1	Homo sapiens	14-26
9348117-1	1997	Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation.	Peptides	105-113	serpin family C member 1	Homo sapiens	136-148
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
9263656-2	1997	The standard antiplatelet and antithrombin agents used today in patients with acute coronary syndromes are aspirin and heparin.	Aspirin	107-114	serpin family C member 1	Homo sapiens	30-42
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
9198206-0	1997	Structural mobility of antithrombin and its modulation by heparin.	Heparin	58-65	serpin family C member 1	Homo sapiens	23-35
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.	Glycine	57-60	serpin family C member 1	Homo sapiens	32-44
9184748-7	1997	Rabbit anti-human ATIII did bind to the alb-hep surface previously exposed to ATIII, confirming the presence of surface bound ATIII.	alb-hep	40-47	serpin family C member 1	Homo sapiens	18-23
9184748-7	1997	Rabbit anti-human ATIII did bind to the alb-hep surface previously exposed to ATIII, confirming the presence of surface bound ATIII.	alb-hep	40-47	serpin family C member 1	Homo sapiens	78-83
9184748-7	1997	Rabbit anti-human ATIII did bind to the alb-hep surface previously exposed to ATIII, confirming the presence of surface bound ATIII.	alb-hep	40-47	serpin family C member 1	Homo sapiens	78-83
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.	epolamine	8-11	serpin family C member 1	Homo sapiens	73-78
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.	epolamine	8-11	serpin family C member 1	Homo sapiens	179-184
9217177-5	1997	Serum cholesterol and triglyceride were associated with increases in factors VII and IX, as well as antithrombin, protein C and protein S; and with increased fibrinogen and factor VIII in women.	Cholesterol	6-17	serpin family C member 1	Homo sapiens	100-112
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
9217177-5	1997	Serum cholesterol and triglyceride were associated with increases in factors VII and IX, as well as antithrombin, protein C and protein S; and with increased fibrinogen and factor VIII in women.	Triglycerides	22-34	serpin family C member 1	Homo sapiens	100-112
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
9217177-7	1997	Smoking status and/or smoking markers were related to fibrinogen, factor IX, antithrombin and protein S. Alcohol intake was related to protein S, and inversely to fibrinogen and antithrombin in men.	Alcohols	105-112	serpin family C member 1	Homo sapiens	178-190
9199820-8	1997	AT levels correlated with vWF (rs = - 0.73, P < 0.01) and creatinine (Rs = -0.70, P < 0.01).	Creatinine	61-71	serpin family C member 1	Homo sapiens	0-2
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.	Sulfates	39-46	serpin family C member 1	Homo sapiens	125-141
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
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
9169007-0	1997	Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity.	Carbohydrates	21-33	serpin family C member 1	Homo sapiens	56-68
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
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
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
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
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.	Glycosaminoglycans	105-122	serpin family C member 1	Homo sapiens	36-48
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.	Sepharose	8-15	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.	Glutamine	79-82	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.	Glutamine	87-90	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.	Glutamine	87-90	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
9169007-8	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.	Glutamine	87-90	serpin family C member 1	Homo sapiens	43-55
9169007-9	1997	These results demonstrate that heterogeneous glycosylation of Asn 155 of recombinant antithrombin is responsible for generating the low heparin affinity glycoform.	Asparagine	62-65	serpin family C member 1	Homo sapiens	85-97
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
9169007-10	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.	Glutamine	249-252	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.	Carbohydrates	32-44	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.	Carbohydrates	32-44	serpin family C member 1	Homo sapiens	221-233
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
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
9158859-0	1997	Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): creation of a novel antithrombin surface.	Polyethylene Terephthalates	43-71	serpin family C member 1	Homo sapiens	102-114
9158859-0	1997	Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): creation of a novel antithrombin surface.	Polyethylene Terephthalates	73-79	serpin family C member 1	Homo sapiens	102-114
9158859-3	1997	The purpose of this study was to covalently immobilize the potent, specific antithrombin agent recombinant hirudin (rHir) to a modified Dacron surface and characterize the in vitro efficacy of thrombin inhibition by this novel biomaterial surface.	Polyethylene Terephthalates	136-142	serpin family C member 1	Homo sapiens	76-88
9251237-4	1997	The diverse functions of heparan sulphate, which range from the control of blood coagulation to the regulation of cell growth and adhesion, depend on the capacity of the chains to activate protein ligands, such as antithrombin III and members of the fibroblast growth factor family.	Heparitin Sulfate	25-41	serpin family C member 1	Homo sapiens	214-230
9065421-0	1997	Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation.	Lysine	0-6	serpin family C member 1	Homo sapiens	28-44
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
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.	Zinc	8-10	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.	Zinc	8-10	serpin family C member 1	Homo sapiens	123-135
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
9147040-0	1997	A unique trisaccharide sequence in heparin mediates the early step of antithrombin III activation.	Trisaccharides	9-22	serpin family C member 1	Homo sapiens	70-86
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
9147040-1	1997	Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation.	Trisaccharides	47-61	serpin family C member 1	Homo sapiens	115-131
9147040-1	1997	Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation.	Trisaccharides	47-61	serpin family C member 1	Homo sapiens	133-139
9147040-1	1997	Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation.	Trisaccharides	47-61	serpin family C member 1	Homo sapiens	241-247
9147040-1	1997	Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation.	Trisaccharides	47-60	serpin family C member 1	Homo sapiens	115-131
9147040-1	1997	Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation.	Trisaccharides	47-60	serpin family C member 1	Homo sapiens	133-139
9147040-1	1997	Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation.	Trisaccharides	47-60	serpin family C member 1	Homo sapiens	241-247
9213829-9	1997	Heparansulphate and sulodexide were able to reduce signs and symptoms with similar degree and to significantly modify t-PA, alpha 2-antiplasmin and ATIII levels without any difference between treatments.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	148-153
9213829-9	1997	Heparansulphate and sulodexide were able to reduce signs and symptoms with similar degree and to significantly modify t-PA, alpha 2-antiplasmin and ATIII levels without any difference between treatments.	glucuronyl glucosamine glycan sulfate	20-30	serpin family C member 1	Homo sapiens	148-153
9065421-0	1997	Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation.	IC 831423	61-84	serpin family C member 1	Homo sapiens	28-44
9065421-2	1997	The purified proteins were used to evaluate the potential role(s) of these residues in the pentasaccharide-mediated activation of ATIII.	pentasaccharide	91-106	serpin family C member 1	Homo sapiens	130-135
9065421-5	1997	In contrast, lysine 114 was found to be critical in the activation of ATIII toward factor Xa.	Lysine	13-19	serpin family C member 1	Homo sapiens	70-75
9065421-6	1997	No activation was observed, even at a pentasaccharide concentration 10 times higher than that required to activate recombinant native ATIII.	pentasaccharide	38-53	serpin family C member 1	Homo sapiens	134-139
9065421-7	1997	These data are the first to demonstrate a pivotal role for lysine 114 in the pentasaccharide-mediated activation of ATIII.	Lysine	59-65	serpin family C member 1	Homo sapiens	116-121
9065421-7	1997	These data are the first to demonstrate a pivotal role for lysine 114 in the pentasaccharide-mediated activation of ATIII.	pentasaccharide	77-92	serpin family C member 1	Homo sapiens	116-121
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.	Calcium Chloride	81-86	serpin family C member 1	Homo sapiens	223-239
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
15622771-0	1997	[The antithrombin action of stichopus japonicus acid mucopolysaccharide (Sjamp) is mediated by heparin cofactor II].	sjamp	73-78	serpin family C member 1	Homo sapiens	5-17
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
9076381-7	1997	Treatment targeted to an antithrombin level of 120% was started with a 2h intravenous infusion before the percutaneous transluminal coronary angioplasty and was repeated, if there were further subnormal values, every 12th hour for 48 h. RESULTS: Angiographic success was 20/25 in the antithrombin group and 21/25 in the placebo group (ns).	Deuterium	71-73	serpin family C member 1	Homo sapiens	25-37
9140889-1	1997	Heparan sulfate proteoglycans produced by vascular endothelium may function physiologically to restrain the migration, multiplication, and phenotypic transition of vascular smooth-muscle cells, and to maintain an anticoagulant luminal surface by bonding and activating antithrombin III.	heparan	0-7	serpin family C member 1	Homo sapiens	269-285
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
9067613-8	1997	In particular, the observed hydrogen bonding of these residues to the body of the molecule in the latent form explains the mechanism for the release of newly formed antithrombin-protease complexes into the circulation for catabolic removal.	Hydrogen	28-36	serpin family C member 1	Homo sapiens	165-177
15622771-4	1997	CONCLUSION: Sjamp was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin.	Dermatan Sulfate	33-49	serpin family C member 1	Homo sapiens	97-109
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
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
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
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
8994426-0	1997	Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate.	Dermatan Sulfate	141-157	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
9013799-8	1997	These results suggest that the fibrinolytic factor release and the antithrombin binding of vascular endothelial cells are impaired by the attack of 15-HPETE, and that the presence of antioxidants prevents the injurious action of lipid hydroperoxide.	Lipid Peroxides	229-248	serpin family C member 1	Homo sapiens	67-79
9017120-3	1997	The thrombin-like enzyme with Gly-Pro-Arg-pNA amidolytic activity was inhibited by human seminal plasma trypsin-like enzyme inhibitor (HSP-TI) and antithrombin III.	gly-pro-arg-pna	30-45	serpin family C member 1	Homo sapiens	147-163
9476567-3	1997	Aspirin and heparin have been used as therapeutic mainstays for acute coronary syndromes, acting as antiplatelet and antithrombin agents, respectively.	Aspirin	0-7	serpin family C member 1	Homo sapiens	117-129
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
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, Low-Molecular-Weight	30-34	serpin family C member 1	Homo sapiens	130-136
9195333-3	1997	In this study, to recognize the mechanism of anticoagulant activity of poly(GEMA)-sulfate, we estimated the binding capacity of antithrombin III to thrombin and some in vitro clotting tests in the presence of poly(GEMA)-sulfate.	poly(glucosyloxyethyl methacrylate) sulfate	71-89	serpin family C member 1	Homo sapiens	128-144
9195333-3	1997	In this study, to recognize the mechanism of anticoagulant activity of poly(GEMA)-sulfate, we estimated the binding capacity of antithrombin III to thrombin and some in vitro clotting tests in the presence of poly(GEMA)-sulfate.	poly(glucosyloxyethyl methacrylate) sulfate	209-227	serpin family C member 1	Homo sapiens	128-144
10214462-3	1997	Significantly higher levels of F VIIC and AT III were found only in the MI-NLP group.	NORLEUCINE PHOSPHONATE	75-78	serpin family C member 1	Homo sapiens	42-48
9469623-6	1997	For coronary artery disease in patients with deficiency of antithrombin activities attributable to either antithrombin III or heparin cofactor II deficiency, argatroban is effective as an anticoagulant.	argatroban	158-168	serpin family C member 1	Homo sapiens	59-71
9469623-6	1997	For coronary artery disease in patients with deficiency of antithrombin activities attributable to either antithrombin III or heparin cofactor II deficiency, argatroban is effective as an anticoagulant.	argatroban	158-168	serpin family C member 1	Homo sapiens	106-122
9469625-1	1997	Argatroban is a direct antithrombin agent developed for the first time by Okamoto et al in 1978.	argatroban	0-10	serpin family C member 1	Homo sapiens	23-35
8983127-4	1997	The dissociation constants of the ATIII-pentasaccharide complex formed by SR 90107A/ORG 31540 and by two close analogues: SR 80327A and SR 80027A in the presence of purified human ATIII were found to be 41 +/- 8, 96 +/- 1 and 3 +/- 1.4 nM (mean +/- sem, n = 3) respectively.	SR 80327A	122-131	serpin family C member 1	Homo sapiens	34-39
9031474-0	1997	A 5-nucleotide insertion in the antithrombin gene causing a quantitative antithrombin deficiency.	5-nucleotide	2-14	serpin family C member 1	Homo sapiens	32-44
9031474-0	1997	A 5-nucleotide insertion in the antithrombin gene causing a quantitative antithrombin deficiency.	5-nucleotide	2-14	serpin family C member 1	Homo sapiens	73-85
8943254-0	1996	Enzymatic preparation of heparin oligosaccharides containing antithrombin III binding sites.	heparin oligosaccharides	25-49	serpin family C member 1	Homo sapiens	61-73
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.	Oligosaccharides	8-24	serpin family C member 1	Homo sapiens	175-187
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
8943254-1	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.	Oligosaccharides	144-160	serpin family C member 1	Homo sapiens	175-187
8943254-5	1996	A hexasaccharide containing a similar structural motif to that found in the antithrombin III binding site and having greatly reduced anticoagulant activity was also isolated.	hexasaccharide	2-16	serpin family C member 1	Homo sapiens	76-92
8943254-8	1996	Sufficient quantities of the decasaccharide were obtained to examine its interaction with antithrombin III using microtitration calorimetry.	decasaccharide	29-43	serpin family C member 1	Homo sapiens	90-106
8943254-9	1996	This decasaccharide bound to antithrombin III with similar avidity as heparin and showed comparable anticoagulant activity, as determined using an antithrombin III dependent anti-factor Xa assay.	decasaccharide	5-19	serpin family C member 1	Homo sapiens	29-45
8943254-9	1996	This decasaccharide bound to antithrombin III with similar avidity as heparin and showed comparable anticoagulant activity, as determined using an antithrombin III dependent anti-factor Xa assay.	decasaccharide	5-19	serpin family C member 1	Homo sapiens	147-163
8943254-10	1996	Interestingly, while both decasaccharide and heparin bound to antithrombin with nanomolar affinity, very little heat of binding was observed.	decasaccharide	26-40	serpin family C member 1	Homo sapiens	62-74
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
9141800-12	1996	Steroid therapy significantly increased the levels of proteins C, protein S. AT-III and fibrinogen as compared to controls.	Steroids	0-7	serpin family C member 1	Homo sapiens	77-83
8910598-0	1996	Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin.	Arginine	8-16	serpin family C member 1	Homo sapiens	76-88
8910598-0	1996	Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin.	Lysine	25-31	serpin family C member 1	Homo sapiens	76-88
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
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
9092408-2	1996	Recently, molecules have been developed which either catalyse the inactivation of factor Xa by the antithrombin (pentasaccharide) or directly inhibit factor Xa (synthetic inhibitor or peptides extracted from the saliva of tics or leeches).	pentasaccharide	113-128	serpin family C member 1	Homo sapiens	99-111
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.	Glycosaminoglycans	70-87	serpin family C member 1	Homo sapiens	148-164
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
8898593-8	1996	Regular alcohol intake predicted multiple changes in vascular risk factors over a five year period including increased concentrations of high density lipoprotein cholesterol and apolipoprotein A I; higher blood pressure; and decreased concentration of antithrombin III.	Alcohols	8-15	serpin family C member 1	Homo sapiens	252-268
8900197-1	1996	LTA cells synthesize a minor population of heparan sulfate proteoglycans (HSPGact) bearing anticoagulant heparan sulfate (HSact) with a specific monosaccharide sequence that accelerates the action of antithrombin (AT).	Heparitin Sulfate	43-58	serpin family C member 1	Homo sapiens	200-212
8900197-1	1996	LTA cells synthesize a minor population of heparan sulfate proteoglycans (HSPGact) bearing anticoagulant heparan sulfate (HSact) with a specific monosaccharide sequence that accelerates the action of antithrombin (AT).	Monosaccharides	145-159	serpin family C member 1	Homo sapiens	200-212
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
9013237-4	1996	Following the debridement under control of diabetes mellitus, antimicrobial agents and argatroban, a newly synthesized antithrombin medicine, were administered.	argatroban	87-97	serpin family C member 1	Homo sapiens	119-131
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
8900394-0	1996	Structure-function relations of antithrombin III-heparin interactions as assessed by biophysical and biological assays and molecular modeling of peptide-pentasaccharide-docked complexes.	pentasaccharide	153-168	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.	A73025	61-92	serpin family C member 1	Homo sapiens	0-5
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
8900394-6	1996	In one case, the Arg residue of the reference peptide corresponding to R129 of ATIII has been replaced by Gln (R129deltaQ peptide), thus mimicking the naturally occurring mutant protein, ATIII Geneva.	Arginine	17-20	serpin family C member 1	Homo sapiens	79-84
8900394-6	1996	In one case, the Arg residue of the reference peptide corresponding to R129 of ATIII has been replaced by Gln (R129deltaQ peptide), thus mimicking the naturally occurring mutant protein, ATIII Geneva.	Glutamine	106-109	serpin family C member 1	Homo sapiens	187-192
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
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
8885144-3	1996	Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII).	Dermatan Sulfate	16-18	serpin family C member 1	Homo sapiens	58-63
8798631-9	1996	Assays with purified reagents show that the fucosylated chondroitin sulfate can potentiate the thrombin inhibition activity of both antithrombin and heparin cofactor II.	Chondroitin Sulfates	56-75	serpin family C member 1	Homo sapiens	132-144
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.	pentasaccharide	33-48	serpin family C member 1	Homo sapiens	111-117
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
8790074-8	1996	Naturally occurring anticoagulant proteins such as antithrombin and protein C fell slightly in women treated with tamoxifen.	Tamoxifen	114-123	serpin family C member 1	Homo sapiens	51-63
8905024-9	1996	Significant reductions of plasma fibrinogen by 14% and AT III by 8% were seen in women who received tamoxifen.	Tamoxifen	100-109	serpin family C member 1	Homo sapiens	55-61
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
8781492-4	1996	Like SR 90107, it shows high affinity for human AT-III (Kd = 3.7 +/- 0.7 nmol/L) and is a potent catalyst of its inhibitory effect with regard to factor Xa (1100 +/- 31 versus 850 +/- 27 anti-Xa U/mg for SR 90107).	PENTA	5-13	serpin family C member 1	Homo sapiens	48-54
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
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.	agrose	103-109	serpin family C member 1	Homo sapiens	0-16
8896339-2	1996	The molecular mass of hamster antithrombin III was estimated at 62.5 kDa and the absorption coefficient (A280 nm 1%, 1 cm) at 6.48 (in 0.1 M sodium phosphate pH 7.0).	sodium phosphate	141-157	serpin family C member 1	Homo sapiens	30-46
8883279-3	1996	Alcohol use was associated with increased levels of factor X and decreased levels of antithrombin III.	Alcohols	0-7	serpin family C member 1	Homo sapiens	85-101
8761481-4	1996	Stimulation of the hepatoma cell line HepG2 with the receptor ligands L-3,5,3"-tri-iodothyronine, all-trans retinoic acid, or their combination, increased production of antithrombin into the culture medium by 1.3-, 1.6-, and 2.0-fold, respectively.	Triiodothyronine	70-96	serpin family C member 1	Homo sapiens	169-181
8702852-0	1996	Requirement of lysine residues outside of the proposed pentasaccharide binding region for high affinity heparin binding and activation of human antithrombin III.	Lysine	15-21	serpin family C member 1	Homo sapiens	144-160
8702852-0	1996	Requirement of lysine residues outside of the proposed pentasaccharide binding region for high affinity heparin binding and activation of human antithrombin III.	pentasaccharide	55-70	serpin family C member 1	Homo sapiens	144-160
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.	Glutamine	45-54	serpin family C member 1	Homo sapiens	23-39
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.	125i-flouresceinamine-heparin	29-58	serpin family C member 1	Homo sapiens	107-112
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.	pentasaccharide	74-89	serpin family C member 1	Homo sapiens	166-171
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
8761481-4	1996	Stimulation of the hepatoma cell line HepG2 with the receptor ligands L-3,5,3"-tri-iodothyronine, all-trans retinoic acid, or their combination, increased production of antithrombin into the culture medium by 1.3-, 1.6-, and 2.0-fold, respectively.	all-trans	98-107	serpin family C member 1	Homo sapiens	169-181
8761481-4	1996	Stimulation of the hepatoma cell line HepG2 with the receptor ligands L-3,5,3"-tri-iodothyronine, all-trans retinoic acid, or their combination, increased production of antithrombin into the culture medium by 1.3-, 1.6-, and 2.0-fold, respectively.	Tretinoin	108-121	serpin family C member 1	Homo sapiens	169-181
8756699-6	1996	The Phe residue of this epitope is highly conserved in members of the serpin superfamily and appears to stabilize the region of the epitope in antithrombin and other serpins by interacting with the protein core.	Phenylalanine	4-7	serpin family C member 1	Homo sapiens	143-155
8908527-3	1996	The use of the 20 micrograms ethinylestradiol formulation was associated with the same pattern of changes, but with lower magnitude (F1+2 + 61.1%, D-dimer +36.0%, antithrombin III -5.3%, protein C +4.6% and protein S-16.0%).	Ethinyl Estradiol	29-45	serpin family C member 1	Homo sapiens	163-179
8908527-4	1996	The changes from baseline were significantly smaller in the 20 micrograms ethinylestradiol group for D-dimer, antithrombin III and protein S than in the 30 micrograms ethinylestradiol group (p = 0.019, p = 0.038 and p = 0.001, respectively).	Ethinyl Estradiol	74-90	serpin family C member 1	Homo sapiens	110-126
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
8741550-9	1996	Left heart bypass with the Bio-Pump without heparin or with an antithrombin agent, argatroban, was used in recent 6 patients.	argatroban	83-93	serpin family C member 1	Homo sapiens	63-75
8819242-0	1996	Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin.	pentasaccharide	87-102	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.	pentasaccharide	87-102	serpin family C member 1	Homo sapiens	144-156
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.	pentasaccharide	40-55	serpin family C member 1	Homo sapiens	108-120
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.	pentasaccharide	40-55	serpin family C member 1	Homo sapiens	128-140
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
8819242-3	1996	Using purified recombinant human coagulation factors and either a clotting or an amidolytic assay for the determination of the residual activity of factor VIIa, we showed that the pentasaccharide was an efficient antithrombin-dependent inhibitor of the coagulant activity of tissue factor-factor VIIa complex.	pentasaccharide	180-195	serpin family C member 1	Homo sapiens	213-225
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
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).	pentasaccharide	200-215	serpin family C member 1	Homo sapiens	122-127
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
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
8776531-4	1996	We report successful coronary stent implantation in a HITTS patient using the antithrombin agent argatroban.	argatroban	97-107	serpin family C member 1	Homo sapiens	78-90
8688424-0	1996	Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155.	Carbohydrates	57-69	serpin family C member 1	Homo sapiens	0-12
8688424-0	1996	Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155.	Asparagine	73-83	serpin family C member 1	Homo sapiens	0-12
8688424-1	1996	The two human plasma antithrombin isoforms, alpha and beta, differ in glycosylation at asparagine 135.	Asparagine	87-97	serpin family C member 1	Homo sapiens	21-33
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., & Gettins, P. G. W. (1993) FEBS Lett.	Heparin	144-151	serpin family C member 1	Homo sapiens	68-80
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., & Gettins, P. G. W. (1993) FEBS Lett.	Adenosine Monophosphate	186-189	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
8688424-9	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.	Carbohydrates	214-226	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
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
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
8679610-8	1996	To test this hypothesis, we have characterized a P14 serine --> tryptophan antithrombin variant.	Serine	53-59	serpin family C member 1	Homo sapiens	78-90
8679610-8	1996	To test this hypothesis, we have characterized a P14 serine --> tryptophan antithrombin variant.	Tryptophan	67-77	serpin family C member 1	Homo sapiens	78-90
8679610-9	1996	From changes in tryptophan fluorescence upon heparin binding, increased affinity for heparin, and partial activation of the variant against factor Xa, we conclude that the proposed mechanism of heparin activation is correct with respect to loop expulsion and that it may consequently be possible to create more highly activated antithrombin variants through suitable hinge region substitutions.	Tryptophan	16-26	serpin family C member 1	Homo sapiens	328-340
8874869-0	1996	A novel nonsense mutation in the antithrombin III gene (Cys-4-->stop) causing recurrent venous thrombosis.	Cysteine	56-59	serpin family C member 1	Homo sapiens	33-49
8874869-1	1996	We describe a novel mutation identified in the antithrombin III (AT-III) propeptide responsible for AT-III deficiency.	propeptide	73-83	serpin family C member 1	Homo sapiens	47-63
8874869-1	1996	We describe a novel mutation identified in the antithrombin III (AT-III) propeptide responsible for AT-III deficiency.	propeptide	73-83	serpin family C member 1	Homo sapiens	65-71
9528269-0	1996	Clinical evaluation of the efficacy of an antithrombin agent "Argatroban" combined with exercise therapy on increase of the skeletal muscle blood flow.	argatroban	62-72	serpin family C member 1	Homo sapiens	42-54
8840467-6	1996	One of the reasons why DHG caused much less bleeding than UFH is thus suggested to be the differences in their affinity for ATIII in plasma.	dhg	23-26	serpin family C member 1	Homo sapiens	124-129
8662679-4	1996	The rate constants of the inactivation of FXIa by C1 inhibitor and by antithrombin III increased up to 117-fold in the presence of glycosaminoglycans.	Glycosaminoglycans	131-149	serpin family C member 1	Homo sapiens	70-86
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
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
8626560-9	1996	Polymer formation was prevented by the addition of synthetic peptides with sequences corresponding to residues P2 to P14 in the reactive center loop of PAI-2 and antithrombin.	Polymers	0-7	serpin family C member 1	Homo sapiens	162-174
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
8718936-8	1996	The relevant calculations, carried out with the help of a computer program, lead to determination of relative second order rate constants of thrombin adsorption and inhibitions by AT and HC in the presence of the polymers.	Polymers	213-221	serpin family C member 1	Homo sapiens	180-182
8718936-9	1996	In addition to thrombin adsorption, polystyrene surfaces bearing only sulphonate groups catalyse inhibition by AT, whereas polystyrene surfaces bearing either aspartate, glycinate or isophthalate sulphonamide groups catalyse both inhibitions by AT and HC.	Polystyrenes	36-47	serpin family C member 1	Homo sapiens	111-113
8718936-9	1996	In addition to thrombin adsorption, polystyrene surfaces bearing only sulphonate groups catalyse inhibition by AT, whereas polystyrene surfaces bearing either aspartate, glycinate or isophthalate sulphonamide groups catalyse both inhibitions by AT and HC.	sulphonate	70-80	serpin family C member 1	Homo sapiens	111-113
8707354-6	1996	Preincubation with anti-thrombin compounds such as hirudin and antithrombin-III-heparin almost completely suppressed the action of thrombin without affecting the actions of other stimuli including IL-1 beta, phorbol 12-myristate 13-acetate (PMA) and TRAP.	Tetradecanoylphorbol Acetate	208-239	serpin family C member 1	Homo sapiens	63-79
8707354-6	1996	Preincubation with anti-thrombin compounds such as hirudin and antithrombin-III-heparin almost completely suppressed the action of thrombin without affecting the actions of other stimuli including IL-1 beta, phorbol 12-myristate 13-acetate (PMA) and TRAP.	Tetradecanoylphorbol Acetate	241-244	serpin family C member 1	Homo sapiens	63-79
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.	Polyethylene Glycols	67-85	serpin family C member 1	Homo sapiens	117-122
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
8642472-5	1996	Homocysteine inhibits the antithrombin III binding activity of endothelial heparan sulfate proteoglycan, thereby suppressing the anticoagulant effect of antithrombin III.	Homocysteine	0-12	serpin family C member 1	Homo sapiens	26-42
8642472-5	1996	Homocysteine inhibits the antithrombin III binding activity of endothelial heparan sulfate proteoglycan, thereby suppressing the anticoagulant effect of antithrombin III.	Homocysteine	0-12	serpin family C member 1	Homo sapiens	153-169
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
8735800-8	1996	Partially carbohydrate-deficient isoforms were demonstrated in antithrombin, protein C, protein S and in alpha 2-antiplasmin, but not in factors II, X and fibrinogen.	Carbohydrates	10-22	serpin family C member 1	Homo sapiens	63-75
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
8857192-0	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
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
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
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
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
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
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
8752690-10	1996	Treatment with antithrombin (argatroban 20mg i.v.	argatroban	29-39	serpin family C member 1	Homo sapiens	15-27
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
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
8928095-5	1996	The bioactivity of HyalSx in terms of FXa and thrombin inactivation increases increasing with sulphation degree but the FXa inactivation seems to be mediated by ATIII, while the aspecific electrostatic interaction seems to play an important role in the inactivation of thrombin.	hyalsx	19-25	serpin family C member 1	Homo sapiens	161-166
8689765-12	1996	Heparan sulphate binds antithrombin III (ATIII), thereby accelerating inactivation of intrinsic coagulation enzymes.	Heparitin Sulfate	0-16	serpin family C member 1	Homo sapiens	23-39
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
8739928-0	1996	The effect of dextran infusion on antithrombin III concentrations and on platelet function during minor surgery.	Dextrans	14-21	serpin family C member 1	Homo sapiens	34-50
8739928-1	1996	The effects of dextran on the antithrombin (AT) III activity and blood coagulation, evaluated with thromboelastography, were investigated in 26 patients (anaesthesia risk class I or II) scheduled for minor surgery under general anaesthesia.	Dextrans	15-22	serpin family C member 1	Homo sapiens	30-51
8739928-8	1996	In the recovery room, the median AT III value was lower in the Dextran than in the Ringer group, 78% and 92%, respectively (P < 0.05).	Dextrans	63-70	serpin family C member 1	Homo sapiens	33-39
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
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
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
8907177-1	1996	Our previous study has shown that depolymerized holothurian glycosaminoglycan (DHG) has two different inhibitory activities in the blood coagulation cascade: heparin cofactor II-dependent thrombin inhibition; and antithrombin III- and heparin cofactor II-independent inhibition of the intrinsic factor Xase complex [Nagase et al.	holothurian glycosaminoglycan	48-77	serpin family C member 1	Homo sapiens	213-229
8907177-1	1996	Our previous study has shown that depolymerized holothurian glycosaminoglycan (DHG) has two different inhibitory activities in the blood coagulation cascade: heparin cofactor II-dependent thrombin inhibition; and antithrombin III- and heparin cofactor II-independent inhibition of the intrinsic factor Xase complex [Nagase et al.	dhg	79-82	serpin family C member 1	Homo sapiens	213-229
9389029-1	1996	The genetic polymorphisms of antithrombin III (AT III) in 5 Chinese populations were studied by isoelectric focusing on polyacrylamide gels followed by immunoblotting.	polyacrylamide	120-134	serpin family C member 1	Homo sapiens	29-45
9389029-1	1996	The genetic polymorphisms of antithrombin III (AT III) in 5 Chinese populations were studied by isoelectric focusing on polyacrylamide gels followed by immunoblotting.	polyacrylamide	120-134	serpin family C member 1	Homo sapiens	47-53
14650442-9	1996	The pentasaccharide did not bind as strongly as the other heparin-derived oligosaccharides, indicating an AT III-independent mechanism.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	106-112
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
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.	Polystyrenes	13-24	serpin family C member 1	Homo sapiens	117-122
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
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
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
8558740-4	1996	One or more NAC deficiencies were found in 15 (30%) patients and included antithrombin III (n = 5), protein C (n = 8), protein S (n = 4), and heparin cofactor II (n = 2).	nac	12-15	serpin family C member 1	Homo sapiens	74-90
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
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
8822125-3	1996	LMWH contains both high and low affinity fragments to antithrombin-III.	Heparin, Low-Molecular-Weight	0-4	serpin family C member 1	Homo sapiens	54-70
8772222-0	1995	Pharmacokinetics and tolerance of the natural pentasaccharide (SR90107/Org31540) with high affinity to antithrombin III in man.	pentasaccharide	46-61	serpin family C member 1	Homo sapiens	103-119
8772222-0	1995	Pharmacokinetics and tolerance of the natural pentasaccharide (SR90107/Org31540) with high affinity to antithrombin III in man.	PENTA	63-70	serpin family C member 1	Homo sapiens	103-119
8772222-1	1995	This paper reports the results of the first administration of the synthetic natural pentasaccharide with high affinity to antithrombin III (NP) in man.	pentasaccharide	84-99	serpin family C member 1	Homo sapiens	122-138
8772223-0	1995	The effect of the synthetic pentasaccharide SR 90107/ORG 31540 on thrombin generation ex vivo is uniquely due to ATIII-mediated neutralization of factor Xa.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	113-118
8772223-5	1995	The plotting of TG inhibition versus SP concentration could be fitted with a good correlation (r = 0.94) to the graphical representation linking [ATIII-SP] to [SP].	TFF2 protein, human	37-39	serpin family C member 1	Homo sapiens	146-151
8772223-5	1995	The plotting of TG inhibition versus SP concentration could be fitted with a good correlation (r = 0.94) to the graphical representation linking [ATIII-SP] to [SP].	TFF2 protein, human	152-154	serpin family C member 1	Homo sapiens	146-151
8772223-6	1995	These results demonstrate that following subcutaneous administration to man, SP inhibits TG ex vivo and likely in vivo exclusively through the same selective ATIII-mediated inhibition of factor Xa as the one elicited in vitro.	TFF2 protein, human	77-79	serpin family C member 1	Homo sapiens	158-163
7586247-0	1995	Prolonged antithrombin activity of low-molecular-weight heparins.	Heparin	56-64	serpin family C member 1	Homo sapiens	10-22
8689765-12	1996	Heparan sulphate binds antithrombin III (ATIII), thereby accelerating inactivation of intrinsic coagulation enzymes.	Heparitin Sulfate	0-16	serpin family C member 1	Homo sapiens	41-46
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
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
8582900-1	1995	The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII.	Polystyrenes	117-128	serpin family C member 1	Homo sapiens	24-40
8582900-1	1995	The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII.	Polystyrenes	117-128	serpin family C member 1	Homo sapiens	42-47
8582900-1	1995	The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII.	Carbon-14	202-205	serpin family C member 1	Homo sapiens	24-40
8582900-1	1995	The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII.	Carbon-14	202-205	serpin family C member 1	Homo sapiens	42-47
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
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
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
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
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
8733245-0	1995	[Antithrombin III dosage using the chromogenic substrate Tos-Gly-Pro-Arg-NAN, in several pathological situations].	N(alpha)-4-tosyl-glycyl-prolyl-arginine-4-nitroanilide	57-76	serpin family C member 1	Homo sapiens	1-17
8733245-3	1995	METHOD: ATIII levels were measured, using the chromogenic substrate Tos-Gly-Pro-Arg-NAN, which is specific for thrombin, and which has been sinthesized at the Biophysical Department of the Escola Paulista de Medicina of the Federal University of Sao Paulo, Brazil.	N(alpha)-4-tosyl-glycyl-prolyl-arginine-4-nitroanilide	68-87	serpin family C member 1	Homo sapiens	8-13
8733245-10	1995	There was a significant correlation between ATIII levels measured using the chromogenic substrate Tos-Gly-Pro-Arg-NAN and those measured using S-2238, produced by Kabi Laboratories.	N(alpha)-4-tosyl-glycyl-prolyl-arginine-4-nitroanilide	98-117	serpin family C member 1	Homo sapiens	44-49
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
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
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
8619306-4	1995	alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B.	Urea	128-132	serpin family C member 1	Homo sapiens	21-67
8619306-4	1995	alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B.	Sodium Dodecyl Sulfate	134-155	serpin family C member 1	Homo sapiens	21-67
8619306-4	1995	alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B.	Edetic Acid	161-169	serpin family C member 1	Homo sapiens	21-67
8588189-0	1995	Heparan-dependent endothelial antithrombin binding is increased by butyrate.	heparan	0-7	serpin family C member 1	Homo sapiens	30-42
8588189-0	1995	Heparan-dependent endothelial antithrombin binding is increased by butyrate.	Butyrates	67-75	serpin family C member 1	Homo sapiens	30-42
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
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
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
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
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
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
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.	Diethylstilbestrol	69-72	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.	ETW	73-76	serpin family C member 1	Homo sapiens	78-94
7673182-7	1995	Mutation of two Asp residues flanking Arg221a (D221A/D222K) almost abolishes the allosteric properties of thrombin and shows that the Na+ binding loop is also involved in direct recognition of protein C and antithrombin.	Aspartic Acid	16-19	serpin family C member 1	Homo sapiens	207-219
7673182-7	1995	Mutation of two Asp residues flanking Arg221a (D221A/D222K) almost abolishes the allosteric properties of thrombin and shows that the Na+ binding loop is also involved in direct recognition of protein C and antithrombin.	arg221a	38-45	serpin family C member 1	Homo sapiens	207-219
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
8551493-4	1995	On the other hand, the therapeutic dose of celiprolol was shown to reduce total platelet aggregation, without any harmful effects on fibrinolytic activity and coagulation inhibitors such as protein C and antithrombin III.	Celiprolol	43-53	serpin family C member 1	Homo sapiens	204-220
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
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
7646463-5	1995	Based on far- and near-UV CD, bv.hat3.N135A has a high degree of conformational similarity to plasma antithrombin.	Cadmium	26-28	serpin family C member 1	Homo sapiens	101-113
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
7482443-0	1995	Functional assay of plasma antithrombin using polyethylene glycol (PEG) defibrinated plasma.	Polyethylene Glycols	46-65	serpin family C member 1	Homo sapiens	27-39
7482443-0	1995	Functional assay of plasma antithrombin using polyethylene glycol (PEG) defibrinated plasma.	Polyethylene Glycols	67-70	serpin family C member 1	Homo sapiens	27-39
7482443-1	1995	Polyethylene glycol(PEG) was used to precipitate fibrinogen to prepare defibrinated plasma in the two stage clotting assay of antithrombin activity.	Polyethylene Glycols	0-19	serpin family C member 1	Homo sapiens	126-138
7482443-1	1995	Polyethylene glycol(PEG) was used to precipitate fibrinogen to prepare defibrinated plasma in the two stage clotting assay of antithrombin activity.	Polyethylene Glycols	20-23	serpin family C member 1	Homo sapiens	126-138
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
7641350-11	1995	The results of TIMI 7 lend support to the use of an antithrombin agent with aspirin in patients with unstable angina.	timi 7	15-21	serpin family C member 1	Homo sapiens	52-64
7641350-11	1995	The results of TIMI 7 lend support to the use of an antithrombin agent with aspirin in patients with unstable angina.	Aspirin	76-83	serpin family C member 1	Homo sapiens	52-64
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
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
7606009-0	1995	Iodine-mediated inactivation of lipid- and nonlipid-enveloped viruses in human antithrombin III concentrate.	Iodine	0-6	serpin family C member 1	Homo sapiens	79-95
7606009-3	1995	Iodine at levels of 0.01% to 0.02% caused between 43% and 94% loss of AT-III activity, as well as degradation of AT-III as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.	Iodine	0-6	serpin family C member 1	Homo sapiens	70-76
7606009-3	1995	Iodine at levels of 0.01% to 0.02% caused between 43% and 94% loss of AT-III activity, as well as degradation of AT-III as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis.	Sodium Dodecyl Sulfate	132-154	serpin family C member 1	Homo sapiens	113-119
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.	Asparagine	42-52	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.	Asparagine	42-52	serpin family C member 1	Homo sapiens	191-207
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.	Serine	74-80	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.	Nitrogen	110-111	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.	Nitrogen	110-111	serpin family C member 1	Homo sapiens	191-207
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
7599134-2	1995	The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192.	n-linked oligosaccharides	33-58	serpin family C member 1	Homo sapiens	10-15
7599134-2	1995	The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192.	Asparagine	71-82	serpin family C member 1	Homo sapiens	10-15
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.	Asparagine	45-55	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	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
7599134-5	1995	Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192.	Nitrogen	39-40	serpin family C member 1	Homo sapiens	33-38
7599134-5	1995	Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192.	n-x-s	65-70	serpin family C member 1	Homo sapiens	33-38
7599134-5	1995	Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192.	n-x-t	83-88	serpin family C member 1	Homo sapiens	33-38
7599134-6	1995	On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position.	n-x-s css	76-85	serpin family C member 1	Homo sapiens	162-167
7599134-6	1995	On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position.	n-x-t	121-126	serpin family C member 1	Homo sapiens	162-167
7599134-6	1995	On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position.	(2-benzoylethyl)trimethylammonium	157-161	serpin family C member 1	Homo sapiens	162-167
7599134-6	1995	On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position.	n-x-s cs	76-84	serpin family C member 1	Homo sapiens	162-167
7599134-9	1995	Thus, serine in the third position of the N135 CS is responsible for its "partial" glycosylation and leads to production of beta-ATIII.	Serine	6-12	serpin family C member 1	Homo sapiens	129-134
7599134-9	1995	Thus, serine in the third position of the N135 CS is responsible for its "partial" glycosylation and leads to production of beta-ATIII.	N-[3-(Trimethoxysilyl)propyl]aniline	42-46	serpin family C member 1	Homo sapiens	129-134
7647008-1	1995	The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis.	Sodium Dodecyl Sulfate	132-135	serpin family C member 1	Homo sapiens	60-76
7647008-1	1995	The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis.	Sodium Dodecyl Sulfate	132-135	serpin family C member 1	Homo sapiens	78-83
7647008-1	1995	The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis.	polyacrylamide	136-150	serpin family C member 1	Homo sapiens	60-76
7647008-1	1995	The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis.	polyacrylamide	136-150	serpin family C member 1	Homo sapiens	78-83
7647008-2	1995	The predominant species of factor Xa-ATIII detected after plasma and plasma to which factor Xa had been added were gel filtered on Sephadex G-200 and Sepharose 4B had apparent M(r) > 200,000, in which factor Xa-ATIII was associated with vitronectin.	sephadex	131-145	serpin family C member 1	Homo sapiens	37-42
7647008-2	1995	The predominant species of factor Xa-ATIII detected after plasma and plasma to which factor Xa had been added were gel filtered on Sephadex G-200 and Sepharose 4B had apparent M(r) > 200,000, in which factor Xa-ATIII was associated with vitronectin.	Sepharose	150-159	serpin family C member 1	Homo sapiens	37-42
8589216-0	1995	Activation of antithrombin III isoforms by heparan sulphate glycosaminoglycans and other sulphated polysaccharides.	heparan sulphate glycosaminoglycans	43-78	serpin family C member 1	Homo sapiens	14-30
8589216-0	1995	Activation of antithrombin III isoforms by heparan sulphate glycosaminoglycans and other sulphated polysaccharides.	Polysaccharides	99-114	serpin family C member 1	Homo sapiens	14-30
8589216-4	1995	High-molecular-weight dextran sulphate was the most effective of those studied, increasing thrombin inhibition by the higher-affinity antithrombin III isoform up to five-fold more efficiently than did heparin fractions with low-affinity for antithrombin III.	Dextran Sulfate	22-38	serpin family C member 1	Homo sapiens	134-150
8589216-4	1995	High-molecular-weight dextran sulphate was the most effective of those studied, increasing thrombin inhibition by the higher-affinity antithrombin III isoform up to five-fold more efficiently than did heparin fractions with low-affinity for antithrombin III.	Dextran Sulfate	22-38	serpin family C member 1	Homo sapiens	241-257
8589216-9	1995	The observed effects of the heparan sulphates on this anticoagulant pathway, although of low potency, are consistent with the hypotheses that these substances naturally regulate blood homeostasis in vascular tissues and that much of this function may be mediated by the higher-affinity antithrombin III isoform.	Heparitin Sulfate	28-45	serpin family C member 1	Homo sapiens	286-302
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
7500917-5	1995	ATIII bound specifically to heparan sulfate residues on the surface of herpesvirus-permissive RK13 cells.	Heparitin Sulfate	28-43	serpin family C member 1	Homo sapiens	0-5
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
7500917-9	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.	Peptides	185-193	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
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
7615164-10	1995	The chondroitin sulfate enhances the affinity of thrombin for thrombomodulin approximately 10- to 20-fold, making thrombomodulin a more potent inhibitor of coagulation, altering thrombin"s conformation and specificity, and accelerating thrombin inhibition by the serpin, antithrombin.	Chondroitin Sulfates	4-23	serpin family C member 1	Homo sapiens	271-283
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
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
7641602-10	1995	In addition to natural and recombinant human antithrombin III, direct antithrombin III-independent thrombin inhibitors have been developed as recombinant hirudin, hirulog, argatroban, boroarginine derivatives and single stranded DNA oligonucleotides (aptanes).	boroarginine	184-196	serpin family C member 1	Homo sapiens	70-86
7641602-10	1995	In addition to natural and recombinant human antithrombin III, direct antithrombin III-independent thrombin inhibitors have been developed as recombinant hirudin, hirulog, argatroban, boroarginine derivatives and single stranded DNA oligonucleotides (aptanes).	Oligonucleotides	233-249	serpin family C member 1	Homo sapiens	70-86
7607583-3	1995	Based on reports of increases in the endogenous anticoagulants (protein C, protein S, antithrombin III and plasminogen) with synthetic androgen therapy, the patient was treated with danazol for 8 weeks.	Danazol	182-189	serpin family C member 1	Homo sapiens	86-102
7730349-2	1995	To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated.	Serine	150-153	serpin family C member 1	Homo sapiens	56-68
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
7730349-2	1995	To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated.	Serine	150-153	serpin family C member 1	Homo sapiens	70-72
7730349-2	1995	To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated.	Leucine	163-166	serpin family C member 1	Homo sapiens	56-68
7730349-2	1995	To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated.	Leucine	163-166	serpin family C member 1	Homo sapiens	70-72
7730349-4	1995	AT-Denver inhibited thrombin and Factor Xa with nearly equimolar stoichiometries and formed SDS-stable complexes with these proteinases, indicating that the diminished inhibitor activity was not due to an enhanced turnover of the inhibitor as a substrate.	Sodium Dodecyl Sulfate	92-95	serpin family C member 1	Homo sapiens	0-2
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.	pentasaccharide	33-48	serpin family C member 1	Homo sapiens	12-24
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
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.	pentasaccharide	34-49	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	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
7721817-3	1995	LAH was shown to be free of HAH (< 0.001%) from the lack of exchange of added fluorescein-labeled HAH into LAH after separating the polysaccharides by antithrombin-agarose chromatography.	lithium aluminium hydride	0-3	serpin family C member 1	Homo sapiens	154-166
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
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.	Polysaccharides	130-145	serpin family C member 1	Homo sapiens	223-235
7721817-9	1995	1H NMR difference spectroscopy of antithrombin complexes with LAH and HAH and competitive binding studies were consistent with LAH accelerating activity being mediated by binding to the same site on the inhibitor as HAH.	Hydrogen	0-2	serpin family C member 1	Homo sapiens	34-46
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
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
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
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
7641602-10	1995	In addition to natural and recombinant human antithrombin III, direct antithrombin III-independent thrombin inhibitors have been developed as recombinant hirudin, hirulog, argatroban, boroarginine derivatives and single stranded DNA oligonucleotides (aptanes).	aptanes	251-258	serpin family C member 1	Homo sapiens	70-86
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
7495073-1	1995	The antithrombin-dependent inhibition of prothrombinase, assembled at a macroscopic surface, was studied under flow conditions utilizing a tubular flow reactor that consists of a phospholipid-coated glass capillary.	Phospholipids	179-191	serpin family C member 1	Homo sapiens	4-16
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.	pentasaccharide	37-52	serpin family C member 1	Homo sapiens	102-118
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
7736468-1	1995	1H NMR and 13C NMR relaxation measurements at different magnetic field strengths were used to study the nature of overall and internal motions, in aqueous solution, of the synthetic pentasaccharide (A-G-A*-I-AM) corresponding to the binding site of heparin for antithrombin III.	pentasaccharide	182-197	serpin family C member 1	Homo sapiens	261-277
7893664-2	1995	The serpins antithrombin, protease nexin 1, and alpha 1-antitrypsin with a reactive-center arginine (Arg-alpha 1-antitrypsin) were found to inhibit the sperm protease acrosin with varying efficiency.	Arginine	91-99	serpin family C member 1	Homo sapiens	12-24
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	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
7888673-0	1995	Depolymerized holothurian glycosaminoglycan with novel anticoagulant actions: antithrombin III- and heparin cofactor II-independent inhibition of factor X activation by factor IXa-factor VIIIa complex and heparin cofactor II-dependent inhibition of thrombin.	holothurian glycosaminoglycan	14-43	serpin family C member 1	Homo sapiens	78-94
7888673-1	1995	The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors.	Polysaccharides	30-44	serpin family C member 1	Homo sapiens	198-214
7888673-1	1995	The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors.	Polysaccharides	30-44	serpin family C member 1	Homo sapiens	216-221
7888673-1	1995	The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors.	holothurian glycosaminoglycan	74-103	serpin family C member 1	Homo sapiens	198-214
7888673-1	1995	The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors.	holothurian glycosaminoglycan	74-103	serpin family C member 1	Homo sapiens	216-221
7888673-1	1995	The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors.	dhg	105-108	serpin family C member 1	Homo sapiens	216-221
7888673-5	1995	These results indicated that DHG has two different inhibitory activities, one being an HCII-dependent thrombin inhibition and the other an ATIII- and HCII-independent inhibition of the coagulation cascade.	dhg	29-32	serpin family C member 1	Homo sapiens	139-144
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
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
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.	pentasaccharide	92-107	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
7873519-4	1995	Unfractionated glycosaminoglycan heparin that had been prepared from porcine intestinal mucosa was examined for its capacity to bind antithrombin III using a new technique developed to quantitate that interaction.	glycosaminoglycan heparin	15-40	serpin family C member 1	Homo sapiens	133-149
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
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.	Oligosaccharides	151-167	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.	Oligosaccharides	151-167	serpin family C member 1	Homo sapiens	196-212
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.	Oligosaccharides	225-241	serpin family C member 1	Homo sapiens	54-70
7749832-7	1995	During the long-term follow-up of three patients with congenital antithrombin III or protein C deficiency, the factor VIIa level was more responsive to changes in the warfarin dose than the INR, and there were generally no corresponding changes of the thrombin-antithrombin III complex (TAT) level.	Warfarin	167-175	serpin family C member 1	Homo sapiens	65-81
7540878-1	1995	The purpose of this pilot study was to determine the effect of recombinant hirudin (r-hirudin) on coagulopathy and the relationship between concentrations of thrombin-antithrombin III (ATIII) complex (TAT) and thrombin-hirudin complex (THC) in patients with disseminated intravascular coagulation (DIC).	Dronabinol	236-239	serpin family C member 1	Homo sapiens	158-183
7540878-1	1995	The purpose of this pilot study was to determine the effect of recombinant hirudin (r-hirudin) on coagulopathy and the relationship between concentrations of thrombin-antithrombin III (ATIII) complex (TAT) and thrombin-hirudin complex (THC) in patients with disseminated intravascular coagulation (DIC).	Dronabinol	236-239	serpin family C member 1	Homo sapiens	185-190
7795154-0	1995	Two novel antithrombin variants, Asn187Asp and Asn187Lys, indicate a functional role for asparagine 187.	Asparagine	89-99	serpin family C member 1	Homo sapiens	10-22
7795154-3	1995	In two families the mutation (6460 AAC-->GAC) results in an asparagine to aspartate substitution and is associated with normal immunological levels of antithrombin but a reduction in functional activity.	Asparagine	63-73	serpin family C member 1	Homo sapiens	154-166
7795154-3	1995	In two families the mutation (6460 AAC-->GAC) results in an asparagine to aspartate substitution and is associated with normal immunological levels of antithrombin but a reduction in functional activity.	Aspartic Acid	77-86	serpin family C member 1	Homo sapiens	154-166
7795154-5	1995	Asparagine 187 is located in the middle of the F helix of antithrombin and forms the major link between the F helix and strand 3 of the A sheet.	Asparagine	0-10	serpin family C member 1	Homo sapiens	58-70
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
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.	Sepharose	148-157	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
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
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
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.	Sepharose	149-158	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.	Sepharose	149-158	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
7762756-5	1995	Its pI and molecular weight were the same as those of a physiological variant of antithrombin III (beta fraction), which is known to lack the asparagine-N-linked oligosaccharide chain at asparagine-135.	asparagine-n-linked oligosaccharide	142-177	serpin family C member 1	Homo sapiens	81-97
7762756-5	1995	Its pI and molecular weight were the same as those of a physiological variant of antithrombin III (beta fraction), which is known to lack the asparagine-N-linked oligosaccharide chain at asparagine-135.	Asparagine	142-152	serpin family C member 1	Homo sapiens	81-97
7588997-0	1995	Effect of sulfated xylans during the interaction of [125I]-thrombin with antithrombin III or heparin cofactor II of human plasma.	Xylans	19-25	serpin family C member 1	Homo sapiens	73-89
7588997-2	1995	Addition of OSXS or SP-54 enhanced the complexation of thrombin with HC-II or with both AT-III and HC-II depending upon the concentration and the duration of the interactions of the sulfated compounds with plasma.	osxs	12-16	serpin family C member 1	Homo sapiens	88-94
7588997-2	1995	Addition of OSXS or SP-54 enhanced the complexation of thrombin with HC-II or with both AT-III and HC-II depending upon the concentration and the duration of the interactions of the sulfated compounds with plasma.	Pentosan Sulfuric Polyester	20-25	serpin family C member 1	Homo sapiens	88-94
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.	osxs	29-33	serpin family C member 1	Homo sapiens	58-64
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.	Pentosan Sulfuric Polyester	38-43	serpin family C member 1	Homo sapiens	58-64
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
7588997-5	1995	The complexations of AT-III-thrombin and HC-II-thrombin were reversed in the presence of 200 micrograms/ml of SP-54 during a 30 s interaction or in presence of 100 micrograms/ml of OSXS during a 2 min interaction.	Pentosan Sulfuric Polyester	110-115	serpin family C member 1	Homo sapiens	21-27
7588997-5	1995	The complexations of AT-III-thrombin and HC-II-thrombin were reversed in the presence of 200 micrograms/ml of SP-54 during a 30 s interaction or in presence of 100 micrograms/ml of OSXS during a 2 min interaction.	osxs	181-185	serpin family C member 1	Homo sapiens	21-27
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
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
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
7716890-2	1995	In a group of patients with medium and severe cardiac failure the administration of sulodexide led to an increased activation of the fibrinolytic potential--a drop of PAI-1 and fibrinogen, to an increased activation of anticoagulatory potential--an increase of AT III and reduced plasma viscosity.	glucuronyl glucosamine glycan sulfate	84-94	serpin family C member 1	Homo sapiens	261-267
7893924-12	1994	Direct inhibition of the activity of AT-III and coagulation factor VIII and other factors by homocysteine was attempted in vitro but could not be shown at HC concentrations known to occur in the plasma of HOCY patients.	Homocysteine	93-105	serpin family C member 1	Homo sapiens	37-43
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
7947827-0	1994	Lysine-heparin interactions in antithrombin.	Lysine	0-6	serpin family C member 1	Homo sapiens	31-43
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.	Lysine	0-6	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	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.	IC 831423	62-85	serpin family C member 1	Homo sapiens	19-31
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
7961924-0	1994	Role of N- and C-terminal amino acids in antithrombin binding to pentasaccharide.	pentasaccharide	65-80	serpin family C member 1	Homo sapiens	41-53
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.	pentasaccharide	162-177	serpin family C member 1	Homo sapiens	141-153
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.	pentasaccharide	162-177	serpin family C member 1	Homo sapiens	224-236
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
7961924-2	1994	The reduction in binding affinity of the pentasaccharide with the N-terminal variants (with substitution mutations Pro-41-->Leu, Arg-47-->Cys and His, Leu-99-->Val and Phe, Gln-118-->Pro, Arg-129-->Gln) compared to normal antithrombin, Kd 200 nM, ranged from 15-984-fold and was generally less than 150-fold.	pentasaccharide	41-56	serpin family C member 1	Homo sapiens	237-249
7961924-3	1994	Reduced binding affinity is assumed to arise mostly by perturbation, direct or indirect, of the initial contact of pentasaccharide with basic residues of antithrombin.	pentasaccharide	115-130	serpin family C member 1	Homo sapiens	154-166
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
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
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
7863481-4	1994	The effect of a denaturing agent (sodium dodecyl sulfate) on the recognition of the plasma antithrombin by a polyclonal antibody was studied in an immuno-enzymatic assay.	Sodium Dodecyl Sulfate	34-56	serpin family C member 1	Homo sapiens	91-103
7878631-6	1994	In age- and race-adjusted analyses, AT III was positively associated with smoking, HDL-cholesterol, triglycerides (men only), and in women, with diabetes and lipoprotein(a).	Cholesterol	87-98	serpin family C member 1	Homo sapiens	36-42
7878631-6	1994	In age- and race-adjusted analyses, AT III was positively associated with smoking, HDL-cholesterol, triglycerides (men only), and in women, with diabetes and lipoprotein(a).	Triglycerides	100-113	serpin family C member 1	Homo sapiens	36-42
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
7841596-18	1994	Whether AT-III in the presence of glycosaminoglycans on cell surfaces expressing TF can function as an auxiliary second physiological regulator is not known.	Glycosaminoglycans	34-52	serpin family C member 1	Homo sapiens	8-14
7841305-5	1994	DS500 inhibited both the PtdInsP and the sulphatide-mediated autoactivation in an antithrombin III independent manner.	Phosphatidylinositol Phosphates	25-32	serpin family C member 1	Homo sapiens	82-98
7841305-5	1994	DS500 inhibited both the PtdInsP and the sulphatide-mediated autoactivation in an antithrombin III independent manner.	Sulfoglycosphingolipids	41-51	serpin family C member 1	Homo sapiens	82-98
7833476-0	1995	Fibrinogen inhibits the heparin cofactor II-mediated antithrombin activity of dermatan sulfate.	Dermatan Sulfate	78-94	serpin family C member 1	Homo sapiens	53-65
7833476-2	1995	The antithrombin activity of several dermatan sulfate preparations has been measured in whole human plasma and found to be -55% of that in purified systems.	Dermatan Sulfate	37-53	serpin family C member 1	Homo sapiens	4-16
7833476-3	1995	Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate.	Dermatan Sulfate	109-125	serpin family C member 1	Homo sapiens	84-96
7833476-3	1995	Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate.	Dermatan Sulfate	218-234	serpin family C member 1	Homo sapiens	84-96
7833476-5	1995	Addition of these proteins to the purified system showed that only fibrinogen inhibited the antithrombin activity of dermatan sulfate and that it did so in a concentration-dependent manner over the physiologic range of plasma fibrinogen levels.	Dermatan Sulfate	117-133	serpin family C member 1	Homo sapiens	92-104
7863710-5	1995	The AT III activity dropped significantly (p < 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 < 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 < 0.001) negative correlation between AT III and heparin levels.	Heparin	86-93	serpin family C member 1	Homo sapiens	75-81
7806495-3	1994	Thrombin is inhibited by the serpins antithrombin and heparin cofactor II (HCiI) in reactions that are accelerated markedly by specific glycosaminoglycans.	Glycosaminoglycans	136-154	serpin family C member 1	Homo sapiens	37-49
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
7981186-1	1994	We have identified three novel mutations of the antithrombin (AT) gene in patients with thrombotic complications: a Cys 128 --> Tyr mutations, a G --> A mutation in the intervening sequence 4 (IVS4) 14 nucleotide 5" to exon 5, and a 9 bp deletion in the 3" end of exon 6 resulting in a short aberrant sequence after Arg 425.	Arginine	316-319	serpin family C member 1	Homo sapiens	48-60
7981186-1	1994	We have identified three novel mutations of the antithrombin (AT) gene in patients with thrombotic complications: a Cys 128 --> Tyr mutations, a G --> A mutation in the intervening sequence 4 (IVS4) 14 nucleotide 5" to exon 5, and a 9 bp deletion in the 3" end of exon 6 resulting in a short aberrant sequence after Arg 425.	Arginine	316-319	serpin family C member 1	Homo sapiens	62-64
7740457-12	1994	The same dose of naroparcil enhanced the formation of thrombin/heparin cofactor II complexes at the expense of thrombin/antithrombin III complexes in plasma incubated with (125I)-human alpha-thrombin and induced the appearance of dermatan sulfate-like material in the plasma of treated rabbits, as measured by a heparin cofactor II-mediated thrombin inhibition assay.	naroparcil	17-27	serpin family C member 1	Homo sapiens	120-136
7757423-0	1994	Feasible synthesis and biological properties of six "non-glycosamino" glycan analogues of the antithrombin III binding heparin pentasaccharide.	glycosamino"	57-69	serpin family C member 1	Homo sapiens	94-110
7757423-0	1994	Feasible synthesis and biological properties of six "non-glycosamino" glycan analogues of the antithrombin III binding heparin pentasaccharide.	Polysaccharides	70-76	serpin family C member 1	Homo sapiens	94-110
7757423-0	1994	Feasible synthesis and biological properties of six "non-glycosamino" glycan analogues of the antithrombin III binding heparin pentasaccharide.	IC 831423	119-142	serpin family C member 1	Homo sapiens	94-110
7757423-1	1994	In this paper, we report the synthesis of "non-glycosamino" glycan analogues 5-10 of the antithrombin III binding pentasaccharide 1.	Glycosaminoglycans	47-66	serpin family C member 1	Homo sapiens	89-105
7757423-1	1994	In this paper, we report the synthesis of "non-glycosamino" glycan analogues 5-10 of the antithrombin III binding pentasaccharide 1.	pentasaccharide	114-129	serpin family C member 1	Homo sapiens	89-105
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
7896748-3	1994	Porcine ATIII was found to consist of 431 amino acid residues, with a calculated molecular weight of 48,930 without carbohydrate.	Carbohydrates	116-128	serpin family C member 1	Homo sapiens	8-13
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
7896748-5	1994	Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds.	Amino Acids, Basic	118-134	serpin family C member 1	Homo sapiens	8-13
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.	Disulfides	149-158	serpin family C member 1	Homo sapiens	8-13
7896748-6	1994	The most notable feature of porcine ATIII was that it possesses only three carbohydrate chains, at Asn136, 156, and 193, whereas other mammalian ATIIIs have four, additional chain being at Asn97; this is replaced by Asp in porcine ATIII.	Carbohydrates	75-87	serpin family C member 1	Homo sapiens	36-41
7896748-6	1994	The most notable feature of porcine ATIII was that it possesses only three carbohydrate chains, at Asn136, 156, and 193, whereas other mammalian ATIIIs have four, additional chain being at Asn97; this is replaced by Asp in porcine ATIII.	ASN 136	99-105	serpin family C member 1	Homo sapiens	36-41
7896748-6	1994	The most notable feature of porcine ATIII was that it possesses only three carbohydrate chains, at Asn136, 156, and 193, whereas other mammalian ATIIIs have four, additional chain being at Asn97; this is replaced by Asp in porcine ATIII.	Aspartic Acid	216-219	serpin family C member 1	Homo sapiens	36-41
7896748-9	1994	Porcine ATIII eluted from the column with a peak at an NaCl concentration of 924 mM while human ATIII eluted at 838 mM NaCl.	Sodium Chloride	55-59	serpin family C member 1	Homo sapiens	8-13
7896748-9	1994	Porcine ATIII eluted from the column with a peak at an NaCl concentration of 924 mM while human ATIII eluted at 838 mM NaCl.	Sodium Chloride	119-123	serpin family C member 1	Homo sapiens	96-101
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
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
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
7957907-0	1994	Antithrombin histidine variants 1H NMR resonance assignments and functional properties.	Histidine	13-22	serpin family C member 1	Homo sapiens	0-12
7957907-0	1994	Antithrombin histidine variants 1H NMR resonance assignments and functional properties.	Hydrogen	32-34	serpin family C member 1	Homo sapiens	0-12
7966143-2	1994	Several antithrombin agents are being developed by chemical and structural optimization of these "hirupeptides".	hirupeptides	98-110	serpin family C member 1	Homo sapiens	8-20
7863468-7	1994	These minor AT III molecules were considered to lack an oligosaccharide sidechain.	Oligosaccharides	56-71	serpin family C member 1	Homo sapiens	12-18
7929178-1	1994	We have investigated the characteristics of clonal L cell mutant VI-7 that has previously been demonstrated to exhibit reduced levels of cell surface proteoglycans containing heparan sulfate (HS) with regions of defined monosaccharide sequence that interact with antithrombin (HSact) (de Agostini, A. L., Lau, H. K., Leone, C., Youssoufian, H., and Rosenberg, R. D. (1990) Proc.	Monosaccharides	220-234	serpin family C member 1	Homo sapiens	263-275
7532447-1	1994	Protein C inhibitor (PCI), antithrombin, and heparin cofactor II are members of the serine proteinase inhibitor (serpin) superfamily that inhibit proteinases at rates which increase in the presence of the glycosaminoglycan heparin.	glycosaminoglycan heparin	205-230	serpin family C member 1	Homo sapiens	27-39
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.	Heparitin Sulfate	72-88	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
7523096-11	1994	Synthetic peptides, that contained the active sites of AT-III and alpha 1-antichymotrypsin, were also inhibitory.	Peptides	10-18	serpin family C member 1	Homo sapiens	55-61
7523554-9	1994	Furthermore, this material inhibits the clotting of nonanticoagulated whole human blood (for > 16 hours at room temperature), perhaps by virtue of binding and activation of antithrombin III by the sulfonic acid residues on the surface-immobilized Cibacron blue.	Sulfonic Acids	200-213	serpin family C member 1	Homo sapiens	176-192
7523554-9	1994	Furthermore, this material inhibits the clotting of nonanticoagulated whole human blood (for > 16 hours at room temperature), perhaps by virtue of binding and activation of antithrombin III by the sulfonic acid residues on the surface-immobilized Cibacron blue.	Cibacron Blue	250-263	serpin family C member 1	Homo sapiens	176-192
7899138-3	1994	A defined pentasaccharide motif was found responsible for the enhancement of the rate of inactivation of factor Xa by antithrombin III.	pentasaccharide	10-25	serpin family C member 1	Homo sapiens	118-134
7932105-3	1994	The procedures were based on the photometric determination of the inactivation of FXa and FIIa after incubation with LMWH in the presence of antithrombin III (AT III).	Heparin, Low-Molecular-Weight	117-121	serpin family C member 1	Homo sapiens	159-165
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
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
8054362-6	1994	Intracellular forms of alpha 2-PI or ATIII synthesized by cells treated with 1 mM MdN were sensitive to endoglycosidase H (Endo H), whereas almost all the secreted forms were resistant, suggesting the presence of complex-type oligosaccharides.	N-methyldeoxynojirimycin	82-85	serpin family C member 1	Homo sapiens	37-42
8054362-6	1994	Intracellular forms of alpha 2-PI or ATIII synthesized by cells treated with 1 mM MdN were sensitive to endoglycosidase H (Endo H), whereas almost all the secreted forms were resistant, suggesting the presence of complex-type oligosaccharides.	Oligosaccharides	226-242	serpin family C member 1	Homo sapiens	37-42
8054362-7	1994	In the presence of 1 mM dMM, cells synthesized Endo H-sensitive alpha 2-PI and ATIII with similar secretion rates.	1-Deoxynojirimycin	24-27	serpin family C member 1	Homo sapiens	79-84
8054362-8	1994	These results suggest that retention of glucose on N-linked oligosaccharides not only retards the exit of alpha 2-PI and ATIII, but also changes the catabolic rate of alpha 2-PI in the endoplasmic reticulum.	Glucose	40-47	serpin family C member 1	Homo sapiens	121-126
8054362-8	1994	These results suggest that retention of glucose on N-linked oligosaccharides not only retards the exit of alpha 2-PI and ATIII, but also changes the catabolic rate of alpha 2-PI in the endoplasmic reticulum.	n-linked oligosaccharides	51-76	serpin family C member 1	Homo sapiens	121-126
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
8026575-5	1994	We have measured the stability to denaturation of one of these non-inhibitor substrate mutants, antithrombin-Hamilton, which has an Ala-->Thr change at position P12 in strand s4A.	Alanine	132-135	serpin family C member 1	Homo sapiens	96-108
8026575-5	1994	We have measured the stability to denaturation of one of these non-inhibitor substrate mutants, antithrombin-Hamilton, which has an Ala-->Thr change at position P12 in strand s4A.	Threonine	141-144	serpin family C member 1	Homo sapiens	96-108
8026575-6	1994	We find that it undergoes the transformation to the more stable form which is observed for inhibitor serpins, from which we conclude that the Ala-->Thr change in antithrombin-Hamilton does not prevent insertion of s4A into beta-sheet A in the cleaved form.	Alanine	142-145	serpin family C member 1	Homo sapiens	165-177
8026575-6	1994	We find that it undergoes the transformation to the more stable form which is observed for inhibitor serpins, from which we conclude that the Ala-->Thr change in antithrombin-Hamilton does not prevent insertion of s4A into beta-sheet A in the cleaved form.	Threonine	151-154	serpin family C member 1	Homo sapiens	165-177
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%.	pentasaccharide	92-107	serpin family C member 1	Homo sapiens	71-83
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%.	pentasaccharide	92-107	serpin family C member 1	Homo sapiens	141-153
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%.	pentasaccharide	92-107	serpin family C member 1	Homo sapiens	141-153
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.	Leucine	81-88	serpin family C member 1	Homo sapiens	200-216
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.	Tyrosine	93-101	serpin family C member 1	Homo sapiens	200-216
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.	Nitrogen	141-142	serpin family C member 1	Homo sapiens	200-216
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.	Cysteine	143-149	serpin family C member 1	Homo sapiens	200-216
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
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
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
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
7664058-0	1994	A mechanism for heparin-induced potentiation of antithrombin III.	Heparin	16-23	serpin family C member 1	Homo sapiens	48-64
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
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
8206990-10	1994	Changing the P2 residue Phe353-->Gly generated a mutant with a reactive site like antithrombin which was better at inhibiting thrombin or urokinase, but was much less active with APC or trypsin.	Glycine	36-39	serpin family C member 1	Homo sapiens	85-97
8042197-0	1994	Characterization of a highly polymorphic trinucleotide short tandem repeat within the human antithrombin gene.	trinucleotide	41-54	serpin family C member 1	Homo sapiens	92-104
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
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
7935513-0	1994	Trinucleotide repeat polymorphism within the human antithrombin gene (AT3): allele frequency data for three population groups.	trinucleotide	0-13	serpin family C member 1	Homo sapiens	51-63
7935513-0	1994	Trinucleotide repeat polymorphism within the human antithrombin gene (AT3): allele frequency data for three population groups.	trinucleotide	0-13	serpin family C member 1	Homo sapiens	70-73
7935513-1	1994	The fifth intron of the human antithrombin gene (AT3) of chromosome 1q23 contains a highly polymorphic short tandem repeat based on the trinucleotide repeat [ATT].	trinucleotide	136-149	serpin family C member 1	Homo sapiens	30-42
7935513-1	1994	The fifth intron of the human antithrombin gene (AT3) of chromosome 1q23 contains a highly polymorphic short tandem repeat based on the trinucleotide repeat [ATT].	trinucleotide	136-149	serpin family C member 1	Homo sapiens	49-52
8176841-5	1994	Incubations of cultured endothelial cells with homocysteine reduced the amount of antithrombin III bound to the cell surface in a dose- and time-dependent fashion.	Homocysteine	47-59	serpin family C member 1	Homo sapiens	82-98
8176841-7	1994	Although neither net negative charge nor proportion in total glycosaminoglycans of cell surface heparan sulfate was altered by homocysteine treatment, a substantial reduction in antithrombin III binding capacity of heparan sulfate isolated from homocysteine-treated endothelial cells was found using both affinity chromatography and dot blot assay techniques.	Heparitin Sulfate	215-230	serpin family C member 1	Homo sapiens	178-194
8176841-8	1994	The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine.	Homocysteine	94-106	serpin family C member 1	Homo sapiens	4-20
8176841-8	1994	The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine.	Cysteine	98-106	serpin family C member 1	Homo sapiens	4-20
8176841-8	1994	The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine.	Mercaptoethanol	121-138	serpin family C member 1	Homo sapiens	4-20
8176841-8	1994	The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine.	Methionine	242-252	serpin family C member 1	Homo sapiens	4-20
8176841-8	1994	The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine.	Alanine	254-261	serpin family C member 1	Homo sapiens	4-20
8052972-0	1994	Platelet deposition induced by severely damaged vessel wall is inhibited by a boroarginine synthetic peptide with antithrombin activity.	boroarginine	78-90	serpin family C member 1	Homo sapiens	114-126
8172176-0	1994	Genetic linkage studies in antithrombin-deficient kindreds using a highly polymorphic trinucleotide short tandem repeat (STR) within the human antithrombin gene.	trinucleotide	86-99	serpin family C member 1	Homo sapiens	27-39
8172176-0	1994	Genetic linkage studies in antithrombin-deficient kindreds using a highly polymorphic trinucleotide short tandem repeat (STR) within the human antithrombin gene.	trinucleotide	86-99	serpin family C member 1	Homo sapiens	143-155
7522311-8	1994	The thrombogenicity of APA may result from their interference with endothelial phospholipids required for antithrombin III and protein C and S anticoagulant activity and prostacyclin synthesis and/or increased endothelial expression of the procoagulants: tissue factor, von Willebrand factor, platelet-activating factor, and plasminogen activator inhibitor type-1.	Phospholipids	79-92	serpin family C member 1	Homo sapiens	106-122
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
8167338-2	1994	Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	158-174
8167338-2	1994	Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan.	Heparitin Sulfate	17-19	serpin family C member 1	Homo sapiens	158-174
8167338-2	1994	Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan.	Oligosaccharides	122-137	serpin family C member 1	Homo sapiens	158-174
8167338-2	1994	Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan.	Glycosaminoglycans	236-253	serpin family C member 1	Homo sapiens	158-174
8167338-6	1994	Specificity studies showed that low-affinity electrostatic interactions clearly did not account for the observed reactivity with heparin, and that APS IgG antiheparin antibodies were specifically reactive with a disaccharide present in the heparin pentasaccharide that binds antithrombin III.	IC 831423	240-263	serpin family C member 1	Homo sapiens	275-291
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
7518511-7	1994	The aggregation induced by neuroblastomas and the pheochromocytoma was also suppressed by pretreatment with an antithrombin agent, argatroban, whereas the aggregation induced by Wilms" tumors was not suppressed by this agent.	argatroban	131-141	serpin family C member 1	Homo sapiens	111-123
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
7512382-3	1994	However, although the MAb remained bound to antithrombin in the presence of heparin, it did not significantly inhibit heparin cofactor activity against thrombin, and increasing concentrations of the antithrombin-binding pentasaccharide progressively unblocked the inhibitory action of the MAb.	pentasaccharide	220-235	serpin family C member 1	Homo sapiens	199-211
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Cysteine	109-112	serpin family C member 1	Homo sapiens	37-49
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Serine	126-129	serpin family C member 1	Homo sapiens	37-49
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Leucine	143-146	serpin family C member 1	Homo sapiens	37-49
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Threonine	160-163	serpin family C member 1	Homo sapiens	37-49
7512382-7	1994	However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B.	Threonine	177-180	serpin family C member 1	Homo sapiens	37-49
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
8003980-2	1994	ATIII attains its full biological activity only upon binding polysulfated oligosaccharides, such as heparin.	polysulfated oligosaccharides	61-90	serpin family C member 1	Homo sapiens	0-5
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
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
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.	Serine	117-123	serpin family C member 1	Homo sapiens	26-38
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
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
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.	Polymers	325-332	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
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.	Sepharose	30-37	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
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
8313964-6	1994	Hydrophobic (Val) or negatively charged (Asp or Glu) substitutions were particularly disruptive, in that these variants exhibited less than 10% wild-type antithrombin or antitrypsin activity.	Aspartic Acid	41-44	serpin family C member 1	Homo sapiens	154-166
8313964-6	1994	Hydrophobic (Val) or negatively charged (Asp or Glu) substitutions were particularly disruptive, in that these variants exhibited less than 10% wild-type antithrombin or antitrypsin activity.	Glutamic Acid	48-51	serpin family C member 1	Homo sapiens	154-166
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
8288594-0	1994	Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III.	Amino Acids, Basic	18-34	serpin family C member 1	Homo sapiens	104-120
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
8180343-4	1994	Heparin binding to antithrombin is mediated by a well-defined unique heparin pentasaccharide sequence.	pentasaccharide	77-92	serpin family C member 1	Homo sapiens	19-31
8180343-5	1994	Interaction between this pentasaccharide sequence and antithrombin induces a conformational change in antithrombin, an alteration that appears to be sufficient to explain the enhanced ability of antithrombin to inhibit factor Xa and related serine proteases, but not thrombin.	pentasaccharide	25-40	serpin family C member 1	Homo sapiens	54-66
8180343-5	1994	Interaction between this pentasaccharide sequence and antithrombin induces a conformational change in antithrombin, an alteration that appears to be sufficient to explain the enhanced ability of antithrombin to inhibit factor Xa and related serine proteases, but not thrombin.	pentasaccharide	25-40	serpin family C member 1	Homo sapiens	102-114
8180343-5	1994	Interaction between this pentasaccharide sequence and antithrombin induces a conformational change in antithrombin, an alteration that appears to be sufficient to explain the enhanced ability of antithrombin to inhibit factor Xa and related serine proteases, but not thrombin.	pentasaccharide	25-40	serpin family C member 1	Homo sapiens	102-114
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
8180343-6	1994	Heparin species with longer polysaccharide chains appear to be required in order to enhance the inhibition of thrombin by antithrombin.	Polysaccharides	28-42	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
8299226-17	1994	SLE IgG anti-HS antibodies recognize a sulfated uronic acid epitope containing 2-O-sulfate which is important in certain functions of HS, including antithrombin III binding.	Uronic Acids	48-59	serpin family C member 1	Homo sapiens	148-164
8299226-17	1994	SLE IgG anti-HS antibodies recognize a sulfated uronic acid epitope containing 2-O-sulfate which is important in certain functions of HS, including antithrombin III binding.	2-o-sulfate	79-90	serpin family C member 1	Homo sapiens	148-164
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
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
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.	Lysine	50-53	serpin family C member 1	Homo sapiens	220-232
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
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
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.	Arginine	0-3	serpin family C member 1	Homo sapiens	53-65
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.	pentasaccharide	120-135	serpin family C member 1	Homo sapiens	53-65
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
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
8186357-2	1994	In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans.	Glycosaminoglycans	111-129	serpin family C member 1	Homo sapiens	40-52
8186357-5	1994	This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule.	Esters	40-45	serpin family C member 1	Homo sapiens	153-165
8186357-5	1994	This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule.	Serine	78-84	serpin family C member 1	Homo sapiens	153-165
8186357-5	1994	This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule.	Arginine	117-125	serpin family C member 1	Homo sapiens	153-165
7951256-0	1994	(ATT) trinucleotide repeats in the antithrombin gene and their use in determining the origin of repeated mutations.	trinucleotide	6-19	serpin family C member 1	Homo sapiens	35-47
7951256-1	1994	Two (ATT) trinucleotide repeat polymorphisms have been identified in the tails of Alu repeat elements in intron 5 of the antithrombin gene.	trinucleotide	10-23	serpin family C member 1	Homo sapiens	121-133
8028997-3	1994	The anticoagulant effect is particularly dependent upon the presence of a specific pentasaccharide sequence, which binds to the proteinase inhibitor, antithrombin.	pentasaccharide	83-98	serpin family C member 1	Homo sapiens	150-162
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
7947469-4	1994	This high-ATIII affinity fraction was immobilized onto a styrene/p-amino styrene random copolymer surface using hydrophilic poly(ethylene oxide) (PEO) spacer groups.	Styrene	57-64	serpin family C member 1	Homo sapiens	10-15
7947469-4	1994	This high-ATIII affinity fraction was immobilized onto a styrene/p-amino styrene random copolymer surface using hydrophilic poly(ethylene oxide) (PEO) spacer groups.	p-amino styrene random copolymer	65-97	serpin family C member 1	Homo sapiens	10-15
7947469-4	1994	This high-ATIII affinity fraction was immobilized onto a styrene/p-amino styrene random copolymer surface using hydrophilic poly(ethylene oxide) (PEO) spacer groups.	Polyethylene Glycols	124-144	serpin family C member 1	Homo sapiens	10-15
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
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
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, Low-Molecular-Weight	135-139	serpin family C member 1	Homo sapiens	79-91
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
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
8263926-1	1993	Human antithrombin has been crystallized by microdialysis at pH 6.7 using 18% (w/v) polyethylene glycol-4000 as precipitant.	polyethylene glycol 4000	84-108	serpin family C member 1	Homo sapiens	6-18
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 < 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
8165617-6	1993	Clexane (M(r) = 4,500) also bound antithrombin III, but both histidine-rich glycoprotein and vitronectin were quantitatively significant neutralising proteins.	Enoxaparin	0-7	serpin family C member 1	Homo sapiens	34-50
8148487-6	1993	We conclude that long-term treatment with tamoxifen for 2 or more years tends to reduce both AT-III and PC, a situation possibly predisposing towards thrombosis.	Tamoxifen	42-51	serpin family C member 1	Homo sapiens	93-99
8241508-6	1993	This was confirmed in a heparin cofactor II-dependent antithrombin assay for DS that showed anticoagulant equivalent to 2.2 +/- 0.3 micrograms/mL (mean +/- SD) of porcine mucosal DS.	Dermatan Sulfate	77-79	serpin family C member 1	Homo sapiens	54-66
8137606-3	1993	All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin.	Heparin, Low-Molecular-Weight	4-16	serpin family C member 1	Homo sapiens	29-45
8137606-3	1993	All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin.	pentasaccharide	55-70	serpin family C member 1	Homo sapiens	29-45
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
8175200-3	1993	Binding of antibodies against factor XII, antithrombin III (ATIII) and platelet receptor GpIb were significantly higher (p < 0.01) on the Duraflo II treated surface.	duraflo ii	141-151	serpin family C member 1	Homo sapiens	42-58
8175200-3	1993	Binding of antibodies against factor XII, antithrombin III (ATIII) and platelet receptor GpIb were significantly higher (p < 0.01) on the Duraflo II treated surface.	duraflo ii	141-151	serpin family C member 1	Homo sapiens	60-65
8243674-0	1993	Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinities.	Carbohydrates	0-12	serpin family C member 1	Homo sapiens	25-37
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
8243674-1	1993	We have changed one of the carbohydrate-bearing asparagine residues of human antithrombin to glutamine by site-directed mutagenesis and expressed the variant antithrombin, N135Q, in baby hamster kidney cells.	Carbohydrates	27-39	serpin family C member 1	Homo sapiens	77-89
8243674-1	1993	We have changed one of the carbohydrate-bearing asparagine residues of human antithrombin to glutamine by site-directed mutagenesis and expressed the variant antithrombin, N135Q, in baby hamster kidney cells.	Asparagine	48-58	serpin family C member 1	Homo sapiens	77-89
7693706-3	1993	Vitronectin complexed to thrombin-antithrombin or C5b-9 is conformationally altered as evidenced by enhanced reactivity with monoclonal antibody 8E6 and binding to heparin; these same alterations also occur when vitronectin is treated with urea (Tomasini, B. R., and Mosher, D.F.	Urea	240-244	serpin family C member 1	Homo sapiens	34-46
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
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
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.	Sodium Dodecyl Sulfate	31-34	serpin family C member 1	Homo sapiens	212-224
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.	Iodine-125	62-66	serpin family C member 1	Homo sapiens	212-224
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
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.	Glycosaminoglycans	165-183	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
8016817-3	1994	Furthermore, the assay was modified by supplementation with either purified antithrombin III or factor V. The synthetic peptide Ac-(D)Phe-Pro-boroArg-OH (DuP 714) was shown to be the most effective inhibitor of thrombin and also had strong inhibitor actions against factor Xa generation.	acetylphenylalanyl-prolyl-boroarginine	128-152	serpin family C member 1	Homo sapiens	76-92
8016817-3	1994	Furthermore, the assay was modified by supplementation with either purified antithrombin III or factor V. The synthetic peptide Ac-(D)Phe-Pro-boroArg-OH (DuP 714) was shown to be the most effective inhibitor of thrombin and also had strong inhibitor actions against factor Xa generation.	acetylphenylalanyl-prolyl-boroarginine	154-161	serpin family C member 1	Homo sapiens	76-92
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
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
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
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
8218292-6	1993	In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen.	IC 831423	49-72	serpin family C member 1	Homo sapiens	90-102
8218292-6	1993	In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen.	IC 831423	49-72	serpin family C member 1	Homo sapiens	136-148
8218292-6	1993	In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen.	pentasaccharide	57-72	serpin family C member 1	Homo sapiens	90-102
8218292-6	1993	In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen.	pentasaccharide	57-72	serpin family C member 1	Homo sapiens	136-148
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
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
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
8227367-7	1993	When the second-order rate constant of PN-2/A beta PP"s inhibition of Factor IXa (2.7 x 10(8) M-1min-1) was compared to that of antithrombin III (3.8 x 10(6) M-1min-1), PN-2/A beta PP was at least a 71-fold more potent inhibitor of Factor IXa than antithrombin III.	beta pp	46-53	serpin family C member 1	Homo sapiens	248-264
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
8309935-2	1993	A general procedure for arriving at 3-D models of disulphide-rich polypeptide systems based on the covalent cross-link constraints has been developed.	disulphide	50-60	serpin family C member 1	Homo sapiens	33-39
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.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	90-102
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.	ps	21-23	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.	ps	21-23	serpin family C member 1	Homo sapiens	108-113
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.	ps	21-23	serpin family C member 1	Homo sapiens	90-102
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
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
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.	Sulfur-35	131-134	serpin family C member 1	Homo sapiens	16-28
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.	Methionine	135-145	serpin family C member 1	Homo sapiens	16-28
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
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.	Sepharose	174-181	serpin family C member 1	Homo sapiens	16-28
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 < 0.03) following heparin initiation with no further significant subsequent decrease.	Heparin	115-122	serpin family C member 1	Homo sapiens	7-23
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
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
8376590-3	1993	Incubations of porcine aortic endothelial cell cultures with homocysteine reduced the amount of antithrombin III bound to the cell surface in a dose- and time-dependent fashion.	Homocysteine	61-73	serpin family C member 1	Homo sapiens	96-112
8376590-4	1993	The inhibitory effect was observed at a homocysteine concentration as low as 0.1 mM, and the maximal suppression occurred at 1 mM of homocysteine after 24 h. In contrast with a marked reduction in the maximal antithrombin III binding capacity (approximately 30% of control), the radioactivity of [35S]sulfate incorporated into heparan sulfate on the cell surface was minimally (< 15%) reduced.	Homocysteine	133-145	serpin family C member 1	Homo sapiens	209-225
8376590-6	1993	Although neither net negative charge nor proportion in total glycosaminoglycans of cell surface heparan sulfate was altered by homocysteine treatment, a substantial reduction in antithrombin III binding capacity of heparan sulfate isolated from homocysteine-treated endothelial cells was found using both affinity chromatography and dot blot assay techniques.	Heparitin Sulfate	215-230	serpin family C member 1	Homo sapiens	178-194
8376590-7	1993	The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine.	Cysteine	103-111	serpin family C member 1	Homo sapiens	4-20
8376590-7	1993	The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine.	Mercaptoethanol	126-143	serpin family C member 1	Homo sapiens	4-20
8376590-7	1993	The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine.	Methionine	242-252	serpin family C member 1	Homo sapiens	4-20
8376590-7	1993	The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine.	Alanine	254-261	serpin family C member 1	Homo sapiens	4-20
8376590-7	1993	The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine.	Valine	266-272	serpin family C member 1	Homo sapiens	4-20
8350363-4	1993	Tamoxifen may also influence risk factors for cardiac and thromboembolic disease (e.g., serum cholesterol and antithrombin III).	Tamoxifen	0-9	serpin family C member 1	Homo sapiens	110-126
8259546-6	1993	DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation.	Heparin, Low-Molecular-Weight	101-105	serpin family C member 1	Homo sapiens	115-120
8259546-7	1993	Compared to plasma containing DS alone, the formation of ATIII-IIa complexes also is increased when the combination of DS and LMWH is added.	Dermatan Sulfate	119-121	serpin family C member 1	Homo sapiens	57-62
8259546-7	1993	Compared to plasma containing DS alone, the formation of ATIII-IIa complexes also is increased when the combination of DS and LMWH is added.	Heparin, Low-Molecular-Weight	126-130	serpin family C member 1	Homo sapiens	57-62
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
8357789-3	1993	To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide.	Cysteine	169-177	serpin family C member 1	Homo sapiens	136-148
8357789-3	1993	To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide.	2-Nitrobenzofuran	183-198	serpin family C member 1	Homo sapiens	136-148
8357789-3	1993	To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide.	Oligosaccharides	310-325	serpin family C member 1	Homo sapiens	136-148
8357789-5	1993	We found (i) that binding to antithrombin of all these oligosaccharides resulted in transmission of conformational change to P1 in the reactive center, (ii) that these oligosaccharides all gave enhancements of the rate of inhibition of factor Xa beyond any contribution from surface approximation, and (iii) that the degree of perturbation of P1 correlated with the enhancement of the rate of factor Xa inhibition that was not due to surface approximation.	Oligosaccharides	55-71	serpin family C member 1	Homo sapiens	29-41
8357789-5	1993	We found (i) that binding to antithrombin of all these oligosaccharides resulted in transmission of conformational change to P1 in the reactive center, (ii) that these oligosaccharides all gave enhancements of the rate of inhibition of factor Xa beyond any contribution from surface approximation, and (iii) that the degree of perturbation of P1 correlated with the enhancement of the rate of factor Xa inhibition that was not due to surface approximation.	Oligosaccharides	168-184	serpin family C member 1	Homo sapiens	29-41
8115989-0	1993	Antithrombotic effects of synthetic pentasaccharide with high affinity for plasma antithrombin III in non-human primates.	pentasaccharide	36-51	serpin family C member 1	Homo sapiens	82-98
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.	pentasaccharide	4-19	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.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	108-113
8238864-5	1993	A hexasaccharide having a 3-O-sulfated glucosamine residue at the reducing end and arising from heparin"s antithrombin III binding site, migrated in an unusual fashion.	hexasaccharide	2-16	serpin family C member 1	Homo sapiens	106-122
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
8343518-2	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
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.	pentasaccharide	125-140	serpin family C member 1	Homo sapiens	141-147
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.	pentasaccharide	125-140	serpin family C member 1	Homo sapiens	141-147
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.	pentasaccharide	125-140	serpin family C member 1	Homo sapiens	141-147
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
7687144-1	1993	Identical or highly similar antigenic determinants, not present in the intact inhibitor, were induced in antithrombin on cleavage of the reactive bond, on formation of a complex between antithrombin and a synthetic reactive-loop tetradecapeptide, and on partial denaturation of antithrombin at low concentrations of guanidinium chloride.	Guanidine	316-336	serpin family C member 1	Homo sapiens	105-117
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.	pentasaccharide	15-30	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	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.	Arginine	137-145	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
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
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
8331144-6	1993	The ATIII binding capacities of the membranes were found to be 91 micrograms/cm2 for the amine-modified and 39 micrograms/cm2 for the epoxy-activated membrane, achieving purities of 75%.	Amines	89-94	serpin family C member 1	Homo sapiens	4-9
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.	Polysaccharides	16-31	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.	Polysaccharides	16-31	serpin family C member 1	Homo sapiens	143-148
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.	Dermatan Sulfate	33-50	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.	Dermatan Sulfate	33-50	serpin family C member 1	Homo sapiens	143-148
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.	fucan	52-57	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.	fucan	52-57	serpin family C member 1	Homo sapiens	143-148
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
8335699-5	1993	The possible presence of a unique binding site for ATIII and HCII, on each sulphated polysaccharide, was also studied.	Polysaccharides	85-99	serpin family C member 1	Homo sapiens	51-56
8392392-4	1993	Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser).	Arginine	156-159	serpin family C member 1	Homo sapiens	111-123
8392392-4	1993	Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser).	Serine	160-163	serpin family C member 1	Homo sapiens	111-123
8392392-4	1993	Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser).	Leucine	200-203	serpin family C member 1	Homo sapiens	111-123
8392392-4	1993	Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser).	Serine	204-207	serpin family C member 1	Homo sapiens	111-123
8392392-6	1993	The therapeutic anticoagulant action of the glycosaminoglycan heparin is believed to depend partially on heparin-accelerated inhibition of proteinases by antithrombin.	glycosaminoglycan heparin	44-69	serpin family C member 1	Homo sapiens	154-166
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).	Oligosaccharides	159-174	serpin family C member 1	Homo sapiens	93-105
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).	Oligosaccharides	0-16	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).	Oligosaccharides	0-16	serpin family C member 1	Homo sapiens	69-74
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
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).	Polyethylene	144-168	serpin family C member 1	Homo sapiens	69-74
8408111-6	1993	Visual confirmation of ATIII binding to immobilized HA-heparin was demonstrated by a gold-labeled double antibody method with imaging by SEM.	ha-heparin	52-62	serpin family C member 1	Homo sapiens	23-28
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.	Glycosaminoglycans	50-68	serpin family C member 1	Homo sapiens	100-105
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
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
8518817-0	1993	Trinucleotide repeat polymorphism in the human antithrombin III (AT3) gene.	trinucleotide	0-13	serpin family C member 1	Homo sapiens	47-63
8518817-0	1993	Trinucleotide repeat polymorphism in the human antithrombin III (AT3) gene.	trinucleotide	0-13	serpin family C member 1	Homo sapiens	65-68
8473344-4	1993	In fact, point mutation of the P1" site from Ser (present in AT-III) to Ile (present in prothrombin) is sufficient to dissociate heparin-dependent thrombin and Factor Xa inhibitory activities.	Serine	45-48	serpin family C member 1	Homo sapiens	61-67
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
8473344-4	1993	In fact, point mutation of the P1" site from Ser (present in AT-III) to Ile (present in prothrombin) is sufficient to dissociate heparin-dependent thrombin and Factor Xa inhibitory activities.	Isoleucine	72-75	serpin family C member 1	Homo sapiens	61-67
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
8491059-12	1993	A highly significant correlation (p < 0.001) was found between phenazone clearance and the prothrombin time, albumin, gamma-globulin, factor V, antithrombin III, fibrinogen and total bilirubin.	Antipyrine	66-75	serpin family C member 1	Homo sapiens	147-163
8463348-9	1993	Albumin, IgG, and antithrombin III were mainly present in the cuprophane eluates.	cuprammonium cellulose	62-72	serpin family C member 1	Homo sapiens	18-34
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.	Sepharose	108-117	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
8443391-8	1993	Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion.	Thymine	137-144	serpin family C member 1	Homo sapiens	52-58
8443391-8	1993	Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion.	Thymine	137-144	serpin family C member 1	Homo sapiens	187-193
8443391-8	1993	Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion.	Cytosine	148-156	serpin family C member 1	Homo sapiens	52-58
8443391-8	1993	Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion.	Cytosine	148-156	serpin family C member 1	Homo sapiens	187-193
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.	Chondroitin Sulfates	4-23	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	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	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
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
8429008-1	1993	Heparin cofactor II and antithrombin are plasma serine proteinase inhibitors whose ability to inhibit alpha-thrombin is accelerated by glycosaminoglycans.	Glycosaminoglycans	135-153	serpin family C member 1	Homo sapiens	24-36
8429008-8	1993	A three-dimensional molecular model of the Quick II active site compared to alpha-thrombin suggested that the heparin cofactor II Leu-Ser-reactive site sequence (P1-P1") is a compatible "pseudosubstrate" in contrast to the Arg-Ser sequence found in antithrombin.	Leucine	130-133	serpin family C member 1	Homo sapiens	249-261
8429040-3	1993	Thrombin is inhibited by the serpins antithrombin III and heparin cofactor II in a reaction that is dramatically accelerated by glycosaminoglycans.	Glycosaminoglycans	128-146	serpin family C member 1	Homo sapiens	37-53
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
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
8456425-0	1993	The effect of antithrombin III-independent thrombin inhibitors and heparin on fibrin accretion onto fibrin-coated polyethylene.	Polyethylene	114-126	serpin family C member 1	Homo sapiens	14-30
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
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.	pentasaccharide	154-169	serpin family C member 1	Homo sapiens	140-145
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.	pentasaccharide	81-96	serpin family C member 1	Homo sapiens	57-62
8456425-8	1993	These studies show that the antithrombin III-independent inhibitors, r-hirudin and PPACK, are more effective inhibitors of fibrin accretion onto fibrin-coated polyethylene than heparin or Hirulog-1.	fibrin-coated polyethylene	145-171	serpin family C member 1	Homo sapiens	28-44
7678252-3	1993	Incorporation of radiolabeled ATIII was detected using polyacrylamide gel electrophoresis (PAGE) and autoradiography.	polyacrylamide	55-69	serpin family C member 1	Homo sapiens	30-35
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
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
8419351-6	1993	A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	133-155	serpin family C member 1	Homo sapiens	44-69
8419351-6	1993	A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	156-170	serpin family C member 1	Homo sapiens	44-69
8421307-1	1993	Human antithrombin III has been crystallized from 18 to 21% (w/v) polyethylene glycol 4000 at pH 7.15.	Polyethylene Glycols	66-85	serpin family C member 1	Homo sapiens	6-22
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
8121125-7	1993	A decrease in antithrombin III observed in heparin group (from 115 +/- 3.2% to 98 +/- 3.4%, p < 0.001) reflected specific action of the drug.	Heparin	43-50	serpin family C member 1	Homo sapiens	14-30
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
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
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
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
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.	pentasaccharide	79-94	serpin family C member 1	Homo sapiens	167-173
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.	lactobionic acid	99-115	serpin family C member 1	Homo sapiens	167-173
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
1366018-2	1992	Studies of the complexing of antithrombin and its variants with heparin fractions and with reactive center loop peptides including intermolecular loop-sheet polymers all support a 3-fold mechanism for the heparin activation of antithrombin.	Polymers	157-165	serpin family C member 1	Homo sapiens	29-41
1366018-2	1992	Studies of the complexing of antithrombin and its variants with heparin fractions and with reactive center loop peptides including intermolecular loop-sheet polymers all support a 3-fold mechanism for the heparin activation of antithrombin.	Polymers	157-165	serpin family C member 1	Homo sapiens	227-239
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
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
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
1331047-6	1992	The two peptides, particularly IIFMGRVANP, directly enhanced the amidolytic activity of thrombin and Factor Xa on the synthetic substrate Boc-Ala-Gly-Arg-MCA (where Boc is t-butoxycarbonyl and MCA is 4-methylcoumarin), which corresponds to residues P3-P1 of the reactive site of antithrombin III, and also on other substrates due to increased Vmax.	(S)-2-(2-((tert-Butoxycarbonyl)amino)propanamido)acetic acid	138-149	serpin family C member 1	Homo sapiens	279-295
1331047-6	1992	The two peptides, particularly IIFMGRVANP, directly enhanced the amidolytic activity of thrombin and Factor Xa on the synthetic substrate Boc-Ala-Gly-Arg-MCA (where Boc is t-butoxycarbonyl and MCA is 4-methylcoumarin), which corresponds to residues P3-P1 of the reactive site of antithrombin III, and also on other substrates due to increased Vmax.	Arginine	150-153	serpin family C member 1	Homo sapiens	279-295
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
1442974-8	1992	There was a significant increase in antithrombin III activity with norethindrone plus ethinyl estradiol at 12 months.	Norethindrone	67-80	serpin family C member 1	Homo sapiens	36-52
1442974-8	1992	There was a significant increase in antithrombin III activity with norethindrone plus ethinyl estradiol at 12 months.	Ethinyl Estradiol	86-103	serpin family C member 1	Homo sapiens	36-52
1333106-4	1992	High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS.	Dermatan Sulfate	14-30	serpin family C member 1	Homo sapiens	50-62
1333106-4	1992	High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS.	Dermatan Sulfate	32-34	serpin family C member 1	Homo sapiens	50-62
1492385-3	1992	The ester, similarly to heparin, inhibited blood coagulation mainly via accelerated thrombin inactivation by means of blood plasma antithrombin III.	Esters	4-9	serpin family C member 1	Homo sapiens	131-147
1326550-0	1992	Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. Structural link between the autolysis loop and the Tyr-Pro-Pro-Trp insertion of thrombin.	des-etw	24-31	serpin family C member 1	Homo sapiens	37-53
1326550-3	1992	Whereas des-ETW resists antithrombin III inactivation with a rate constant (Kon) approximately 350-fold slower than for thrombin, des-ETW is remarkably sensitive to the Kunitz inhibitors, with inhibition constants (Ki) decreased from 2.6 microM to 34 nM for the soybean trypsin inhibitor and from 52 microM to 1.8 microM for the bovine pancreatic trypsin inhibitor.	des-etw	8-15	serpin family C member 1	Homo sapiens	24-40
1390700-6	1992	An analog with an 18-membered lactam ring showed higher antithrombin activity (IC50 = 0.57 microM) than the corresponding analogs with 17- or 16-membered rings and was 2-fold more potent than its linear counterpart.	Lactams	30-36	serpin family C member 1	Homo sapiens	56-68
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
1390919-5	1992	The 3-fold lower binding enthalpy in Tris can be attributed to the transfer of a proton from the buffer to the heparin-ATIII complex.	Tromethamine	37-41	serpin family C member 1	Homo sapiens	119-124
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
1433937-1	1992	A pregnant woman with congenital antithrombin III (AT III) deficiency was given AT III concentrate and warfarin at the first and after 36th week of gestation periods and at the other gestation period, respectively.	Warfarin	103-111	serpin family C member 1	Homo sapiens	33-49
1433937-1	1992	A pregnant woman with congenital antithrombin III (AT III) deficiency was given AT III concentrate and warfarin at the first and after 36th week of gestation periods and at the other gestation period, respectively.	Warfarin	103-111	serpin family C member 1	Homo sapiens	51-57
1440655-6	1992	In SDS-PAGE inactivation of human antithrombin III was correlated with the occurrence of two cleavage products.	Sodium Dodecyl Sulfate	3-6	serpin family C member 1	Homo sapiens	34-50
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
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.	Sepharose	105-112	serpin family C member 1	Homo sapiens	13-29
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.	Sodium Chloride	87-91	serpin family C member 1	Homo sapiens	13-29
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
1440521-1	1992	Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively.	Pyruvaldehyde	191-204	serpin family C member 1	Homo sapiens	116-132
1412223-7	1992	These findings, together with our previous report upon tryptophan modification of antithrombin III [1] suggest that the nature of the molecule is such that considerable care must be taken in interpretation of results when investigating the structure/function relationships of this protein by chemical modification.	Tryptophan	55-65	serpin family C member 1	Homo sapiens	82-98
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
1418069-12	1992	Therefore, the anticoagulant activity of the synthesized laminarin sulfates is due to the interaction at an early stage of the coagulation cascade and neither to a direct inhibition of Factor Xa and IIa nor to an indirect effect mediated by antithrombin III.	laminarin sulfate	57-75	serpin family C member 1	Homo sapiens	241-257
1418078-0	1992	Fibrinogen and antithrombin III blood levels fluctuations during isoniazid or isoniazid plus rifampicin administration.	Isoniazid	65-74	serpin family C member 1	Homo sapiens	15-31
1418078-0	1992	Fibrinogen and antithrombin III blood levels fluctuations during isoniazid or isoniazid plus rifampicin administration.	Isoniazid	78-87	serpin family C member 1	Homo sapiens	15-31
1418078-0	1992	Fibrinogen and antithrombin III blood levels fluctuations during isoniazid or isoniazid plus rifampicin administration.	Rifampin	93-103	serpin family C member 1	Homo sapiens	15-31
1440521-1	1992	Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively.	sodium carbonate	61-77	serpin family C member 1	Homo sapiens	116-132
1440521-1	1992	Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively.	Sodium Chloride	95-99	serpin family C member 1	Homo sapiens	116-132
1440521-1	1992	Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively.	Pyruvaldehyde	191-204	serpin family C member 1	Homo sapiens	134-140
1447499-5	1992	If AT-III levels were above 0.30 U/ml, SF levels remained low, whereas SF levels were increased in patients with AT-III levels below 0.30 U/ml.	sf	39-41	serpin family C member 1	Homo sapiens	3-9
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
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
1447499-5	1992	If AT-III levels were above 0.30 U/ml, SF levels remained low, whereas SF levels were increased in patients with AT-III levels below 0.30 U/ml.	sf	71-73	serpin family C member 1	Homo sapiens	113-119
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.	Sepharose	170-179	serpin family C member 1	Homo sapiens	142-158
1618758-0	1992	Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions.	pentasaccharide	33-48	serpin family C member 1	Homo sapiens	12-24
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.	IC 831423	35-58	serpin family C member 1	Homo sapiens	14-26
1618758-0	1992	Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions.	pentasaccharide	33-48	serpin family C member 1	Homo sapiens	76-88
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
1618758-1	1992	Resolution of the antithrombin conformational change contribution to heparin rate enhancement.	Heparin	69-76	serpin family C member 1	Homo sapiens	18-30
1618758-3	1992	The aim of these studies was to elucidate the pentasaccharide contribution to heparin"s accelerating effect on antithrombin-proteinase reactions.	pentasaccharide	46-61	serpin family C member 1	Homo sapiens	111-123
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
1618758-4	1992	Pentasaccharide and full-length heparins bound antithrombin with comparable high affinities (KD values of 36 +/- 11 and 10 +/- 3 nM, respectively, at I 0.15) and induced highly similar protein fluorescence, ultraviolet and circular dichroism changes in the inhibitor.	pentasaccharide	0-15	serpin family C member 1	Homo sapiens	47-59
1618758-6	1992	Second order rate constants for antithrombin reactions with thrombin and factor Xa were maximally enhanced by the pentasaccharide only 1.7-fold for thrombin, but a substantial 270-fold for factor Xa, in an ionic strength-independent manner at saturating oligosaccharide.	pentasaccharide	114-129	serpin family C member 1	Homo sapiens	32-44
1618758-6	1992	Second order rate constants for antithrombin reactions with thrombin and factor Xa were maximally enhanced by the pentasaccharide only 1.7-fold for thrombin, but a substantial 270-fold for factor Xa, in an ionic strength-independent manner at saturating oligosaccharide.	Oligosaccharides	254-269	serpin family C member 1	Homo sapiens	32-44
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
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
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
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.	Calcium	0-7	serpin family C member 1	Homo sapiens	115-120
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
1394292-5	1992	The heparin cofactor II-mediated antithrombin activity of the oversulfated fucans also increased significantly with increase in sulfate content.	Sulfates	66-73	serpin family C member 1	Homo sapiens	33-45
1394292-7	1992	However, the increment of the anticoagulant and the antithrombin effects gradually decreased with increase in the sulfate content of the fucans.	Sulfates	114-121	serpin family C member 1	Homo sapiens	52-64
1394292-7	1992	However, the increment of the anticoagulant and the antithrombin effects gradually decreased with increase in the sulfate content of the fucans.	fucans	137-143	serpin family C member 1	Homo sapiens	52-64
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
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
1315739-6	1992	In assays with heparin oligosaccharides of known size, only the antithrombin-thrombin reaction exhibited a sharp threshold for rate enhancement at 14-16 saccharide units.	heparin oligosaccharides	15-39	serpin family C member 1	Homo sapiens	64-76
1569192-4	1992	A G to T transition at nucleotide 10038 results in the substitution of Met to an Arg, converting alpha 1-AT into an Arg-Ser protease inhibitor (serpin) that inhibited thrombin and Factor Xa more effectively than antithrombin III.	Arginine	81-84	serpin family C member 1	Homo sapiens	212-228
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
1505142-6	1992	In order to accomplish this a total of 18 to 22 monosaccharide units is necessary including a specific pentasaccharide binding site for antithrombin III.	Monosaccharides	48-62	serpin family C member 1	Homo sapiens	136-152
1505142-6	1992	In order to accomplish this a total of 18 to 22 monosaccharide units is necessary including a specific pentasaccharide binding site for antithrombin III.	pentasaccharide	103-118	serpin family C member 1	Homo sapiens	136-152
1519214-6	1992	These findings suggest that untreated antithrombin III deficient subjects generate more thrombin than their non-deficient family members and that warfarin inhibits this thrombin formation.	Warfarin	146-154	serpin family C member 1	Homo sapiens	38-54
1519763-0	1992	Enzyme-linked immunosorbent assay for proteolytically inactivated antithrombin-III: use of sodium dodecyl sulfate to eliminate signal due to intact antithrombin-III.	Sodium Dodecyl Sulfate	91-113	serpin family C member 1	Homo sapiens	66-82
1519763-4	1992	Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III.	Sodium Dodecyl Sulfate	6-28	serpin family C member 1	Homo sapiens	133-139
1519763-4	1992	Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III.	Sodium Dodecyl Sulfate	30-33	serpin family C member 1	Homo sapiens	133-139
1519763-4	1992	Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III.	Sodium Dodecyl Sulfate	30-33	serpin family C member 1	Homo sapiens	166-172
1519763-5	1992	It seems likely that the SDS alters the intact AT-III so that it is not detected in the ELISA.	Sodium Dodecyl Sulfate	25-28	serpin family C member 1	Homo sapiens	47-53
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
1566349-1	1992	This is the first study of the antithrombin III-heparan sulfate natural anticoagulant pathway in human kidneys.	Heparitin Sulfate	48-63	serpin family C member 1	Homo sapiens	31-47
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
1554734-7	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 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 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
1566349-3	1992	Enzymatic studies were done to show that the antithrombin III was anchored to endothelium by molecules of heparan sulfate.	Heparitin Sulfate	106-121	serpin family C member 1	Homo sapiens	45-61
1566349-4	1992	Displacement studies were done with glycosaminoglycans to show that the antithrombin III was bound to its glycosaminoglycan anchor via a heparinlike binding site, and replacement studies showed that antithrombin III could be returned to the same endothelial cells from which it was displaced.	Glycosaminoglycans	36-54	serpin family C member 1	Homo sapiens	72-88
1566349-4	1992	Displacement studies were done with glycosaminoglycans to show that the antithrombin III was bound to its glycosaminoglycan anchor via a heparinlike binding site, and replacement studies showed that antithrombin III could be returned to the same endothelial cells from which it was displaced.	Glycosaminoglycans	36-53	serpin family C member 1	Homo sapiens	72-88
1566349-5	1992	Immunocytochemical studies of biopsies showed that normally functioning renal allografts manifested the endothelial antithrombin III-heparan sulfate anticoagulant pathway.	Heparitin Sulfate	133-148	serpin family C member 1	Homo sapiens	116-132
1566349-7	1992	It is concluded that compromise of the antithrombin III-heparan sulfate natural anticoagulant pathway results in compromised renal function in transplanted kidneys.	Heparitin Sulfate	56-71	serpin family C member 1	Homo sapiens	39-55
1547341-0	1992	Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity.	Glycine	41-44	serpin family C member 1	Homo sapiens	0-16
1547341-0	1992	Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity.	Aspartic Acid	48-51	serpin family C member 1	Homo sapiens	0-16
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
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
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
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
1731639-6	1992	Depolymerization products with 20 or more sugar units retain significant anticoagulant potencies as measured by their effect in accelerating the neutralization of factor Xa by antithrombin.	Sugars	42-47	serpin family C member 1	Homo sapiens	176-188
1311598-0	1992	1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments.	Hydrogen	0-2	serpin family C member 1	Homo sapiens	70-86
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
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.	Hydrogen	21-23	serpin family C member 1	Homo sapiens	58-70
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
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.	pentasaccharide	248-263	serpin family C member 1	Homo sapiens	58-70
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
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
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.	hexasaccharide-2	32-48	serpin family C member 1	Homo sapiens	136-148
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.	octasaccharide-2	50-66	serpin family C member 1	Homo sapiens	136-148
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.	octasaccharide-1	72-88	serpin family C member 1	Homo sapiens	136-148
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.	Hydrogen	149-151	serpin family C member 1	Homo sapiens	136-148
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
1542853-7	1992	Fibrinogen concentration and antithrombin-III level were lowest in the CS group but were not decreased critically during the entire investigation period.	Cesium	71-73	serpin family C member 1	Homo sapiens	29-45
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
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
1321995-7	1992	Diisopropyl fluorophosphate-treated thrombin inhibited the binding between AT III and FR-860, but not that between AT III and UF-heparin.	Isoflurophate	0-27	serpin family C member 1	Homo sapiens	75-81
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
1546950-3	1992	70% of cell-free-derived normal AT-III-(1-432)-polypeptide as a peak between 0.2 M- and 0.7 M-NaCl.	Sodium Chloride	94-98	serpin family C member 1	Homo sapiens	32-38
1546950-11	1992	The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained.	disulphide	21-31	serpin family C member 1	Homo sapiens	68-74
1546950-11	1992	The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained.	Cysteine	45-48	serpin family C member 1	Homo sapiens	68-74
1546950-11	1992	The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained.	Cysteine	57-60	serpin family C member 1	Homo sapiens	68-74
1546950-12	1992	Mutations in full-length AT-III at Cys-430 had no effect on the ability of AT-III to bind heparin.	Cysteine	35-38	serpin family C member 1	Homo sapiens	25-31
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
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
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
1733939-4	1992	One of these oligosaccharides was derived from heparin"s ATIII-binding site.	Oligosaccharides	13-29	serpin family C member 1	Homo sapiens	57-62
1733939-5	1992	In an effort to find the ATIII-binding site precursor, the structures of several minor oligosaccharides were determined.	Oligosaccharides	87-103	serpin family C member 1	Homo sapiens	25-30
1733939-7	1992	An oligosaccharide arising from the ATIII-binding site precursor was found that comprised only 0.8 mol % of the oligosaccharide product mixture.	Oligosaccharides	3-18	serpin family C member 1	Homo sapiens	36-41
1733939-7	1992	An oligosaccharide arising from the ATIII-binding site precursor was found that comprised only 0.8 mol % of the oligosaccharide product mixture.	Oligosaccharides	112-127	serpin family C member 1	Homo sapiens	36-41
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.	Oligosaccharides	5-20	serpin family C member 1	Homo sapiens	85-90
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
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
1739360-0	1992	Antithrombin III level, fibrinogen level, and platelet count changes with adjuvant tamoxifen therapy.	Tamoxifen	83-92	serpin family C member 1	Homo sapiens	0-16
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
1739360-4	1992	Antithrombin III levels, elevated at baseline evaluation, decreased in tamoxifen-treated subjects at 6 months, but no subject exhibited a drop to clinically significant levels.	Tamoxifen	71-80	serpin family C member 1	Homo sapiens	0-16
1585693-2	1992	The activity of AT III is decreased in metabolic acidosis, hyperlipoproteinemias and by lipid peroxides.	Lipid Peroxides	88-103	serpin family C member 1	Homo sapiens	16-22
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
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
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
1319616-2	1992	From CY222 (MMW 3,770) as well as from CY216 and its three fractions the material with high affinity to antithrombin III (AT III) was obtained by chromatography on immobilised AT III.	Nadroparin	39-44	serpin family C member 1	Homo sapiens	104-120
1319616-2	1992	From CY222 (MMW 3,770) as well as from CY216 and its three fractions the material with high affinity to antithrombin III (AT III) was obtained by chromatography on immobilised AT III.	Nadroparin	39-44	serpin family C member 1	Homo sapiens	122-128
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
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
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.	octadecasaccharide	96-114	serpin family C member 1	Homo sapiens	73-89
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
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
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.	octadecasaccharide	96-114	serpin family C member 1	Homo sapiens	138-154
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
1579900-7	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
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.	pentasaccharide	75-90	serpin family C member 1	Homo sapiens	50-66
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.	Glucuronic Acid	142-146	serpin family C member 1	Homo sapiens	50-66
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.	Glucuronic Acid	30-34	serpin family C member 1	Homo sapiens	50-66
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
1637525-8	1992	The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III).	Glucose	70-77	serpin family C member 1	Homo sapiens	180-197
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
1637525-8	1992	The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III).	Glucose	70-77	serpin family C member 1	Homo sapiens	199-205
1637525-8	1992	The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III).	Lactic Acid	82-89	serpin family C member 1	Homo sapiens	180-197
1637525-8	1992	The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III).	Lactic Acid	82-89	serpin family C member 1	Homo sapiens	199-205
1379965-2	1992	It consists of heparan, dermatan and chondroitin sulfate; a small proportion of heparan sulfate (4%) has high affinity for antithrombin III (AT III).	Heparitin Sulfate	80-95	serpin family C member 1	Homo sapiens	123-139
1379965-2	1992	It consists of heparan, dermatan and chondroitin sulfate; a small proportion of heparan sulfate (4%) has high affinity for antithrombin III (AT III).	Heparitin Sulfate	80-95	serpin family C member 1	Homo sapiens	141-147
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
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
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
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).	Sugars	220-225	serpin family C member 1	Homo sapiens	103-119
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
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
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
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
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
1604438-0	1992	A useful restriction analysis for the determination of human antithrombin III variants with mutations from Ala 382 to Ala 384.	Alanine	107-110	serpin family C member 1	Homo sapiens	61-77
1604438-0	1992	A useful restriction analysis for the determination of human antithrombin III variants with mutations from Ala 382 to Ala 384.	Alanine	118-121	serpin family C member 1	Homo sapiens	61-77
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
1763970-4	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.	Polysaccharides	180-194	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
1773617-9	1991	The decrease in apolipoprotein A1 and increase in antithrombin III may be related either to the decrease in estradiol levels induced by the treatment or to the effect of the progestogen itself.	Estradiol	108-117	serpin family C member 1	Homo sapiens	50-66
1953677-7	1991	We also studied the affinity of the endothelial heparan sulphate chains towards two presumptive biological ligands, namely antithrombin III and lipoprotein lipase.	Heparitin Sulfate	48-64	serpin family C member 1	Homo sapiens	123-139
1953677-8	1991	A major part of the endothelial heparan sulphate chains showed a weak affinity for antithrombin III and the affinity was essentially lost on heparinase digestion.	Heparitin Sulfate	32-48	serpin family C member 1	Homo sapiens	83-99
1837769-3	1991	Treatment with picotamide significantly reduced circulating platelet aggregates, beta-TG and TxB2 levels, without change of 6-keto-PGF-alpha values, with reduction of F VIII-C and slight increase of plasminogen and ATIII levels.	picotamide	15-25	serpin family C member 1	Homo sapiens	215-220
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
1940573-3	1991	The IXa-AT III complex in the eluate was then measured by using polystyrene balls coated with immobilized rabbit anti-AT III antibody-binding fragments and anti-factor IX (anti-FIX) antibody-binding fragments labeled with beta-D-galactosidase.	Polystyrenes	64-75	serpin family C member 1	Homo sapiens	8-14
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
1776135-3	1991	Arginine-406 is located at the 12th amino acid residue from the reactive site on the C-terminal side of AT-III in a core region of the molecule which has been highly conserved during evolution of serine protease inhibitor (serpin) family.	Arginine	0-8	serpin family C member 1	Homo sapiens	104-110
1746447-7	1991	Although antiplatelet and antithrombin agents such as aspirin and heparin help to decrease rethrombosis, these agents are far from ideal.	Aspirin	54-61	serpin family C member 1	Homo sapiens	26-38
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
1660219-2	1991	The plasma levels of thrombin-antithrombin III complex (TAT) and alpha 2 plasmin inhibitor complex (PIC) were significantly elevated after TAE, concurrently with a decrease in antithrombin III and antiplasmin (alpha 2-plasmin inhibitor) levels.	tae	139-142	serpin family C member 1	Homo sapiens	30-46
1683643-2	1991	In this study multipoint linkage analysis of two Duffy-linked families given a combined LOD score of 8.65 to establish that the Duffy-linked CMT1B gene exists in the 18 centimorgan region between the antithrombin III gene and the Duffy/sodium-potassium ATPase loci.	Sodium	236-242	serpin family C member 1	Homo sapiens	200-216
1683643-2	1991	In this study multipoint linkage analysis of two Duffy-linked families given a combined LOD score of 8.65 to establish that the Duffy-linked CMT1B gene exists in the 18 centimorgan region between the antithrombin III gene and the Duffy/sodium-potassium ATPase loci.	Potassium	243-252	serpin family C member 1	Homo sapiens	200-216
1797807-2	1991	Poly(sodium vinyl sulfonate) is a water-soluble synthetic polymer and activates antithrombin III to exert nonthrombogenicity that was dependent on the molecular weight.	lyapolate	0-27	serpin family C member 1	Homo sapiens	80-96
1804603-7	1991	The mechanism of aspirin may be the inhibition of TXA2 and Fn synthesis and decreased consumption of AT-III.	Aspirin	17-24	serpin family C member 1	Homo sapiens	101-107
1741682-2	1991	The negative correlation between the degree of irreversibility of plasma protein adsorption and the amount of adsorbed AT-III for HEP, immobilized onto the polymer surface passivated with HSA, FG, and plasma was found.	Polymers	156-163	serpin family C member 1	Homo sapiens	119-125
1744977-5	1991	In addition, thrombin inactivation by antithrombin III was accelerated on the endothelial surface, providing strong evidence that heparan sulfate on the surface of endothelial cells exerts a heparin-like activity.	Heparitin Sulfate	130-145	serpin family C member 1	Homo sapiens	38-54
1839430-3	1991	Patients treated with heparan sulphate also showed an increased fibrinolytic activity and a reduced antithrombin III consumption, both of which were statistically significant.	Heparitin Sulfate	22-38	serpin family C member 1	Homo sapiens	100-116
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
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
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
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.	Calcium Chloride	176-181	serpin family C member 1	Homo sapiens	79-95
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
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
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.	Sepharose	54-63	serpin family C member 1	Homo sapiens	17-29
1814829-2	1991	Our findings were: (1) CAAE could induce aggregation and alpha-granule release reaction in the washed human platelet suspension; thus it could activate the platelets; (2) the aggregation effect of CAAE was inhibited by albumin and affected by Ca2+, Mg2+ concentration; (3) heparin and/or AT III did not inhibit the aggregation activation of CAAE, but alpha 2MG markedly inhibited it; (4) the aggregation activity of CAAE was associated with the serine protease activity.	caae	23-27	serpin family C member 1	Homo sapiens	288-294
1814829-2	1991	Our findings were: (1) CAAE could induce aggregation and alpha-granule release reaction in the washed human platelet suspension; thus it could activate the platelets; (2) the aggregation effect of CAAE was inhibited by albumin and affected by Ca2+, Mg2+ concentration; (3) heparin and/or AT III did not inhibit the aggregation activation of CAAE, but alpha 2MG markedly inhibited it; (4) the aggregation activity of CAAE was associated with the serine protease activity.	caae	197-201	serpin family C member 1	Homo sapiens	288-294
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
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
1868237-2	1991	Frameshift mutations of one base and two bases, respectively, were found to have occurred in two unrelated patients at the same GAG codon (Glu 245) within exon 4 of the ATIII gene.	Glutamic Acid	139-142	serpin family C member 1	Homo sapiens	169-174
1837483-8	1991	These data suggest that danazol is potentially useful therapy that may increase levels of natural anticoagulants in patients with thrombotic illnesses in which ATIII, PC and PS are low or normal.	Danazol	24-31	serpin family C member 1	Homo sapiens	160-165
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
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
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
1911389-4	1991	To remove the normal component, the antithrombin was passed through a column of thrombin-Sepharose.	Sepharose	89-98	serpin family C member 1	Homo sapiens	36-48
1911389-5	1991	On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin.	Sodium Dodecyl Sulfate	3-26	serpin family C member 1	Homo sapiens	126-138
1911389-5	1991	On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin.	polyacrylamide	27-41	serpin family C member 1	Homo sapiens	126-138
1911389-5	1991	On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin.	Sodium Dodecyl Sulfate	63-66	serpin family C member 1	Homo sapiens	126-138
1911389-5	1991	On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin.	Sepharose	111-120	serpin family C member 1	Homo sapiens	126-138
1911389-8	1991	One site of cleavage was unambiguously ascertained to be the Arg 393-Ser 394 reactive site bond, by NH2 terminal sequencing of the cleaved variant antithrombin: 10 steps beginning at the P1" position, Ser-Leu-Asn-Pro-Asn-Arg,..., were clearly identified.	Ser-Leu-Asn-Pro-Asn-Arg	201-224	serpin family C member 1	Homo sapiens	147-159
1911389-13	1991	The present results with antithrombin Glasgow II suggest that all the alanine residues at the base of the reactive site loop in positions P12-10 may be important for the formation of a stabilized inhibitor-thrombin complex.	Alanine	70-77	serpin family C member 1	Homo sapiens	25-37
1873224-4	1991	However, in quantitative AT III deficiencies, only three mutations have been described: Pro 407 to Leu and A1a404 to Thr (both located in the C-terminal part of the AT III molecule) and also a frameshift in exon IIIa.	Threonine	117-120	serpin family C member 1	Homo sapiens	25-31
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
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
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.	pentasaccharide	66-81	serpin family C member 1	Homo sapiens	99-104
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.	Phospholipids	213-225	serpin family C member 1	Homo sapiens	99-104
1716644-2	1991	Chlorthalidone produced a slight decrease in clearance of anti-Xa activity from 7.1 +/- 1.0 to 6.6 +/- 0.8 mL/min and a decrease of the volume of distribution from 0.20 +/- 0.05 to 0.16 +/- 0.04 L/kg, whereas the volume of distribution of antithrombin activity increased from 0.14 +/- 0.05 to 0.26 +/- 0.10 L/kg (all differences P less than .05).	Chlorthalidone	0-14	serpin family C member 1	Homo sapiens	239-251
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
1920862-9	1991	To reduce the high TAT under the deficient state of ATIII, MD805, a synthetic thrombin inhibitor, was introduced to avoid further consumption of ATIII.	argatroban	59-64	serpin family C member 1	Homo sapiens	52-57
1920862-9	1991	To reduce the high TAT under the deficient state of ATIII, MD805, a synthetic thrombin inhibitor, was introduced to avoid further consumption of ATIII.	argatroban	59-64	serpin family C member 1	Homo sapiens	145-150
2048592-6	1991	Plasma levels of contraceptive steroids also were related to changes in the most extreme levels of antithrombin III.	Steroids	31-39	serpin family C member 1	Homo sapiens	99-115
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
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
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
1649042-8	1991	In HCC patients, AT III levels were related to the total cholesterol level (R2 = 0.317), whereas in the cirrhotic patients it correlated with the prothrombin level (R2 = 0.274).	Cholesterol	57-68	serpin family C member 1	Homo sapiens	17-23
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
2029579-4	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.	Sepharose	70-79	serpin family C member 1	Homo sapiens	5-11
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.	Sodium Dodecyl Sulfate	125-147	serpin family C member 1	Homo sapiens	5-11
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.	polyacrylamide	148-162	serpin family C member 1	Homo sapiens	5-11
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.	Sodium Dodecyl Sulfate	184-187	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.	Sepharose	111-120	serpin family C member 1	Homo sapiens	13-19
1908914-8	1991	In patients with accelerated fibrinolysis, PAI-C values correlated with t-PA antigen (r = 0.838), PAI-1 antigen (r = 0.519), ATIII activity (r = -0.669) (p less than 0.01) and D dimer levels (r = 0.391, p less than 0.05).	pai-c	43-48	serpin family C member 1	Homo sapiens	125-130
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
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.	Sepharose	72-81	serpin family C member 1	Homo sapiens	25-31
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
1833126-5	1991	Treatment with the low and high dose contraceptive increased the plasma levels of ethinyl estradiol (728 +/- 139 and 1438 +/- 212 vs. 0 fmol/l [low and high dose vs. control], means +/- SEM, P less than 0.001) and fibrinogen (2.3 +/- 0.1 and 2.6 +/- 0.1 vs. 2.0 +/- 0.1 g/l, P less than 0.05); and decreased antithrombin III activity (95 +/- 3 and 92 +/- 3 vs. 101 +/- 3 %, P less than 0.05).	Ethinyl Estradiol	82-99	serpin family C member 1	Homo sapiens	308-324
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
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
1870264-5	1991	Nucleotide sequencing of exon 6 of AT III gene showed a G to T transitional mutation resulting in the conversion of arginine-406 to methionine coexisted with normal allele which encodes arginine.	Arginine	116-124	serpin family C member 1	Homo sapiens	35-41
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.	Sepharose	35-44	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.	Sepharose	35-44	serpin family C member 1	Homo sapiens	164-180
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
2015284-1	1991	The technique of competitive chromogenic substrate hydrolysis is used to examine the inhibitory effects of sucrose and glycerol on the inactivation of thrombin by antithrombin III.	Sucrose	107-114	serpin family C member 1	Homo sapiens	163-179
2015284-1	1991	The technique of competitive chromogenic substrate hydrolysis is used to examine the inhibitory effects of sucrose and glycerol on the inactivation of thrombin by antithrombin III.	Glycerol	119-127	serpin family C member 1	Homo sapiens	163-179
2057915-0	1991	Influence of tryptophan modification upon digestion of antithrombin III by elastase.	Tryptophan	13-23	serpin family C member 1	Homo sapiens	55-71
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.	Tryptophan	25-35	serpin family C member 1	Homo sapiens	48-64
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.	dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium	68-120	serpin family C member 1	Homo sapiens	48-64
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.	hnbsb	122-127	serpin family C member 1	Homo sapiens	48-64
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.	hnbsb	122-127	serpin family C member 1	Homo sapiens	259-275
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.	2-hydroxy-5-nitrobenzyl	78-101	serpin family C member 1	Homo sapiens	48-64
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.	(2S,5R)-5-pentyltetrahydrofuran-2-ol	122-125	serpin family C member 1	Homo sapiens	48-64
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.	(2S,5R)-5-pentyltetrahydrofuran-2-ol	122-125	serpin family C member 1	Homo sapiens	259-275
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
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.	Sepharose	319-328	serpin family C member 1	Homo sapiens	48-64
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
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
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
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
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.	Sepharose	134-143	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.	Sodium Dodecyl Sulfate	196-199	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.	Sodium Dodecyl Sulfate	196-199	serpin family C member 1	Homo sapiens	76-82
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.	Sodium Dodecyl Sulfate	196-199	serpin family C member 1	Homo sapiens	76-82
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
2029579-5	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.	Sepharose	134-143	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
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.	Sepharose	166-175	serpin family C member 1	Homo sapiens	34-40
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.	Carbohydrates	42-54	serpin family C member 1	Homo sapiens	73-89
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
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.	Glycosaminoglycans	164-181	serpin family C member 1	Homo sapiens	73-89
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.	Carbohydrates	247-260	serpin family C member 1	Homo sapiens	73-89
1999418-7	1991	For example, interactions of the sulfate monoanion are important for the binding of heparin, a sulfated glycosaminoglycan, to antithrombin III.	sulfate monoanion	33-50	serpin family C member 1	Homo sapiens	126-142
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
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
2044614-11	1991	The fluctuations in ATIII levels in childhood nephrotic syndrome are determined by the response to steroids and not by the renal histology per se.	Steroids	99-107	serpin family C member 1	Homo sapiens	20-25
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
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.	Sepharose	35-44	serpin family C member 1	Homo sapiens	204-220
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
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.	Benzethonium	29-32	serpin family C member 1	Homo sapiens	166-182
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
1848441-8	1991	The anti Xa activity peak seen after adding AT III to plasma was much higher with heparin than with enoxaparin.	Enoxaparin	100-110	serpin family C member 1	Homo sapiens	44-50
1848441-9	1991	In urine, biological activities, measured with AT III supplementation, were higher with enoxaparin than with heparin.	Enoxaparin	88-98	serpin family C member 1	Homo sapiens	47-53
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
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
1703436-4	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
1794749-4	1991	A pentasaccharide with high affinity for antithrombin III and the C-terminal dodecapeptide fragment of hirudin (hirugen) which occupy the anion-binding and fibrin(ogen) recognition exosites of alpha-thrombin, respectively, could not significantly inhibit factor VIII and factor V activation.	pentasaccharide	2-17	serpin family C member 1	Homo sapiens	41-57
1831314-0	1991	[Antithrombin-III-control in Marcumar patients in oral surgery].	Phenprocoumon	29-37	serpin family C member 1	Homo sapiens	1-17
2024235-4	1991	Administration of azathioprine (AZA), cyclosporine A (CSA) or both as immunosuppressive therapy did not affect HC II levels, but CSA seems to have raised plasma AT III.	Azathioprine	18-30	serpin family C member 1	Homo sapiens	161-167
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
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
2019613-0	1991	Interaction of poly(sodium vinyl sulfonate) and its surface graft with antithrombin III.	poly	15-19	serpin family C member 1	Homo sapiens	71-87
1896523-0	1991	6-Pentadecylsalicylic acid: an antithrombin component isolated from the stem of Rhus semialata var.	anacardic acid	0-26	serpin family C member 1	Homo sapiens	31-43
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
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, Low-Molecular-Weight	54-58	serpin family C member 1	Homo sapiens	248-260
2019613-0	1991	Interaction of poly(sodium vinyl sulfonate) and its surface graft with antithrombin III.	lyapolate	20-42	serpin family C member 1	Homo sapiens	71-87
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.	lyapolate	0-28	serpin family C member 1	Homo sapiens	139-155
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.	lyapolate	30-33	serpin family C member 1	Homo sapiens	139-155
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
2019613-2	1991	The conformational change of antithrombin III was investigated in terms of the intrinsic fluorescence of tryptophan residue, the extrinsic fluorescence using 1,6-diphenyl-1,3,5-hexatriene as fluorescent probe, and Fourier-transform infrared spectroscopy.	Tryptophan	105-115	serpin family C member 1	Homo sapiens	29-45
2019613-2	1991	The conformational change of antithrombin III was investigated in terms of the intrinsic fluorescence of tryptophan residue, the extrinsic fluorescence using 1,6-diphenyl-1,3,5-hexatriene as fluorescent probe, and Fourier-transform infrared spectroscopy.	Diphenylhexatriene	158-187	serpin family C member 1	Homo sapiens	29-45
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.	Trinitrobenzenesulfonic Acid	39-70	serpin family C member 1	Homo sapiens	105-121
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.	lyapolate	76-79	serpin family C member 1	Homo sapiens	105-121
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
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
1664095-5	1991	The clearance of the antithrombin activity of a LMWH is higher than that of the antifactor Xa activity.	Heparin, Low-Molecular-Weight	48-52	serpin family C member 1	Homo sapiens	21-33
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
2062560-2	1991	Both the variant and normal antithrombin component were purified by affinity chromatography on heparin Sepharose.	Sepharose	103-112	serpin family C member 1	Homo sapiens	28-40
1959799-3	1991	So, high plasma L-homocysteine concentration could play a role in the low antithrombin III activity level.	Homocysteine	16-30	serpin family C member 1	Homo sapiens	74-90
2084825-0	1990	Pyridoxine reduces cholesterol and low-density lipoprotein and increases antithrombin III activity in 80-year-old men with low plasma pyridoxal 5-phosphate.	Pyridoxine	0-10	serpin family C member 1	Homo sapiens	73-89
1948084-0	1991	A new synthetic pentasaccharide with increased anti-factor Xa activity: possible role for anionic clusters in the interaction of heparin and antithrombin III.	pentasaccharide	16-31	serpin family C member 1	Homo sapiens	141-157
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
2084825-1	1990	We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels.	Pyridoxine	33-43	serpin family C member 1	Homo sapiens	167-183
2084825-1	1990	We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels.	Pyridoxine	33-43	serpin family C member 1	Homo sapiens	185-191
2084825-1	1990	We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels.	Pyridoxal Phosphate	252-273	serpin family C member 1	Homo sapiens	185-191
2084825-1	1990	We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels.	Pyridoxal Phosphate	275-278	serpin family C member 1	Homo sapiens	185-191
2084825-5	1990	The mechanism by which pyridoxine acts is unclear but it is hypothesized that pyridoxine-derived PLP may enhance the catabolism of LDL and the activity of AT III by inhibiting their glycosylation.	Pyridoxine	23-33	serpin family C member 1	Homo sapiens	155-161
2084825-5	1990	The mechanism by which pyridoxine acts is unclear but it is hypothesized that pyridoxine-derived PLP may enhance the catabolism of LDL and the activity of AT III by inhibiting their glycosylation.	Pyridoxine	78-88	serpin family C member 1	Homo sapiens	155-161
2229057-0	1990	Important role of arginine 129 in heparin-binding site of antithrombin III.	Arginine	18-26	serpin family C member 1	Homo sapiens	58-74
2290238-6	1990	Then she was treated with AT III concentrate and urokinase and her asthmatic symptom was significantly improved and steroid hormone could be easily reduced.	Steroids	116-131	serpin family C member 1	Homo sapiens	26-32
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.	Arginine	130-133	serpin family C member 1	Homo sapiens	31-36
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.	Lysine	137-140	serpin family C member 1	Homo sapiens	31-36
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.	Arginine	64-67	serpin family C member 1	Homo sapiens	106-111
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
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.	Lysine	38-41	serpin family C member 1	Homo sapiens	212-217
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.	Arginine	47-50	serpin family C member 1	Homo sapiens	212-217
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.	Lysine	56-59	serpin family C member 1	Homo sapiens	212-217
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.	Arginine	69-72	serpin family C member 1	Homo sapiens	212-217
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.	pentasaccharide	152-167	serpin family C member 1	Homo sapiens	212-217
2226466-0	1990	Inhibition of factor X and factor V activation by dermatan sulfate and a pentasaccharide with high affinity for antithrombin III in human plasma.	pentasaccharide	73-88	serpin family C member 1	Homo sapiens	112-128
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
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.	pentasaccharide	76-91	serpin family C member 1	Homo sapiens	115-131
2207328-3	1990	AT-III messenger RNA (mRNA) transcripts derived from this construct were translated in an mRNA-dependent rabbit reticulocyte lysate (RRL) system containing (35S)methionine.	Methionine	161-171	serpin family C member 1	Homo sapiens	0-6
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
2207328-4	1990	Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III.	Sodium Dodecyl Sulfate	112-134	serpin family C member 1	Homo sapiens	94-100
2207328-4	1990	Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III.	polyacrylamide	135-149	serpin family C member 1	Homo sapiens	94-100
2207328-4	1990	Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III.	Sodium Dodecyl Sulfate	171-174	serpin family C member 1	Homo sapiens	94-100
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
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.	Sepharose	8-17	serpin family C member 1	Homo sapiens	78-84
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.	Sodium Chloride	127-131	serpin family C member 1	Homo sapiens	78-84
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.	Sodium Chloride	100-104	serpin family C member 1	Homo sapiens	13-19
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
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
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
2292586-1	1990	The tributylammonium salt of a porcine heparin subfraction with low affinity for antithrombin III (Mr 7,500-18,000; anti-clotting activity, 7 USP units/mg), having degrees of sulfate substitution at D-glucosamine and L-iduronic acid residues of GlcNS 0.786, GlcN6s 0.628, and IdoA2s 0.682 mol, was reacted with 10 or 20 mol of pyridine-sulfur trioxide per mol equiv.	tributylammonium salt	4-25	serpin family C member 1	Homo sapiens	81-97
2292586-3	1990	Affinity chromatography of the sulfated products on antithrombin III-Sepharose gel indicated that the polysaccharide acquired some affinity for the protein following the sulfation, as shown by the increase in the proportion of the high-affinity heparin fraction (%) from 1.1 to 6.7.	Sepharose	69-78	serpin family C member 1	Homo sapiens	52-68
2292586-3	1990	Affinity chromatography of the sulfated products on antithrombin III-Sepharose gel indicated that the polysaccharide acquired some affinity for the protein following the sulfation, as shown by the increase in the proportion of the high-affinity heparin fraction (%) from 1.1 to 6.7.	Polysaccharides	102-116	serpin family C member 1	Homo sapiens	52-68
2292586-4	1990	Biological examination of these products indicated that sulfation at natural positions along with the polysaccharide chain resulted in significant increases in all the activities (blood anti-clotting, anti-Factor IIa, and anti-Factor Xa), and in the strength of intrinsic fluorescence of antithrombin III.	Polysaccharides	102-116	serpin family C member 1	Homo sapiens	288-304
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
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
1962908-4	1990	Smaller molecules (18 or more monosaccharide units in length) are required to catalyze the thrombin-AT III reaction.	Monosaccharides	30-44	serpin family C member 1	Homo sapiens	100-106
1962908-6	1990	The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	13-19
1962908-6	1990	The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II.	3-o	55-58	serpin family C member 1	Homo sapiens	13-19
1962908-6	1990	The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II.	Glucosamine	68-79	serpin family C member 1	Homo sapiens	13-19
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
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.	Dalteparin	71-78	serpin family C member 1	Homo sapiens	96-102
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., & 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	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
2175954-1	1990	Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min.	Epoprostenol	54-66	serpin family C member 1	Homo sapiens	0-16
2175954-1	1990	Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min.	Epoprostenol	54-66	serpin family C member 1	Homo sapiens	18-23
2175954-1	1990	Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min.	Epoprostenol	68-72	serpin family C member 1	Homo sapiens	0-16
2175954-1	1990	Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min.	Epoprostenol	68-72	serpin family C member 1	Homo sapiens	18-23
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.	Epoprostenol	30-34	serpin family C member 1	Homo sapiens	0-5
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
2175954-3	1990	ATIII-dependent PGI2 production was significantly inhibited by pretreatment of HUVEC with beta-D-xylosides or heparitinase, though neither pretreatment affected thrombin-induced PGI2 production.	Epoprostenol	16-20	serpin family C member 1	Homo sapiens	0-5
2175954-3	1990	ATIII-dependent PGI2 production was significantly inhibited by pretreatment of HUVEC with beta-D-xylosides or heparitinase, though neither pretreatment affected thrombin-induced PGI2 production.	xylosides	90-106	serpin family C member 1	Homo sapiens	0-5
2175954-3	1990	ATIII-dependent PGI2 production was significantly inhibited by pretreatment of HUVEC with beta-D-xylosides or heparitinase, though neither pretreatment affected thrombin-induced PGI2 production.	Epoprostenol	178-182	serpin family C member 1	Homo sapiens	0-5
2175954-5	1990	ATIII-dependent PGI2 production was completely abolished.	Epoprostenol	16-20	serpin family C member 1	Homo sapiens	0-5
2175954-6	1990	These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production.	Epoprostenol	62-66	serpin family C member 1	Homo sapiens	81-86
2175954-6	1990	These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production.	Glycosaminoglycans	109-127	serpin family C member 1	Homo sapiens	81-86
2175954-6	1990	These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production.	Epoprostenol	194-198	serpin family C member 1	Homo sapiens	81-86
2175954-7	1990	The ATIII-induced PGI2 production is very different from that induced by thrombin.	Epoprostenol	18-22	serpin family C member 1	Homo sapiens	4-9
2264021-0	1990	Effect of a synthetic thrombin-inhibitor MD805 on the reaction between thrombin and plasma antithrombin-III.	argatroban	41-46	serpin family C member 1	Homo sapiens	91-107
2264021-4	1990	As a result, MD805 would serve as a protective agent for ATIII from being consumed, in addition to its potent thrombin-inhibitory activity without the aid of ATIII.	argatroban	13-18	serpin family C member 1	Homo sapiens	57-62
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
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
1977621-3	1990	N-terminal sequencing of antithrombin from two individuals, heterozygous for the Dublin mutation, showed the presence of a truncated antithrombin in which the N-terminal dipeptide is absent.	Dipeptides	170-179	serpin family C member 1	Homo sapiens	25-37
1977621-3	1990	N-terminal sequencing of antithrombin from two individuals, heterozygous for the Dublin mutation, showed the presence of a truncated antithrombin in which the N-terminal dipeptide is absent.	Dipeptides	170-179	serpin family C member 1	Homo sapiens	133-145
2202741-9	1990	Furthermore, specific binding of 125I-labeled antithrombin III to the endothelial cell surface was reduced to 40-60% of control by cytokines.	Iodine-125	33-37	serpin family C member 1	Homo sapiens	46-62
2147914-2	1990	Ticlopidine and aspirin/dipyridamole, but not xanthinol nicotinate, improved platelet aggregation, reduced beta-thromboglobulin, platelet factor IV and fibrinopeptide A concentrations, and increased antithrombin III concentrations and red blood cell filterability.	Ticlopidine	0-11	serpin family C member 1	Homo sapiens	199-215
2147914-2	1990	Ticlopidine and aspirin/dipyridamole, but not xanthinol nicotinate, improved platelet aggregation, reduced beta-thromboglobulin, platelet factor IV and fibrinopeptide A concentrations, and increased antithrombin III concentrations and red blood cell filterability.	Aspirin	16-23	serpin family C member 1	Homo sapiens	199-215
2147914-2	1990	Ticlopidine and aspirin/dipyridamole, but not xanthinol nicotinate, improved platelet aggregation, reduced beta-thromboglobulin, platelet factor IV and fibrinopeptide A concentrations, and increased antithrombin III concentrations and red blood cell filterability.	Dipyridamole	24-36	serpin family C member 1	Homo sapiens	199-215
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
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.	Warfarin	101-109	serpin family C member 1	Homo sapiens	50-56
2402772-5	1990	Immediately after treatment of plasma with 2-percent TNBP, the recovery of factors VIII, IX, and V and antithrombin III was 80, 90, 40, and 100 percent, respectively.	tributyl phosphate	53-57	serpin family C member 1	Homo sapiens	103-119
2390061-0	1990	Re-formation of disulphide bonds in reduced antithrombin III.	disulphide	16-26	serpin family C member 1	Homo sapiens	44-60
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.	disulphide	47-57	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.	disulphide	47-57	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	68-71	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.	Cysteine	68-71	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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.	Cysteine	74-77	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.	Cysteine	74-77	serpin family C member 1	Homo sapiens	24-30
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
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.	Cysteine	70-73	serpin family C member 1	Homo sapiens	57-63
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.	Cysteine	76-79	serpin family C member 1	Homo sapiens	57-63
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.	Cysteine	76-79	serpin family C member 1	Homo sapiens	57-63
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.	Cysteine	76-79	serpin family C member 1	Homo sapiens	57-63
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.	Polysaccharides	61-75	serpin family C member 1	Homo sapiens	27-43
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
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).	pentasaccharide heparin	14-37	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	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
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).	pentasaccharide	14-29	serpin family C member 1	Homo sapiens	85-101
2207233-3	1990	Amongst these antithrombogenic surfaces, this study demonstrates that some insoluble amino acid sulphamide derivatives of polystyrene strongly potentiate heparin cofactor II, in addition to antithrombin III.	amino acid sulphamide	85-106	serpin family C member 1	Homo sapiens	190-206
2207233-3	1990	Amongst these antithrombogenic surfaces, this study demonstrates that some insoluble amino acid sulphamide derivatives of polystyrene strongly potentiate heparin cofactor II, in addition to antithrombin III.	Polystyrenes	122-133	serpin family C member 1	Homo sapiens	190-206
2207233-4	1990	In contrast, an insoluble polystyrene sulphonate and, to a lesser extent, an insoluble heparin copolymer, are better catalysts of antithrombin III.	polystyrene sulphonate	26-48	serpin family C member 1	Homo sapiens	130-146
2207233-4	1990	In contrast, an insoluble polystyrene sulphonate and, to a lesser extent, an insoluble heparin copolymer, are better catalysts of antithrombin III.	heparin copolymer	87-104	serpin family C member 1	Homo sapiens	130-146
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
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
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
2173168-6	1990	Antithrombin III levels were significantly higher at the end of the observation period in the LMW heparin group (p less than 0.005).	Heparin, Low-Molecular-Weight	94-105	serpin family C member 1	Homo sapiens	0-16
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
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
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
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
2115298-9	1990	Antithrombin III decreased in the gestodene group but was unchanged in levonorgestrel-treated women.	Gestodene	34-43	serpin family C member 1	Homo sapiens	0-16
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
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
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
2121564-2	1990	Cyclandelate induced a reduction in euglobulin lysis time, an increase in tissue plasminogen activator concentration and a reduction in plasminogen activator inhibitor, alpha 2-antiplasmin and immunological fibrinogen concentrations, but no changes in antithrombin III and plasminogen concentrations were observed.	Cyclandelate	0-12	serpin family C member 1	Homo sapiens	252-268
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
1973278-0	1990	The confirmation of preclinical familial antithrombin deficiency using polymorphism and specific oligonucleotide probes .	Oligonucleotides	97-112	serpin family C member 1	Homo sapiens	41-53
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
2142236-6	1990	These hormonal changes including the increase of SHBG at the dose levels of 220-680 mg and the decrease of antithrombin III (220-680 mg) may be attributed to a weak estrogen-like effect of toremifene.	Toremifene	189-199	serpin family C member 1	Homo sapiens	107-123
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
2112878-0	1990	Intravenous nitroglycerin-induced heparin resistance: a qualitative antithrombin III abnormality.	Nitroglycerin	12-25	serpin family C member 1	Homo sapiens	68-84
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
2112878-10	1990	A nitroglycerin-induced qualitative ATIII abnormality may be the underlying mechanism.	Nitroglycerin	2-15	serpin family C member 1	Homo sapiens	36-41
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
2372510-3	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.	Sepharose	177-186	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
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.	Warfarin	115-123	serpin family C member 1	Homo sapiens	179-195
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
2214165-2	1990	Commercially available AT III concentrates showed heterogeneity on agarose gel isoelectric focusing, however, they inhibited thrombin in the same manner.	Sepharose	67-74	serpin family C member 1	Homo sapiens	23-29
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
2164263-7	1990	With the pentasaccharide a striking saturation of the inhibition is observed, due to saturation of the antithrombin III.	pentasaccharide	9-24	serpin family C member 1	Homo sapiens	103-119
2353343-3	1990	The nonspecific interaction of thrombin with calcium ions prolonged fibrinogen-clotting and neutralization by antithrombin III (AT III) in the absence of heparin.	Calcium	45-52	serpin family C member 1	Homo sapiens	110-126
2353343-3	1990	The nonspecific interaction of thrombin with calcium ions prolonged fibrinogen-clotting and neutralization by antithrombin III (AT III) in the absence of heparin.	Calcium	45-52	serpin family C member 1	Homo sapiens	128-134
2160076-7	1990	Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins.	Serine	25-28	serpin family C member 1	Homo sapiens	135-151
2160076-7	1990	Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins.	Serine	25-28	serpin family C member 1	Homo sapiens	153-159
2160076-7	1990	Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins.	Tyrosine	77-80	serpin family C member 1	Homo sapiens	135-151
2160076-7	1990	Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins.	Tyrosine	77-80	serpin family C member 1	Homo sapiens	153-159
2194315-2	1990	To define the molecular basis for the variant AT III, we used a combination of genomic amplification followed by cloning, sequencing, and hybridization with allele-specific oligonucleotide probes.	Oligonucleotides	173-188	serpin family C member 1	Homo sapiens	46-52
2194315-3	1990	We obtained evidence for a cytosine to thymine transition in exon 2 (codon 47) of the AT III gene in the proband.	Cytosine	27-35	serpin family C member 1	Homo sapiens	86-92
2194315-3	1990	We obtained evidence for a cytosine to thymine transition in exon 2 (codon 47) of the AT III gene in the proband.	Thymine	39-46	serpin family C member 1	Homo sapiens	86-92
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
2363123-5	1990	This variant AT III was purified, separated from the normal protein by heparin-Sepharose chromatography and was eluted with increased NaCl concentrations.	Sepharose	79-88	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.	Sodium Chloride	134-138	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.	Sodium Chloride	61-65	serpin family C member 1	Homo sapiens	23-29
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
2363123-9	1990	The abnormal AT III showed a normal antiprotease activity, a normal molecular weight by SDS-PAGE, but displayed only a partial immunological identity with the normal protein.	Sodium Dodecyl Sulfate	88-91	serpin family C member 1	Homo sapiens	13-19
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
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
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
1690736-0	1990	Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin.	Ala-Ala-Ala-Ser-Thr	50-69	serpin family C member 1	Homo sapiens	32-48
2394749-10	1990	The predicted reactive site (P1-P1") of this J6 protein is Arg-Ser, which is the same as that of antithrombin III.	Arginine	59-62	serpin family C member 1	Homo sapiens	97-113
2394749-10	1990	The predicted reactive site (P1-P1") of this J6 protein is Arg-Ser, which is the same as that of antithrombin III.	Serine	63-66	serpin family C member 1	Homo sapiens	97-113
1690736-5	1990	By analyzing a CNBr fragment of the thrombin-antithrombin III complex that reacts with the antibody we localized the epitope for the antibody to a strongly hydrophobic residue 382-386 peptide segment, Ala-Ala-Ala-Ser-Thr, of the inhibitor, which is also contiguous with a hydrophobic amino acid Ala at its carboxyl terminus.	Alanine	201-204	serpin family C member 1	Homo sapiens	45-61
2358716-3	1990	1) After chemotherapy, the levels of fibrinogen were increased, ATIII was decreased significantly in cases in the NC.PD group compared with the PR.CR group (p less than 0.05).	Palladium	117-119	serpin family C member 1	Homo sapiens	64-69
2331700-0	1990	Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III.	pentasaccharide	20-35	serpin family C member 1	Homo sapiens	85-101
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
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, Low-Molecular-Weight	61-65	serpin family C member 1	Homo sapiens	162-167
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
2196192-3	1990	The subcutaneous and intravenous LMWH and heparin administration increases basal depressed ATIII activity in diabetic patients.	Heparin, Low-Molecular-Weight	33-37	serpin family C member 1	Homo sapiens	91-96
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
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
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.	phosphotungstate	0-16	serpin family C member 1	Homo sapiens	40-56
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
2339364-0	1990	Phosphotungstate as a useful eluent for antithrombin III purification by heparin-agarose affinity chromatography.	Sepharose	81-88	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.	pta	41-44	serpin family C member 1	Homo sapiens	71-87
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.	pta	41-44	serpin family C member 1	Homo sapiens	89-94
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
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
2339364-2	1990	In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography.	Sepharose	107-116	serpin family C member 1	Homo sapiens	71-87
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.	Sepharose	107-116	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
2339364-3	1990	Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M.	Sepharose	36-45	serpin family C member 1	Homo sapiens	6-11
2339364-3	1990	Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M.	Sodium Chloride	66-70	serpin family C member 1	Homo sapiens	6-11
2339364-3	1990	Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M.	Sodium Chloride	85-89	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
2339367-3	1990	The AT-III deficient plasma is prepared by passage of plasma through a heparin-agarose column.	Sepharose	79-86	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
2405068-0	1990	Novel sulfated polysaccharides: dissociation of anti-human immunodeficiency virus activity from antithrombin activity.	Polysaccharides	15-30	serpin family C member 1	Homo sapiens	96-108
2405068-5	1990	These results indicate that the anti-HIV activity of sulfated polysaccharides can be dissociated from their antithrombin activity.	Polysaccharides	62-77	serpin family C member 1	Homo sapiens	108-120
2154054-5	1990	Instead, we now use gabexate mesilate, which blocks the coagulation cascade without the aid of antithrombin III and works as an anticoagulant.	Gabexate	20-37	serpin family C member 1	Homo sapiens	95-111
2315891-0	1990	Influence of chemical modification of tryptophan residues on the properties of human antithrombin III.	Tryptophan	38-48	serpin family C member 1	Homo sapiens	85-101
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.	Tryptophan	72-82	serpin family C member 1	Homo sapiens	95-111
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.	Tryptophan	72-82	serpin family C member 1	Homo sapiens	306-322
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.	dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium	115-167	serpin family C member 1	Homo sapiens	95-111
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.	2-hydroxy-5-nitrobenzyl	255-278	serpin family C member 1	Homo sapiens	95-111
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
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.	Tryptophan	312-322	serpin family C member 1	Homo sapiens	227-243
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.	Tryptophan	386-389	serpin family C member 1	Homo sapiens	227-243
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
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
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
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
1697824-7	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
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
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.	pentasaccharide	36-51	serpin family C member 1	Homo sapiens	138-154
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.	Methylglycosides	52-68	serpin family C member 1	Homo sapiens	138-154
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.	as-g-a	70-76	serpin family C member 1	Homo sapiens	138-154
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
2275918-3	1990	Polymers substituted with aryl sulfonate and carboxyl groups specifically interact with antithrombin III and serine-proteases involved in the coagulation of blood.	Polymers	0-8	serpin family C member 1	Homo sapiens	88-104
2275918-3	1990	Polymers substituted with aryl sulfonate and carboxyl groups specifically interact with antithrombin III and serine-proteases involved in the coagulation of blood.	Arylsulfonates	26-40	serpin family C member 1	Homo sapiens	88-104
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
1705601-0	1990	[A photometric method of determining the activity of antithrombin III using a peptide coumarylamide substrate].	coumarylamide	86-99	serpin family C member 1	Homo sapiens	53-69
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.	Glycosaminoglycans	240-258	serpin family C member 1	Homo sapiens	123-139
2083874-4	1990	The active site for antithrombin is a specific pentasaccharide sequence containing 3-O-sulfated D-glucosamine.	pentasaccharide	47-62	serpin family C member 1	Homo sapiens	20-32
2083874-4	1990	The active site for antithrombin is a specific pentasaccharide sequence containing 3-O-sulfated D-glucosamine.	Glucosamine	96-109	serpin family C member 1	Homo sapiens	20-32
2079995-6	1990	In contrast, ATIII and Plg correlated directly with serum albumin and inversely with cholesterol and urine protein excretion.	Cholesterol	85-96	serpin family C member 1	Homo sapiens	13-18
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
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
2154059-5	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
2154059-6	1990	In SDS-polyacrylamide gel electrophoresis and immunoblotting analysis, we found a complex formation of ATIII with both human and rabbit TM (and further confirmed their presence with isoelectrofocusing electrophoresis- data not shown).	Sodium Dodecyl Sulfate	3-6	serpin family C member 1	Homo sapiens	103-108
2154059-6	1990	In SDS-polyacrylamide gel electrophoresis and immunoblotting analysis, we found a complex formation of ATIII with both human and rabbit TM (and further confirmed their presence with isoelectrofocusing electrophoresis- data not shown).	polyacrylamide	7-21	serpin family C member 1	Homo sapiens	103-108
2313207-2	1990	Danazol (an attenuated synthetic androgen) already shown to be capable of compensating for a lack of certain antiproteases, was given in doses of 200 mg 3 times per day for 10 days, resulting in a rapid rise (mean 21.2%) in antithrombin III values.	Danazol	0-7	serpin family C member 1	Homo sapiens	224-240
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
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
1705601-1	1990	Toz-Gly-Pro-Arg-4-methylcoumaryl-7-amide is recommended for antithrombin-III (AT-III) photometry as a substrate.	toz-gly-pro-arg-4-methylcoumaryl-7-amide	0-40	serpin family C member 1	Homo sapiens	60-76
1705601-1	1990	Toz-Gly-Pro-Arg-4-methylcoumaryl-7-amide is recommended for antithrombin-III (AT-III) photometry as a substrate.	toz-gly-pro-arg-4-methylcoumaryl-7-amide	0-40	serpin family C member 1	Homo sapiens	78-84
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
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
33794550-4	2021	Tissue factor pathway inhibitor and the strongest physiological anticoagulant antithrombin are attached to the endothelial cell surface by heparan sulfate.	Heparitin Sulfate	139-154	serpin family C member 1	Homo sapiens	78-90
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
33822598-2	2021	A critical role for expulsion of the RCL hinge from a native stabilizing interaction with the hydrophobic core in the activation mechanism has been proposed from reports that antithrombin variants that block this change through engineered disulfide bonds block activation.	Disulfides	239-248	serpin family C member 1	Homo sapiens	175-187
25855774-5	2015	Notably, in the puromycin aminonucleoside model, hyperfibrinogenemia and antithrombin deficiency were also correlated with proteinuria severity, consistent with reports in human nephrotic syndrome.	Puromycin Aminonucleoside	16-41	serpin family C member 1	Homo sapiens	73-85
33234593-0	2021	A quantitative method to detect non-antithrombin-binding 3-O-sulfated units in heparan sulfate.	3-o	57-60	serpin family C member 1	Homo sapiens	36-48
33234593-0	2021	A quantitative method to detect non-antithrombin-binding 3-O-sulfated units in heparan sulfate.	Heparitin Sulfate	79-94	serpin family C member 1	Homo sapiens	36-48
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
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
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
34529138-8	2022	Compared with before TACE, the maximum diameter of tumor was significantly decreased after TACE; ECOG was increased at 3d after TACE, while was decreased at 28d and 90d after TACE (P < 0.05); QOL and HAMA had no significant change at 3d after TACE, while increased significantly at 28d and 90d after TACE (all P < 0.05).	Chlorotrianisene	21-25	serpin family C member 1	Homo sapiens	116-121
34529138-8	2022	Compared with before TACE, the maximum diameter of tumor was significantly decreased after TACE; ECOG was increased at 3d after TACE, while was decreased at 28d and 90d after TACE (P < 0.05); QOL and HAMA had no significant change at 3d after TACE, while increased significantly at 28d and 90d after TACE (all P < 0.05).	Chlorotrianisene	128-132	serpin family C member 1	Homo sapiens	116-121
34529138-8	2022	Compared with before TACE, the maximum diameter of tumor was significantly decreased after TACE; ECOG was increased at 3d after TACE, while was decreased at 28d and 90d after TACE (P < 0.05); QOL and HAMA had no significant change at 3d after TACE, while increased significantly at 28d and 90d after TACE (all P < 0.05).	Chlorotrianisene	300-304	serpin family C member 1	Homo sapiens	116-121
2088576-0	1990	Location of disulfide bonds in antithrombin III.	Disulfides	12-21	serpin family C member 1	Homo sapiens	31-47
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	201-210	serpin family C member 1	Homo sapiens	29-45
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	201-210	serpin family C member 1	Homo sapiens	47-52
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	201-210	serpin family C member 1	Homo sapiens	278-283
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	256-265	serpin family C member 1	Homo sapiens	29-45
2088576-1	1990	Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII.	Disulfides	256-265	serpin family C member 1	Homo sapiens	47-52
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
34927362-8	2022	The introduced N-glycans exhibited position-specific effects on the interaction with two FXa inhibitors: tissue factor pathway inhibitor (TFPI) and antithrombin (ATIII).	n-glycans	15-24	serpin family C member 1	Homo sapiens	148-160
34927362-8	2022	The introduced N-glycans exhibited position-specific effects on the interaction with two FXa inhibitors: tissue factor pathway inhibitor (TFPI) and antithrombin (ATIII).	n-glycans	15-24	serpin family C member 1	Homo sapiens	162-167
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
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.	Fondaparinux	161-173	serpin family C member 1	Homo sapiens	104-109
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.	Heparitin Sulfate	126-128	serpin family C member 1	Homo sapiens	78-90
34955853-2	2021	Low molecular weight heparin (LMWH) is one of the most widely used anticoagulants although LMWHs differ in their anti-Xa, antithrombin, and anticoagulant activities.	Heparin, Low-Molecular-Weight	0-28	serpin family C member 1	Homo sapiens	122-134
34955853-2	2021	Low molecular weight heparin (LMWH) is one of the most widely used anticoagulants although LMWHs differ in their anti-Xa, antithrombin, and anticoagulant activities.	Heparin, Low-Molecular-Weight	30-34	serpin family C member 1	Homo sapiens	122-134
34091123-14	2021	010); AT III% was negatively predicted by the C-P classification (P = 0.000); copper levels, adjusted for C-P classification, were predicted by AT III% (P = 0.020) and fibrinogen concentrations, but not by PT% (P = 0.09).	Copper	78-84	serpin family C member 1	Homo sapiens	144-150
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
34091123-0	2021	Copper concentrations are prevalently associated with antithrombin III, but also with prothrombin time and fibrinogen in patients with liver cirrhosis: A cross-sectional retrospective study.	Copper	0-6	serpin family C member 1	Homo sapiens	54-70
34091123-13	2021	Among the previous parameters, to which serum albumin was added, the unique predictor of copper levels was AT III%, at multiple regression (P = 0.	Copper	89-95	serpin family C member 1	Homo sapiens	107-113
34091123-16	2021	On the basis that oxidants may enhance the activity of the extrinsic coagulation cascade, ultimately leading to thrombin formation, via their combined effects on stimulation of tissue factor activity and inhibition of fibrinolytic pathways, the positive relationship of copper to coagulation/hypercoagulation parameters (mainly AT III) in our research could find a plausible interpretation.	Copper	270-276	serpin family C member 1	Homo sapiens	328-334
34881176-1	2021	Serpinc1 is a serine protease inhibitor in the coagulation cascade, but its role in tumor biology remains obscure.	Serine	14-20	serpin family C member 1	Homo sapiens	0-8
34881176-8	2021	Subsequent unbiased quantitative proteomic and ubiquitinome analyses identify that multiple poly-ubiquitination of proteins involved in signal pathways (such as autophagy, apoptosis, lactate metabolism, and VEGF signaling) are regulated by serpinc1.	Lactic Acid	183-190	serpin family C member 1	Homo sapiens	240-248
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
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
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
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
34307597-16	2021	SAS and SDS scores were significantly lower in the observation group than in the control group at 3 d after operation (P < 0.05).	sds	8-11	serpin family C member 1	Homo sapiens	95-101
34324733-5	2021	Notably, inhibition of neddylation with MLN4924 suppressed both ubiquitination and degradation of antithrombin, which is recapitulated by silencing of the neddylation enzymes, NAE1, UBA3, and UBE2M, with small interfering RNA (siRNA).	pevonedistat	40-47	serpin family C member 1	Homo sapiens	98-110
34381261-13	2021	Conclusion: Argatroban may be more cost-effective during ECMO therapy in patients with low antithrombin III levels without increased risk of adverse events.	argatroban	12-22	serpin family C member 1	Homo sapiens	91-107
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
34256393-0	2021	Antithrombin resistance rescues clotting defect of homozygous prothrombin-Tyr510N dysprothrombinemia.	tyr510n	74-81	serpin family C member 1	Homo sapiens	0-12
35592395-3	2022	A number of endogenous anticoagulant proteins, such as antithrombin and heparin cofactor II, are members of the serine protease inhibitor (SERPIN) family.	Serine	112-118	serpin family C member 1	Homo sapiens	55-67
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
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
35086148-10	2022	Plasma levels of fibrinogen, antithrombin, protein C and TFPI decreased, and free protein S increased in tamoxifen, but not in AI, users.	Tamoxifen	105-114	serpin family C member 1	Homo sapiens	29-41
34790076-3	2021	This case report describes a critically ill premature infant with a progressive, occlusive inferior vena cava thrombus who received supplemental ATIII during enoxaparin treatment.	Enoxaparin	158-168	serpin family C member 1	Homo sapiens	145-150
35563651-2	2022	The action of plasmin is counteracted by alpha2-antiplasmin, alpha2-macroglobulin, TAFI, and other serine protease inhibitors (antithrombin and alpha2-antitrypsin) and PN-1 (protease nexin 1).	Serine	99-105	serpin family C member 1	Homo sapiens	127-139
35124550-0	2022	Miniaturized antithrombin III affinity monolithic columns coupled to TOF-MS for the selective capture and release of fondaparinux a high affinity antithrombin III ligand.	Fondaparinux	117-129	serpin family C member 1	Homo sapiens	13-29
35124550-0	2022	Miniaturized antithrombin III affinity monolithic columns coupled to TOF-MS for the selective capture and release of fondaparinux a high affinity antithrombin III ligand.	Fondaparinux	117-129	serpin family C member 1	Homo sapiens	146-162
35124550-1	2022	This work explores the capability of antithrombin III-functionalized capillary monolithic columns (in-line coupled with MS detection) to selectively capture, release and detect high affinity binders of antithrombin III (AT III) from oligosaccharides mixtures.	Oligosaccharides	233-249	serpin family C member 1	Homo sapiens	37-53
35124550-1	2022	This work explores the capability of antithrombin III-functionalized capillary monolithic columns (in-line coupled with MS detection) to selectively capture, release and detect high affinity binders of antithrombin III (AT III) from oligosaccharides mixtures.	Oligosaccharides	233-249	serpin family C member 1	Homo sapiens	202-218
35124550-1	2022	This work explores the capability of antithrombin III-functionalized capillary monolithic columns (in-line coupled with MS detection) to selectively capture, release and detect high affinity binders of antithrombin III (AT III) from oligosaccharides mixtures.	Oligosaccharides	233-249	serpin family C member 1	Homo sapiens	220-226
35124550-2	2022	The in-situ characterization of home-made AT III affinity columns was done by frontal affinity chromatography coupled to MS detection using fondaparinux as model ligand.	Fondaparinux	140-152	serpin family C member 1	Homo sapiens	42-48
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.	Fondaparinux	190-202	serpin family C member 1	Homo sapiens	109-125
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
35486842-0	2022	Two SERPINC1 variants affecting N-glycosylation of Asn224 cause severe thrombophilia not detected by functional assays.	Nitrogen	32-33	serpin family C member 1	Homo sapiens	4-12
35486842-9	2022	Our study shows new elements involved in the regulation of N-glycosylation, a key post-translational modification that, according to our results affects folding, secretion and function, providing new evidence of the pathogenic consequence of an incorrect N-glycosylation of antithrombin.	Nitrogen	59-60	serpin family C member 1	Homo sapiens	274-286
35410277-9	2022	At 3-d after the operation, the VAS (Visual analogue scale) was 4.64 +- 1.78 and 3.00 +- 1.71, and the ODI (Oswestry disability index) was 67.44 +- 11.37% and 56.73 +- 10.59% in TLF and NTLF group, respectively (P < 0.05).	ntlf	186-190	serpin family C member 1	Homo sapiens	0-6
35013785-10	2022	Reduced CBL-48 h was shown to be most closely associated with the level of Antithrombin-III being decreased in females.	Chlorambucil	8-11	serpin family C member 1	Homo sapiens	75-91
35062299-0	2022	Modulation of HIV Replication in Monocyte-Derived Macrophages (MDM) by Host Antiviral Factors Secretory Leukocyte Protease Inhibitor and Serpin Family C Member 1 Induced by Steroid Hormones.	Steroids	173-180	serpin family C member 1	Homo sapiens	137-161
35387724-12	2022	Correlation analysis showed that there was a clear positive correlation between AT III and TBil in the dead patients of HBV liver failure group and the survival and death patients of non-HBV liver failure group (r values were 0.069, 0.341, 0.064, and P values were 0.723, 1.196 and 0.761, respectively); there was a significant inverse correlation between AT III and TBil in the HBV liver failure group (r = -0.105, P = 0.745).	Bilirubin	91-95	serpin family C member 1	Homo sapiens	356-362
35387724-12	2022	Correlation analysis showed that there was a clear positive correlation between AT III and TBil in the dead patients of HBV liver failure group and the survival and death patients of non-HBV liver failure group (r values were 0.069, 0.341, 0.064, and P values were 0.723, 1.196 and 0.761, respectively); there was a significant inverse correlation between AT III and TBil in the HBV liver failure group (r = -0.105, P = 0.745).	Bilirubin	367-371	serpin family C member 1	Homo sapiens	80-86
35062299-5	2022	Our in vitro results suggest that treatment with high doses of estrogen and progesterone promotes the expression of host antiviral factors Secretory leukocyte protease inhibitor (SLPI) and Serpin family C member 1 (SERPIN C1) among others produced in response to HIV-1 infection.	Progesterone	76-88	serpin family C member 1	Homo sapiens	189-213
35062299-5	2022	Our in vitro results suggest that treatment with high doses of estrogen and progesterone promotes the expression of host antiviral factors Secretory leukocyte protease inhibitor (SLPI) and Serpin family C member 1 (SERPIN C1) among others produced in response to HIV-1 infection.	Progesterone	76-88	serpin family C member 1	Homo sapiens	215-224
35062299-7	2022	SERPIN C1 is a plasma protease inhibitor that regulates the blood coagulation cascade by the inhibition of thrombin and other activated serine proteases of the coagulation system.	Serine	136-142	serpin family C member 1	Homo sapiens	0-9
2597694-0	1989	Phosphate promotes glycation of antithrombin III which interferes with heparin binding.	Phosphates	0-9	serpin family C member 1	Homo sapiens	32-48
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
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.	Glucosamine	44-55	serpin family C member 1	Homo sapiens	109-121
35481431-6	2022	These assess the capacity of low-molecular-mass heparins to accelerate the inhibition of factor Xa and factor IIa by antithrombin.	low-molecular-mass heparins	29-56	serpin family C member 1	Homo sapiens	117-129
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
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
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
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
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
2597694-4	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.	Phosphates	100-109	serpin family C member 1	Homo sapiens	34-46
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.	Phosphates	129-138	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
2614848-1	1989	Crystals of bovine antithrombin III were obtained in the presence of metal ions with ammonium sulphate as precipitating agent.	Metals	69-74	serpin family C member 1	Homo sapiens	19-35
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
2614848-1	1989	Crystals of bovine antithrombin III were obtained in the presence of metal ions with ammonium sulphate as precipitating agent.	Ammonium Sulfate	85-102	serpin family C member 1	Homo sapiens	19-35
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
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
2629459-3	1989	Perturbation of the endothelial proteoglycan metabolism by beta-D-xyloside resulted in a reduced biosynthesis of cell surface heparan sulfate, and impaired antithrombin III binding to endothelial cells in parallel with an inhibition of endothelial cell heparin-like activity.	xylosides	59-74	serpin family C member 1	Homo sapiens	156-172
2483984-2	1989	It was showed: (1) Fn, alpha 2-MG. AT-III activity were considerably decreased in COPD, when compare with that of controls; (2) there is a negative correlation between the value of PaCO2, r = -0.719, P less than 0.01.	paco2	181-186	serpin family C member 1	Homo sapiens	35-41
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
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
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
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
2609289-8	1989	The abnormal ATIII was also found to elute from heparin agarose at a lower ionic strength than normal ATIII.	Sepharose	56-63	serpin family C member 1	Homo sapiens	13-18
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.	phenylalanyl-prolyl-arginine-chloromethyl ketone	90-123	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
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.	Sepharose	35-44	serpin family C member 1	Homo sapiens	78-94
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
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
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
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
2478364-0	1989	The heparin and pentosan polysulfate binding sites of human antithrombin overlap but are not identical.	Pentosan Sulfuric Polyester	16-36	serpin family C member 1	Homo sapiens	60-72
2478364-3	1989	This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding.	Polysaccharides	48-62	serpin family C member 1	Homo sapiens	145-157
2478364-3	1989	This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding.	Lysine	102-105	serpin family C member 1	Homo sapiens	145-157
2478364-3	1989	This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding.	Lysine	114-117	serpin family C member 1	Homo sapiens	145-157
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
2478364-8	1989	On the other hand, pentosan polysulfate protects only Lys-125 and causes no appreciable conformational change, although it is also capable of enhancing the antithrombin-thrombin interaction.	Pentosan Sulfuric Polyester	19-39	serpin family C member 1	Homo sapiens	156-168
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
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.	Pentosan Sulfuric Polyester	52-72	serpin family C member 1	Homo sapiens	90-102
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.	Lysine	115-118	serpin family C member 1	Homo sapiens	90-102
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
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
2688761-3	1989	There is evidence for an analogous acceleratory mechanism in vivo, that functions by the binding of antithrombin to a subpopulation of heparan sulphate proteoglycans intercalated in the surface of endothelial cells.	Heparitin Sulfate	135-151	serpin family C member 1	Homo sapiens	100-112
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
2512688-2	1989	Although ATIII at 20 mInh.U/ml slightly but significantly inhibited thrombin-induced prostacyclin production, neither unfractionated heparin (UFH) nor low molecular weight heparin (LMWH) at 1 U/ml accelerated the inhibitory effect of ATIII.	Epoprostenol	85-97	serpin family C member 1	Homo sapiens	9-14
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
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
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
2679069-7	1989	It is concluded that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-ATIII mechanism.	Warfarin	35-43	serpin family C member 1	Homo sapiens	123-128
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
2679069-7	1989	It is concluded that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-ATIII mechanism.	Heparitin Sulfate	107-122	serpin family C member 1	Homo sapiens	123-128
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
2818566-3	1989	Using two methods, we have studied the potentiating effects of a series of heparin (poly)saccharides with high affinity for antithrombin and mean Mr ranging from approx.	heparin (poly)saccharides	75-100	serpin family C member 1	Homo sapiens	124-136
2529852-0	1989	Effect of a heparan sulphate with high affinity for antithrombin III upon inactivation of thrombin and coagulation factor Xa.	Heparitin Sulfate	12-28	serpin family C member 1	Homo sapiens	52-68
2529852-1	1989	The kinetics of inhibition of human alpha-thrombin and coagulation Factor Xa by antithrombin III were examined under pseudo-first-order reaction conditions as a function of the concentration of heparan sulphate with high affinity for antithrombin III.	Heparitin Sulfate	194-210	serpin family C member 1	Homo sapiens	80-96
2529852-1	1989	The kinetics of inhibition of human alpha-thrombin and coagulation Factor Xa by antithrombin III were examined under pseudo-first-order reaction conditions as a function of the concentration of heparan sulphate with high affinity for antithrombin III.	Heparitin Sulfate	194-210	serpin family C member 1	Homo sapiens	234-250
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
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 sulphate	142-158	serpin family C member 1	Homo sapiens	66-82
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).	Heparitin Sulfate	122-138	serpin family C member 1	Homo sapiens	44-60
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
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
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.	Sepharose	80-89	serpin family C member 1	Homo sapiens	13-25
2818566-5	1989	First, catalytic amounts of heparin (poly)saccharide were added to purified systems containing thrombin and either heparin cofactor II or antithrombin.	heparin (poly)saccharide	28-52	serpin family C member 1	Homo sapiens	138-150
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.	DEAE-Dextran	121-134	serpin family C member 1	Homo sapiens	13-25
2818566-10	1989	In this situation, where the inhibitors competed for thrombin and for the (poly)saccharides, it was found that, provided the latter were of high affinity for antithrombin and exceeded a Mr of 5400, thrombin inhibition in plasma was mediated largely through antithrombin.	Polysaccharides	74-91	serpin family C member 1	Homo sapiens	158-170
2818566-10	1989	In this situation, where the inhibitors competed for thrombin and for the (poly)saccharides, it was found that, provided the latter were of high affinity for antithrombin and exceeded a Mr of 5400, thrombin inhibition in plasma was mediated largely through antithrombin.	Polysaccharides	74-91	serpin family C member 1	Homo sapiens	257-269
2818566-11	1989	Polysaccharides of Mr exceeding 8000 that were of low affinity for antithrombin accelerated thrombin inhibition in plasma through their interaction with heparin cofactor II.	Polysaccharides	0-15	serpin family C member 1	Homo sapiens	67-79
2818566-12	1989	High concentrations of saccharides of Mr 1700-5400 exhibited a size-dependent acceleration of thrombin inhibition, not through their interaction with antithrombin, but through their interaction with heparin cofactor II.	Carbohydrates	23-34	serpin family C member 1	Homo sapiens	150-162
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
2598315-0	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
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
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).	ha-heparin	120-130	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).	histidinoalanine	120-122	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).	histidinoalanine	120-122	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).	histidinoalanine	120-122	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
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).	la-heparin	287-297	serpin family C member 1	Homo sapiens	112-118
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
2544589-0	1989	Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages.	Disulfides	101-110	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
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
2544589-4	1989	The study shows that the three disulfide linkages of AT-III can be sequentially reduced, with Cys8-Cys128 being the most sensitive, followed by Cys21-Cys95, while Cys247-Cys430 is the most resistant to the mild reduction conditions.	Disulfides	31-40	serpin family C member 1	Homo sapiens	53-59
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.	lysyl	144-149	serpin family C member 1	Homo sapiens	102-108
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.	lysyl	144-149	serpin family C member 1	Homo sapiens	275-281
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
2508258-5	1989	After 90 min, in plasma samples containing anti-rt-PA-IgG to inhibit in vitro effects, fibrinogen was decreased to 54%, plasminogen to 52%, alpha 2-antiplasmin to 25%, alpha 2-macroglobulin to 90% and antithrombin III to 85% of initial values.	Hydrocortisone	48-50	serpin family C member 1	Homo sapiens	201-217
2508258-5	1989	After 90 min, in plasma samples containing anti-rt-PA-IgG to inhibit in vitro effects, fibrinogen was decreased to 54%, plasminogen to 52%, alpha 2-antiplasmin to 25%, alpha 2-macroglobulin to 90% and antithrombin III to 85% of initial values.	Protactinium	51-53	serpin family C member 1	Homo sapiens	201-217
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
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.	Sodium Chloride	86-90	serpin family C member 1	Homo sapiens	34-40
2598315-4	1989	LA-heparin and dextran sulfate (DS) were also found to accelerate the thrombin/AT III reaction rate, but neither substance catalyzed the formation of the complex in the presence of 0.1 M NaCl at pH 7.4.	la-heparin	0-10	serpin family C member 1	Homo sapiens	79-85
2598315-4	1989	LA-heparin and dextran sulfate (DS) were also found to accelerate the thrombin/AT III reaction rate, but neither substance catalyzed the formation of the complex in the presence of 0.1 M NaCl at pH 7.4.	Dextran Sulfate	15-30	serpin family C member 1	Homo sapiens	79-85
2598315-4	1989	LA-heparin and dextran sulfate (DS) were also found to accelerate the thrombin/AT III reaction rate, but neither substance catalyzed the formation of the complex in the presence of 0.1 M NaCl at pH 7.4.	Dextran Sulfate	32-34	serpin family C member 1	Homo sapiens	79-85
2598315-5	1989	LA-heparin was also confirmed to compete with HA-heparin for enhancement of the thrombin/AT III reaction.	la-heparin	0-10	serpin family C member 1	Homo sapiens	89-95
2598315-5	1989	LA-heparin was also confirmed to compete with HA-heparin for enhancement of the thrombin/AT III reaction.	ha-heparin	46-56	serpin family C member 1	Homo sapiens	89-95
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.	Sodium Chloride	144-148	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
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
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
2799755-1	1989	We investigated the effect on thrombin generation in plasma of the pentasaccharide that represent the AT III/binding site in heparin.	pentasaccharide	67-82	serpin family C member 1	Homo sapiens	102-108
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
2749614-0	1989	Dissociation of the thrombin/antithrombin III reaction from amidolytic activity of the enzyme at high salt concentration.	Salts	102-106	serpin family C member 1	Homo sapiens	29-45
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.	Octasaccharide	86-100	serpin family C member 1	Homo sapiens	132-144
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
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
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
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
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
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
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
2722864-1	1989	Antithrombin pescara, ARG393 to pro, caused by a CGT to CCT mutation.	Proline	32-35	serpin family C member 1	Homo sapiens	0-12
2722864-11	1989	Using specific oligonucleotide hybridization, we demonstrated that the molecular defect of antithrombin Pescara is caused by a CGT to CCT mutation in codon 393.	Oligonucleotides	15-30	serpin family C member 1	Homo sapiens	91-103
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
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.	Sepharose	97-106	serpin family C member 1	Homo sapiens	12-24
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.	Sepharose	145-154	serpin family C member 1	Homo sapiens	12-24
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
2615648-5	1989	The amino acid abnormality in ten out of 12 cases had arisen at a CpG dinucleotide; this confirms the CpG sequence as a "hotspot" in the antithrombin gene and explains the observed frequency of occurrence of the same variant antithrombins in diverse populations.	Dinucleoside Phosphates	70-82	serpin family C member 1	Homo sapiens	137-149
2796953-5	1989	However, there was close relationship between PFN and antithrombin III, alpha 2-plasmin inhibitor, factor XIII, retinol binding protein and transferrin, which represent hemostasis, fibrinolytic system and nutritional status, respectively.	(R)-Fenoprofen	46-49	serpin family C member 1	Homo sapiens	54-70
2763270-0	1989	C-terminal peptide alcohol, acid and amide analogs of desulfato hirudin54-65 as antithrombin agents.	Amides	37-42	serpin family C member 1	Homo sapiens	80-92
2749614-2	1989	Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations.	Sodium Chloride	85-89	serpin family C member 1	Homo sapiens	30-46
2749614-2	1989	Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations.	Sodium Chloride	85-89	serpin family C member 1	Homo sapiens	48-54
2749614-2	1989	Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations.	Sodium Chloride	121-125	serpin family C member 1	Homo sapiens	30-46
2749614-2	1989	Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations.	Sodium Chloride	121-125	serpin family C member 1	Homo sapiens	48-54
2678856-6	1989	In the high-dose corticosteroid group the values of antithrombin and functional kallikrein inhibition was significantly higher than in the non-steroid group.	Steroids	24-31	serpin family C member 1	Homo sapiens	52-64
2742816-13	1989	The simulated rate of formation and final concentration of a particular oligosaccharide which contains a portion of heparin"s ATIII binding site were similar to those observed experimentally.	Oligosaccharides	72-87	serpin family C member 1	Homo sapiens	126-131
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
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
2512688-0	1989	Interaction of thrombin with heparin cofactor II and antithrombin III on prostacyclin production by cultured endothelial cells.	Epoprostenol	73-85	serpin family C member 1	Homo sapiens	53-69
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
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
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
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
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
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
2466666-9	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
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
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
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
2466666-10	1989	The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds.	Disulfides	188-197	serpin family C member 1	Homo sapiens	96-112
2466666-10	1989	The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds.	Disulfides	188-197	serpin family C member 1	Homo sapiens	116-132
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
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.	Sodium Dodecyl Sulfate	267-289	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.	Sodium Dodecyl Sulfate	267-289	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.	Sodium Dodecyl Sulfate	291-294	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.	Sodium Dodecyl Sulfate	291-294	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.	Sodium Dodecyl Sulfate	267-289	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.	Sodium Dodecyl Sulfate	291-294	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.	polyacrylamide	296-310	serpin family C member 1	Homo sapiens	40-45
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.	Lysine	92-95	serpin family C member 1	Homo sapiens	34-46
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.	polyacrylamide	296-310	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.	polyacrylamide	296-310	serpin family C member 1	Homo sapiens	134-139
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
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
2492530-0	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
2492530-0	1989	Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236.	Lysine	90-96	serpin family C member 1	Homo sapiens	28-44
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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	146-152	serpin family C member 1	Homo sapiens	34-46
2492530-1	1989	Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III.	Lysine	0-3	serpin family C member 1	Homo sapiens	78-94
2492530-1	1989	Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III.	Lysine	9-12	serpin family C member 1	Homo sapiens	78-94
2492530-1	1989	Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III.	Lysine	9-12	serpin family C member 1	Homo sapiens	78-94
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.	Water	6-11	serpin family C member 1	Homo sapiens	150-166
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.	Lysine	92-95	serpin family C member 1	Homo sapiens	34-46
2492530-12	1989	At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%.	Lysine	71-74	serpin family C member 1	Homo sapiens	13-25
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.	4-n,n-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid	35-97	serpin family C member 1	Homo sapiens	150-166
2492530-12	1989	At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%.	Lysine	83-86	serpin family C member 1	Homo sapiens	13-25
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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	99-107	serpin family C member 1	Homo sapiens	150-166
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.	Lysine	131-137	serpin family C member 1	Homo sapiens	150-166
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
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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	28-36	serpin family C member 1	Homo sapiens	0-12
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
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
2492530-6	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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	82-88	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
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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	60-66	serpin family C member 1	Homo sapiens	34-46
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.	Lysine	83-86	serpin family C member 1	Homo sapiens	34-46
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.	Lysine	92-95	serpin family C member 1	Homo sapiens	34-46
2492530-12	1989	At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%.	Lysine	83-86	serpin family C member 1	Homo sapiens	13-25
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.	Lysine	17-20	serpin family C member 1	Homo sapiens	101-113
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.	Lysine	17-20	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.	Lysine	17-20	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.	Lysine	26-29	serpin family C member 1	Homo sapiens	101-113
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.	Lysine	26-29	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.	Lysine	26-29	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.	Lysine	26-29	serpin family C member 1	Homo sapiens	101-113
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
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.	Lysine	26-29	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.	Lysine	26-29	serpin family C member 1	Homo sapiens	145-157
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
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
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
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
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.	Sepharose	114-123	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
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
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
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
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
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
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.	Lysine	26-29	serpin family C member 1	Homo sapiens	101-113
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.	Lysine	26-29	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.	Lysine	26-29	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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	249-255	serpin family C member 1	Homo sapiens	101-113
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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	249-255	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.	4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate	249-255	serpin family C member 1	Homo sapiens	145-157
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
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.	4-aminobenzamidine	154-172	serpin family C member 1	Homo sapiens	59-71
2735662-8	1989	Drugs which act primarily on factor Xa (oligosaccharides) or thrombin by non-ATIII pathways (dermatan sulfate) are less efficient than UFH as antithrombotic drugs.	Dermatan Sulfate	93-109	serpin family C member 1	Homo sapiens	77-82
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
2798989-2	1989	The mean of AT III level in patients with COBP was 40.5% and was 96.8% in the controls.	cobp	42-46	serpin family C member 1	Homo sapiens	12-18
2713873-1	1989	spectroscopy, of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III.	IC 831423	59-82	serpin family C member 1	Homo sapiens	92-108
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.	Histidine	37-46	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	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
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.	Histidine	42-51	serpin family C member 1	Homo sapiens	204-209
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
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.	pentasaccharide	102-117	serpin family C member 1	Homo sapiens	128-133
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
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
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
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)-.	pentasaccharide	48-63	serpin family C member 1	Homo sapiens	4-16
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)-.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	105-111	serpin family C member 1	Homo sapiens	4-16
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)-.	6-oso3	112-118	serpin family C member 1	Homo sapiens	4-16
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)-.	glca-glcnso3	120-132	serpin family C member 1	Homo sapiens	4-16
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)-.	3,6-di-oso3)	133-145	serpin family C member 1	Homo sapiens	4-16
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)-.	ido a	146-151	serpin family C member 1	Homo sapiens	4-16
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)-.	2-oso3)- glcnso3	152-168	serpin family C member 1	Homo sapiens	4-16
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)-.	6-oso3	169-175	serpin family C member 1	Homo sapiens	4-16
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
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
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
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
2730347-2	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.	Polysaccharides	101-116	serpin family C member 1	Homo sapiens	144-160
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
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.	2,2,2-trifluoroethanesulfonyl chloride	17-32	serpin family C member 1	Homo sapiens	125-137
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
2561387-3	1989	The definite mode of action remains unknown, but LMWH act at different steps like coagulation (by AT III), fibrinolysis, blood cells, endothelial cells.	Heparin, Low-Molecular-Weight	49-53	serpin family C member 1	Homo sapiens	98-104
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
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
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
2910359-3	1989	Displacement of 125I-labeled antithrombin III specifically bound to endothelial cells by unlabeled histidine-rich glycoprotein was much less potent than that by unlabeled antithrombin III.	Iodine-125	16-20	serpin family C member 1	Homo sapiens	29-45
2917133-4	1989	The antithrombin was isolated by heparin Sepharose affinity chromatography.	Heparin	33-40	serpin family C member 1	Homo sapiens	4-16
2917133-4	1989	The antithrombin was isolated by heparin Sepharose affinity chromatography.	Sepharose	41-50	serpin family C member 1	Homo sapiens	4-16
2917133-7	1989	The antithrombin was further purified by chromatography on thrombin-Sepharose (to remove the normal component), reduced, S-carboxymethylated and fragmented with cyanogen bromide.	Sepharose	68-77	serpin family C member 1	Homo sapiens	4-16
2917133-7	1989	The antithrombin was further purified by chromatography on thrombin-Sepharose (to remove the normal component), reduced, S-carboxymethylated and fragmented with cyanogen bromide.	Cyanogen Bromide	161-177	serpin family C member 1	Homo sapiens	4-16
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
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
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
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
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
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
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
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
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
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
2807044-4	1989	During pyridoxine and folate treatment, antithrombin III activity rapidly returned to normal; factor VII increased and beta-thromboglobulin decreased.	Pyridoxine	7-17	serpin family C member 1	Homo sapiens	40-56
2807044-4	1989	During pyridoxine and folate treatment, antithrombin III activity rapidly returned to normal; factor VII increased and beta-thromboglobulin decreased.	Folic Acid	22-28	serpin family C member 1	Homo sapiens	40-56
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.	Polyvinyl Alcohol	24-41	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.	Glutaral	59-73	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
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
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
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
2562205-5	1989	Studies in several laboratories have demonstrated that a specific pentasaccharide sequence is required for AT III binding.	pentasaccharide	66-81	serpin family C member 1	Homo sapiens	107-113
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.	Oligosaccharides	0-15	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.	Oligosaccharides	0-15	serpin family C member 1	Homo sapiens	184-189
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.	Oligosaccharides	66-81	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.	Oligosaccharides	66-81	serpin family C member 1	Homo sapiens	184-189
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
2922702-6	1989	Although oligosaccharides of degree of polymerization (dp) 18 and 20 showed significant ATIII and HCII mediated anti-IIa activities no separation of these activities resulted.	Oligosaccharides	9-25	serpin family C member 1	Homo sapiens	88-93
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
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
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
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
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.	pentasaccharide	84-99	serpin family C member 1	Homo sapiens	162-178
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
3232125-4	1988	Previous biochemical studies showed the 3-O-desulfated pentasaccharide to have a low affinity binding to AT III and to be devoid of the high anti-factor Xa activity characteristic of the pentasaccharide.	3-o-desulfated pentasaccharide	40-70	serpin family C member 1	Homo sapiens	105-111
3232125-4	1988	Previous biochemical studies showed the 3-O-desulfated pentasaccharide to have a low affinity binding to AT III and to be devoid of the high anti-factor Xa activity characteristic of the pentasaccharide.	pentasaccharide	55-70	serpin family C member 1	Homo sapiens	105-111
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.	Heparitin Sulfate	36-52	serpin family C member 1	Homo sapiens	214-219
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.	Heparitin Sulfate	36-52	serpin family C member 1	Homo sapiens	379-395
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.	Heparitin Sulfate	269-285	serpin family C member 1	Homo sapiens	214-219
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
3266555-2	1988	Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI).	chloramine-T	60-72	serpin family C member 1	Homo sapiens	196-212
3266555-2	1988	Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI).	chloramine-T	60-72	serpin family C member 1	Homo sapiens	214-220
3266555-2	1988	Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI).	chloramine-T	74-76	serpin family C member 1	Homo sapiens	196-212
3266555-2	1988	Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI).	chloramine-T	74-76	serpin family C member 1	Homo sapiens	214-220
3266555-4	1988	The inactivation of alpha 1-PI, alpha 2-PI and AT III in plasma by oxidants is the result of a specific oxidative damage since C1-inhibitor, serine proteinases and complexes of plasmin and alpha 2-PI were chloramine resistant under the conditions used.	chloramine	205-215	serpin family C member 1	Homo sapiens	47-53
3179438-0	1988	Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity.	Guanine	57-64	serpin family C member 1	Homo sapiens	0-16
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
2851191-6	1988	This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma.	Glycosaminoglycans	27-44	serpin family C member 1	Homo sapiens	193-209
2851191-6	1988	This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma.	Glycosaminoglycans	27-44	serpin family C member 1	Homo sapiens	283-299
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, Low-Molecular-Weight	32-44	serpin family C member 1	Homo sapiens	127-143
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
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
3169017-2	1988	A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups.	pentasaccharide	12-27	serpin family C member 1	Homo sapiens	108-124
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
3169017-2	1988	A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups.	Sulfates	140-147	serpin family C member 1	Homo sapiens	108-124
3169017-6	1988	This suggests that they belong to a secondary sub-region of interaction with antithrombin III, the primary one being accounted for by other critical parts of the structure and particularly the trisaccharide sequence placed at the non-reducing end of the pentasaccharide.	Trisaccharides	193-206	serpin family C member 1	Homo sapiens	77-93
3169017-6	1988	This suggests that they belong to a secondary sub-region of interaction with antithrombin III, the primary one being accounted for by other critical parts of the structure and particularly the trisaccharide sequence placed at the non-reducing end of the pentasaccharide.	pentasaccharide	254-269	serpin family C member 1	Homo sapiens	77-93
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
3169238-0	1988	Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II.	Phosphates	43-52	serpin family C member 1	Homo sapiens	0-12
3169238-0	1988	Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II.	polyanions	64-74	serpin family C member 1	Homo sapiens	0-12
3169238-1	1988	We have examined the antithrombin effects of various phosphate-containing polyanions (including linear polyphosphates, polynucleotides and the phosphoserine glycoprotein, phosvitin) on the glycosaminoglycan-binding plasma proteinase inhibitors, antithrombin III (ATIII) and heparin cofactor II (HCII).	Phosphates	53-62	serpin family C member 1	Homo sapiens	21-33
3169238-1	1988	We have examined the antithrombin effects of various phosphate-containing polyanions (including linear polyphosphates, polynucleotides and the phosphoserine glycoprotein, phosvitin) on the glycosaminoglycan-binding plasma proteinase inhibitors, antithrombin III (ATIII) and heparin cofactor II (HCII).	polyanions	74-84	serpin family C member 1	Homo sapiens	21-33
2458152-9	1988	Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III.	Disulfides	30-39	serpin family C member 1	Homo sapiens	130-146
2458152-12	1988	The change in vitronectin induced by thrombin-antithrombin III, therefore, is a physiological correlate of urea treatment and of adsorption of vitronectin onto tissue culture plastic (as is done in cell adhesion assays).	Urea	107-111	serpin family C member 1	Homo sapiens	46-62
3224125-5	1988	Desorption of proteins from the polymeric interface by means of polycations (polybrene and polylysine) showed that the inactive complex T-AT is more quantitatively and easily released than thrombin.	Hexadimethrine Bromide	77-86	serpin family C member 1	Homo sapiens	138-140
3224125-5	1988	Desorption of proteins from the polymeric interface by means of polycations (polybrene and polylysine) showed that the inactive complex T-AT is more quantitatively and easily released than thrombin.	Polylysine	91-101	serpin family C member 1	Homo sapiens	138-140
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
3060987-1	1988	The effect on plasma antithrombin III (AT III) and protein C on a supplement with polyunsaturated fatty acids (PUFA"s) was investigated in a double-blind study in 36 patients with stable angina pectoris.	Fatty Acids, Unsaturated	82-109	serpin family C member 1	Homo sapiens	21-37
3060987-3	1988	Both oil supplements resulted in a statistically significant decrease in AT III activity, but there were no differences between the two different types of PUFA"s.	Oils	5-8	serpin family C member 1	Homo sapiens	73-79
2686903-5	1989	We thus found that MD805 could be used as an anticoagulant drug when an AT III-deficient patient required anticoagulation in the extracorporeal circulation.	argatroban	19-24	serpin family C member 1	Homo sapiens	72-78
2522237-0	1989	Effects of high dose medroxyprogesterone acetate treatment on antithrombin III and other plasma proteins in males with renal cell or prostatic carcinoma.	Medroxyprogesterone Acetate	21-48	serpin family C member 1	Homo sapiens	62-78
2522237-1	1989	In 18 patients, 12 with renal cell and 6 with prostatic carcinoma treatment with high dose medroxyprogesterone acetate (MPA) significantly increased serum antithrombin III and haptoglobin concentrations.	Medroxyprogesterone Acetate	91-118	serpin family C member 1	Homo sapiens	155-171
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
3238650-5	1988	These and other results established the approximately 120,000 Mr component to be an inactive, disulphide-linked variant antithrombin and albumin complex.	disulphide	94-104	serpin family C member 1	Homo sapiens	120-132
3238652-1	1988	Three patients with familial antithrombin III (ATIII) deficiency, who also have histories of thromboembolism, were treated with oxymetholone in combination with warfarin.	Oxymetholone	128-140	serpin family C member 1	Homo sapiens	29-45
3238652-1	1988	Three patients with familial antithrombin III (ATIII) deficiency, who also have histories of thromboembolism, were treated with oxymetholone in combination with warfarin.	Oxymetholone	128-140	serpin family C member 1	Homo sapiens	47-52
3238652-4	1988	The levels of plasma ATIII, alpha 1-antitrypsin, plasminogen and Cl-inactivator were significantly increased in all patients after the introduction of oxymetholone therapy.	Oxymetholone	151-163	serpin family C member 1	Homo sapiens	21-26
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
2973992-1	1988	Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 X 10(7) M-1.min-1) and the prothrombinase:ATIII interaction by 2900-fold (k2, 2.5 X 10(7) M-1.min-1).	Heparitin Sulfate	0-16	serpin family C member 1	Homo sapiens	56-61
2973992-1	1988	Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 X 10(7) M-1.min-1) and the prothrombinase:ATIII interaction by 2900-fold (k2, 2.5 X 10(7) M-1.min-1).	Heparitin Sulfate	0-16	serpin family C member 1	Homo sapiens	115-120
2973992-1	1988	Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 X 10(7) M-1.min-1) and the prothrombinase:ATIII interaction by 2900-fold (k2, 2.5 X 10(7) M-1.min-1).	Heparitin Sulfate	0-16	serpin family C member 1	Homo sapiens	115-120
3196877-6	1988	The inhibition of thrombin generation by the LMWH was comparable with that of standard heparin on the basis of their respective antithrombin specific activities, but not on the basis of their antifactor Xa activities.	Heparin, Low-Molecular-Weight	45-49	serpin family C member 1	Homo sapiens	128-140
3228593-0	1988	Adjuvant tamoxifen in primary breast cancer: influence on plasma lipids and antithrombin III levels.	Tamoxifen	9-18	serpin family C member 1	Homo sapiens	76-92
3186090-2	1988	The purpose of this study was to evaluate the relationship between plasma antithrombin III activity and both clotting parameters (platelet count and fibrinopeptide A) and renal parameters (serum creatinine and uric acid concentration).	Creatinine	195-205	serpin family C member 1	Homo sapiens	74-90
3186090-2	1988	The purpose of this study was to evaluate the relationship between plasma antithrombin III activity and both clotting parameters (platelet count and fibrinopeptide A) and renal parameters (serum creatinine and uric acid concentration).	Uric Acid	210-219	serpin family C member 1	Homo sapiens	74-90
3179438-0	1988	Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity.	Adenine	68-75	serpin family C member 1	Homo sapiens	0-16
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
3179438-9	1988	Codon 382 codes for alanine in the normal allele and for threonine in the antithrombin-III-Hamilton allele.	Alanine	20-27	serpin family C member 1	Homo sapiens	74-90
3179438-9	1988	Codon 382 codes for alanine in the normal allele and for threonine in the antithrombin-III-Hamilton allele.	Threonine	57-66	serpin family C member 1	Homo sapiens	74-90
3179438-11	1988	We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases.	Threonine	54-63	serpin family C member 1	Homo sapiens	79-95
3179438-11	1988	We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases.	Threonine	54-63	serpin family C member 1	Homo sapiens	316-332
3179438-11	1988	We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases.	Alanine	68-75	serpin family C member 1	Homo sapiens	79-95
3179438-11	1988	We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases.	Alanine	68-75	serpin family C member 1	Homo sapiens	316-332
3179448-4	1988	Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393.	Oligonucleotides	46-62	serpin family C member 1	Homo sapiens	212-217
3179448-4	1988	Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393.	Oligonucleotides	46-62	serpin family C member 1	Homo sapiens	292-297
3179448-4	1988	Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393.	Oligonucleotides	46-61	serpin family C member 1	Homo sapiens	212-217
3179448-4	1988	Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393.	Oligonucleotides	46-61	serpin family C member 1	Homo sapiens	292-297
3179448-5	1988	These oligonucleotide probes should prove useful as an alternative method for early detection of the ATIII variants.	Oligonucleotides	6-21	serpin family C member 1	Homo sapiens	101-106
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
2464199-2	1988	In contrast to a current hypothesis the antithrombin III independent effect of PPS on blood coagulation is not caused by preventing the binding of the factors IX, IXa, X, Xa, VIII, V, Va and II onto procoagulant phospholipids.	Pentosan Sulfuric Polyester	79-82	serpin family C member 1	Homo sapiens	40-56
2464199-11	1988	We postulate therefore that the antithrombin III independent inhibitory effect of PPS on thrombin generation on blood coagulation is by interaction with factor VIIIa.	Pentosan Sulfuric Polyester	82-85	serpin family C member 1	Homo sapiens	32-48
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
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.	Pentosan Sulfuric Polyester	56-59	serpin family C member 1	Homo sapiens	98-114
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
3218731-0	1988	Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin.	Glycosaminoglycans	63-81	serpin family C member 1	Homo sapiens	115-131
3218731-3	1988	This has been used to compare the binding of a range of glycosaminoglycans and other sulfated polymers to antithrombin III and thrombin, a major inhibitor of and a central protease in the coagulation system, respectively.	Glycosaminoglycans	56-74	serpin family C member 1	Homo sapiens	106-122
3218731-3	1988	This has been used to compare the binding of a range of glycosaminoglycans and other sulfated polymers to antithrombin III and thrombin, a major inhibitor of and a central protease in the coagulation system, respectively.	Polymers	94-102	serpin family C member 1	Homo sapiens	106-122
3218731-4	1988	The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide.	Glycosaminoglycans	67-85	serpin family C member 1	Homo sapiens	89-105
3218731-4	1988	The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide.	Glycosaminoglycans	67-85	serpin family C member 1	Homo sapiens	138-154
3218731-4	1988	The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide.	pentasaccharide	163-178	serpin family C member 1	Homo sapiens	89-105
3218731-4	1988	The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide.	pentasaccharide	163-178	serpin family C member 1	Homo sapiens	138-154
3218731-4	1988	The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide.	pentasaccharide	271-286	serpin family C member 1	Homo sapiens	89-105
3218731-5	1988	Highly sulfated synthetic polymers will, however, bind antithrombin III by a second mechanism.	Polymers	26-34	serpin family C member 1	Homo sapiens	55-71
3201396-7	1988	Calcium (1 mM) increased the inhibition reaction rates of native and modified forms of factor Xa with antithrombin III by 20-30%.	Calcium	0-7	serpin family C member 1	Homo sapiens	102-118
3187966-0	1988	Prevention of thrombin/antithrombin III reaction in the presence of protamine or polybrene.	Hexadimethrine Bromide	81-90	serpin family C member 1	Homo sapiens	23-39
3187966-1	1988	The rate of the thrombin/antithrombin III (AT III) reaction was decreased in the presence of free polybrene or protamine.	Hexadimethrine Bromide	98-107	serpin family C member 1	Homo sapiens	16-41
3187966-1	1988	The rate of the thrombin/antithrombin III (AT III) reaction was decreased in the presence of free polybrene or protamine.	Hexadimethrine Bromide	98-107	serpin family C member 1	Homo sapiens	43-49
3187966-3	1988	The reaction was also prevented when either thrombin or AT III was transferred into noncoated tubes after instantaneous contact with protamine-coated tubes or tubes with polybrene.	Hexadimethrine Bromide	170-179	serpin family C member 1	Homo sapiens	56-62
2902851-0	1988	Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II.	Chondroitin	24-35	serpin family C member 1	Homo sapiens	102-118
2902851-0	1988	Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II.	Dermatan Sulfate	40-57	serpin family C member 1	Homo sapiens	102-118
2902851-6	1988	The antithrombin III-Factor Xa interaction was potentiated by all other GAGs studied to a degree similar to that of heparin pentasaccharide with high affinity for antithrombin III.	IC 831423	116-139	serpin family C member 1	Homo sapiens	4-20
2902851-6	1988	The antithrombin III-Factor Xa interaction was potentiated by all other GAGs studied to a degree similar to that of heparin pentasaccharide with high affinity for antithrombin III.	IC 831423	116-139	serpin family C member 1	Homo sapiens	163-179
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
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
3187951-4	1988	The propositus" AT III was coeluted with normal AT III from an heparin-sepharose column.	Sepharose	71-80	serpin family C member 1	Homo sapiens	16-22
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
3187951-9	1988	SDS-PAGE experiments performed in purified system and immunoblots obtained from plasma showed that the two variants have different behaviour: in the case of AT III Charleville thrombin induced an apparent 5 k delta increase in molecular mass, probably due to a conformational change.	Sodium Dodecyl Sulfate	0-3	serpin family C member 1	Homo sapiens	157-163
3208245-0	1988	Binding of heparin to antithrombin III: a chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue.	Glucosamine	101-126	serpin family C member 1	Homo sapiens	22-38
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
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
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
3191114-7	1988	Proline-407 is located 14 amino acids C-terminal to the reactive site arginine of ATIII in a core region of the molecule that has been highly conserved during evolution of the serine protease inhibitor (serpin) gene family.	Proline	0-7	serpin family C member 1	Homo sapiens	82-87
3191114-7	1988	Proline-407 is located 14 amino acids C-terminal to the reactive site arginine of ATIII in a core region of the molecule that has been highly conserved during evolution of the serine protease inhibitor (serpin) gene family.	Arginine	70-78	serpin family C member 1	Homo sapiens	82-87
3191114-8	1988	The location of this proline in the crystal structure of the homologous serpin alpha 1-antitrypsin suggests that the leucine substitution in ATIII-Utah may interfere with correct folding of the mutant gene product, leading to its rapid turnover and the low antithrombin levels observed in patient plasmas.	Proline	21-28	serpin family C member 1	Homo sapiens	141-146
3191114-8	1988	The location of this proline in the crystal structure of the homologous serpin alpha 1-antitrypsin suggests that the leucine substitution in ATIII-Utah may interfere with correct folding of the mutant gene product, leading to its rapid turnover and the low antithrombin levels observed in patient plasmas.	Proline	21-28	serpin family C member 1	Homo sapiens	257-269
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
3191114-10	1988	Patient antithrombin III, isolated by affinity chromatography on heparin-Sepharose, was reacted with purified thrombin.	Sepharose	73-82	serpin family C member 1	Homo sapiens	8-24
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
3391345-0	1988	Demonstration of altered antithrombin III activity due to nonenzymatic glycosylation at glucose concentration expected to be encountered in severely diabetic patients.	Glucose	88-95	serpin family C member 1	Homo sapiens	25-41
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
3246651-0	1988	[Interaction between oleic acid and human antithrombin III].	Oleic Acid	21-31	serpin family C member 1	Homo sapiens	42-58
3246652-0	1988	[Effect of various kinds of fatty acids on the human antithrombin III activity].	Fatty Acids	28-39	serpin family C member 1	Homo sapiens	53-69
3215905-0	1988	Permeability of a heparin-polyvinyl alcohol hydrogel to thrombin and antithrombin III.	Polyvinyl Alcohol	26-43	serpin family C member 1	Homo sapiens	69-85
2973155-1	1988	Recent evidence suggests that heparan sulfate on endothelial cell surfaces acts as a catalyst for the neutralization of thrombin by antithrombin III (AT III).	Heparitin Sulfate	30-45	serpin family C member 1	Homo sapiens	132-148
2973155-1	1988	Recent evidence suggests that heparan sulfate on endothelial cell surfaces acts as a catalyst for the neutralization of thrombin by antithrombin III (AT III).	Heparitin Sulfate	30-45	serpin family C member 1	Homo sapiens	150-156
2973155-3	1988	We evaluated the ability of cultured human fibroblasts to catalyze the interaction between thrombin and AT III and found that heparan sulfate produced by post-confluent fibroblasts was anticoagulantly active.	Heparitin Sulfate	126-141	serpin family C member 1	Homo sapiens	104-110
2973155-5	1988	These results indicate that fibroblasts do produce an anticoagulantly active species of heparan sulfate and that the normal interaction between AT III and thrombin may be driven by initial release of heparan sulfate from the cell surface by thrombin followed by AT III interaction with the soluble thrombin-heparan sulfate complex.	Heparitin Sulfate	200-215	serpin family C member 1	Homo sapiens	144-150
2973155-5	1988	These results indicate that fibroblasts do produce an anticoagulantly active species of heparan sulfate and that the normal interaction between AT III and thrombin may be driven by initial release of heparan sulfate from the cell surface by thrombin followed by AT III interaction with the soluble thrombin-heparan sulfate complex.	Heparitin Sulfate	200-215	serpin family C member 1	Homo sapiens	144-150
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
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
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
3413737-4	1988	Two populations of ATIII were detected by affinity chromatography on heparin-sepharose from affected members" plasma.	Sepharose	77-86	serpin family C member 1	Homo sapiens	19-24
3413737-5	1988	The ATIII unbound to sepharose beads was devoid of heparin cofactor activity and showed a lack of anodal migration in CIE in the presence of heparin.	Sepharose	21-30	serpin family C member 1	Homo sapiens	4-9
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
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
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
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
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
3377765-2	1988	The resulting oligosaccharides were fractionated by gel filtration chromatography and tested for the ability to stimulate inhibition of thrombin by purified heparin cofactor II or antithrombin.	Oligosaccharides	14-30	serpin family C member 1	Homo sapiens	180-192
3377765-3	1988	Oligosaccharides containing greater than or equal to 18 monosaccharide units were active with antithrombin, while larger oligosaccharides were required for activity with heparin cofactor II.	Oligosaccharides	0-16	serpin family C member 1	Homo sapiens	94-106
3377765-3	1988	Oligosaccharides containing greater than or equal to 18 monosaccharide units were active with antithrombin, while larger oligosaccharides were required for activity with heparin cofactor II.	Monosaccharides	56-70	serpin family C member 1	Homo sapiens	94-106
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
3408716-2	1988	These forms have two chains disulfide linked and are of the same molecular weight as native antithrombin III.	Disulfides	28-37	serpin family C member 1	Homo sapiens	92-108
3408716-3	1988	1H NMR spectroscopy has been used to characterize these proteins and to compare them to one another and to native antithrombin III.	Hydrogen	0-2	serpin family C member 1	Homo sapiens	114-130
3414028-0	1988	[Blood antithrombin III levels after prolonged administration of heparin].	Heparin	65-72	serpin family C member 1	Homo sapiens	7-23
3162733-1	1988	Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow.	Histidine	90-99	serpin family C member 1	Homo sapiens	103-115
3162733-5	1988	Following treatment of these pools with trypsin, fast atom bombardment mass spectrometry identified tryptic peptides (found also in normal antithrombin treated in the same way) that corresponded to amino acid sequences Gly339-Lys370 and Val400-Met423.	Peptides	108-116	serpin family C member 1	Homo sapiens	139-151
3162733-6	1988	The tryptic peptides, corresponding to amino acid sequences Ala371-Arg393 and Ser394-Arg399 were present in both variant preparations in greatly reduced amounts compared to a normal antithrombin preparation.	Peptides	12-20	serpin family C member 1	Homo sapiens	182-194
3162733-7	1988	However, two novel tryptic peptides of molecular mass (M + H)+ 2976 and 2952 were identified in the digests of antithrombin Northwick Park and Glasgow, respectively.	Peptides	27-35	serpin family C member 1	Homo sapiens	111-123
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
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
3360140-3	1988	Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl.	Sepharose	60-69	serpin family C member 1	Homo sapiens	0-12
3360140-3	1988	Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl.	Sodium Chloride	137-141	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
3260695-1	1988	Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction.	Arginine	51-59	serpin family C member 1	Homo sapiens	0-16
3044341-3	1988	The AT III expression vectors carrying the hCMV enhancer were used to establish stable BHK cell-lines by a new and fast G418/methotrexate selection protocol, which express up to 12 micrograms AT III/10(6) cells/24h after 40-50 days.	antibiotic G 418	120-124	serpin family C member 1	Homo sapiens	4-10
3044341-3	1988	The AT III expression vectors carrying the hCMV enhancer were used to establish stable BHK cell-lines by a new and fast G418/methotrexate selection protocol, which express up to 12 micrograms AT III/10(6) cells/24h after 40-50 days.	Methotrexate	125-137	serpin family C member 1	Homo sapiens	4-10
3345487-4	1988	The reduced antithrombin III activity previously described in patients receiving tamoxifen for metastatic breast cancer may reflect disease activity rather than a direct effect of tamoxifen on blood coagulation.	Tamoxifen	81-90	serpin family C member 1	Homo sapiens	12-28
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.	Glycosaminoglycans	40-58	serpin family C member 1	Homo sapiens	142-154
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
3349100-2	1988	AT-III, isolated from normal human plasma by means of heparin affinity and ion-exchange chromatography, was incubated with 0-0.5 M glucose in neutral phosphate buffer at 37 degrees C. The extent of non-enzymatic glycation could be monitored by uptake of radioactivity as well as by binding to a phenylboronate affinity resin, which effectively retards AT-III containing ketoamine-linked glucose.	Glucose	131-138	serpin family C member 1	Homo sapiens	0-6
3349100-6	1988	Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule.	Carbon-14	27-30	serpin family C member 1	Homo sapiens	123-129
3349100-6	1988	Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule.	Glucose	31-38	serpin family C member 1	Homo sapiens	123-129
3349100-6	1988	Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule.	Cyanogen Bromide	63-79	serpin family C member 1	Homo sapiens	123-129
3349100-6	1988	Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule.	Carbon-14	147-150	serpin family C member 1	Homo sapiens	123-129
3349100-6	1988	Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule.	Glucose	151-158	serpin family C member 1	Homo sapiens	123-129
3348170-6	1988	After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference.	Sodium Nitrite	6-11	serpin family C member 1	Homo sapiens	108-114
3348170-6	1988	After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference.	Dermatan Sulfate	37-39	serpin family C member 1	Homo sapiens	108-114
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
3348170-8	1988	With commercially available reagents, both NaNO2/acetic acid treatment of DS and anti-AT-III treatment of plasma were needed to eliminate heparin/AT-III interference.	Acetic Acid	49-60	serpin family C member 1	Homo sapiens	146-152
3383824-5	1988	Negative associations between alcohol, fibrinogen and antithrombin III and positive associations between fibre, polyunsaturated fat and antithrombin III are of possible clinical or public health importance.	Alcohols	30-37	serpin family C member 1	Homo sapiens	54-70
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
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
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
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
3342861-0	1988	Correlation between plasma levels of selenium and antithrombin-III.	Selenium	37-45	serpin family C member 1	Homo sapiens	50-66
3342861-2	1988	Patients and controls showed a positive correlation between AT-III and selenium levels (r = 0.27, p = 0.015).	Selenium	71-79	serpin family C member 1	Homo sapiens	60-66
3342861-5	1988	The increased AT-III levels were correlated with the use of warfarin and beta blockers in the patients, but these drugs could not explain the comparatively low selenium levels in the patients.	Warfarin	60-68	serpin family C member 1	Homo sapiens	14-20
3342861-9	1988	The relation between AT-III and selenium should be further evaluated.	Selenium	32-40	serpin family C member 1	Homo sapiens	21-27
3166432-12	1988	At 5 U/ml (approximately 8.6 x 10(-8) M) antithrombin III markedly inhibited contractions of basilar arteries to prostaglandin E2 but had no effect of contractions elicited by 10(-6) M serotonin in the umbilical artery, nor did aprotinin (5 x 10(-4) M).	Dinoprostone	113-129	serpin family C member 1	Homo sapiens	41-57
3166432-12	1988	At 5 U/ml (approximately 8.6 x 10(-8) M) antithrombin III markedly inhibited contractions of basilar arteries to prostaglandin E2 but had no effect of contractions elicited by 10(-6) M serotonin in the umbilical artery, nor did aprotinin (5 x 10(-4) M).	Serotonin	185-194	serpin family C member 1	Homo sapiens	41-57
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.	Polyvinyl Alcohol	64-81	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
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
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.	Epinephrine	76-86	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
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.	Sepharose	59-68	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
3363529-5	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.	cief	248-252	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
3349502-0	1988	Synthesis of methyl glycoside derivatives of tri- and penta-saccharides related to the antithrombin III-binding sequence of heparin, employing cellobiose as a key starting-material.	Methylglycosides	13-29	serpin family C member 1	Homo sapiens	87-103
3349502-0	1988	Synthesis of methyl glycoside derivatives of tri- and penta-saccharides related to the antithrombin III-binding sequence of heparin, employing cellobiose as a key starting-material.	tri- and penta-saccharides	45-71	serpin family C member 1	Homo sapiens	87-103
3349502-6	1988	The pentasaccharide 3 binds strongly to antithrombin III with an association constant almost equivalent to that of high-affinity heparin, but the trisaccharide 4 appears not to bind.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	40-56
3178141-3	1988	Genetically determined structural polymorphism of antithrombin III has been observed using ultra narrow pH polyacrylamide isoelectric focusing gels, followed by immunoblotting.	polyacrylamide	107-121	serpin family C member 1	Homo sapiens	50-66
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
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
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
2465220-0	1988	Investigations of antithrombin III-activity in patients after myocardial infarction and a long-term coumarin therapy.	coumarin	100-108	serpin family C member 1	Homo sapiens	18-34
2465220-5	1988	However, we were unable to confirm the comparatively marked increase AT III for dicoumarol treatment found by Roka and Bleyl.	Dicumarol	80-90	serpin family C member 1	Homo sapiens	69-75
2465220-7	1988	Our values of the mean AT III-activity were in the lower normal range for patients with long-term coumarin therapy.	coumarin	98-106	serpin family C member 1	Homo sapiens	23-29
3260695-1	1988	Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction.	Arginine	51-59	serpin family C member 1	Homo sapiens	18-24
3260695-1	1988	Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction.	Serine	60-66	serpin family C member 1	Homo sapiens	0-16
3260695-1	1988	Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction.	Serine	60-66	serpin family C member 1	Homo sapiens	18-24
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
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.	Adenosine Diphosphate	13-16	serpin family C member 1	Homo sapiens	144-160
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
3335825-8	1988	The titer of antithrombin III was reduced in the group given 20 micrograms ethinyl estradiol, but not in the groups given 5 or 10 micrograms.	Ethinyl Estradiol	75-92	serpin family C member 1	Homo sapiens	13-29
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
3041550-3	1988	Increased activity of vitamin K-dependent clotting factors partially counterbalanced by a rather high level of antithrombin III were also detected.	Vitamin K	22-31	serpin family C member 1	Homo sapiens	111-127
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
3132590-4	1988	AT III isoforms were examined by isoelectric focusing in polyacrylamide gels (IEF/PA) and immunoblotting, and no changes were observed throughout the study period.	polyacrylamide	57-71	serpin family C member 1	Homo sapiens	0-6
3121595-7	1987	259, 935-938) have shown that selective chemical modification of a limited number of lysine residues in antithrombin III causes drastic loss of its heparin cofactor activity.	Lysine	85-91	serpin family C member 1	Homo sapiens	104-120
3121595-8	1987	We have performed chemical modification of antithrombin III with trinitrobenzene sulfonic acid in order to determine the location of these lysine residues.	Trinitrobenzenesulfonic Acid	65-94	serpin family C member 1	Homo sapiens	43-59
3121595-8	1987	We have performed chemical modification of antithrombin III with trinitrobenzene sulfonic acid in order to determine the location of these lysine residues.	Lysine	139-145	serpin family C member 1	Homo sapiens	43-59
3121595-9	1987	When antithrombin III was treated with 100 M excess of trinitrobenzene sulfonic acid for 10 min, about 3.2 mol of amino group per mol of antithrombin III were modified.	Trinitrobenzenesulfonic Acid	55-84	serpin family C member 1	Homo sapiens	5-21
3121595-9	1987	When antithrombin III was treated with 100 M excess of trinitrobenzene sulfonic acid for 10 min, about 3.2 mol of amino group per mol of antithrombin III were modified.	Trinitrobenzenesulfonic Acid	55-84	serpin family C member 1	Homo sapiens	137-153
3121595-12	1987	These results were obtained by comparing and analyzing the cyanogen bromide fragments derived from native antithrombin III and the 10-min modified antithrombin III.	Cyanogen Bromide	59-75	serpin family C member 1	Homo sapiens	106-122
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
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%).	Trinitrobenzenesulfonic Acid	63-92	serpin family C member 1	Homo sapiens	5-21
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
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
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
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
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
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
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
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
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.	pentasaccharide	221-236	serpin family C member 1	Homo sapiens	200-212
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.	pentasaccharide	90-105	serpin family C member 1	Homo sapiens	121-133
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
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.	Heparitin Sulfate	159-174	serpin family C member 1	Homo sapiens	200-212
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
3426230-10	1987	HCII differs from antithrombin III, which contains an essential disulfide bond for heparin-dependent thrombin inhibition (Longas, M. O., et al.	Disulfides	64-73	serpin family C member 1	Homo sapiens	18-34
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
3680513-5	1987	The mean F1 + 2 level in antithrombin-deficient individuals on warfarin was significantly elevated (mean = 0.714 nM) as compared with that in anticoagulated subjects with protein C deficiency (mean = 0.205 nM) or in those without an inherited thrombotic disorder (P less than 0.01) at equivalent levels of intensity of oral anticoagulation.	Warfarin	63-71	serpin family C member 1	Homo sapiens	25-37
3680513-6	1987	We therefore conclude that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-antithrombin mechanism.	Warfarin	41-49	serpin family C member 1	Homo sapiens	129-141
3680513-6	1987	We therefore conclude that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-antithrombin mechanism.	Heparitin Sulfate	113-128	serpin family C member 1	Homo sapiens	129-141
3689206-0	1987	Modulation of glycosaminoglycan production and antithrombin III binding by cultured aortic endothelial cells treated with 4-methylumbelliferyl-beta-D-xyloside.	methylumbelliferyl-beta-D-xyloside	122-158	serpin family C member 1	Homo sapiens	47-63
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
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.	Heparitin Sulfate	91-106	serpin family C member 1	Homo sapiens	153-169
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.	Heparitin Sulfate	179-194	serpin family C member 1	Homo sapiens	153-169
3689206-5	1987	Incubation of cell cultures with beta-D-xyloside resulted in a reduction of maximum antithrombin III binding by approximately 65% with little alteration in binding affinity.	xylosides	33-48	serpin family C member 1	Homo sapiens	84-100
3689206-8	1987	Whereas the size of heparan sulfate chains derived from the cell surface was not altered by xyloside treatment, they appeared to have slightly less net negative charge and a significantly reduced proportion of the molecule with high affinity for antithrombin III in the presence of xyloside.	Heparitin Sulfate	20-35	serpin family C member 1	Homo sapiens	246-262
3689206-11	1987	These results suggest that beta-D-xyloside caused a dose-dependent decrease in production as well as some subtle structural alterations of cell-surface-associated heparan sulfate, which could serve as binding sites for antithrombin III on the endothelial cells and mediate enhancing the anticoagulant activity of this protein.	xylosides	27-42	serpin family C member 1	Homo sapiens	219-235
3689206-11	1987	These results suggest that beta-D-xyloside caused a dose-dependent decrease in production as well as some subtle structural alterations of cell-surface-associated heparan sulfate, which could serve as binding sites for antithrombin III on the endothelial cells and mediate enhancing the anticoagulant activity of this protein.	Heparitin Sulfate	163-178	serpin family C member 1	Homo sapiens	219-235
3427019-0	1987	Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III.	3-o	16-19	serpin family C member 1	Homo sapiens	107-123
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
3667601-5	1987	The fraction of biologically active ATIII has been purified from total ATIII by affinity fractionation on heparin-Sepharose.	Sepharose	114-123	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
3654616-0	1987	Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park".	Disulfides	24-33	serpin family C member 1	Homo sapiens	41-53
3654616-0	1987	Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park".	Disulfides	24-33	serpin family C member 1	Homo sapiens	76-88
3427019-0	1987	Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III.	Glucosamine	38-49	serpin family C member 1	Homo sapiens	107-123
3654616-0	1987	Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park".	Disulfides	24-33	serpin family C member 1	Homo sapiens	76-88
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
3654616-6	1987	In this communication, we present evidence that this Mr approximately 120,000 variant component is comprised of an antithrombin-albumin covalent disulfide-linked complex.	Disulfides	145-154	serpin family C member 1	Homo sapiens	115-127
3427019-2	1987	The octasaccharide produced a maximum 48% increase in intrinsic fluorescence at 37 degrees C and a rate of factor Xa inhibition of 6 X 10(5) M-1 s-1 as measured by stopped-flow fluorometry at 25 degrees C. The basal rate of the antithrombin-factor Xa interaction observed in the absence of oligosaccharide was 2 X 10(3) M-1 s-1.	Octasaccharide	4-18	serpin family C member 1	Homo sapiens	228-240
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
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
3624272-5	1987	The amidolytic and proteolytic activities of the enzyme were readily inhibited by phenylmethanesulfonyl fluoride, p-amidinophenylmethanesulfonyl fluoride, chloromethyl ketones, and human antithrombin III.	Phenylmethylsulfonyl Fluoride	82-112	serpin family C member 1	Homo sapiens	187-203
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
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
3690577-0	1987	Synthesis of heparin fragments: a methyl alpha-pentaoside with high affinity for antithrombin III.	methyl alpha-pentaoside	34-57	serpin family C member 1	Homo sapiens	81-97
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.	methyl alpha-glycoside	34-56	serpin family C member 1	Homo sapiens	189-205
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.	pentasaccharide	64-79	serpin family C member 1	Homo sapiens	189-205
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
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
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
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
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
3280421-10	1988	Antithrombin III can be isolated by linkage to its cofactor, heparin, on heparin-Sepharose.	Sepharose	81-90	serpin family C member 1	Homo sapiens	0-16
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
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
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.	Proline	102-105	serpin family C member 1	Homo sapiens	43-59
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.	Arginine	110-113	serpin family C member 1	Homo sapiens	43-59
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.	Tryptophan	121-124	serpin family C member 1	Homo sapiens	43-59
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
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.	Glutamic Acid	24-27	serpin family C member 1	Homo sapiens	255-271
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.	Glycine	28-31	serpin family C member 1	Homo sapiens	255-271
2448885-1	1987	Decreases in platelet count, fibrinogen concentration, factor VIII, antithrombin III and alpha 2-antiplasmin activities, increase in FDP-D fraction, and pleural effusion were observed transiently at early fever stage of DHF at grade II, indicating DHF patients had manifestations of the acute type of DIC with increased permeability of vascular wall.	dhf	220-223	serpin family C member 1	Homo sapiens	68-84
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
3624220-2	1987	A large portion of the polysaccharide chains of both preparations bound with high affinity to immobilized antithrombin.	Polysaccharides	23-37	serpin family C member 1	Homo sapiens	106-118
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
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
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
3607780-0	1987	Long-term adjuvant therapy with tamoxifen: effects on sex hormone binding globulin and antithrombin III.	Tamoxifen	32-41	serpin family C member 1	Homo sapiens	87-103
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
3649921-0	1987	Heparin promotes the inactivation of antithrombin by neutrophil elastase.	Heparin	0-7	serpin family C member 1	Homo sapiens	37-49
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
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
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
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
3624220-3	1987	Titrations monitored by tryptophan fluorescence showed that clam polysaccharide chains with Mr approximately 22,500 contained up to three binding sites for antithrombin and that the binding constants for the interaction of these chains with antithrombin were higher than those reported for mammalian heparin of comparable size.	Polysaccharides	65-79	serpin family C member 1	Homo sapiens	156-168
3624220-3	1987	Titrations monitored by tryptophan fluorescence showed that clam polysaccharide chains with Mr approximately 22,500 contained up to three binding sites for antithrombin and that the binding constants for the interaction of these chains with antithrombin were higher than those reported for mammalian heparin of comparable size.	Polysaccharides	65-79	serpin family C member 1	Homo sapiens	241-253
3624220-5	1987	The content of these saccharide sequences was found to increase with increasing affinity of the parent polysaccharide for antithrombin.	Carbohydrates	21-31	serpin family C member 1	Homo sapiens	122-134
3624220-5	1987	The content of these saccharide sequences was found to increase with increasing affinity of the parent polysaccharide for antithrombin.	Polysaccharides	103-117	serpin family C member 1	Homo sapiens	122-134
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
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
3663509-4	1987	Plasma from the propositus was precipitated with dextran sulphate, applied to heparin-Sepharose and the AT III stepwise eluted with NaCl.	Sodium Chloride	132-136	serpin family C member 1	Homo sapiens	104-110
3663509-5	1987	The AT III had a reduced ability to inactivate thrombin, when this was monitored by substrate hydrolysis or by SDS polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	111-114	serpin family C member 1	Homo sapiens	4-10
3663509-5	1987	The AT III had a reduced ability to inactivate thrombin, when this was monitored by substrate hydrolysis or by SDS polyacrylamide gel electrophoresis.	polyacrylamide	115-129	serpin family C member 1	Homo sapiens	4-10
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
3663509-7	1987	AT III from the patient was reapplied to heparin-Sepharose and eluted with a NaCl gradient.	Sepharose	49-58	serpin family C member 1	Homo sapiens	0-6
3663509-7	1987	AT III from the patient was reapplied to heparin-Sepharose and eluted with a NaCl gradient.	Sodium Chloride	77-81	serpin family C member 1	Homo sapiens	0-6
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
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
2955820-10	1987	Efficiency of low-mol-wt heparins to inhibit degradation of heparan sulfate in ECM decreased with their main molecular size, and a synthetic pentasaccharide, representing the binding site to antithrombin III, was devoid of inhibitory activity.	pentasaccharide	141-156	serpin family C member 1	Homo sapiens	191-207
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
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
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
3609301-0	1987	Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135.	Carbohydrates	48-60	serpin family C member 1	Homo sapiens	25-41
3609301-0	1987	Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135.	Asparagine	74-77	serpin family C member 1	Homo sapiens	25-41
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.	Sepharose	58-67	serpin family C member 1	Homo sapiens	117-129
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
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.	Oligosaccharides	140-155	serpin family C member 1	Homo sapiens	117-129
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.	Asparagine	166-169	serpin family C member 1	Homo sapiens	117-129
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
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.	Fluorescein-5-isothiocyanate	33-60	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
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
2442830-0	1987	Mechanism of potentiation of antithrombin III [AT-III] inhibition by sulfated xylans.	Xylans	78-84	serpin family C member 1	Homo sapiens	29-45
2442830-0	1987	Mechanism of potentiation of antithrombin III [AT-III] inhibition by sulfated xylans.	Xylans	78-84	serpin family C member 1	Homo sapiens	47-53
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.	Xylans	13-19	serpin family C member 1	Homo sapiens	82-88
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
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.	Pentosan Sulfuric Polyester	56-61	serpin family C member 1	Homo sapiens	82-88
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.	benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide	181-203	serpin family C member 1	Homo sapiens	82-88
2442830-4	1987	Study of the high affinity binding of the xylan sulfates to AT-III-Sepharose column showed that the amount of the xylan sulfate recovered in the eluates from this peak was greatly increased with an increase in molecular weight (MW).	Pentosan Sulfuric Polyester	42-56	serpin family C member 1	Homo sapiens	60-66
2442830-4	1987	Study of the high affinity binding of the xylan sulfates to AT-III-Sepharose column showed that the amount of the xylan sulfate recovered in the eluates from this peak was greatly increased with an increase in molecular weight (MW).	Sepharose	67-76	serpin family C member 1	Homo sapiens	60-66
2442830-4	1987	Study of the high affinity binding of the xylan sulfates to AT-III-Sepharose column showed that the amount of the xylan sulfate recovered in the eluates from this peak was greatly increased with an increase in molecular weight (MW).	Pentosan Sulfuric Polyester	42-55	serpin family C member 1	Homo sapiens	60-66
2442830-7	1987	The results also suggested an interaction between larchwood xylan sulfate and IIa which may potentiate an interaction between AT-III and IIa.	larchwood xylan sulfate	50-73	serpin family C member 1	Homo sapiens	126-132
3664518-0	1987	Conformation of the pentasaccharide corresponding to the binding site of heparin to antithrombin-III.	pentasaccharide	20-35	serpin family C member 1	Homo sapiens	84-100
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
3306136-5	1987	An increase of the activity of plasminogen, alpha 2-antiplasmin, and antithrombin III, and in the concentration of alpha 1-protease inhibitor in ascites was induced by the dexamethasone injection.	Dexamethasone	172-185	serpin family C member 1	Homo sapiens	69-85
3663595-2	1987	The denaturation of human and bovine antithrombin III by guanidine hydrochloride has been followed by 1H NMR spectroscopy.	Guanidine	57-80	serpin family C member 1	Homo sapiens	37-53
3663595-2	1987	The denaturation of human and bovine antithrombin III by guanidine hydrochloride has been followed by 1H NMR spectroscopy.	Hydrogen	102-104	serpin family C member 1	Homo sapiens	37-53
3663595-5	1987	258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III.	Histidine	155-165	serpin family C member 1	Homo sapiens	175-191
3663595-5	1987	258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III.	Histidine	155-165	serpin family C member 1	Homo sapiens	237-253
3663595-5	1987	258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III.	Histidine	216-226	serpin family C member 1	Homo sapiens	175-191
3663595-5	1987	258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III.	Histidine	216-226	serpin family C member 1	Homo sapiens	237-253
3663595-6	1987	These two histidines in human antithrombin III are assigned to residue 1 and, more tentatively, to residue 65.	Histidine	10-20	serpin family C member 1	Homo sapiens	30-46
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.	Histidine	60-69	serpin family C member 1	Homo sapiens	121-137
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
3663595-12	1987	Thermal denaturation also leads to major perturbation of these two histidine resonances in human antithrombin III, though stable intermediates in the unfolding were not detected.	Histidine	67-76	serpin family C member 1	Homo sapiens	97-113
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
3110143-0	1987	Identification of a lysyl residue in antithrombin which is essential for heparin binding.	lysyl	20-25	serpin family C member 1	Homo sapiens	37-49
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
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.	lysyl	18-23	serpin family C member 1	Homo sapiens	51-63
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
3110143-1	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.	Pyridoxal Phosphate	168-190	serpin family C member 1	Homo sapiens	51-63
3110143-2	1987	Modification of antithrombin with limiting amounts of reagent yields an average incorporation of the phosphopyridoxyl label into 1 lysine/protein molecule (Pecon, J. M., and Blackburn, M. N. (1984) J. Biol.	phosphopyridoxyl	101-117	serpin family C member 1	Homo sapiens	16-28
3110143-2	1987	Modification of antithrombin with limiting amounts of reagent yields an average incorporation of the phosphopyridoxyl label into 1 lysine/protein molecule (Pecon, J. M., and Blackburn, M. N. (1984) J. Biol.	Lysine	131-137	serpin family C member 1	Homo sapiens	16-28
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
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.	Sepharose	80-89	serpin family C member 1	Homo sapiens	29-41
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.	Sepharose	80-89	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
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
3110143-9	1987	This peptide corresponds to a tryptic fragment including residues 115-129 in the sequence of antithrombin, with the modified residue identified as Lys-125.	Lysine	147-150	serpin family C member 1	Homo sapiens	93-105
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
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.	Lysine	32-38	serpin family C member 1	Homo sapiens	141-153
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
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
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.	Disulfides	203-212	serpin family C member 1	Homo sapiens	141-153
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
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
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.	hydroxy-nitrobenzyl	4-23	serpin family C member 1	Homo sapiens	205-221
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.	(2S,5R)-5-pentyltetrahydrofuran-2-ol	25-28	serpin family C member 1	Homo sapiens	205-221
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.	Tryptophan	57-67	serpin family C member 1	Homo sapiens	205-221
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.	Tryptophan	30-40	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.	hydroxynitrobenzyl	69-87	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	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
3584126-11	1987	Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin.	hydroxynitrobenzyl	28-46	serpin family C member 1	Homo sapiens	90-102
3584126-11	1987	Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin.	hydroxynitrobenzyl	28-46	serpin family C member 1	Homo sapiens	218-230
3584126-11	1987	Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin.	Tryptophan	73-83	serpin family C member 1	Homo sapiens	90-102
3584126-11	1987	Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin.	Tryptophan	73-83	serpin family C member 1	Homo sapiens	218-230
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
3584127-4	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.	Sepharose	98-107	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
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
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
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
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
2955807-0	1987	Comparative effect of heparin and heparan sulphate on two abnormal antithrombin III type 3 variants.	Heparitin Sulfate	34-50	serpin family C member 1	Homo sapiens	67-83
2955807-2	1987	The abnormal species were purified using affinity chromatography on Sepharose bound anti-AT III antibodies.	Sepharose	68-77	serpin family C member 1	Homo sapiens	89-95
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
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.	Heparitin Sulfate	116-132	serpin family C member 1	Homo sapiens	151-157
2955807-7	1987	At this concentration of heparan sulphate the two abnormal AT III still exhibit a heparin cofactor activity below 10%.	Heparitin Sulfate	25-41	serpin family C member 1	Homo sapiens	59-65
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
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
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
2955307-0	1987	[Effect of a cyproterone-estradiol combination administered cutaneously on antithrombin III].	cyproterone-estradiol	13-34	serpin family C member 1	Homo sapiens	75-91
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
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
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
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
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
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
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
3567355-4	1987	By heparin-Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl.	Sepharose	11-20	serpin family C member 1	Homo sapiens	37-43
3567355-4	1987	By heparin-Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl.	Sodium Chloride	138-142	serpin family C member 1	Homo sapiens	37-43
3494558-1	1987	Our observation that the effect of a patient"s autoantibody with a potent antithrombin activity could be inhibited by toluidine blue and methylene blue led us to investigate the effect of these dyes in several immunochemical reactions in vitro.	Tolonium Chloride	118-132	serpin family C member 1	Homo sapiens	74-86
3494558-1	1987	Our observation that the effect of a patient"s autoantibody with a potent antithrombin activity could be inhibited by toluidine blue and methylene blue led us to investigate the effect of these dyes in several immunochemical reactions in vitro.	Methylene Blue	137-151	serpin family C member 1	Homo sapiens	74-86
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
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.	Glutamic Acid	50-53	serpin family C member 1	Homo sapiens	255-271
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.	Alanine	54-57	serpin family C member 1	Homo sapiens	255-271
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.	Glutamic Acid	50-53	serpin family C member 1	Homo sapiens	255-271
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.	Leucine	83-86	serpin family C member 1	Homo sapiens	255-271
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.	Glutamic Acid	50-53	serpin family C member 1	Homo sapiens	255-271
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.	Alanine	197-200	serpin family C member 1	Homo sapiens	255-271
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.	Glutamic Acid	50-53	serpin family C member 1	Homo sapiens	255-271
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.	Leucine	213-216	serpin family C member 1	Homo sapiens	255-271
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
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
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
3572202-7	1987	The AT III recovered in urine was almost all inactive, as demonstrated by the quantitative assays and by the H-CIE runs; on the contrary, the findings obtained by functional assays, H-CIE, and CIEF runs on dialysate samples failed to demonstrate any major alteration in the AT III molecule.	h-cie	109-114	serpin family C member 1	Homo sapiens	4-10
3572202-7	1987	The AT III recovered in urine was almost all inactive, as demonstrated by the quantitative assays and by the H-CIE runs; on the contrary, the findings obtained by functional assays, H-CIE, and CIEF runs on dialysate samples failed to demonstrate any major alteration in the AT III molecule.	h-cie	182-187	serpin family C member 1	Homo sapiens	4-10
3603738-0	1987	[Antithrombin activity of methyl esters of arginine-containing peptides].	methyl esters	26-39	serpin family C member 1	Homo sapiens	1-13
3603738-0	1987	[Antithrombin activity of methyl esters of arginine-containing peptides].	Arginine	43-51	serpin family C member 1	Homo sapiens	1-13
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
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
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
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
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.	Pentosan Sulfuric Polyester	50-71	serpin family C member 1	Homo sapiens	135-151
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.	Phospholipids	52-64	serpin family C member 1	Homo sapiens	190-206
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
3580302-4	1987	Furthermore, this variant component is present in plasma as an approximately 120,000 MW inactive antithrombin III complex that can be reduced with dithiothreitol to MW approximately 60,000, indicating disulphide bridging.	Dithiothreitol	147-161	serpin family C member 1	Homo sapiens	97-113
3580302-4	1987	Furthermore, this variant component is present in plasma as an approximately 120,000 MW inactive antithrombin III complex that can be reduced with dithiothreitol to MW approximately 60,000, indicating disulphide bridging.	disulphide	201-211	serpin family C member 1	Homo sapiens	97-113
3581111-2	1987	experiments conducted on synthetic fragments of glycosaminoglycans, one of them representing the pentasaccharidic sequence present in heparin and responsible for the binding to antithrombin III, and the others being related to this sequence.	Glycosaminoglycans	48-66	serpin family C member 1	Homo sapiens	177-193
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
3606566-8	1987	Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS.	polyacrylamide	180-194	serpin family C member 1	Homo sapiens	56-72
3606566-8	1987	Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS.	Sodium Dodecyl Sulfate	242-245	serpin family C member 1	Homo sapiens	56-72
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
3603409-6	1987	Affinity chromatography on heparin-Sepharose revealed two populations of AT III, one of which was devoid of heparin cofactor activity.	Sepharose	35-44	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
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
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.	estrogen-progesterone	425-446	serpin family C member 1	Homo sapiens	42-58
3615614-3	1987	Anti-vitamin K treatment is the only effective therapy proposed to patients suffering from a hereditary deficiency in antithrombin III.	Vitamin K	5-14	serpin family C member 1	Homo sapiens	118-134
3590108-0	1987	Affinity of antithrombin III for insoluble modified polystyrene.	Polystyrenes	52-63	serpin family C member 1	Homo sapiens	12-28
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.	Polystyrenes	34-46	serpin family C member 1	Homo sapiens	169-175
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
3590108-9	1987	When thrombin is adsorbed on the surface of the polymer, AT III cannot interact with the specific seryl residue of the enzyme.	Polymers	48-55	serpin family C member 1	Homo sapiens	57-63
3826410-1	1987	Unlike in the case of some other species, the plasma curve of iodine-labeled antithrombin III (I-AT-III) in rabbits requires fitting with a three-term exponential function for obtaining reliable estimates of the catabolic rate and distribution of I-AT-III among various body compartments (Carlson, Atencio, and Simon.	Iodine	62-68	serpin family C member 1	Homo sapiens	97-103
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.	sephadex	0-8	serpin family C member 1	Homo sapiens	206-222
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.	carboxymethyl-coenzyme A	29-42	serpin family C member 1	Homo sapiens	206-222
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.	benzylamine	56-67	serpin family C member 1	Homo sapiens	206-222
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
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
3567176-2	1987	1H NMR has been used to characterize and compare the structures of antithrombin III from human, bovine, and porcine plasma as well as to investigate the interactions of each of these proteins with heparin fragments of defined length.	Hydrogen	0-2	serpin family C member 1	Homo sapiens	67-83
3801671-9	1987	Interaction of thrombin Tokushima with antithrombin III was much slower than "thrombin" when followed by SDS-PAGE.	Sodium Dodecyl Sulfate	105-108	serpin family C member 1	Homo sapiens	39-55
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
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
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
3812468-0	1987	An autoantibody with potent antithrombin activity whose action could be inhibited by toluidine blue or methylene blue.	Tolonium Chloride	85-99	serpin family C member 1	Homo sapiens	28-40
3812468-0	1987	An autoantibody with potent antithrombin activity whose action could be inhibited by toluidine blue or methylene blue.	Methylene Blue	103-117	serpin family C member 1	Homo sapiens	28-40
3812468-5	1987	However, the antithrombin activity of this anticoagulant could be neutralized by toluidine blue or methylene blue ex vivo.	Tolonium Chloride	81-95	serpin family C member 1	Homo sapiens	13-25
3812468-5	1987	However, the antithrombin activity of this anticoagulant could be neutralized by toluidine blue or methylene blue ex vivo.	Methylene Blue	99-113	serpin family C member 1	Homo sapiens	13-25
3569629-0	1987	Daily rapid blood glucose variations may condition antithrombin III biologic activity but not its plasma concentration in insulin-dependent diabetes.	Blood Glucose	12-25	serpin family C member 1	Homo sapiens	51-67
3569629-3	1987	The variations of both plasma glucose and labile HbA1 were inversely correlated to the alterations of ATIII activity (r = -0.71 and r = -0.73, respectively, p less than 0.001), while no change in ATIII plasma concentration was present.	Glucose	30-37	serpin family C member 1	Homo sapiens	102-107
3569629-4	1987	These data suggest a direct role of glucose in determining rapid alteration of ATIII biologic activity, in vivo, in diabetes, probably mediated by labile non-enzymatic glycation.	Glucose	36-43	serpin family C member 1	Homo sapiens	79-84
2433298-5	1987	AT III (1-6 U/ml) reduced basal tone and significantly inhibited, in a concentration-dependent manner, the contractile responses to K+, 5-HT, PGD2, PGF2 alpha, and plasmin.	Prostaglandin D2	142-146	serpin family C member 1	Homo sapiens	0-6
2433298-5	1987	AT III (1-6 U/ml) reduced basal tone and significantly inhibited, in a concentration-dependent manner, the contractile responses to K+, 5-HT, PGD2, PGF2 alpha, and plasmin.	Dinoprost	148-152	serpin family C member 1	Homo sapiens	0-6
2433298-1	1987	Isolated human basilar arteries were used in this study to evaluate the inhibitory effect of antithrombin III (AT III), thrombin, and alpha 2-macroglobulin (alpha 2-M) on contractions elicited by K+, serotonin (5-HT), prostaglandin (PG) D2, PGF2 alpha, and plasmin.	Serotonin	200-209	serpin family C member 1	Homo sapiens	93-109
3602050-3	1987	In contrast to the antithrombin activity, toxicity and side effects of the amidino compounds are not dependent on the position of the amidino group within the molecule.	amidino	75-82	serpin family C member 1	Homo sapiens	19-31
2955429-5	1987	Introduction of amino acids between the arylsulfonyl blocking group and amino nitrogen influence particularly the antithrombin activity.	hydrazine	72-86	serpin family C member 1	Homo sapiens	114-126
2955429-8	1987	It is concluded that the N alpha-moiety is of decisive importance for the antithrombin activity of derivatives of 4-amidinophenylalanine.	4-carbamimidoyl-L-phenylalanine	114-136	serpin family C member 1	Homo sapiens	74-86
3105116-3	1987	Sephacryl S-200 gel chromatography of serum demonstrated that the neoantigen eluted with the first two, early eluting protein peaks; thus the neoantigen had a higher molecular weight than native antithrombin.	sephacryl S 200	0-15	serpin family C member 1	Homo sapiens	195-207
3105116-5	1987	Sephacryl S-200 chromatography of factor IX concentrate-treated hemophilic plasma also showed an early eluting peak of antithrombin antigen of more cathodal mobility than normal in crossed immunoelectrophoresis.	sephacryl s	0-11	serpin family C member 1	Homo sapiens	119-131
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
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
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.	125i-fluoresceinamine	0-21	serpin family C member 1	Homo sapiens	152-168
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
3619144-6	1987	II is likely that its antithrombin activity in vivo is restricted to the areas rich in dermatan sulfate.	Dermatan Sulfate	87-103	serpin family C member 1	Homo sapiens	22-34
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
2441925-4	1987	Polysaccharides are antithrombin-III and heparin co-factor-II dependent or independent regarding their biological activity.	Polysaccharides	0-15	serpin family C member 1	Homo sapiens	20-36
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
3783325-4	1986	During pyridoxine treatment, antithrombin III activity was rapidly restored to normal; factor VII increased and beta-thromboglobulin decreased.	Pyridoxine	7-17	serpin family C member 1	Homo sapiens	29-45
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
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
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
3563966-4	1986	A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography.	Sepharose	76-85	serpin family C member 1	Homo sapiens	21-37
3563966-5	1986	Affinity adsorption of the propositus" plasma to human alpha-thrombin immobilized on sepharose beads revealed defective binding of the antithrombin III to thrombin-sepharose.	Sepharose	164-173	serpin family C member 1	Homo sapiens	135-151
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
3114102-3	1987	Crossed immunoelectrophoresis of AT III on heparin-agarose was also carried out in plasma and serum.	Sepharose	51-58	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
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
3114102-7	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.	Sepharose	123-130	serpin family C member 1	Homo sapiens	105-111
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.	Sepharose	123-130	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
3817736-9	1987	In the antithrombin III group and the antithrombin III plus heparin group, however, creatinine clearance was moderately elevated while FENa and CH2O remained unchanged as compared with the values before the burn.	Creatinine	84-94	serpin family C member 1	Homo sapiens	38-54
3817736-10	1987	The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, creatinine clearance and CH2O.	Creatinine	121-131	serpin family C member 1	Homo sapiens	4-20
3817736-10	1987	The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, creatinine clearance and CH2O.	Formaldehyde	146-150	serpin family C member 1	Homo sapiens	4-20
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
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
2444745-0	1987	[A modified method of determining antithrombin III activity by diffusion in thrombin agarose].	Sepharose	85-92	serpin family C member 1	Homo sapiens	34-50
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
2436331-2	1986	Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively.	Pentosan Sulfuric Polyester	12-32	serpin family C member 1	Homo sapiens	81-87
2436331-2	1986	Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively.	Pentosan Sulfuric Polyester	34-37	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
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
2432917-3	1986	The SPS varied in their relative activities as catalysts of thrombin inhibition by purified AT III or HC II.	Sodium phenolsulfonate	4-7	serpin family C member 1	Homo sapiens	92-98
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
2432917-4	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.	Dermatan Sulfate	44-61	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
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
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
3782075-1	1986	Oligosaccharides (10-20 monosaccharide units) with high affinity for antithrombin, as well as larger high-affinity heparin fractions (having relative molecular masses between 6,000 and 21,500), all markedly accelerated the inhibition of Factor Xa by antithrombin.	Oligosaccharides	0-16	serpin family C member 1	Homo sapiens	69-81
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.	Oligosaccharides	28-44	serpin family C member 1	Homo sapiens	133-145
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
3782075-3	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.	Monosaccharides	70-84	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.	Monosaccharides	70-84	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.	octadecasaccharide	66-84	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	109-117	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
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.	Monosaccharides	277-291	serpin family C member 1	Homo sapiens	52-64
3771538-5	1986	This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III.	hexasaccharide	5-19	serpin family C member 1	Homo sapiens	249-265
3771538-5	1986	This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III.	heparin oligosaccharides	125-149	serpin family C member 1	Homo sapiens	46-62
3771538-5	1986	This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III.	heparin oligosaccharides	125-149	serpin family C member 1	Homo sapiens	249-265
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
2432917-7	1986	The anticoagulant activities of these last four SPS in plasma depleted of both AT III and HC II were similar to their respective activities in normal plasma.	Sodium phenolsulfonate	48-51	serpin family C member 1	Homo sapiens	79-85
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
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
3771538-5	1986	This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III.	hexasaccharide	5-19	serpin family C member 1	Homo sapiens	46-62
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
2432675-4	1986	On the other hand, dextran sulfate accelerated antithrombin III-thrombin reaction only about 40-fold less than heparin.	Dextran Sulfate	19-34	serpin family C member 1	Homo sapiens	47-63
2429788-5	1986	Incubation of normal plasma with 250 nmol/l glucose (a level approximately 6 X higher than encountered in uncontrolled diabetes) resulted in a 17% and 6% decrease in antithrombin III and alpha 1-proteinase inhibitor activities.	Glucose	44-51	serpin family C member 1	Homo sapiens	166-182
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
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
3790498-4	1986	When both factor Va and phospholipid were present during prothrombin activation, factor Xa inhibition by antithrombin III was reduced about 10-fold, with a second-order rate constant of 1.3 X 10(5) M-1 min-1.	Phospholipids	24-36	serpin family C member 1	Homo sapiens	105-121
3790498-5	1986	Factor Xa in the prothrombin activation mixture that contained both factor Va and phospholipid was even more protected from inhibition by the antithrombin III-heparin complex.	Phospholipids	82-94	serpin family C member 1	Homo sapiens	142-158
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
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.	Phospholipids	190-202	serpin family C member 1	Homo sapiens	60-76
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
2432885-10	1986	Synthetic pentasaccharides, bearing the minimal sequence for binding to antithrombin III, did not bind to endothelial cells.	pentasaccharides	10-26	serpin family C member 1	Homo sapiens	72-88
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
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
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
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.	IC 831423	32-55	serpin family C member 1	Homo sapiens	79-95
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
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
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.	Carbohydrates	49-62	serpin family C member 1	Homo sapiens	148-160
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
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.	Tryptophan	192-195	serpin family C member 1	Homo sapiens	148-160
2425853-2	1986	Affinity chromatography of the fraction with antithrombin III-agarose yielded two chondroitin sulfate proteoglycans of a non-binding (proteoglycan IA) and binding (proteoglycan IB) nature.	Sepharose	62-69	serpin family C member 1	Homo sapiens	45-61
2425853-2	1986	Affinity chromatography of the fraction with antithrombin III-agarose yielded two chondroitin sulfate proteoglycans of a non-binding (proteoglycan IA) and binding (proteoglycan IB) nature.	Chondroitin Sulfates	82-101	serpin family C member 1	Homo sapiens	45-61
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
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
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
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
3775688-4	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.	pentasaccharide	91-106	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
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
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.	Sodium Chloride	128-132	serpin family C member 1	Homo sapiens	241-247
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
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
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.	Sepharose	129-138	serpin family C member 1	Homo sapiens	203-215
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
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
3731451-0	1986	Polyethylene glycol can be validly omitted from chromogenic peptide substrate assay for antithrombin III.	Polyethylene Glycols	0-19	serpin family C member 1	Homo sapiens	88-104
3731451-1	1986	To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants.	Polysorbates	161-169	serpin family C member 1	Homo sapiens	72-88
3731451-1	1986	To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants.	Polysorbates	161-169	serpin family C member 1	Homo sapiens	100-116
3731451-1	1986	To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants.	Polyethylene Glycols	173-192	serpin family C member 1	Homo sapiens	72-88
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
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.	Sodium Chloride	59-74	serpin family C member 1	Homo sapiens	136-152
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.	Salts	26-30	serpin family C member 1	Homo sapiens	81-97
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
3095926-0	1986	Acetylation of antithrombin III by aspirin.	Aspirin	35-42	serpin family C member 1	Homo sapiens	15-31
3095926-2	1986	Since aspirin (acetylsalicylic acid) is known to acetylate numerous biologic macromolecules, the effect of aspirin on antithrombin III was investigated.	Aspirin	107-114	serpin family C member 1	Homo sapiens	118-134
3095926-3	1986	It was found that antithrombin III is irreversibly inactivated by treatment with aspirin.	Aspirin	81-88	serpin family C member 1	Homo sapiens	18-34
3095926-8	1986	Amino group analysis of aspirin-treated antithrombin III using trinitrobenzenesulfonic acid revealed that one to two primary amino groups are lost relative to the untreated antithrombin III.	Aspirin	24-31	serpin family C member 1	Homo sapiens	40-56
3095926-8	1986	Amino group analysis of aspirin-treated antithrombin III using trinitrobenzenesulfonic acid revealed that one to two primary amino groups are lost relative to the untreated antithrombin III.	Aspirin	24-31	serpin family C member 1	Homo sapiens	173-189
3095926-8	1986	Amino group analysis of aspirin-treated antithrombin III using trinitrobenzenesulfonic acid revealed that one to two primary amino groups are lost relative to the untreated antithrombin III.	Trinitrobenzenesulfonic Acid	63-91	serpin family C member 1	Homo sapiens	40-56
3095926-9	1986	It is concluded that the reaction of aspirin with antithrombin III results in specific acetylation of lysine residues.	Aspirin	37-44	serpin family C member 1	Homo sapiens	50-66
3095926-9	1986	It is concluded that the reaction of aspirin with antithrombin III results in specific acetylation of lysine residues.	Lysine	102-108	serpin family C member 1	Homo sapiens	50-66
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
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
3526065-1	1986	Urinary antithrombin III (AT III) related antigen was analyzed by SDS-polyacrylamide gel electrophoresis and Western blotting, and the nitrocellulose membrane was scanned with a 2-wavelength TLC scanner.	Sodium Dodecyl Sulfate	66-69	serpin family C member 1	Homo sapiens	26-32
3526065-1	1986	Urinary antithrombin III (AT III) related antigen was analyzed by SDS-polyacrylamide gel electrophoresis and Western blotting, and the nitrocellulose membrane was scanned with a 2-wavelength TLC scanner.	polyacrylamide	70-84	serpin family C member 1	Homo sapiens	26-32
3526065-5	1986	Further, the "index" revealed a significant proportional correlation with the total bilirubin and direct bilirubin, and also a significant inversely proportional correlation with the plasma AT III, suggesting that the "index" tends to become higher as liver function decreases.	Bilirubin	84-93	serpin family C member 1	Homo sapiens	190-196
3526065-5	1986	Further, the "index" revealed a significant proportional correlation with the total bilirubin and direct bilirubin, and also a significant inversely proportional correlation with the plasma AT III, suggesting that the "index" tends to become higher as liver function decreases.	Bilirubin	105-114	serpin family C member 1	Homo sapiens	190-196
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
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.	polyvinyl sulfate	38-64	serpin family C member 1	Homo sapiens	94-100
3738862-1	1986	The changes that take place when a therapeutic antithrombin III (AT III) concentrate is heated in the presence of citrate ion have been assessed.	Citric Acid	114-121	serpin family C member 1	Homo sapiens	47-63
3738862-1	1986	The changes that take place when a therapeutic antithrombin III (AT III) concentrate is heated in the presence of citrate ion have been assessed.	Citric Acid	114-121	serpin family C member 1	Homo sapiens	65-71
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
3733936-1	1986	Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates.	cross	0-5	serpin family C member 1	Homo sapiens	89-105
3733936-1	1986	Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates.	Polystyrenes	13-25	serpin family C member 1	Homo sapiens	89-105
3733936-1	1986	Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates.	l-arginyl methyl ester	40-62	serpin family C member 1	Homo sapiens	89-105
3754869-5	1986	Complex formation between S-protein and thrombin, and between S-protein, thrombin, and ATIII, was demonstrated by agarose gel electrophoresis and by two-dimensional immunoelectrophoresis of purified proteins and in recalcified, clotted plasma.	Sepharose	114-121	serpin family C member 1	Homo sapiens	87-92
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
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
3486013-5	1986	These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor.	sodium dodecyl sulfatepolyacrylamide	143-179	serpin family C member 1	Homo sapiens	105-117
3486013-5	1986	These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor.	Sodium Dodecyl Sulfate	201-204	serpin family C member 1	Homo sapiens	105-117
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
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
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
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.	polyacrylamide	179-193	serpin family C member 1	Homo sapiens	64-80
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.	Sodium Dodecyl Sulfate	233-255	serpin family C member 1	Homo sapiens	64-80
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
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.	Dihydroergotamine	90-93	serpin family C member 1	Homo sapiens	72-88
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
3715788-5	1986	When tested by affinity chromatography on heparin Sepharose, this abnormal AT III did not bind to heparin.	Sepharose	50-59	serpin family C member 1	Homo sapiens	75-81
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
3715796-0	1986	Thrombosis prophylaxis in an AT III deficient pregnant woman: application of a low molecular weight heparinoid.	Heparinoids	100-110	serpin family C member 1	Homo sapiens	29-35
3013215-3	1986	The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin.	metaperiodate	46-55	serpin family C member 1	Homo sapiens	123-135
3013215-3	1986	The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin.	metaperiodate	46-55	serpin family C member 1	Homo sapiens	265-277
3013215-3	1986	The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin.	Glycols	166-172	serpin family C member 1	Homo sapiens	123-135
3013215-3	1986	The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin.	Glycols	166-172	serpin family C member 1	Homo sapiens	265-277
3013215-3	1986	The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin.	Glucuronic Acid	203-220	serpin family C member 1	Homo sapiens	265-277
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.	metaperiodate	39-48	serpin family C member 1	Homo sapiens	276-288
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
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
3754413-3	1986	Both antithrombin and heparin cofactor activities of heparin cofactor II are inactivated by the arginine-specific reagent, 2,3-butanedione.	Arginine	96-104	serpin family C member 1	Homo sapiens	5-17
3754413-3	1986	Both antithrombin and heparin cofactor activities of heparin cofactor II are inactivated by the arginine-specific reagent, 2,3-butanedione.	Diacetyl	123-138	serpin family C member 1	Homo sapiens	5-17
3754413-5	1986	Quantitation of arginyl residues following butanedione modification shows a loss of about four residues for total inactivation, one of which is essential for antithrombin activity.	Diacetyl	43-54	serpin family C member 1	Homo sapiens	158-170
3754413-11	1986	The results indicate that arginyl residues are critical for both antithrombin and heparin binding activities.	arginyl	26-33	serpin family C member 1	Homo sapiens	65-77
3711199-1	1986	Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III.	Polystyrenes	10-22	serpin family C member 1	Homo sapiens	145-161
3725864-4	1986	The exchange of the glycine residue by prolin in compounds former described caused a decreased antithrombin effect.	Glycine	20-27	serpin family C member 1	Homo sapiens	95-107
3711199-1	1986	Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III.	sulphonate	40-50	serpin family C member 1	Homo sapiens	145-161
3711199-1	1986	Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III.	l-arginyl methyl ester	55-77	serpin family C member 1	Homo sapiens	145-161
3711199-1	1986	Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III.	paom	79-83	serpin family C member 1	Homo sapiens	145-161
3708627-9	1986	This synthetic pentasaccharide binds to antithrombin III with an association constant similar to that of high-affinity heparin and elicits a potent anti-factor Xa activity in plasma.	pentasaccharide	15-30	serpin family C member 1	Homo sapiens	40-56
3960724-0	1986	Antithrombin III tours gene: identification of a point mutation leading to an arginine----cysteine replacement in a silent deficiency.	arginine----cysteine	78-98	serpin family C member 1	Homo sapiens	0-16
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
3947650-1	1986	Fluorescence polarization has been used to study the kinetics of the combination of thrombin with antithrombin and its catalysis by the polysaccharide heparin.	polysaccharide heparin	136-158	serpin family C member 1	Homo sapiens	98-110
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
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
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
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
3512602-4	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.	Sepharose	55-64	serpin family C member 1	Homo sapiens	37-43
3512602-5	1986	When thrombin-antithrombin (TAT) complexes were formed by incubating with excess thrombin, SDS-polyacrylamide gel electrophoresis (PAGE) analysis revealed that half the patient AT-III formed TAT complexes while the remainder migrated as free AT-III.	Sodium Dodecyl Sulfate	91-94	serpin family C member 1	Homo sapiens	14-26
3512602-5	1986	When thrombin-antithrombin (TAT) complexes were formed by incubating with excess thrombin, SDS-polyacrylamide gel electrophoresis (PAGE) analysis revealed that half the patient AT-III formed TAT complexes while the remainder migrated as free AT-III.	polyacrylamide	95-109	serpin family C member 1	Homo sapiens	14-26
3512602-7	1986	The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa.	Sodium Dodecyl Sulfate	104-107	serpin family C member 1	Homo sapiens	26-32
3512602-7	1986	The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa.	Sodium Dodecyl Sulfate	104-107	serpin family C member 1	Homo sapiens	34-40
3512602-7	1986	The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa.	Sodium Dodecyl Sulfate	104-107	serpin family C member 1	Homo sapiens	34-40
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
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.	tris-salts	8-18	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.	Sulfates	37-44	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.	Phosphates	46-55	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.	Acetates	60-67	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.	Acetates	60-67	serpin family C member 1	Homo sapiens	124-130
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.	Chlorides	70-78	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.	Chlorides	70-78	serpin family C member 1	Homo sapiens	124-130
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
3715809-1	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.	Sepharose	147-156	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.	Sepharose	147-156	serpin family C member 1	Homo sapiens	124-130
3715809-2	1986	AT III was also partially eluted from the column with sodium acetate, but not Tris acetate.	Sodium Acetate	54-68	serpin family C member 1	Homo sapiens	0-6
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
3949798-5	1986	An octasaccharide with characteristic marked ability to accelerate the inactivation of Factor Xa by antithrombin retained greater than 50% of its activity even at a histidine-rich glycoprotein/oligosaccharide molar ratio of 500:1.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	100-112
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.	pentasaccharide	112-127	serpin family C member 1	Homo sapiens	91-103
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
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
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
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.	QAE	0-3	serpin family C member 1	Homo sapiens	73-89
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.	sephadex a	4-14	serpin family C member 1	Homo sapiens	73-89
2421433-0	1986	Pentosan polysulphate: activation of heparin cofactor II or antithrombin III according to molecular weight fractionation.	Pentosan Sulfuric Polyester	0-21	serpin family C member 1	Homo sapiens	60-76
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
3961733-5	1986	When heparin was bound to antithrombin III-Sepharose, the aggregating activity eluted totally in the high-affinity fraction.	Sepharose	43-52	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
3942133-7	1986	The addition of danazol therapy led to a sustained rise in the antithrombin III level.	Danazol	16-23	serpin family C member 1	Homo sapiens	63-79
3725864-4	1986	The exchange of the glycine residue by prolin in compounds former described caused a decreased antithrombin effect.	DL-Proline	39-45	serpin family C member 1	Homo sapiens	95-107
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
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
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
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
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
3080419-1	1986	Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity.	prolylleucine	20-27	serpin family C member 1	Homo sapiens	66-78
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
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
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
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.	Arginine	56-59	serpin family C member 1	Homo sapiens	66-72
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
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.	Arginine	124-132	serpin family C member 1	Homo sapiens	66-72
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.	Arginine	134-137	serpin family C member 1	Homo sapiens	66-72
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
3090830-0	1986	Antithrombin III during high-dose cytosine arabinoside therapy with or without asparaginase.	Cytarabine	34-54	serpin family C member 1	Homo sapiens	0-16
2436525-15	1986	Heparan sulfate did not inhibit intrinsic prothrombin activation but catalyzed the inhibition of the thrombin generated by the formation of thrombin-antithrombin III complex.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	149-165
3080419-5	1986	The amino acid sequence of the peptide from antithrombin III Basel had a single substitution of Pro (normal) by Leu (abnormal) at position 41.	Leucine	112-115	serpin family C member 1	Homo sapiens	44-56
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.	Arginine	33-36	serpin family C member 1	Homo sapiens	144-160
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.	Tryptophan	56-59	serpin family C member 1	Homo sapiens	144-160
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
3080419-7	1986	Although additional amino acid substitutions in antithrombin III Basel cannot be ruled out, this Pro-Leu replacement could cause a conformational change by increasing both the helical structure and the hydrophobicity around residue 41.	prolylleucine	97-104	serpin family C member 1	Homo sapiens	48-64
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
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
3940555-3	1986	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and crossed immunoelectrophoresis (CIE) showed the purified AT III to be homogeneous.	sodium dodecyl sulfate-polyacrylamide	0-37	serpin family C member 1	Homo sapiens	129-135
2430807-9	1986	Antithrombin activity was increased during warfarin treatment.	Warfarin	43-51	serpin family C member 1	Homo sapiens	0-12
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
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.	Polysaccharides	21-35	serpin family C member 1	Homo sapiens	221-237
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.	dissacharide	61-73	serpin family C member 1	Homo sapiens	221-237
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
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
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.	Glucose	187-194	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.	Glucose	187-194	serpin family C member 1	Homo sapiens	267-272
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
3583099-2	1986	This alteration is glycemia level-dependent, there existing an inverse correlation between fluctuations of daily blood glucose level, labile glycosylated hemoglobin and ATIII activity.	Glucose	119-126	serpin family C member 1	Homo sapiens	169-174
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
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
3583099-5	1986	These data suggest a role for glucose, probably through a labile nonenzymatic glycation process, in determining the alteration of ATIII biological activity.	Glucose	30-37	serpin family C member 1	Homo sapiens	130-135
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
3153215-1	1986	Thirteen children with ALL and L-asp-induced alterations of the coagulation system were treated with fresh-frozen plasma and antithrombin III (AT III) concentrate.	Aspartic Acid	31-36	serpin family C member 1	Homo sapiens	125-141
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
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
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
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
3004419-10	1985	Immunoprecipitation at different chase times with monospecific antisera showed that castanospermine markedly decreased the secretion rates of alpha 1-antitrypsin, caeruloplasmin and, to a lesser extent, that of antithrombin-III.	castanospermine	84-99	serpin family C member 1	Homo sapiens	211-227
2415521-4	1985	Upon prolonged boiling in SDS it dissociates into 56- and 32-kDa components which co-migrate in SDS-PAGE with purified antithrombin III and thrombin, respectively.	Sodium Dodecyl Sulfate	26-29	serpin family C member 1	Homo sapiens	119-135
2415521-6	1985	Thrombin-antithrombin III complex, from either serum or recalcified clotted plasma, bound to vitronectin immobilized on Sepharose or plastic.	Sepharose	120-129	serpin family C member 1	Homo sapiens	9-25
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
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
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
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
3865174-2	1985	The synthetic oligodeoxyribonucleotides obtained were successfully tested in comparison with a classical mixed probe for their capacity to identify specific cDNA clones of human antithrombin III.	Oligodeoxyribonucleotides	14-39	serpin family C member 1	Homo sapiens	178-194
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
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
4071470-0	1985	Analysis of antithrombin III microheterogeneity by isoelectric focusing in polyacrylamide gels and immunoblotting.	polyacrylamide	75-89	serpin family C member 1	Homo sapiens	12-28
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
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
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
3863104-4	1985	Arginine-modified heparin cofactor II showed a comparable percentage loss of both antichymotrypsin and antithrombin activities.	Arginine	0-8	serpin family C member 1	Homo sapiens	103-115
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
4060104-3	1985	Danazol, a 17-alkyl derivative of ethinyl testosterone, which has been used to treat other antiprotease deficiency states, was assessed in the management of two men with antithrombin deficiency.	Danazol	0-7	serpin family C member 1	Homo sapiens	170-182
4064026-0	1985	Synthesis, from cellobiose, of a trisaccharide closely related to the GlcNAc----GlcA----GlcN segment of the antithrombin-binding sequence of heparin.	Trisaccharides	33-46	serpin family C member 1	Homo sapiens	108-120
4064026-0	1985	Synthesis, from cellobiose, of a trisaccharide closely related to the GlcNAc----GlcA----GlcN segment of the antithrombin-binding sequence of heparin.	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	70-76	serpin family C member 1	Homo sapiens	108-120
4070344-2	1985	The antithrombin effect decreased by substituting the 1-naphthylsulfonyl by the 8-quinolinesulfonyl residue.	1-naphthylsulfonyl	54-72	serpin family C member 1	Homo sapiens	4-16
4070344-2	1985	The antithrombin effect decreased by substituting the 1-naphthylsulfonyl by the 8-quinolinesulfonyl residue.	8-quinolinesulfonyl	80-99	serpin family C member 1	Homo sapiens	4-16
4060104-4	1985	In a dose of 600 mg a day danazol appeared to correct the antithrombin deficiency.	Danazol	26-33	serpin family C member 1	Homo sapiens	58-70
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
4082101-4	1985	Polyacrylamide gel electrophoresis (PAGE) and high pressure liquid chromatography (HPLC) on a TSK column suggest that AT III Charleville forms unstable complexes with thrombin from which a modified protein is rapidly released.	polyacrylamide	0-14	serpin family C member 1	Homo sapiens	118-124
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
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
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
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
3937259-4	1985	When stimulated by arachidonic acid, the platelets released AT III antigen together with immunoreactive fibrinogen.	Arachidonic Acid	19-35	serpin family C member 1	Homo sapiens	60-66
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
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
2411030-5	1985	Following infusion of HES and albumin, plasma fibrinogen and antithrombin-III levels fell slightly due to plasma volume expansion and hemodilution.	Hydroxyethyl Starch Derivatives	22-25	serpin family C member 1	Homo sapiens	61-77
4035646-0	1985	The role of the carbohydrate moiety for the inhibitory activity of antithrombin III.	Carbohydrates	16-28	serpin family C member 1	Homo sapiens	67-83
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
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
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
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.	Stanozolol	214-224	serpin family C member 1	Homo sapiens	6-22
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.	Stanozolol	214-224	serpin family C member 1	Homo sapiens	24-30
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.	Stanozolol	214-224	serpin family C member 1	Homo sapiens	344-350
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
4003344-3	1985	Stanozolol raised the plasma levels of AT-III, demonstrating a sparing effect on the AT-III needed.	Stanozolol	0-10	serpin family C member 1	Homo sapiens	39-45
4003344-3	1985	Stanozolol raised the plasma levels of AT-III, demonstrating a sparing effect on the AT-III needed.	Stanozolol	0-10	serpin family C member 1	Homo sapiens	85-91
4003387-7	1985	As an extension of these findings, we examined the effect of Zn+2 on the inhibition of thrombin by antithrombin-III (AT-III).	Zinc	61-65	serpin family C member 1	Homo sapiens	99-115
4003387-8	1985	The presence of as little as 0.006 mM Zn+2 in an incubating mixture of thrombin and AT-III severely reduced the inhibitory activity of AT-III towards thrombin.	Zinc	38-42	serpin family C member 1	Homo sapiens	84-90
4003387-8	1985	The presence of as little as 0.006 mM Zn+2 in an incubating mixture of thrombin and AT-III severely reduced the inhibitory activity of AT-III towards thrombin.	Zinc	38-42	serpin family C member 1	Homo sapiens	135-141
4003387-10	1985	It is suggested that Zn+2 can form a complex with thrombin, which results in altered reactivity towards fibrinogen and decreased inhibition by AT-III.	Zinc	21-25	serpin family C member 1	Homo sapiens	143-149
2859508-4	1985	Haemostatic tests in cyclosporin-treated and azathioprine-treated patients and normal subjects (10 in each group) showed increased concentrations of factor VIII C, fibrinogen, antithrombin III, and protein C in the cyclosporin-treated patients.	Cyclosporine	21-32	serpin family C member 1	Homo sapiens	176-192
2859508-4	1985	Haemostatic tests in cyclosporin-treated and azathioprine-treated patients and normal subjects (10 in each group) showed increased concentrations of factor VIII C, fibrinogen, antithrombin III, and protein C in the cyclosporin-treated patients.	Azathioprine	45-57	serpin family C member 1	Homo sapiens	176-192
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
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
2408362-3	1985	Results of in vivo studies were as follows: following infusion of 1 liter of 6 percent HES into healthy subjects, fibrinogen and antithrombin-III concentrations fell slightly due to plasma volume expansion and consequent dilution.	Hydroxyethyl Starch Derivatives	87-90	serpin family C member 1	Homo sapiens	129-145
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
3985961-0	1985	Mono- and bidimensional 500 MHz 1H-NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: evidence for conformational peculiarity of the sulfated iduronate residue.	pentasaccharide	62-77	serpin family C member 1	Homo sapiens	130-146
3985961-0	1985	Mono- and bidimensional 500 MHz 1H-NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: evidence for conformational peculiarity of the sulfated iduronate residue.	Iduronic Acid	204-213	serpin family C member 1	Homo sapiens	130-146
3985961-5	1985	Such a departure, leading to different orientation and spacing of essential sulfate groups, may have implications for high-affinity binding to AT-III.	essential sulfate	66-83	serpin family C member 1	Homo sapiens	143-149
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
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
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
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).	Glycosaminoglycans	47-65	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.	pentasaccharide	24-39	serpin family C member 1	Homo sapiens	84-90
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
4035368-3	1985	A pentasaccharide analogue lacking this 3-0-sulfate group and two different tetrasaccharides, each being part of the pentasaccharide sequence with AT III affinity, have also been synthesized.	tetrasaccharides	76-92	serpin family C member 1	Homo sapiens	147-153
4035368-3	1985	A pentasaccharide analogue lacking this 3-0-sulfate group and two different tetrasaccharides, each being part of the pentasaccharide sequence with AT III affinity, have also been synthesized.	pentasaccharide	117-132	serpin family C member 1	Homo sapiens	147-153
4035368-4	1985	The pentasaccharide with high affinity for AT III also shows high antifactor Xa activity and, in vivo, antithrombotic activity.	pentasaccharide	4-19	serpin family C member 1	Homo sapiens	43-49
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
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.	octadecasaccharide	96-114	serpin family C member 1	Homo sapiens	206-218
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
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
3986191-0	1985	Denaturation behavior of antithrombin in guanidinium chloride.	Guanidine	41-61	serpin family C member 1	Homo sapiens	25-37
3986191-2	1985	The structural stability of the protease inhibitor antithrombin from bovine plasma was examined as a function of the concentration of guanidinium chloride (GdmCl).	Guanidine	134-154	serpin family C member 1	Homo sapiens	51-63
3986191-4	1985	Spectroscopic and hydrodynamic analyses suggest that the intermediate state which exists at 1.5 M GdmCl involves a partial unfolding of the antithrombin molecule that exposes regions of the polypeptide chain through which slow, intermolecular association subsequently takes place.	Guanidine	98-103	serpin family C member 1	Homo sapiens	140-152
3986191-9	1985	Analyses of bovine antithrombin in 6 M GdmCl indicated that the second transition reflects the total unfolding of the protein to a disulfide-cross-linked random coil.	Guanidine	39-44	serpin family C member 1	Homo sapiens	19-31
3986191-9	1985	Analyses of bovine antithrombin in 6 M GdmCl indicated that the second transition reflects the total unfolding of the protein to a disulfide-cross-linked random coil.	Disulfides	131-140	serpin family C member 1	Homo sapiens	19-31
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
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
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
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
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
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.	Disulfides	17-26	serpin family C member 1	Homo sapiens	88-104
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
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
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
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
3873118-2	1985	Stanozolol treatment resulted in significant (p less than 0.01) increases between the 14th and 1st preoperative days in the plasma concentrations of plasminogen (3.4 to 4.9 Cu/ml) and antithrombin III (107% to 132%); t-PA levels did not increase significantly (6.0 to 16.0 mU/ml; p greater than 0.1).	Stanozolol	0-10	serpin family C member 1	Homo sapiens	184-200
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
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
3967090-3	1985	AT III was purified from normal and propositus plasma by sulfate dextran precipitation followed by heparin affinity chromatography.	Dextran Sulfate	57-72	serpin family C member 1	Homo sapiens	0-6
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
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
3973461-4	1985	Antithrombin (AT) binding by heparinized PMA materials (compared with PMA control beads) ranged from no AT binding for the material heparinized with carbodiimide (PMA-Alb-Hep(EDC] to 3.6 micrograms/ml packed beads for the material heparinized by radical polymerization (PMA-MA-Hep).	Tetradecanoylphorbol Acetate	41-44	serpin family C member 1	Homo sapiens	0-12
3973461-4	1985	Antithrombin (AT) binding by heparinized PMA materials (compared with PMA control beads) ranged from no AT binding for the material heparinized with carbodiimide (PMA-Alb-Hep(EDC] to 3.6 micrograms/ml packed beads for the material heparinized by radical polymerization (PMA-MA-Hep).	Carbodiimides	149-161	serpin family C member 1	Homo sapiens	0-12
3973461-4	1985	Antithrombin (AT) binding by heparinized PMA materials (compared with PMA control beads) ranged from no AT binding for the material heparinized with carbodiimide (PMA-Alb-Hep(EDC] to 3.6 micrograms/ml packed beads for the material heparinized by radical polymerization (PMA-MA-Hep).	ethylene dichloride	175-178	serpin family C member 1	Homo sapiens	0-12
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
2578296-2	1985	Several materials were highly active in factor Xa inhibition and the reaction rate at constant factor Xa concentration appeared to be predicted by the extent of intrinsic antithrombin III fluorescence change induced by the polysaccharide.	Polysaccharides	223-237	serpin family C member 1	Homo sapiens	171-187
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
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
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
2579452-0	1985	Comparison between the effect of pentosan polysulphate heparin and antithrombin III injections in antithrombin III deficient patients.	pentosan polysulphate heparin	33-62	serpin family C member 1	Homo sapiens	98-114
2579452-1	1985	Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway.	Pentosan Sulfuric Polyester	0-21	serpin family C member 1	Homo sapiens	63-79
2579452-1	1985	Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway.	Pentosan Sulfuric Polyester	0-21	serpin family C member 1	Homo sapiens	81-87
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
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
2579452-7	1985	The marked effect of pentosan polysulphate on thrombin and factor Xa generation in these patients is due to its AT III independent mechanism of action.	Pentosan Sulfuric Polyester	21-42	serpin family C member 1	Homo sapiens	112-118
3965464-0	1985	Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding.	Carbohydrates	75-87	serpin family C member 1	Homo sapiens	37-53
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
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
3965464-1	1985	Two distinct forms of antithrombin III were isolated by chromatography of normal human plasma on heparin-Sepharose.	Sepharose	105-114	serpin family C member 1	Homo sapiens	22-38
3965464-2	1985	The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized.	Sodium Chloride	106-110	serpin family C member 1	Homo sapiens	16-28
3965464-2	1985	The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized.	Sodium Chloride	106-110	serpin family C member 1	Homo sapiens	46-52
3965464-2	1985	The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized.	Sodium Chloride	106-110	serpin family C member 1	Homo sapiens	134-150
3965464-5	1985	Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha.	Carbohydrates	0-12	serpin family C member 1	Homo sapiens	161-167
3965464-5	1985	Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha.	Hexosamines	114-124	serpin family C member 1	Homo sapiens	161-167
3965464-5	1985	Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha.	N-Acetylneuraminic Acid	146-157	serpin family C member 1	Homo sapiens	161-167
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.	Carbohydrates	107-119	serpin family C member 1	Homo sapiens	6-22
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
3975871-0	1985	Inhibition of antithrombin III by lipid peroxides.	Lipid Peroxides	34-49	serpin family C member 1	Homo sapiens	14-30
3975871-1	1985	A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids.	Lipid Peroxides	76-91	serpin family C member 1	Homo sapiens	38-54
3975871-1	1985	A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids.	Lipid Peroxides	76-91	serpin family C member 1	Homo sapiens	56-62
3975871-1	1985	A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids.	Fatty Acids, Unsaturated	122-145	serpin family C member 1	Homo sapiens	38-54
3975871-1	1985	A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids.	Fatty Acids, Unsaturated	122-145	serpin family C member 1	Homo sapiens	56-62
3975871-2	1985	Lipid peroxides markedly reduced the thrombin neutralising activity of plasma and purified At III with or without albumin carrier.	Lipid Peroxides	0-15	serpin family C member 1	Homo sapiens	91-97
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
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.	Sepharose	8-17	serpin family C member 1	Homo sapiens	121-127
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
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.	Lipid Peroxides	98-113	serpin family C member 1	Homo sapiens	121-127
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
3975871-4	1985	Results from electrophoretic studies suggested that interaction between lipid peroxides and At III increased the negative charge of the At III molecule; however, no aggregation of the At III molecule was observed.	Lipid Peroxides	72-87	serpin family C member 1	Homo sapiens	92-98
3975871-4	1985	Results from electrophoretic studies suggested that interaction between lipid peroxides and At III increased the negative charge of the At III molecule; however, no aggregation of the At III molecule was observed.	Lipid Peroxides	72-87	serpin family C member 1	Homo sapiens	136-142
3975871-4	1985	Results from electrophoretic studies suggested that interaction between lipid peroxides and At III increased the negative charge of the At III molecule; however, no aggregation of the At III molecule was observed.	Lipid Peroxides	72-87	serpin family C member 1	Homo sapiens	136-142
3975871-5	1985	Lipid peroxidation is being increasingly recognised as a factor in the pathogenesis of several disease states, and it is possible that local inhibition of At III by lipid peroxides could contribute towards the development of a thrombotic event.	Lipid Peroxides	165-180	serpin family C member 1	Homo sapiens	155-161
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
3868345-5	1985	AT III 25 U/kg and in combination with heparin showed marginal effects, 50 U/kg AT III resulted in increased survival rate and time, improvement of pathological changes of coagulation parameters and of blood urea nitrogen and serum creatinine levels.	Urea	208-212	serpin family C member 1	Homo sapiens	80-86
3868345-1	1985	Intraperitoneal application of carbon tetrachloride into rabbits caused high mortality due to liver damage with increase of serum transaminases, coagulation disorders, and decrease of antithrombin III (AT III) blood levels.	Carbon Tetrachloride	31-51	serpin family C member 1	Homo sapiens	202-208
3868345-5	1985	AT III 25 U/kg and in combination with heparin showed marginal effects, 50 U/kg AT III resulted in increased survival rate and time, improvement of pathological changes of coagulation parameters and of blood urea nitrogen and serum creatinine levels.	Nitrogen	213-221	serpin family C member 1	Homo sapiens	80-86
3868345-5	1985	AT III 25 U/kg and in combination with heparin showed marginal effects, 50 U/kg AT III resulted in increased survival rate and time, improvement of pathological changes of coagulation parameters and of blood urea nitrogen and serum creatinine levels.	Creatinine	232-242	serpin family C member 1	Homo sapiens	80-86
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
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
4007636-0	1985	Treatment of familial antithrombin-III deficiency with danazol.	Danazol	55-62	serpin family C member 1	Homo sapiens	22-38
4007636-1	1985	3 individuals from 2 unrelated families with recurrent thromboses and quantitative deficiencies of antithrombin III (AT-III) were treated with danazol, 600 mg daily for 4 months.	Danazol	143-150	serpin family C member 1	Homo sapiens	99-115
4007636-1	1985	3 individuals from 2 unrelated families with recurrent thromboses and quantitative deficiencies of antithrombin III (AT-III) were treated with danazol, 600 mg daily for 4 months.	Danazol	143-150	serpin family C member 1	Homo sapiens	117-123
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
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
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
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
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
6442470-3	1984	The patients with CH were further classified into two groups: in group CH-I, whose consciousness state was stupor or further deteriorated including coma on admission, the excretion rate of AT III RA was 18.08 +/- 2.50 X 10(-4) ml/min.	Radium	196-198	serpin family C member 1	Homo sapiens	189-195
6531759-5	1984	Examination of Lineweaver-Burk plots showed nonlinearity at high concentrations of S-2238 as used in the antithrombin III assays.	S 2238	83-89	serpin family C member 1	Homo sapiens	105-121
6084876-0	1984	Purification and biological property of heparin cofactor II: activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans.	Dextran Sulfate	119-134	serpin family C member 1	Homo sapiens	99-115
6084876-0	1984	Purification and biological property of heparin cofactor II: activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans.	Glycosaminoglycans	147-165	serpin family C member 1	Homo sapiens	99-115
6084876-3	1984	Chem., 257, 2162, 1982) and abilities of dextran sulfate and various glycosaminoglycans to activate the antithrombin activities of HC II and antithrombin III (AT III) were studied.	Glycosaminoglycans	69-87	serpin family C member 1	Homo sapiens	104-116
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.	Dextran Sulfate	0-15	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.	Dextran Sulfate	0-15	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	40-47	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	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
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.	Sulfates	8-15	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.	Sulfates	8-15	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
6084876-8	1984	When mixed with thrombin in the presence of dermatan sulfate, normal human plasma showed antithrombin activity which was not due to AT III but to HC II only.	Dermatan Sulfate	44-60	serpin family C member 1	Homo sapiens	89-101
6525533-7	1984	In the antithrombin III group and the antithrombin III plus heparin group, however, creatinine clearance (Clcr) was moderately elevated while FENa and CH2O remained unchanged as compared with the values before the burn.	Creatinine	84-94	serpin family C member 1	Homo sapiens	38-54
6525533-7	1984	In the antithrombin III group and the antithrombin III plus heparin group, however, creatinine clearance (Clcr) was moderately elevated while FENa and CH2O remained unchanged as compared with the values before the burn.	clcr	106-110	serpin family C member 1	Homo sapiens	38-54
6525533-8	1984	The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, Clcr and CH2O.	clcr	121-125	serpin family C member 1	Homo sapiens	4-20
6525533-8	1984	The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, Clcr and CH2O.	Formaldehyde	130-134	serpin family C member 1	Homo sapiens	4-20
6150297-0	1984	Danazol raises antithrombin III levels in cases of familial deficiency.	Danazol	0-7	serpin family C member 1	Homo sapiens	15-31
6530392-1	1984	Whale heparin was partially digested with a purified heparinase and the oligosaccharide fractions with 8-20 monosaccharide units were isolated from the digest by gel filtration on Sephadex G-50, followed by affinity chromatography on a column of antithrombin III immobilized on Sepharose 4B.	Oligosaccharides	72-87	serpin family C member 1	Homo sapiens	246-262
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	Octasaccharide	169-183	serpin family C member 1	Homo sapiens	79-95
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	Octasaccharide	169-183	serpin family C member 1	Homo sapiens	149-165
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	hexadecasaccharide	198-216	serpin family C member 1	Homo sapiens	79-95
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	hexadecasaccharide	198-216	serpin family C member 1	Homo sapiens	149-165
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	octadecasaccharide	230-248	serpin family C member 1	Homo sapiens	79-95
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	eicosasaccharide	263-279	serpin family C member 1	Homo sapiens	79-95
6530392-2	1984	A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide.	eicosasaccharide	263-279	serpin family C member 1	Homo sapiens	149-165
6530392-5	1984	The present observations, together with those so far reported, suggest that the presence of the former structural elements, specifically IdUA(2S)alpha 1----4GlcNS(6S), as well as the antithrombin III-binding pentasaccharide at the proper positions in the molecules of whale heparin oligosaccharides is essential for the manifestation of high inhibitory activity for thrombin in the presence of antithrombin III.	pentasaccharide	208-223	serpin family C member 1	Homo sapiens	183-199
6530392-5	1984	The present observations, together with those so far reported, suggest that the presence of the former structural elements, specifically IdUA(2S)alpha 1----4GlcNS(6S), as well as the antithrombin III-binding pentasaccharide at the proper positions in the molecules of whale heparin oligosaccharides is essential for the manifestation of high inhibitory activity for thrombin in the presence of antithrombin III.	heparin oligosaccharides	274-298	serpin family C member 1	Homo sapiens	183-199
6525337-0	1984	Sequence variation in heparin octasaccharides with high affinity for antithrombin III.	heparin octasaccharides	22-45	serpin family C member 1	Homo sapiens	69-85
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
3838602-0	1985	Histidine-rich glycoprotein inhibits the antithrombin activity of heparin cofactor II in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	116-132	serpin family C member 1	Homo sapiens	41-53
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.	Nitrous Acid	22-34	serpin family C member 1	Homo sapiens	138-150
6335402-2	1984	The rate of inactivation of factor Xa by antithrombin III was found to be decreased in the presence of phospholipid vesicles with high affinity for factor Xa.	Phospholipids	103-115	serpin family C member 1	Homo sapiens	41-57
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
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.	Octasaccharide	74-88	serpin family C member 1	Homo sapiens	138-150
6525337-3	1984	When bound to antithrombin, both octasaccharides produce a 40% enhancement in the intrinsic fluorescence of the protease inhibitor and a rate of human factor Xa inhibition of 5 X 10(5) M-1 s-1 as monitored by stopped-flow fluorometry.	octasaccharides	33-48	serpin family C member 1	Homo sapiens	14-26
6525337-4	1984	This suggests that the conformation of antithrombin in the region of the factor Xa binding site is similar when the protease inhibitor is complexed with either octasaccharide.	Octasaccharide	160-174	serpin family C member 1	Homo sapiens	39-51
6395434-1	1984	A technique is described to completely remove antithrombin III (AT) from small amounts of human plasma by immunoaffinity chromatography on antibodies against human AT linked to Sepharose 4B.	Sepharose	177-186	serpin family C member 1	Homo sapiens	46-62
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
6395434-1	1984	A technique is described to completely remove antithrombin III (AT) from small amounts of human plasma by immunoaffinity chromatography on antibodies against human AT linked to Sepharose 4B.	Sepharose	177-186	serpin family C member 1	Homo sapiens	64-66
6395434-1	1984	A technique is described to completely remove antithrombin III (AT) from small amounts of human plasma by immunoaffinity chromatography on antibodies against human AT linked to Sepharose 4B.	Sepharose	177-186	serpin family C member 1	Homo sapiens	164-166
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
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.	Dermatan Sulfate	218-234	serpin family C member 1	Homo sapiens	238-240
6209821-1	1984	In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54).	Pentosan Sulfuric Polyester	152-173	serpin family C member 1	Homo sapiens	3-19
6209821-0	1984	Identification of heparin cofactor II as the principal plasma cofactor for the antithrombin activity of pentosan polysulphate (SP54).	Pentosan Sulfuric Polyester	104-125	serpin family C member 1	Homo sapiens	79-91
6209821-1	1984	In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54).	Pentosan Sulfuric Polyester	175-179	serpin family C member 1	Homo sapiens	3-19
6209821-0	1984	Identification of heparin cofactor II as the principal plasma cofactor for the antithrombin activity of pentosan polysulphate (SP54).	Pentosan Sulfuric Polyester	127-131	serpin family C member 1	Homo sapiens	79-91
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
6209821-1	1984	In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54).	Dermatan Sulfate	128-145	serpin family C member 1	Homo sapiens	3-19
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
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
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
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
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
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
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
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
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
6520110-0	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
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
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
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.	sephacryl s	21-32	serpin family C member 1	Homo sapiens	114-130
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
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
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 methyl ester	100-120	serpin family C member 1	Homo sapiens	28-44
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.	heparinylglycine	134-150	serpin family C member 1	Homo sapiens	28-44
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.	heparinylglycine methyl ester	164-193	serpin family C member 1	Homo sapiens	28-44
6207810-0	1984	Effect of a pentosan polysulphate upon thrombin and factor Xa inactivation by antithrombin III.	Pentosan Sulfuric Polyester	12-33	serpin family C member 1	Homo sapiens	78-94
6207810-7	1984	In the presence of pentosan polysulphate the dissociation constant for the initial complex of antithrombin III and thrombin was shown to be reduced from approx.	Pentosan Sulfuric Polyester	19-40	serpin family C member 1	Homo sapiens	94-110
6207810-9	1984	An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate.	Oligosaccharides	3-18	serpin family C member 1	Homo sapiens	102-118
6207810-9	1984	An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate.	Oligosaccharides	3-18	serpin family C member 1	Homo sapiens	151-167
6207810-9	1984	An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate.	8-10 saccharide	30-45	serpin family C member 1	Homo sapiens	102-118
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
6207810-10	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.	Polysaccharides	320-334	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
6209818-0	1984	Abolition by dextran sulfate of the heparin-accelerated antithrombin III/thrombin reaction.	Dextran Sulfate	13-28	serpin family C member 1	Homo sapiens	56-72
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
6209818-1	1984	Dextran sulfate did not inhibit the amidolytic activity of thrombin on Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide, but abolished inhibition of the enzyme with antithrombin III (AT III) in the presence of heparin.	Dextran Sulfate	0-15	serpin family C member 1	Homo sapiens	157-173
6209818-1	1984	Dextran sulfate did not inhibit the amidolytic activity of thrombin on Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide, but abolished inhibition of the enzyme with antithrombin III (AT III) in the presence of heparin.	Dextran Sulfate	0-15	serpin family C member 1	Homo sapiens	175-181
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.	Dextran Sulfate	40-55	serpin family C member 1	Homo sapiens	132-138
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
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
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
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
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
6435583-5	1984	This induced a rise in AT III activity to over 100% and enabled early introduction of anti-vitamin K therapy.	Vitamin K	91-100	serpin family C member 1	Homo sapiens	23-29
6486808-0	1984	The role of tryptophan residues in heparin-antithrombin interactions.	Tryptophan	12-22	serpin family C member 1	Homo sapiens	43-55
6486808-1	1984	A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide.	Tryptophan	9-19	serpin family C member 1	Homo sapiens	31-43
6235872-1	1984	Heparan with a low affinity for antithrombin III has previously been demonstrated to inhibit thrombin generation in both normal plasma and plasma depleted of antithrombin III.	heparan	0-7	serpin family C member 1	Homo sapiens	32-48
6486808-1	1984	A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide.	dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium	67-118	serpin family C member 1	Homo sapiens	31-43
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
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.	Glycosaminoglycans	214-232	serpin family C member 1	Homo sapiens	103-115
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.	Octasaccharide	39-53	serpin family C member 1	Homo sapiens	17-29
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
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.	dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium	104-156	serpin family C member 1	Homo sapiens	17-29
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.	Tryptophan	207-217	serpin family C member 1	Homo sapiens	17-29
6486808-4	1984	Fluorescence quenching experiments indicated that the modifiable tryptophan groups of antithrombin were exposed to the solvent environment.	Tryptophan	65-75	serpin family C member 1	Homo sapiens	86-98
6486808-5	1984	Based upon these data, it was proposed that the loss of "heparin cofactor" activity of antithrombin must be predominantly due to an inability of the modified protease inhibitor to undergo a conformational transition required for mucopolysaccharide-dependent "activation" of the macromolecule.	Glycosaminoglycans	229-247	serpin family C member 1	Homo sapiens	87-99
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.	Polystyrenes	49-60	serpin family C member 1	Homo sapiens	18-34
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.	Polystyrenes	49-60	serpin family C member 1	Homo sapiens	36-42
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
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
6235872-1	1984	Heparan with a low affinity for antithrombin III has previously been demonstrated to inhibit thrombin generation in both normal plasma and plasma depleted of antithrombin III.	heparan	0-7	serpin family C member 1	Homo sapiens	158-174
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
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
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
6235872-5	1984	In contrast, dermatan sulfate inhibited thrombin generation in both normal and antithrombin III-depleted plasma.	Dermatan Sulfate	13-29	serpin family C member 1	Homo sapiens	79-95
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.	2-diethylaminoethanol	52-56	serpin family C member 1	Homo sapiens	0-16
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
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.	sephadex	57-65	serpin family C member 1	Homo sapiens	0-16
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
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
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
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
6235872-8	1984	These results suggest that heparan sulfate acts primarily by potentiating antithrombin III, while dermatan sulfate acts by potentiating heparin cofactor II.	Heparitin Sulfate	27-42	serpin family C member 1	Homo sapiens	74-90
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
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
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
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
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
6495267-3	1984	The generation of thrombin by lipid peroxides is also enhanced by their inhibitory action on antithrombin III.	Lipid Peroxides	30-45	serpin family C member 1	Homo sapiens	93-109
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
6746897-1	1984	We have examined the role of heparinlike molecules in the regulation of coagulation by perfusing rat hindquarters with purified human thrombin and with its plasma inhibitor, antithrombin.	heparinlike	29-40	serpin family C member 1	Homo sapiens	174-186
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
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.	Glycosaminoglycans	10-29	serpin family C member 1	Homo sapiens	104-116
6746897-7	1984	Finally, addition of diisofluorophosphate-thrombin to the enzyme perfusion stream reduced the amount of thrombin-antithrombin complex formed in the animal by 30-40%, which suggested that thrombin bound to the endothelium as well as enzyme free in solution are accessible to antithrombin that has interacted with heparinlike molecules present on the endothelium.	diisofluorophosphate	21-41	serpin family C member 1	Homo sapiens	113-125
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.	Dextran Sulfate	65-80	serpin family C member 1	Homo sapiens	0-16
6746897-7	1984	Finally, addition of diisofluorophosphate-thrombin to the enzyme perfusion stream reduced the amount of thrombin-antithrombin complex formed in the animal by 30-40%, which suggested that thrombin bound to the endothelium as well as enzyme free in solution are accessible to antithrombin that has interacted with heparinlike molecules present on the endothelium.	diisofluorophosphate	21-41	serpin family C member 1	Homo sapiens	274-286
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
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.	Serotonin	56-65	serpin family C member 1	Homo sapiens	77-93
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.	Dermatan Sulfate	155-171	serpin family C member 1	Homo sapiens	77-93
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
6329378-9	1984	Vitamin K increased the quantity of prothrombin secreted by twofold, without affecting the rate of secretion over a five-day culture period, and had an apparent transient inhibitory effect on secretion of antithrombin III.	Vitamin K	0-9	serpin family C member 1	Homo sapiens	205-221
6145672-6	1984	Among these putrescine-binding proteins, we identified, with the help of corresponding specific antisera, four protease inhibitors: alpha 2-macroglobulin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and antithrombin III.	Putrescine	12-22	serpin family C member 1	Homo sapiens	205-221
6426771-2	1984	In view of this literature, a study of patients on tamoxifen was initiated to determine if a paradoxical estrogenic effect was present as evidenced by lowered levels of antithrombin III (AT III).	Tamoxifen	51-60	serpin family C member 1	Homo sapiens	169-185
6426771-13	1984	The finding of lowered functional activity of AT III in 42% of tamoxifen-treated patients is preliminary in nature and will require larger confirmatory studies, including further clinical correlation of this observation.	Tamoxifen	63-72	serpin family C member 1	Homo sapiens	46-52
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
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
6740570-4	1984	HRH was fractionated further by chromatography on a column of AT-III bound to concanavalin A-Sepharose.	Sepharose	93-102	serpin family C member 1	Homo sapiens	62-68
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
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
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
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
6733045-1	1984	Platelets and phospholipids have been shown to protect factor Xa from inhibition by the heparin--antithrombin III complex.	Phospholipids	14-27	serpin family C member 1	Homo sapiens	97-113
6733045-7	1984	These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin.	Phospholipids	76-89	serpin family C member 1	Homo sapiens	161-177
6733045-7	1984	These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin.	Phospholipids	76-89	serpin family C member 1	Homo sapiens	219-235
6733045-7	1984	These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin.	Calcium	129-136	serpin family C member 1	Homo sapiens	161-177
6733045-7	1984	These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin.	Calcium	129-136	serpin family C member 1	Homo sapiens	219-235
6237371-3	1984	Isomeric compounds of N alpha-arylsulfonylated amides of omega-amidinophenyl-alpha-aminoalkylcarboxylic acids--N alpha-amidinophenylsulfonylated amides or N alpha-arylsulfonylated amidino anilides of omega-phenyl-alpha-aminoalkylcarboxylic acids, respectively--possess weak antithrombin activity as compared to the derivatives of the basic structure.	n alpha-arylsulfonylated amides	22-53	serpin family C member 1	Homo sapiens	274-286
6237371-3	1984	Isomeric compounds of N alpha-arylsulfonylated amides of omega-amidinophenyl-alpha-aminoalkylcarboxylic acids--N alpha-amidinophenylsulfonylated amides or N alpha-arylsulfonylated amidino anilides of omega-phenyl-alpha-aminoalkylcarboxylic acids, respectively--possess weak antithrombin activity as compared to the derivatives of the basic structure.	n alpha-arylsulfonylated amidino anilides	155-196	serpin family C member 1	Homo sapiens	274-286
6426525-0	1984	Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation.	Sugars	45-51	serpin family C member 1	Homo sapiens	25-41
6426525-0	1984	Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation.	Sugars	45-50	serpin family C member 1	Homo sapiens	25-41
6426525-1	1984	A variety of neutral and acidic sugars and related compounds were evaluated in terms of their effect on the midpoint, Td, of the thermal denaturation curve of antithrombin III.	Sugars	32-38	serpin family C member 1	Homo sapiens	159-175
6426525-4	1984	Several compounds were shown to be effective in preserving antithrombin III activity during pasteurization for 10 h at 60 degrees C. However, the presence of reducing sugars invariably resulted in a decrease in activity following pasteurization, in spite of their ability to increase Td.	Sugars	167-173	serpin family C member 1	Homo sapiens	59-75
6426525-5	1984	In fact, when antithrombin III was pasteurized in the presence of 2 M glucose and 0.5 M citrate, it steadily lost its ability to inhibit thrombin even though Td under these conditions was 10 degrees C higher than in citrate alone where activity was preserved.	Glucose	70-77	serpin family C member 1	Homo sapiens	14-30
6426525-5	1984	In fact, when antithrombin III was pasteurized in the presence of 2 M glucose and 0.5 M citrate, it steadily lost its ability to inhibit thrombin even though Td under these conditions was 10 degrees C higher than in citrate alone where activity was preserved.	Citric Acid	88-95	serpin family C member 1	Homo sapiens	14-30
6426525-5	1984	In fact, when antithrombin III was pasteurized in the presence of 2 M glucose and 0.5 M citrate, it steadily lost its ability to inhibit thrombin even though Td under these conditions was 10 degrees C higher than in citrate alone where activity was preserved.	Citric Acid	216-223	serpin family C member 1	Homo sapiens	14-30
6742427-6	1984	The assay has been used to follow the generation of Xa-antithrombin complex in kinetic situations by the addition of 1 microM Ile-Glu-Gly-Arg-chloro- methylketone to the ELISA sampling buffer, and it has also been used in plasma systems, where a 20-fold reduction in the sensitivity of the assay is observed.	isoleucyl-glutamyl-glycyl-arginine chloromethyl ketone	126-162	serpin family C member 1	Homo sapiens	55-67
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
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
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
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
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
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
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.	Coumarins	158-167	serpin family C member 1	Homo sapiens	0-16
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
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
6740566-6	1984	The mean AT-III concentration during coumarin treatment was higher than after coumarin treatment.	coumarin	37-45	serpin family C member 1	Homo sapiens	9-15
6740566-6	1984	The mean AT-III concentration during coumarin treatment was higher than after coumarin treatment.	coumarin	78-86	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
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).	Monosaccharides	246-260	serpin family C member 1	Homo sapiens	64-80
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
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
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
6747440-3	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.	Sepharose	131-140	serpin family C member 1	Homo sapiens	0-16
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.	DEAE-Sephadex A-50	177-195	serpin family C member 1	Homo sapiens	0-16
6747440-4	1984	Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis showed that only approximately half of the purified antithrombin III was capable of forming a complex with thrombin.	sodium dodecyl sulfate-polyacrylamide	0-37	serpin family C member 1	Homo sapiens	144-160
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.	Salts	116-120	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
6747440-7	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.	Sepharose	171-180	serpin family C member 1	Homo sapiens	141-157
6424998-0	1984	Antithrombin activity of gold sodium thiomalate.	Gold Sodium Thiomalate	25-47	serpin family C member 1	Homo sapiens	0-12
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
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
6609435-0	1984	Bleeding tendency possibly related to increased plasma antithrombin III activity in patient treated with piroxicam.	Piroxicam	105-114	serpin family C member 1	Homo sapiens	55-71
6729779-6	1984	Since the secondary injection of protamin sulphate (after the end of the perfusion with the thrombin-heparin mixture) was precipitating the DIC syndrome, such attempts to decrease AT III in man are not feasible.	protamin sulphate	33-50	serpin family C member 1	Homo sapiens	180-186
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
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
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
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
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
6546700-10	1984	Interaction with antithrombin III is slower than normal when followed by SDS gel electrophoresis and inhibition of the amidolytic activity of thrombin on S2238.	Sodium Dodecyl Sulfate	73-76	serpin family C member 1	Homo sapiens	17-33
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
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
6721831-1	1984	Oligosaccharides of well-defined molecular size were prepared from heparin by nitrous acid depolymerization, affinity chromatography on immobilized antithrombin III (see footnote on Nomenclature) and gel chromatography on Sephadex G-50.	Oligosaccharides	0-16	serpin family C member 1	Homo sapiens	148-164
6721831-2	1984	High affinity (for antithrombin III) octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides were prepared, as well as oligosaccharides of larger size than octadecasaccharide.	octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides	37-106	serpin family C member 1	Homo sapiens	19-35
6721831-2	1984	High affinity (for antithrombin III) octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides were prepared, as well as oligosaccharides of larger size than octadecasaccharide.	Oligosaccharides	133-149	serpin family C member 1	Homo sapiens	19-35
6721831-2	1984	High affinity (for antithrombin III) octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides were prepared, as well as oligosaccharides of larger size than octadecasaccharide.	octadecasaccharide	170-188	serpin family C member 1	Homo sapiens	19-35
6721831-3	1984	The inhibition of Factor Xa by antithrombin III was greatly accelerated by all of these oligosaccharides, the specific anti-Factor Xa activity being invariably greater than 1300 units/mumol.	Oligosaccharides	88-104	serpin family C member 1	Homo sapiens	31-47
6722255-0	1984	Catalysis of the generation of thrombin-antithrombin complex by insoluble anticoagulant polystyrene derivatives.	Polystyrenes	88-99	serpin family C member 1	Homo sapiens	40-52
6739525-4	1984	The greatest antithrombin effect shows N alpha-(2- naphthylsulphonylglycyl )-4- amidinophenylalaninpiperidi d with a Ki-value of 6 X 10(-9) mol/l using S-2238 as a substrate.	n alpha-(2- naphthylsulphonylglycyl )-4- amidinophenylalaninpiperidi d	39-109	serpin family C member 1	Homo sapiens	13-25
6739525-4	1984	The greatest antithrombin effect shows N alpha-(2- naphthylsulphonylglycyl )-4- amidinophenylalaninpiperidi d with a Ki-value of 6 X 10(-9) mol/l using S-2238 as a substrate.	Sulfur	152-153	serpin family C member 1	Homo sapiens	13-25
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
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.	muccopolysaccharide	132-151	serpin family C member 1	Homo sapiens	30-46
6722255-4	1984	The protease-antiprotease complex has an affinity for the polymer surface which is higher than that of antithrombin but lower than that of thrombin.	Polymers	58-65	serpin family C member 1	Homo sapiens	103-115
6719385-1	1984	Interaction of human antithrombin III (AT III) with human alpha-thrombin coupled to Sepharose 4B was investigated.	Sepharose	84-93	serpin family C member 1	Homo sapiens	21-37
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
6696918-1	1984	Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene.	Carbohydrates	104-116	serpin family C member 1	Homo sapiens	34-50
6696918-1	1984	Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene.	metaperiodate	155-164	serpin family C member 1	Homo sapiens	34-50
6696918-1	1984	Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene.	Fluorescein	217-228	serpin family C member 1	Homo sapiens	34-50
6719385-1	1984	Interaction of human antithrombin III (AT III) with human alpha-thrombin coupled to Sepharose 4B was investigated.	Sepharose	84-93	serpin family C member 1	Homo sapiens	39-45
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.	Sepharose	9-18	serpin family C member 1	Homo sapiens	140-146
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
6698980-7	1984	Circular dichroism studies showed that the disruption of the first unfolding domain in antithrombin III by low concentration of guanidinium chloride (Villanueva, G. B., and Allen, N. (1983) J. Biol.	Guanidine	128-148	serpin family C member 1	Homo sapiens	87-103
6696918-1	1984	Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene.	pyrene	233-239	serpin family C member 1	Homo sapiens	34-50
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.	Warfarin	10-18	serpin family C member 1	Homo sapiens	121-137
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
6721831-7	1984	An octadecasaccharide is therefore the smallest heparin fragment (prepared by nitrous acid depolymerization) that can accelerate thrombin inhibition by antithrombin III.	octadecasaccharide	3-21	serpin family C member 1	Homo sapiens	152-168
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
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
6422851-5	1984	The products obtained after removal of sugars from antithrombin retained thrombin-neutralizing activity.	Sugars	39-45	serpin family C member 1	Homo sapiens	51-63
6422851-7	1984	Thus, the sugar residues of thrombin and antithrombin are not required for the formation of enzyme-inhibitor complexes or for the other activities that were measured.	Sugars	10-15	serpin family C member 1	Homo sapiens	41-53
6698980-14	1984	A model of the antithrombin III-binding octasaccharide (Lindahl, U., Backstrom, G., Thunberg, L., and Leder, I. G. (1980) Proc.	Octasaccharide	40-54	serpin family C member 1	Homo sapiens	15-31
6698980-19	1984	These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III.	Lysine	55-61	serpin family C member 1	Homo sapiens	219-235
6698980-19	1984	These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III.	Sulfates	144-151	serpin family C member 1	Homo sapiens	219-235
6698980-19	1984	These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III.	Octasaccharide	166-180	serpin family C member 1	Homo sapiens	219-235
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
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
6583694-1	1984	We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin.	Monosaccharides	56-70	serpin family C member 1	Homo sapiens	183-195
6583694-1	1984	We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin.	Octasaccharide	86-100	serpin family C member 1	Homo sapiens	183-195
6583694-1	1984	We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin.	Oligosaccharides	164-179	serpin family C member 1	Homo sapiens	183-195
6583694-2	1984	Different fragments of the octasaccharide were prepared by enzymatic digestion and the avidities of these oligosaccharides for antithrombin were determined by equilibrium dialysis.	Octasaccharide	27-41	serpin family C member 1	Homo sapiens	127-139
6583694-2	1984	Different fragments of the octasaccharide were prepared by enzymatic digestion and the avidities of these oligosaccharides for antithrombin were determined by equilibrium dialysis.	Oligosaccharides	106-122	serpin family C member 1	Homo sapiens	127-139
6583694-6	1984	We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule.	Uronic Acids	49-60	serpin family C member 1	Homo sapiens	223-235
6232045-0	1984	[Acute effects of sulodexide on the lipid profile and on antithrombin III in patients with chronic renal insufficiency in hemodialysis treatment].	glucuronyl glucosamine glycan sulfate	18-28	serpin family C member 1	Homo sapiens	57-73
6420409-0	1984	Pyridoxylation of essential lysines in the heparin-binding site of antithrombin III.	Lysine	28-35	serpin family C member 1	Homo sapiens	67-83
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
6420409-1	1984	Pyridoxal 5"-phosphate was used to selectively modify lysine residues on antithrombin III.	Pyridoxal Phosphate	0-22	serpin family C member 1	Homo sapiens	73-89
6420409-1	1984	Pyridoxal 5"-phosphate was used to selectively modify lysine residues on antithrombin III.	Lysine	54-60	serpin family C member 1	Homo sapiens	73-89
6420409-2	1984	Pyridoxal 5"-phosphate was incubated with antithrombin, and the Schiff base was reduced with sodium borohydride.	Pyridoxal Phosphate	0-22	serpin family C member 1	Homo sapiens	42-54
6420409-3	1984	A maximum of 3-4 pyridoxal 5"-phosphate groups per antithrombin molecule are bound at high concentrations of pyridoxal 5"-phosphate.	4 pyridoxal 5"-phosphate	15-39	serpin family C member 1	Homo sapiens	51-63
6420409-3	1984	A maximum of 3-4 pyridoxal 5"-phosphate groups per antithrombin molecule are bound at high concentrations of pyridoxal 5"-phosphate.	Pyridoxal Phosphate	17-39	serpin family C member 1	Homo sapiens	51-63
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
6420409-5	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.	Pyridoxal Phosphate	93-112	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.	Lysine	31-37	serpin family C member 1	Homo sapiens	69-85
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
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.	phosphopyridoxyl	37-53	serpin family C member 1	Homo sapiens	54-66
6583694-6	1984	We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule.	tetrasaccharide	97-112	serpin family C member 1	Homo sapiens	223-235
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
6420409-10	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.	Tryptophan	160-170	serpin family C member 1	Homo sapiens	54-66
6583694-6	1984	We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule.	n-acetyl glucosamine o6-sulfate	143-174	serpin family C member 1	Homo sapiens	223-235
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.	phosphopyridoxyl	184-200	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
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
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
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.	Tryptophan	34-44	serpin family C member 1	Homo sapiens	56-72
6693405-8	1984	The site of labeling corresponds to Trp 49, which is located within the disulfide-stabilized loops near the NH2-terminal end of the antithrombin III molecule.	Tryptophan	36-39	serpin family C member 1	Homo sapiens	132-148
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.	dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium	78-128	serpin family C member 1	Homo sapiens	56-72
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
6693405-8	1984	The site of labeling corresponds to Trp 49, which is located within the disulfide-stabilized loops near the NH2-terminal end of the antithrombin III molecule.	Disulfides	72-81	serpin family C member 1	Homo sapiens	132-148
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
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
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
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
6231919-0	1984	Inhibition by heparin-modulated antithrombin III of amidolysis catalysed by m beta-acrosin.	beta-acrosin	78-90	serpin family C member 1	Homo sapiens	32-48
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
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.	Heparitin Sulfate	86-102	serpin family C member 1	Homo sapiens	15-31
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.	cellulose sulphate	104-122	serpin family C member 1	Homo sapiens	15-31
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.	Dextran Sulfate	124-140	serpin family C member 1	Homo sapiens	15-31
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.	xylan sulphate	145-159	serpin family C member 1	Homo sapiens	15-31
6233149-3	1984	A significant decrease in antithrombin III (AT-III) activity of 27% (range 7-46%) was found in patients on an initially high-dose estrogen (diethylstilbestrol) treatment regime.	Diethylstilbestrol	140-158	serpin family C member 1	Homo sapiens	26-42
6233149-3	1984	A significant decrease in antithrombin III (AT-III) activity of 27% (range 7-46%) was found in patients on an initially high-dose estrogen (diethylstilbestrol) treatment regime.	Diethylstilbestrol	140-158	serpin family C member 1	Homo sapiens	44-50
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
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
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
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
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
6083907-10	1984	Cortisone and protamine chloride were found to exert direct effects on AT III function and concentration independent of the AT III defects mentioned.	Cortisone	0-9	serpin family C member 1	Homo sapiens	71-77
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
6334690-2	1984	In vitro hepatocyte-uptake studies with antithrombin III-proteinase complexes confirmed the hepatocyte uptake and degradation of these complexes, and demonstrated the formation of a disulfide interchange product between the ligand and a cellular protein.	Disulfides	182-191	serpin family C member 1	Homo sapiens	40-56
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
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
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
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.	Oligosaccharides	178-194	serpin family C member 1	Homo sapiens	232-244
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
6582486-2	1984	Abnormal antithrombin III was reduced, S-pyridylethylated, and treated with cyanogen bromide.	Cyanogen Bromide	76-92	serpin family C member 1	Homo sapiens	9-25
6582486-6	1984	Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama.	Arginine	72-80	serpin family C member 1	Homo sapiens	94-110
6582486-6	1984	Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama.	Arginine	72-80	serpin family C member 1	Homo sapiens	94-106
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
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).	Sepharose	178-187	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).	Sepharose	178-187	serpin family C member 1	Homo sapiens	91-97
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-sepharose	189-191	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-sepharose	189-191	serpin family C member 1	Homo sapiens	91-97
6516292-3	1984	Pasteurization of the AT III concentrate in the presence of 0.5 M sodium citrate to minimize the risk of hepatitis decreases the recovery by about 20% and induces changes in the patterns obtained by polyacrylamide gel electrophoresis and by crossed immunoelectrophoresis in heparinized agarose gel.	Sodium Citrate	66-80	serpin family C member 1	Homo sapiens	22-28
6516292-3	1984	Pasteurization of the AT III concentrate in the presence of 0.5 M sodium citrate to minimize the risk of hepatitis decreases the recovery by about 20% and induces changes in the patterns obtained by polyacrylamide gel electrophoresis and by crossed immunoelectrophoresis in heparinized agarose gel.	polyacrylamide	199-213	serpin family C member 1	Homo sapiens	22-28
6516292-3	1984	Pasteurization of the AT III concentrate in the presence of 0.5 M sodium citrate to minimize the risk of hepatitis decreases the recovery by about 20% and induces changes in the patterns obtained by polyacrylamide gel electrophoresis and by crossed immunoelectrophoresis in heparinized agarose gel.	Sepharose	286-293	serpin family C member 1	Homo sapiens	22-28
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
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
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
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
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
6643505-2	1983	Reactions were monitored continuously through the loss of fluorescence intensity accompanying the displacement of the reversible inhibitor dansylarginine-N-(3-ethyl-1,5-pentanediyl)amide from thrombin upon its interaction with antithrombin III.	dansylarginine N-(3-ethyl-1,5-pentanediyl)amide	139-186	serpin family C member 1	Homo sapiens	227-243
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
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
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
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
6607710-3	1983	In each case, an inhibitor with remarkably similar properties to human antithrombin was isolated by affinity chromatography on immobilized porcine heparin.	porcine heparin	139-154	serpin family C member 1	Homo sapiens	71-83
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
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
6640109-7	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
6640109-7	1983	The abnormal antithrombin ("Chicago") was found to elute from heparin-Sepharose at a higher ionic strength than normal inhibitor.	Sepharose	70-79	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
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
6643466-2	1983	The presence of two unfolding domains in antithrombin III during its denaturation in guanidinium chloride has previously been reported (Villanueva, G. B., and Allen, N. (1983) J. Biol.	Guanidine	85-105	serpin family C member 1	Homo sapiens	41-57
6195981-4	1983	Both groups exhibited below normal antithrombin III and plasminogen levels, with significantly lower antithrombin III levels noted in the HES group postoperatively (41.9 +/- 11.8% versus 56.6 +/- 9.9%; p = 0.006).	Hydroxyethyl Starch Derivatives	138-141	serpin family C member 1	Homo sapiens	101-117
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%.	Tryptophan	13-23	serpin family C member 1	Homo sapiens	127-143
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
6651824-3	1983	In contrast, the synthetic pentasaccharide strongly binds to AT-III (Ka: 7.10(6)M-1) forming an equimolar complex and also enhances the AT-III inhibitory activity towards factor Xa.	pentasaccharide	27-42	serpin family C member 1	Homo sapiens	61-67
6651824-3	1983	In contrast, the synthetic pentasaccharide strongly binds to AT-III (Ka: 7.10(6)M-1) forming an equimolar complex and also enhances the AT-III inhibitory activity towards factor Xa.	pentasaccharide	27-42	serpin family C member 1	Homo sapiens	136-142
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.	pentasaccharide	41-56	serpin family C member 1	Homo sapiens	160-166
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
6640057-0	1983	Affinity of purified thrombin or antithrombin III for two insoluble anticoagulant polystyrene derivatives: I.	Polystyrenes	82-93	serpin family C member 1	Homo sapiens	33-49
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
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
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
6192845-1	1983	The inactivation of human coagulation factor Xa by the plasma proteinase inhibitors alpha 1-antitrypsin, antithrombin III and alpha 2-macroglobulin in purified systems was found to be accelerated by the divalent cations Ca2+, Mn2+ and Mg2+.	Manganese(2+)	226-230	serpin family C member 1	Homo sapiens	105-121
6192845-1	1983	The inactivation of human coagulation factor Xa by the plasma proteinase inhibitors alpha 1-antitrypsin, antithrombin III and alpha 2-macroglobulin in purified systems was found to be accelerated by the divalent cations Ca2+, Mn2+ and Mg2+.	magnesium ion	235-239	serpin family C member 1	Homo sapiens	105-121
6192845-2	1983	The rate constant for the inhibition of factor Xa by antithrombin III rose from 2.62 X 10(4) M-1 X min-1 in the absence of divalent cations to a maximum of 6.40 X 10(4) M-1 X min-1 at 5 mM Ca2+, 8.10 X 10(4) M-1 X min-1 at 5 mM Mn2+, with a slight decrease in rate at higher cation concentrations.	Manganese(2+)	228-232	serpin family C member 1	Homo sapiens	53-69
6625618-0	1983	Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin.	Calcium	0-7	serpin family C member 1	Homo sapiens	39-55
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
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
6625618-1	1983	The present study has shown that calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction.	Calcium	33-40	serpin family C member 1	Homo sapiens	72-88
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
6625618-2	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.	Calcium	211-218	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
6625618-8	1983	The apparent kinetic parameters for the heparin-catalyzed antithrombin III/thrombin reaction were determined in the presence and absence of calcium.	Calcium	140-147	serpin family C member 1	Homo sapiens	58-74
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
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
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
6889048-1	1983	In 34 girls who were treated with large doses of ethinylestradiol because of expected excessive tall stature, antithrombin activity in the blood was followed before, during, and after treatment.	Ethinyl Estradiol	49-65	serpin family C member 1	Homo sapiens	110-122
6136676-0	1983	Effect of stanozolol on antithrombin III and protein C.	Stanozolol	10-20	serpin family C member 1	Homo sapiens	24-40
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
6410910-1	1983	Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage.	polyethylene glycol 400	63-86	serpin family C member 1	Homo sapiens	0-16
6885772-0	1983	The antithrombin-binding sequence in heparin.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
6885772-2	1983	An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	41-53
6885772-2	1983	An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit.	l-iduronosyl-n-acetylglucosaminyl-6-o-sulfate	143-188	serpin family C member 1	Homo sapiens	41-53
6885772-2	1983	An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit.	Disaccharides	210-222	serpin family C member 1	Homo sapiens	41-53
6885772-3	1983	After digestion of this octasaccharide with alpha-L-iduronidase and N-acetylglucosamine-6-sulfate sulfatase, two fractions, with high and low affinity for antithrombin, respectively, were isolated by affinity chromatography on antithrombin-Sepharose.	Octasaccharide	24-38	serpin family C member 1	Homo sapiens	155-167
6885772-3	1983	After digestion of this octasaccharide with alpha-L-iduronidase and N-acetylglucosamine-6-sulfate sulfatase, two fractions, with high and low affinity for antithrombin, respectively, were isolated by affinity chromatography on antithrombin-Sepharose.	Sepharose	240-249	serpin family C member 1	Homo sapiens	155-167
6885772-6	1983	This less degraded heptasaccharide retained high affinity for antithrombin.	Xyloglucan Heptasaccharide	19-34	serpin family C member 1	Homo sapiens	62-74
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.	Sulfates	27-34	serpin family C member 1	Homo sapiens	141-153
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.	Acetylglucosamine	48-67	serpin family C member 1	Homo sapiens	141-153
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
6603874-3	1983	As a result of fractionation of products on the column with DEAE-Sephadex A-50, some fractions that have thrombin amidase activity (splitting of the substrate S-2238) and high antithrombin activity were obtained.	DEAE-Sephadex A-50	60-78	serpin family C member 1	Homo sapiens	176-188
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
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.	deae-agarose	80-92	serpin family C member 1	Homo sapiens	16-28
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
6410910-1	1983	Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage.	polyethylene glycol 400	63-86	serpin family C member 1	Homo sapiens	18-24
6410910-1	1983	Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage.	polyethylene glycol 400	88-91	serpin family C member 1	Homo sapiens	0-16
6410910-1	1983	Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage.	polyethylene glycol 400	88-91	serpin family C member 1	Homo sapiens	18-24
6410910-2	1983	The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated.	polyethylene glycol 400	4-7	serpin family C member 1	Homo sapiens	91-97
6410910-2	1983	The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated.	polyethylene glycol 400	4-7	serpin family C member 1	Homo sapiens	116-122
6410910-2	1983	The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated.	peg-sup	21-28	serpin family C member 1	Homo sapiens	91-97
6410910-8	1983	They differed, however, in that the PEG-sup and AT III-HCF demonstrated considerably reduced progressive antithrombin function assessed over 30 min.	polyethylene glycol 400	36-39	serpin family C member 1	Homo sapiens	105-117
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.	sephacryl	92-101	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
6410910-10	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.	sephacryl	173-182	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.	sephacryl	173-182	serpin family C member 1	Homo sapiens	192-198
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
6410910-13	1983	On the basis of these observations, it is postulated that AT III purified by PEG precipitation is in an aggregated form and that aggregate formation and dissolution is associated with AT III progressive activity.	polyethylene glycol 400	77-80	serpin family C member 1	Homo sapiens	58-64
6679287-1	1983	The treatment of three patients suffering from carbon tetrachloride intoxication with antithrombin III and plasma derivatives is reported.	Carbon Tetrachloride	47-67	serpin family C member 1	Homo sapiens	86-102
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
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.	Polysaccharides	137-151	serpin family C member 1	Homo sapiens	26-38
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.	Polysaccharides	137-151	serpin family C member 1	Homo sapiens	159-171
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
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
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
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
6636041-4	1983	After administration of aspirin (acetylsalicylic acid), however, AT-III levels increased presumably due to inhibition of coagulation activities.	Aspirin	24-31	serpin family C member 1	Homo sapiens	65-71
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
6636041-4	1983	After administration of aspirin (acetylsalicylic acid), however, AT-III levels increased presumably due to inhibition of coagulation activities.	Aspirin	33-53	serpin family C member 1	Homo sapiens	65-71
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
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	barium chloride	173-188	serpin family C member 1	Homo sapiens	22-38
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	barium chloride	173-188	serpin family C member 1	Homo sapiens	40-46
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	barium chloride	173-188	serpin family C member 1	Homo sapiens	49-65
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	Ammonium Sulfate	193-209	serpin family C member 1	Homo sapiens	22-38
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
6305982-5	1983	ATIII cDNA clones were identified by hybridization to a mixture of synthetic oligodeoxynucleotides encoding amino acids 251-256 of the ATIII protein sequence.	Oligodeoxyribonucleotides	77-98	serpin family C member 1	Homo sapiens	0-5
6305982-5	1983	ATIII cDNA clones were identified by hybridization to a mixture of synthetic oligodeoxynucleotides encoding amino acids 251-256 of the ATIII protein sequence.	Oligodeoxyribonucleotides	77-98	serpin family C member 1	Homo sapiens	135-140
6193602-1	1983	Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl.	Pentosan Sulfuric Polyester	0-21	serpin family C member 1	Homo sapiens	88-93
6193602-1	1983	Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl.	Pentosan Sulfuric Polyester	23-26	serpin family C member 1	Homo sapiens	88-93
6193602-1	1983	Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl.	Sepharose	94-103	serpin family C member 1	Homo sapiens	88-93
6193602-1	1983	Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl.	Sodium Chloride	120-124	serpin family C member 1	Homo sapiens	88-93
6193602-7	1983	The antiheparin effect of PPS was also observed in a purified system in obviating the heparin potentiation of the rate of inhibition of thrombin by antithrombin III.	Pentosan Sulfuric Polyester	26-29	serpin family C member 1	Homo sapiens	148-164
6193602-8	1983	Observations showed that at higher concentrations of PPS it acted by directly inhibiting thrombin without the intervention of antithrombin III but also to potentiate the rate of fibrin monomer polymerization.	Pentosan Sulfuric Polyester	53-56	serpin family C member 1	Homo sapiens	126-142
6857515-0	1983	Effects of low-dose warfarin on antithrombin III levels in morbidly obese patients.	Warfarin	20-28	serpin family C member 1	Homo sapiens	32-48
6879515-0	1983	Differential AT III-response to oral and parenteral administration of 17 beta-estradiol.	Estradiol	70-87	serpin family C member 1	Homo sapiens	13-19
6612689-0	1983	The effect of variable fat diets and cholesterol-lowering drugs on Antithrombin III levels in hyperlipoproteinemic and normal subjects.	Cholesterol	37-48	serpin family C member 1	Homo sapiens	67-83
6687888-1	1983	We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma.	Glycosaminoglycans	38-56	serpin family C member 1	Homo sapiens	141-157
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	Ammonium Sulfate	193-209	serpin family C member 1	Homo sapiens	40-46
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	Sepharose	265-274	serpin family C member 1	Homo sapiens	22-38
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	Sepharose	265-274	serpin family C member 1	Homo sapiens	40-46
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	Sepharose	265-274	serpin family C member 1	Homo sapiens	49-65
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	DEAE-Dextran	284-297	serpin family C member 1	Homo sapiens	22-38
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	DEAE-Dextran	284-297	serpin family C member 1	Homo sapiens	40-46
6636046-1	1983	A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography.	DEAE-Dextran	284-297	serpin family C member 1	Homo sapiens	49-65
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
6885810-0	1983	Demonstration of a two-domain structure of antithrombin III during its denaturation in guanidinium chloride.	Guanidine	87-107	serpin family C member 1	Homo sapiens	43-59
6885810-1	1983	The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy.	Urea	46-50	serpin family C member 1	Homo sapiens	26-42
6885810-1	1983	The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy.	Guanidine	55-75	serpin family C member 1	Homo sapiens	26-42
6885810-1	1983	The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy.	Guanidine	77-82	serpin family C member 1	Homo sapiens	26-42
6687888-1	1983	We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma.	Glycosaminoglycans	38-56	serpin family C member 1	Homo sapiens	159-164
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
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
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
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
6687802-5	1983	The results suggest that heparin cofactor II differs from antithrombin III with respect to the mucopolysaccharide binding site.	Glycosaminoglycans	95-113	serpin family C member 1	Homo sapiens	58-74
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
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
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
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
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
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
6832015-0	1983	[Perioperative plasma antithrombin activity with "low-dose" heparin prophylaxis.	Heparin	60-67	serpin family C member 1	Homo sapiens	22-34
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
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.	Edetic Acid	187-191	serpin family C member 1	Homo sapiens	124-140
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
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
6830338-6	1983	The individual, nadir levels of FN, AT III, prealbumin, and transferrin were lower (p less than 0.01) in the septic group A than in B and C. Within the septic group, the nadir levels of AT III, but not those of FN, were lower (p less than 0.01) in the 14 nonsurvivors than in the 19 survivors.	nadir	170-175	serpin family C member 1	Homo sapiens	186-192
6830362-3	1983	Analysis of the data revealed that patients with high triglyceride levels also have a high incidence of low antithrombin III activity and increased platelet aggregation.	Triglycerides	54-66	serpin family C member 1	Homo sapiens	108-124
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
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
6845270-4	1983	Molecular forms of AT III produced in plasma treated with coagulation enzymes, or in serum, were assessed by measuring immunoreactive AT III in fractions obtained by gel filtration chromatography on Sephadex G-200.	sephadex	199-213	serpin family C member 1	Homo sapiens	19-25
6830263-0	1983	Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation.	Disulfides	20-29	serpin family C member 1	Homo sapiens	44-60
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
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
6830263-3	1983	Alkylation of mildly reduced antithrombin III with [3H]iodacetic acid followed by digestion with cyanogen bromide yielded two major labeled peptides.	[3h]iodacetic acid	51-69	serpin family C member 1	Homo sapiens	29-45
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Disulfides	39-48	serpin family C member 1	Homo sapiens	57-73
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Disulfides	39-48	serpin family C member 1	Homo sapiens	150-166
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Cysteine	90-93	serpin family C member 1	Homo sapiens	57-73
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Cysteine	90-93	serpin family C member 1	Homo sapiens	150-166
6830263-7	1983	These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines.	Cysteine	102-105	serpin family C member 1	Homo sapiens	57-73
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
6845286-0	1983	Antithrombin III-binding capacity of heparin-sepharose as a function of activation temperature and duration.	Sepharose	45-54	serpin family C member 1	Homo sapiens	0-16
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
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
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
6338832-1	1983	The inhibition of thrombin by antithrombin-III involves formation of a 1:1 covalent complex between protease and inhibitor and concomitant cleavage of the antithrombin-III peptide chain after Arg-385.	Arginine	192-195	serpin family C member 1	Homo sapiens	30-46
6338832-1	1983	The inhibition of thrombin by antithrombin-III involves formation of a 1:1 covalent complex between protease and inhibitor and concomitant cleavage of the antithrombin-III peptide chain after Arg-385.	Arginine	192-195	serpin family C member 1	Homo sapiens	155-171
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
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
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
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.	Sepharose	57-64	serpin family C member 1	Homo sapiens	149-165
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.	Sodium Chloride	94-98	serpin family C member 1	Homo sapiens	149-165
6403706-8	1983	Minimal alterations were seen with the levonorgestrel preparation, whereas those containing norethindrone or ethynodiol diacetate showed marked increases in factors I, VII, VIII and X and plasminogen, associated with a decrease in antithrombin III.	Norethindrone	92-105	serpin family C member 1	Homo sapiens	231-247
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
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.	Dipyridamole	160-172	serpin family C member 1	Homo sapiens	30-36
6403706-8	1983	Minimal alterations were seen with the levonorgestrel preparation, whereas those containing norethindrone or ethynodiol diacetate showed marked increases in factors I, VII, VIII and X and plasminogen, associated with a decrease in antithrombin III.	Ethynodiol Diacetate	109-129	serpin family C member 1	Homo sapiens	231-247
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
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
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
6132465-4	1982	Studies on binding to Antithrombin III - Sepharose showed that sulphated guaran and a fraction of the aminated and sulphated alginic acid was bound, whereas no binding occurred with sulphated alginic acid.	Sepharose	41-50	serpin family C member 1	Homo sapiens	22-38
6868150-3	1983	Relations were found connecting polar (delta) and steric (Es) characteristics of substituent (R) in R-C6H4-SO2-Arg-OCH3 esters with their antithrombin activity in vitro or with efficiency of their thrombin-catalyzed hydrolysis.	Einsteinium	58-60	serpin family C member 1	Homo sapiens	138-150
6868150-3	1983	Relations were found connecting polar (delta) and steric (Es) characteristics of substituent (R) in R-C6H4-SO2-Arg-OCH3 esters with their antithrombin activity in vitro or with efficiency of their thrombin-catalyzed hydrolysis.	r-c6h4-so2-arg-och3 esters	100-126	serpin family C member 1	Homo sapiens	138-150
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
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
6132465-6	1982	The two alginic acid preparations showed Antithrombin III-dependent inhibition of thrombin, whereas the sulphated guaran inhibits both by Antithrombin III-dependent and independent mechanisms.	Alginic Acid	8-20	serpin family C member 1	Homo sapiens	41-57
6132465-4	1982	Studies on binding to Antithrombin III - Sepharose showed that sulphated guaran and a fraction of the aminated and sulphated alginic acid was bound, whereas no binding occurred with sulphated alginic acid.	Alginic Acid	125-137	serpin family C member 1	Homo sapiens	22-38
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
6961402-0	1982	Circular dichroism spectroscopy of heparin-antithrombin interactions.	Heparin	35-42	serpin family C member 1	Homo sapiens	43-55
6961402-1	1982	We have utilized circular dichroism spectroscopy to examine the interaction of antithrombin with heparin-derived oligosaccharides and mucopolysaccharides of various sizes.	heparin-derived oligosaccharides	97-129	serpin family C member 1	Homo sapiens	79-91
6961402-1	1982	We have utilized circular dichroism spectroscopy to examine the interaction of antithrombin with heparin-derived oligosaccharides and mucopolysaccharides of various sizes.	Glycosaminoglycans	134-153	serpin family C member 1	Homo sapiens	79-91
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.	octadecasaccharide	46-64	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	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
6961402-15	1982	Given our method for generating the above data, these spectral alterations must be associated with the binding of a second critical domain of the mucopolysaccharide to antithrombin that is required for rapid complex formation with thrombin or the activation of the protease inhibitor with respect to the neutralization of the latter enzyme.	Glycosaminoglycans	146-164	serpin family C member 1	Homo sapiens	168-180
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
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
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
6812990-1	1982	Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO).	chromozym TH	97-109	serpin family C member 1	Homo sapiens	0-16
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
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
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
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.	Sepharose	139-148	serpin family C member 1	Homo sapiens	40-56
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.	Sepharose	139-148	serpin family C member 1	Homo sapiens	122-138
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
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
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
7164033-8	1982	This antithrombin III independent inhibition of the activation of prothrombin was also evident when activated platelets were used as the source of the procoagulant phospholipids.	Phospholipids	164-177	serpin family C member 1	Homo sapiens	5-21
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
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
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.	Glycosaminoglycans	172-190	serpin family C member 1	Homo sapiens	4-20
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
7158775-0	1982	Preparation of three types of heparin-sepharose and their binding activities to thrombin and antithrombin III.	Sepharose	38-47	serpin family C member 1	Homo sapiens	93-109
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
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.	Sepharose	56-63	serpin family C member 1	Homo sapiens	126-138
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
7109075-3	1982	A loading dose of 15 mg. diethylstilbestrol daily resulted in a marked decrease in plasma antithrombin III activity (mean 0.24 U. per ml.).	Diethylstilbestrol	25-43	serpin family C member 1	Homo sapiens	90-106
7117524-0	1982	Permanent activation of antithrombin by covalent attachment of heparin oligosaccharides.	heparin oligosaccharides	63-87	serpin family C member 1	Homo sapiens	24-36
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
7082587-7	1982	The two populations of AT III were separated by affinity chromatography on heparin-agarose.	Sepharose	83-90	serpin family C member 1	Homo sapiens	23-29
7082587-8	1982	50% of the patients" AT III bound to the agarose beads.	Sepharose	41-48	serpin family C member 1	Homo sapiens	21-27
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
6285503-7	1982	Furthermore, a significant decrease in both antithrombin III levels and basal and venostasis-stimulated plasminogen activator levels were seen in glibenclamide patients.	Glyburide	146-159	serpin family C member 1	Homo sapiens	44-60
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
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
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
6461438-4	1982	This assay using Bz-Leu-Ala-Arg-NE is a highly sensitive method for detecting prothrombin, thrombin and antithrombin III in human plasma.	bz-leu-ala-arg	17-31	serpin family C member 1	Homo sapiens	104-120
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
6807052-3	1982	Antithrombin III (AT III) was always found along the inside of thickened TBM in every atrophic nephron, but not found in the sclerotic GT nor along the thickened BC.	metsulfuron methyl	73-76	serpin family C member 1	Homo sapiens	0-16
6807052-3	1982	Antithrombin III (AT III) was always found along the inside of thickened TBM in every atrophic nephron, but not found in the sclerotic GT nor along the thickened BC.	metsulfuron methyl	73-76	serpin family C member 1	Homo sapiens	18-24
6807052-6	1982	At III was easily dissociated from the thickened TBM after the incubation in warm (37 degrees C) 0.01 M phosphate buffered saline of various pH (pH 4.0, pH 7.2 or pH 10.0) and cold (4 degrees C) or warm (37 degrees C) 0.75 M hydrazine solutions of the same pH, while alpha 1AT was not dissociated from the atrophic nephrons after the incubation in all solutions.	Phosphate-Buffered Saline	104-129	serpin family C member 1	Homo sapiens	0-6
6807052-6	1982	At III was easily dissociated from the thickened TBM after the incubation in warm (37 degrees C) 0.01 M phosphate buffered saline of various pH (pH 4.0, pH 7.2 or pH 10.0) and cold (4 degrees C) or warm (37 degrees C) 0.75 M hydrazine solutions of the same pH, while alpha 1AT was not dissociated from the atrophic nephrons after the incubation in all solutions.	hydrazine	225-234	serpin family C member 1	Homo sapiens	0-6
7037067-0	1982	Differential role of fractionated heparin in antithrombin-III proteolysis.	Heparin	34-41	serpin family C member 1	Homo sapiens	45-61
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
7037067-2	1982	Proteolysis of residual AT-III was assessed on the basis of distribution of radioactivity in SDS-polyacrylamide gels after electrophoresis.	Sodium Dodecyl Sulfate	93-96	serpin family C member 1	Homo sapiens	24-30
7037067-2	1982	Proteolysis of residual AT-III was assessed on the basis of distribution of radioactivity in SDS-polyacrylamide gels after electrophoresis.	polyacrylamide	97-111	serpin family C member 1	Homo sapiens	24-30
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
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
7083257-0	1982	Further characterization of the antithrombin-binding sequence in heparin.	Heparin	65-72	serpin family C member 1	Homo sapiens	32-44
7083257-1	1982	An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin and previously found to have the following predominant structure (see formula in text) has been studied further.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	41-53
7083257-10	1982	These results suggest that the 6-sulfate group in unit 2 may be involved in antithrombin binding.	Sulfates	33-40	serpin family C member 1	Homo sapiens	76-88
7083257-11	1982	It is concluded that the antithrombin binding site in heparin is represented by the pentasaccharide sequence extending from unit 2 to unit 6 of the octasaccharide studied.	pentasaccharide	84-99	serpin family C member 1	Homo sapiens	25-37
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
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
6802163-2	1982	Normal and sclerotic CSs accelerated the inactivation of thrombin by antithrombin III to an equal extent.	Chondroitin Sulfates	21-24	serpin family C member 1	Homo sapiens	69-85
7059522-0	1982	A novel semi-synthetic sulphated polysaccharide with potent antithrombin activity.	Polysaccharides	33-47	serpin family C member 1	Homo sapiens	60-72
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.	Glycosaminoglycans	40-58	serpin family C member 1	Homo sapiens	74-86
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
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
7064134-2	1982	In essence the approach takes advantage of the fact that synthetic substrates, e.g. N-alpha-p-tosyl-L-glycyl-L-prolyl-L-arginine-p-nitroanilide, bind to the active site of thrombin, which slows the rate of reaction with antithrombin III.	n-alpha-p-tosyl-l-glycyl-l-prolyl-l-arginine-p-nitroanilide	84-143	serpin family C member 1	Homo sapiens	220-236
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
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
6187640-1	1982	Tri-calciumphosphate was found to have not only a known adsorption capacity for factors of the prothrombin complex, but also for antithrombin III.	tricalcium phosphate	0-20	serpin family C member 1	Homo sapiens	129-145
6187640-4	1982	Liberating antithrombin III from calciumphosphate is made with care without using any concentrated salt solutions.	calcium phosphate	33-49	serpin family C member 1	Homo sapiens	11-27
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
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.	Lysine	121-127	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
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
7342649-0	1981	Vitamin K dependent clotting factors and their inhibitor--with special reference to prothrombin and antithrombin III.	Vitamin K	0-9	serpin family C member 1	Homo sapiens	100-116
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
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
6183640-0	1982	[A study of antithrombin systems during heparin therapy].	Heparin	40-47	serpin family C member 1	Homo sapiens	12-24
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
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
7157229-4	1982	In contrast thrombin, antithrombin III and factor Xa adsorb on the surface of such insoluble polymers.	Polymers	93-101	serpin family C member 1	Homo sapiens	22-38
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
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
7107605-5	1982	Furthermore, incubation of the mastocytoma endoglucuronidase with a heparin octasaccharide having high affinity for antithrombin failed to cleave the beta-glucuronidic linkage in the antithrombin-binding region.	heparin octasaccharide	68-90	serpin family C member 1	Homo sapiens	116-128
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
7107605-8	1982	The loss of bio-affinity resulting from cleavage of this linkage in the antithrombin-binding heparin octasaccharide was utilized to construct a sensitive, specific, and simple assay method for the platelet endoglucuronidase.	heparin octasaccharide	93-115	serpin family C member 1	Homo sapiens	72-84
7173439-1	1982	Acetylcholine entailed a release of substance possessing activity of the blood plasma antithrombin III into the intestinal vascular bed and activated to some extent the release of antifibrinolytic compounds.	Acetylcholine	0-13	serpin family C member 1	Homo sapiens	86-102
7147215-0	1982	Effect of sulfinpyrazone upon antithrombin III and platelet factor 4 in chronic renal failure.	Sulfinpyrazone	10-24	serpin family C member 1	Homo sapiens	30-46
7147215-3	1982	Sulfinpyrazone, a drug capable of reducing the frequency of thrombotic events in uremic patients, allows return toward normal of the AT III while reducing to normal the plasma concentration of PF4.	Sulfinpyrazone	0-14	serpin family C member 1	Homo sapiens	133-139
7147215-4	1982	Thus, suppression of platelet function by sulfinpyrazone appears to reduce in vivo clotting, and thus reduces consumption of AT III.	Sulfinpyrazone	42-56	serpin family C member 1	Homo sapiens	125-131
7082848-6	1982	Turnover studies were made in the patient using her own purified AT-III labeled with 131I, (*I).	Iodine-131	85-89	serpin family C member 1	Homo sapiens	65-71
7112497-2	1982	Specific antithrombin activity in plasma showed a negative correlation with triglyceride levels.	Triglycerides	76-88	serpin family C member 1	Homo sapiens	9-21
7112497-3	1982	The consumption of antithrombin activity during blood clotting was negatively correlated with both serum total triglyceride and heparin precipitable lipoprotein and positively correlated with serum high density lipoprotein cholesterol.	Triglycerides	111-123	serpin family C member 1	Homo sapiens	19-31
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
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
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
6179183-5	1982	Our data indicate that pentosan polysulphate has more marked effects in vivo than in vitro, that the action of the drug on clotting is mediated mainly via an At III-independent pathway, and that its effects are not confined to the coagulation system.	Pentosan Sulfuric Polyester	23-44	serpin family C member 1	Homo sapiens	158-164
7101236-0	1982	Inhibition of thrombin-neutralizing activity of antithrombin III by steroid hormones.	Steroids	68-84	serpin family C member 1	Homo sapiens	48-64
7101236-11	1982	ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone.	Cholesterol	76-87	serpin family C member 1	Homo sapiens	12-18
7101236-11	1982	ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone.	Cortisone	89-98	serpin family C member 1	Homo sapiens	12-18
7101236-11	1982	ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone.	Testosterone	100-112	serpin family C member 1	Homo sapiens	12-18
7101236-11	1982	ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone.	Progesterone	117-129	serpin family C member 1	Homo sapiens	12-18
7101236-12	1982	Our studies suggest a direct effect of estrogens and other steroids on AT III, altering its specific neutralization of thrombin.	Steroids	59-67	serpin family C member 1	Homo sapiens	71-77
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.	Oligosaccharides	147-162	serpin family C member 1	Homo sapiens	122-138
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
7112509-0	1982	Preparation of highly stable antithrombin-sepharose and utilization for the fractionation of heparin.	Sepharose	42-51	serpin family C member 1	Homo sapiens	29-41
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
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
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
6977539-7	1982	The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor.	Ammonia	94-101	serpin family C member 1	Homo sapiens	13-25
6977539-7	1982	The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor.	Ammonia	94-101	serpin family C member 1	Homo sapiens	41-53
6977539-7	1982	The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor.	Hydroxylamine	105-118	serpin family C member 1	Homo sapiens	13-25
6977539-7	1982	The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor.	Hydroxylamine	105-118	serpin family C member 1	Homo sapiens	41-53
6977539-9	1982	The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin.	Arginine	168-171	serpin family C member 1	Homo sapiens	72-84
6977539-9	1982	The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin.	Arginine	168-171	serpin family C member 1	Homo sapiens	212-224
6977539-9	1982	The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin.	Serine	172-175	serpin family C member 1	Homo sapiens	72-84
6977539-9	1982	The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin.	Serine	172-175	serpin family C member 1	Homo sapiens	212-224
7083257-11	1982	It is concluded that the antithrombin binding site in heparin is represented by the pentasaccharide sequence extending from unit 2 to unit 6 of the octasaccharide studied.	Octasaccharide	148-162	serpin family C member 1	Homo sapiens	25-37
6173074-11	1982	Cephalin was shown to inhibit the rate of reaction between factor Xa and antithrombin III.	Phosphatidylethanolamines	0-8	serpin family C member 1	Homo sapiens	73-89
7134791-4	1982	The high antithrombin III level in the Eskimos may at least partly be a consequence of a high dietary intake of polyunsaturated fatty acids.	Fatty Acids, Unsaturated	112-139	serpin family C member 1	Homo sapiens	9-25
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
6175043-3	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.	Sepharose	269-278	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
7073686-0	1982	Potentiation by calcium ions of the antithrombin III inhibition of thrombin.	Calcium	16-23	serpin family C member 1	Homo sapiens	36-52
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
7053378-2	1982	This methodology is able to subdivide the active mucopolysaccharide pools of molecular weight 6,000 to 8,000 (LMW) or 18,000 to 22,000 (HMW) into various species with descending affinities for antithrombin as well as decreasing anticoagulant potencies.	Glycosaminoglycans	49-67	serpin family C member 1	Homo sapiens	193-205
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
7053378-6	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.	Glycosaminoglycans	230-248	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
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.	Glycosaminoglycans	169-187	serpin family C member 1	Homo sapiens	152-164
6176339-0	1982	[Separation and purification of antithrombin III, thrombin and carboxypeptidase N using affinity sorption on the copolymer hydroxyalkylmethacrylate with immobilized heparin (heparinoid)].	copolymer hydroxyalkylmethacrylate	113-147	serpin family C member 1	Homo sapiens	32-48
7035043-0	1982	Paradoxical behaviour of antithrombin III during hemodialysis and its prevention with prostacyclin.	Epoprostenol	86-98	serpin family C member 1	Homo sapiens	25-41
6177612-0	1982	Benzamidine derivatives--relationship between antithrombin activity and structure.	benzamidine	0-11	serpin family C member 1	Homo sapiens	46-58
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
6460338-4	1981	Treatment with sulphinpyrazone resulted in lengthening of both platelet and fibrinogen survival, a rise in ATIII but no change in the beta tg or PF4 concentrations.	Sulfinpyrazone	15-30	serpin family C member 1	Homo sapiens	107-112
7298649-6	1981	The extent of the increase in 8-anilino-1-naphthalene sulfonate fluorescence correlates roughly with the loss of antithrombin activity and with the extent of protein aggregation as determined by high pressure liquid chromatography.	8-anilino-1-naphthalenesulfonic acid	30-63	serpin family C member 1	Homo sapiens	113-125
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
7337233-0	1981	Fractionation of heparin using antithrombin III reversibly bound to concanavalin A-sepharose.	Sepharose	83-92	serpin family C member 1	Homo sapiens	31-47
7308558-0	1981	The antithrombin-binding sequence of heparin.	Heparin	37-44	serpin family C member 1	Homo sapiens	4-16
7287751-0	1981	Binding of high affinity heparin to antithrombin III.	Heparin	25-32	serpin family C member 1	Homo sapiens	36-52
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
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
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.	Iodides	230-236	serpin family C member 1	Homo sapiens	42-54
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
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
7295594-0	1981	Abnormal migration of serum antithrombin III in patients on coumarin therapy by cross-immunoelectrophoresis.	coumarin	60-68	serpin family C member 1	Homo sapiens	28-44
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
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.	Octasaccharide	84-98	serpin family C member 1	Homo sapiens	122-138
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.	Octasaccharide	84-98	serpin family C member 1	Homo sapiens	264-280
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.	Sepharose	238-250	serpin family C member 1	Homo sapiens	122-138
7338523-3	1981	Fifty percent inactivation activities of the octasaccharide for thrombin and factor Xa in the presence of antithrombin III were 2 and 6.5 times, respectively, higher than those of the initial heparin.	Octasaccharide	45-59	serpin family C member 1	Homo sapiens	106-122
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
6812990-1	1982	Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO).	chromozym TH	97-109	serpin family C member 1	Homo sapiens	18-24
7029926-3	1981	In glomerular proteinuria (20 patients not on steroid therapy) the plasma level of AT III correlated inversely to the renal AT III clearance.	Steroids	46-53	serpin family C member 1	Homo sapiens	83-89
6812990-1	1982	Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO).	tos-gly-arg-p-nitroanilide	111-137	serpin family C member 1	Homo sapiens	0-16
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
6812990-1	1982	Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO).	boehringer	139-149	serpin family C member 1	Homo sapiens	0-16
6812990-1	1982	Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO).	thiobenzyl benzyloxycarbonyl-L-lysinate	164-213	serpin family C member 1	Homo sapiens	0-16
6812990-1	1982	Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO).	du pont	215-222	serpin family C member 1	Homo sapiens	0-16
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
6800057-0	1981	Antithrombin III levels during heparin therapy.	Heparin	31-38	serpin family C member 1	Homo sapiens	0-16
7314061-0	1981	Bidimensional immunoelectrophoresis abnormal migration of serum antithrombin III in coumarin-treated patients.	coumarin	84-92	serpin family C member 1	Homo sapiens	64-80
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
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
7325974-0	1981	The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence.	heparin oligosaccharide	17-40	serpin family C member 1	Homo sapiens	110-126
7325974-3	1981	spectra of heparin oligosaccharides (essentially octasaccharides), having high affinity for antithrombin III and high anti-(Factor Xa) activity, prepared by three independent approaches (extraction, partial deaminative cleavage with HNO2 and partial depolymerization with bacterial heparinase), leading to different terminal residues, have been studied and compared with those of the corresponding inactive species.	heparin oligosaccharides	11-35	serpin family C member 1	Homo sapiens	92-108
7325974-3	1981	spectra of heparin oligosaccharides (essentially octasaccharides), having high affinity for antithrombin III and high anti-(Factor Xa) activity, prepared by three independent approaches (extraction, partial deaminative cleavage with HNO2 and partial depolymerization with bacterial heparinase), leading to different terminal residues, have been studied and compared with those of the corresponding inactive species.	octasaccharides	49-64	serpin family C member 1	Homo sapiens	92-108
6167624-5	1981	The shared antigenic determinant appeared to be carbohydrate in nature in that native and guanidine-treated AT III, but not periodate oxidized AT III, were capable of inhibiting the mitogenic activity of the serum when added continuously to the cultures.	Carbohydrates	48-60	serpin family C member 1	Homo sapiens	108-114
6167624-5	1981	The shared antigenic determinant appeared to be carbohydrate in nature in that native and guanidine-treated AT III, but not periodate oxidized AT III, were capable of inhibiting the mitogenic activity of the serum when added continuously to the cultures.	Guanidine	90-99	serpin family C member 1	Homo sapiens	108-114
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
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
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
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
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
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
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
7284440-1	1981	Purified antithrombin III has been reported to have bound glucocerebroside, the major glycolipid of plasma.	Glucosylceramides	58-74	serpin family C member 1	Homo sapiens	9-25
7284440-1	1981	Purified antithrombin III has been reported to have bound glucocerebroside, the major glycolipid of plasma.	Glycolipids	86-96	serpin family C member 1	Homo sapiens	9-25
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
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
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
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
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
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
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
6113018-1	1981	1 The ability of several sulphated polysaccharide anticoagulants to prevent alpha 1-antitrypsin inhibition of thrombin paralleled their ability to potentiate antithrombin III inhibition of thrombin.	Polysaccharides	35-49	serpin family C member 1	Homo sapiens	158-174
6113018-3	1981	2 These results are consistent with the possibility that a direct polysaccharide-proteinase interaction may be involved in the sulphated polysaccharide-modulated inhibition of thrombin by antithrombin III.	Polysaccharides	66-80	serpin family C member 1	Homo sapiens	188-204
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
6790279-1	1981	Previous studies have shown that a modified form of antithrombin, cleaved at a single Arg-Ser bond near the carboxy-terminal end of the chain, is formed during the reaction with thrombin concurrent with the formation of the inactive enzyme-inhibitor complex.	Arginine	86-89	serpin family C member 1	Homo sapiens	52-64
6790279-1	1981	Previous studies have shown that a modified form of antithrombin, cleaved at a single Arg-Ser bond near the carboxy-terminal end of the chain, is formed during the reaction with thrombin concurrent with the formation of the inactive enzyme-inhibitor complex.	Serine	90-93	serpin family C member 1	Homo sapiens	52-64
7317004-0	1981	Dansyl (5-dimethylaminonaphthalene-1-sulphonyl)-heparin binds antithrombin III and platelet factor 4 at separate sites.	dansyl (5-dimethylaminonaphthalene-1-sulphonyl)-heparin	0-55	serpin family C member 1	Homo sapiens	62-78
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.	dansyl-(5-dimethylaminonaphthalene-1-sulphonyl)-heparin	69-124	serpin family C member 1	Homo sapiens	0-16
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
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
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
7218490-2	1981	Both patients had abnormally low antithrombin III levels, which improved to normal levels with warfarin ;sodium therapy.	Warfarin	95-103	serpin family C member 1	Homo sapiens	33-49
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
7226527-1	1981	When compared to values obtained in healthy normolipidemic normal weight control subjects, the plasma antithrombin III level determined by immunological, clotting and thrombin-agarose diffusion techniques was found to be obviously decreased in patients with decompensated cirrhosis of the liver and slightly but significantly increased in hyperlipidemic and especially in hypertriglyceridemic subjects.	Sepharose	176-183	serpin family C member 1	Homo sapiens	102-118
7226527-2	1981	Plasma antithrombin III was positively correlated with serum cholesterol level, the logarithm of serum triglyceride concentration and serum pseudocholinesterase activity.	Cholesterol	61-72	serpin family C member 1	Homo sapiens	7-23
7226527-2	1981	Plasma antithrombin III was positively correlated with serum cholesterol level, the logarithm of serum triglyceride concentration and serum pseudocholinesterase activity.	Triglycerides	103-115	serpin family C member 1	Homo sapiens	7-23
7226527-4	1981	It is suggested that the accelerated fatty acid and lipoprotein turnover occurring in many subjects with type IIb and type IV hyperlipoproteinemia might be accompanied by an enhanced hepatic protein synthesis involving various liver secretion enzymes and clotting factors as well as antithrombin III.	Fatty Acids	37-47	serpin family C member 1	Homo sapiens	283-299
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
7215671-0	1981	Effect of dithiothreitol on the modulation of antithrombin III activity by sulphated polysaccharides.	Dithiothreitol	10-24	serpin family C member 1	Homo sapiens	46-62
7215671-0	1981	Effect of dithiothreitol on the modulation of antithrombin III activity by sulphated polysaccharides.	Polysaccharides	85-100	serpin family C member 1	Homo sapiens	46-62
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
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
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
6783500-3	1981	Dependent on enzyme concentration, however, granulocytic elastase induced progressive inactivation of antithrombin III leading to an almost complete loss of the thrombin inhibitory activity at a molar ratio of elastase: antithrombin III = 0.4:1 within 5 min at 25 degrees C. Antithrombin III is not drastically degraded by elastase as revealed by polyacrylamide gel electrophoretic and rocket immunoelectrophoretic investigations.	polyacrylamide	347-361	serpin family C member 1	Homo sapiens	102-118
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
6940150-2	1981	Direct measurements of the kinetic behavior of the hexasaccharides, octasaccharides, and decasaccharides showed that these fractions greatly enhanced the rate of Factor Xa inactivation by antithrombin.	hexasaccharides	51-66	serpin family C member 1	Homo sapiens	188-200
6800672-0	1981	Practical requirements for immunochemical analysis of antithrombin III in agarose gels.	Sepharose	74-81	serpin family C member 1	Homo sapiens	54-70
6800672-1	1981	This report emphasizes the importance charged groups affixed to the agarose gel matrix have on immunoprecipitation of antithrombin III (AT) and of its protease complexes.	Sepharose	68-75	serpin family C member 1	Homo sapiens	118-134
6940150-2	1981	Direct measurements of the kinetic behavior of the hexasaccharides, octasaccharides, and decasaccharides showed that these fractions greatly enhanced the rate of Factor Xa inactivation by antithrombin.	decasaccharides	89-104	serpin family C member 1	Homo sapiens	188-200
6940150-5	1981	The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain.	hexasaccharides	19-34	serpin family C member 1	Homo sapiens	313-325
6940150-5	1981	The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain.	hexasaccharides	19-34	serpin family C member 1	Homo sapiens	367-379
6940150-5	1981	The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain.	decasaccharides	57-72	serpin family C member 1	Homo sapiens	313-325
6940150-5	1981	The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain.	decasaccharides	57-72	serpin family C member 1	Homo sapiens	367-379
6940150-6	1981	The smallest complex carbohydrate fragment that accelerated the inactivation of thrombin by antithrombin had approximately 14 residues.	Carbohydrates	21-33	serpin family C member 1	Homo sapiens	92-104
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
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
6168228-0	1981	The interaction of protein-bound heparin and antithrombin III.	Heparin	33-40	serpin family C member 1	Homo sapiens	45-61
7225714-2	1981	2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin.	Dermatan Sulfate	7-24	serpin family C member 1	Homo sapiens	81-87
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
6168228-4	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
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
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
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
6783633-0	1981	Preparation of biologically active fluorescent heparin composed of fluorescein-labeled species and its behavior to antithrombin III.	Fluorescein	67-78	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
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
7039127-4	1981	The enhanced activity of antithrombin III, found most frequently in the treatment with indirect anticoagulants, renal transplantations, and application of anabolic steroids, has given no data of clinical importance so far.	Steroids	164-172	serpin family C member 1	Homo sapiens	25-41
6455833-0	1981	The effects of orchiectomy, oestrogens and cyproterone-acetate on the antithrombin-III concentration in carcinoma of the prostate.	Cyproterone Acetate	43-62	serpin family C member 1	Homo sapiens	70-86
6455833-6	1981	During cyproterone-acetate treatment there was a slight but significant increase in AT-III at 2 months.	Cyproterone Acetate	7-26	serpin family C member 1	Homo sapiens	84-90
7213665-5	1980	The data obtained from affinity chromatography of these fractions on antithrombin III-Sepharose also substantiated the observed difference in anticoagulant activity.	Sepharose	86-95	serpin family C member 1	Homo sapiens	69-85
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
6781095-3	1980	Affinity chromatography on antithrombin-Sepharose separated a distinct high-affinity fraction (4-5% of the total material).	Sepharose	40-49	serpin family C member 1	Homo sapiens	27-39
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.	Sepharose	83-95	serpin family C member 1	Homo sapiens	0-16
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
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
7469415-0	1980	Binding of heparin to antithrombin III: The use of dansyl and rhodamine labels.	Rhodamines	62-71	serpin family C member 1	Homo sapiens	22-38
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
6448845-1	1980	A low molecular weight preparation of porcine heparin (specific anticoagulation activity = 125 units/mg) was fractionated to obtain a mucopolysaccharide product of 6500 daltons (specific anticoagulant activity = 373 units/mg) that is homogeneous with respect to its interaction with antithrombin.	Glycosaminoglycans	134-152	serpin family C member 1	Homo sapiens	283-295
6448845-3	1980	Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion.	Fluorescamine	30-43	serpin family C member 1	Homo sapiens	115-127
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
6448845-3	1980	Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion.	Glycosaminoglycans	80-98	serpin family C member 1	Homo sapiens	115-127
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
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
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
6448846-17	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.	Glycosaminoglycans	87-105	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
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.	Glycosaminoglycans	187-205	serpin family C member 1	Homo sapiens	116-128
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
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
7457881-0	1980	Immobilization of heparin with trichloro-s-triazine: purification of mouse antithrombin.	cyanuric chloride	31-51	serpin family C member 1	Homo sapiens	75-87
7449596-9	1980	Our observation that depression of AT III levels in young diabetic females was closely correlated with elevations of fasting serum glucose and HbA1 suggests that strict diabetic control may help prevent hypercoagulability in diabetes.	Glucose	131-138	serpin family C member 1	Homo sapiens	35-41
6776145-7	1980	A complex with antithrombin III is detected by dodecyl sulfate gel electrophoresis.	dodecyl sulfate	47-62	serpin family C member 1	Homo sapiens	15-31
7437065-0	1980	The interaction of heparin with thrombin and antithrombin.	Heparin	19-26	serpin family C member 1	Homo sapiens	45-57
7239054-0	1980	[Determination of antithrombin III in a group workers with long-term exposure to carbon disulfide (CS2)].	Carbon Disulfide	81-97	serpin family C member 1	Homo sapiens	18-34
6450073-0	1980	Modification by anionic polysaccharides of the antithrombin III inhibition of plasmin.	Polysaccharides	24-39	serpin family C member 1	Homo sapiens	47-63
7213342-2	1980	Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III.	Carbon-14	63-66	serpin family C member 1	Homo sapiens	22-38
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
7209874-0	1980	Preparation and partial characterization of human plasma depleted of antithrombin-III by heparin-sepharose affinity chromatography.	Sepharose	97-106	serpin family C member 1	Homo sapiens	69-85
7426659-11	1980	Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis.	Sodium Dodecyl Sulfate	0-22	serpin family C member 1	Homo sapiens	71-87
7426659-11	1980	Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis.	Sodium Dodecyl Sulfate	0-22	serpin family C member 1	Homo sapiens	145-161
7426659-11	1980	Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis.	Sodium Dodecyl Sulfate	24-27	serpin family C member 1	Homo sapiens	71-87
7426659-11	1980	Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis.	Sodium Dodecyl Sulfate	24-27	serpin family C member 1	Homo sapiens	145-161
7426659-11	1980	Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis.	polyacrylamide	29-43	serpin family C member 1	Homo sapiens	71-87
7426659-11	1980	Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis.	polyacrylamide	29-43	serpin family C member 1	Homo sapiens	145-161
7426659-13	1980	The inactivating cleavage occurred within a disulfide loop of the antithrombin III molecule, since the lower molecular weight species was detected only under reducing conditions.	Disulfides	44-53	serpin family C member 1	Homo sapiens	66-82
7213342-4	1980	Discontinuous polyacrylamide-gel electrophoresis of the reduced dissociation fragments of the complex in the presence of sodium dodecyl sulphate reveals two antithrombin III bands that do not resolve during electrophoresis without reduction.	polyacrylamide	14-28	serpin family C member 1	Homo sapiens	157-173
7213342-4	1980	Discontinuous polyacrylamide-gel electrophoresis of the reduced dissociation fragments of the complex in the presence of sodium dodecyl sulphate reveals two antithrombin III bands that do not resolve during electrophoresis without reduction.	Sodium Dodecyl Sulfate	121-144	serpin family C member 1	Homo sapiens	157-173
7213342-11	1980	The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s).	Arginine	117-125	serpin family C member 1	Homo sapiens	50-66
7213342-11	1980	The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s).	Arginine	140-148	serpin family C member 1	Homo sapiens	50-66
7213342-11	1980	The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s).	carboxylic ester	165-181	serpin family C member 1	Homo sapiens	50-66
7213342-11	1980	The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s).	disulphide	253-263	serpin family C member 1	Homo sapiens	50-66
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
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
7417484-1	1980	Antithrombin III has been shown to contain three disulphide bridges.	disulphide	49-59	serpin family C member 1	Homo sapiens	0-16
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
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
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
7406509-0	1980	Tryptophan residue at the heparin binding site in antithrombin III.	Tryptophan	0-10	serpin family C member 1	Homo sapiens	50-66
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
7406510-0	1980	Structural studies of the carbohydrate moiety of human antithrombin III.	Carbohydrates	26-38	serpin family C member 1	Homo sapiens	55-71
6159941-1	1980	1 Comparison of the effects of sulphated polysaccharides on thrombin-induced clotting of normal and antithrombin III-deficient plasmas suggests the involvement of antithrombin III (AT III) in the anticoagulant activities of cellulose, dextran and xylan sulphates.	Cellulose	224-233	serpin family C member 1	Homo sapiens	181-187
6159941-1	1980	1 Comparison of the effects of sulphated polysaccharides on thrombin-induced clotting of normal and antithrombin III-deficient plasmas suggests the involvement of antithrombin III (AT III) in the anticoagulant activities of cellulose, dextran and xylan sulphates.	Dextrans	235-242	serpin family C member 1	Homo sapiens	181-187
6159941-1	1980	1 Comparison of the effects of sulphated polysaccharides on thrombin-induced clotting of normal and antithrombin III-deficient plasmas suggests the involvement of antithrombin III (AT III) in the anticoagulant activities of cellulose, dextran and xylan sulphates.	xylan sulphates	247-262	serpin family C member 1	Homo sapiens	181-187
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
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
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
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
7455972-2	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).	Sepharose	181-188	serpin family C member 1	Homo sapiens	22-38
7455972-4	1980	In the other, the antithrombin III displayed a decreased electrophoretic mobility in the heparinized agarose gel.	Sepharose	101-108	serpin family C member 1	Homo sapiens	18-34
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
7455972-5	1980	The relatively low affinity of this antithrombin III to heparin could be directly proved by the heparin-agarose affinity chromatography, too.	Sepharose	104-111	serpin family C member 1	Homo sapiens	36-52
7455979-0	1980	Stanazolol treatment in an AT III deficient patient.	Stanozolol	0-10	serpin family C member 1	Homo sapiens	27-33
7372626-0	1980	Structural studies on the carbohydrate portion of human antithrombin III.	Carbohydrates	26-38	serpin family C member 1	Homo sapiens	56-72
7372626-1	1980	Human antithrombin III has been shown to contain four identical N-glycosidically linked carbohydrate chain per molecule.	Nitrogen	64-65	serpin family C member 1	Homo sapiens	6-22
7372626-1	1980	Human antithrombin III has been shown to contain four identical N-glycosidically linked carbohydrate chain per molecule.	Carbohydrates	88-100	serpin family C member 1	Homo sapiens	6-22
7372626-4	1980	As a result of these studies, the following structures is proposed for the carbohydrate chains in human antithrombin III: (formula: see text).	Carbohydrates	75-87	serpin family C member 1	Homo sapiens	104-120
6155418-0	1980	The effect of a sulfated polysaccharide on antithrombin III.	Polysaccharides	25-39	serpin family C member 1	Homo sapiens	43-59
6155418-2	1980	We have investigated the potentiation of AT-III inhibition of factors Xa, IIa, and plasmin by the heparinoid substance SP-54.	Heparinoids	98-118	serpin family C member 1	Homo sapiens	41-47
6155418-2	1980	We have investigated the potentiation of AT-III inhibition of factors Xa, IIa, and plasmin by the heparinoid substance SP-54.	Pentosan Sulfuric Polyester	119-124	serpin family C member 1	Homo sapiens	41-47
6155418-4	1980	SP-54 potentiated AT-III inhibition of factors Xa and IIa in the absence of heparin.	Pentosan Sulfuric Polyester	0-5	serpin family C member 1	Homo sapiens	18-24
6155418-6	1980	SP-54 also potentiated the AT-III inhibition of plasmin action.	Pentosan Sulfuric Polyester	0-5	serpin family C member 1	Homo sapiens	27-33
6966584-1	1980	The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively.	Glycine	101-104	serpin family C member 1	Homo sapiens	60-76
6966584-1	1980	The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively.	Arginine	105-108	serpin family C member 1	Homo sapiens	60-76
6966584-1	1980	The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively.	ala-asn	113-120	serpin family C member 1	Homo sapiens	60-76
7377131-3	1980	The thrombin remaining after neutralization by AT-III cleaves a chromophore, p-nitroaniline, from the substrate, which can then te quantified in a spectrophotometer.	4-nitroaniline	77-91	serpin family C member 1	Homo sapiens	47-53
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
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
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
6772690-7	1980	The thrombin agarose (total antithrombin) gel diffusion technique correlated less well with the chromogenic (r = 0.65; P less than 0.01) and Mancini immunoassay (r = 0.45; P less than 0.01) methods.	Sepharose	13-20	serpin family C member 1	Homo sapiens	28-40
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
6102938-0	1980	Effect of sulphated polysaccharides on clotting of plasma deficient in antithrombin III [proceedings].	Polysaccharides	20-35	serpin family C member 1	Homo sapiens	71-87
7378640-0	1980	Evidence for antithrombin III involvement in the anticoagulant activity of cellulose sulphate.	cellulose sulphate	75-93	serpin family C member 1	Homo sapiens	13-29
7378640-1	1980	1 Cellulose sulphate, like heparin, prolonged the clotting time in partial thromboplastin time (PTT) assays, inhibited the amidolytic activity of thrombin, was without effect on amidolysis catalysed by activated coagulation factor X(Xa), and potentiated the inhibition of both thrombin and Xa by antithrombin III (AT).	cellulose sulphate	2-20	serpin family C member 1	Homo sapiens	296-312
7404500-0	1980	A versatile assay method of antithrombin III using thrombin and Tos-Gly-Pro-Arg-Pna.	chromozym TH	64-83	serpin family C member 1	Homo sapiens	28-44
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
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.	cyclo(tyrosyl-tyrosyl)	23-30	serpin family C member 1	Homo sapiens	67-79
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.	tryptophanyl	35-47	serpin family C member 1	Homo sapiens	67-79
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
7353045-1	1980	The exposure to solvent of the aromatic amino acid residues of free bovine antithrombin was probed by three different methods, which gave comparable results.	Amino Acids, Aromatic	31-50	serpin family C member 1	Homo sapiens	75-87
7353045-3	1980	Fluorescence quenching experiments indicated that 60% of the tryptophanyl fluorescence of antithrombin arose from exposed residues.	tryptophanyl	61-73	serpin family C member 1	Homo sapiens	90-102
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
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.	Amino Acids, Aromatic	118-138	serpin family C member 1	Homo sapiens	26-38
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
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
7368150-1	1980	The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides.	Glycosaminoglycans	141-160	serpin family C member 1	Homo sapiens	94-110
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.	Glycosaminoglycans	141-160	serpin family C member 1	Homo sapiens	112-118
7368150-3	1980	A semi-synthetic heparin analogue showed no evidence of binding to At III, but a sample of heparan sulphate did interact with At III at a concentration 3 times that of heparin.	Heparitin Sulfate	91-107	serpin family C member 1	Homo sapiens	126-132
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
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
7356660-0	1980	The heparin binding site of antithrombin III.	Heparin	4-11	serpin family C member 1	Homo sapiens	28-44
7356660-2	1980	Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III.	Tryptophan	89-99	serpin family C member 1	Homo sapiens	25-41
7356660-2	1980	Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III.	Tryptophan	89-99	serpin family C member 1	Homo sapiens	238-254
7356660-2	1980	Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III.	dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide	108-158	serpin family C member 1	Homo sapiens	25-41
7356660-2	1980	Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III.	dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide	108-158	serpin family C member 1	Homo sapiens	238-254
7356660-2	1980	Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III.	hydroxynitrobenzyl	196-214	serpin family C member 1	Homo sapiens	25-41
7356660-2	1980	Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III.	hydroxynitrobenzyl	196-214	serpin family C member 1	Homo sapiens	238-254
7356660-8	1980	These results indicate that the integrity of a specific tryptophan residue is critical to the binding of heparin to antithrombin III.	Tryptophan	56-66	serpin family C member 1	Homo sapiens	116-132
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
6154613-0	1980	Involvement of antithrombin III in anticoagulant effects of sulphated polysaccharides [proceedings].	Polysaccharides	70-85	serpin family C member 1	Homo sapiens	15-31
7371952-0	1980	Inhibition by antithrombin III of carrageenan- and xylan SP54-induced aggregation of human blood platelets [proceedings].	Carrageenan	34-45	serpin family C member 1	Homo sapiens	14-30
7371952-0	1980	Inhibition by antithrombin III of carrageenan- and xylan SP54-induced aggregation of human blood platelets [proceedings].	Pentosan Sulfuric Polyester	51-61	serpin family C member 1	Homo sapiens	14-30
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
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.	Dihydroergotamine	108-111	serpin family C member 1	Homo sapiens	45-61
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
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
7192096-1	1980	5th Communication: Further characterization by affinity chromatography on antithrombin-sepharose and its comparison with a commercially available heparin.	Sepharose	87-96	serpin family C member 1	Homo sapiens	74-86
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
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
7192096-2	1980	A highly potent heparin (Heparin Schering) was characterized in comparison to commercial heparin by affinity chromatography on antithrombin-III-sepharose.	Sepharose	144-153	serpin family C member 1	Homo sapiens	127-143
7192096-4	1980	The specific biological activities per microgram uronic acid and elution pattern on antithrombin-sepharose of high affinity heparin fraction were similar for both heparin preparations.	Sepharose	97-106	serpin family C member 1	Homo sapiens	84-96
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
7417594-4	1980	Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure.	Sepharose	47-59	serpin family C member 1	Homo sapiens	5-11
7417594-4	1980	Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure.	Polyvinyl Alcohol	61-78	serpin family C member 1	Homo sapiens	5-11
7417594-4	1980	Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure.	Polyhydroxyethyl Methacrylate	80-110	serpin family C member 1	Homo sapiens	5-11
7417594-4	1980	Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure.	Silicones	115-123	serpin family C member 1	Homo sapiens	5-11
7417594-4	1980	Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure.	Nylons	131-136	serpin family C member 1	Homo sapiens	5-11
7417594-4	1980	Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure.	Cyanogen Bromide	144-160	serpin family C member 1	Homo sapiens	5-11
6935668-0	1980	Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin.	Glucosamine	28-41	serpin family C member 1	Homo sapiens	57-69
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
6935668-1	1980	An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid.	Octasaccharide	3-17	serpin family C member 1	Homo sapiens	41-53
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
6935668-1	1980	An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid.	Nitrous Acid	118-130	serpin family C member 1	Homo sapiens	41-53
6935668-6	1980	Similar treatment of an analogous tetrasaccharide derived from heparin with low affinity for antithrombin failed to produce any disulfated anhydromannitol.	tetrasaccharide	34-49	serpin family C member 1	Homo sapiens	93-105
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.	3-sulfated glucosamine	27-49	serpin family C member 1	Homo sapiens	136-148
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
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
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
7213342-2	1980	Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III.	Carbon-14	63-66	serpin family C member 1	Homo sapiens	140-156
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
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
7213342-2	1980	Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III.	methoxyamine	67-93	serpin family C member 1	Homo sapiens	22-38
7213342-2	1980	Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III.	methoxyamine	67-93	serpin family C member 1	Homo sapiens	140-156
7213342-2	1980	Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III.	Carbon-14	127-130	serpin family C member 1	Homo sapiens	22-38
7213342-2	1980	Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III.	Carbon-14	127-130	serpin family C member 1	Homo sapiens	140-156
6792695-4	1980	In the presence of coagulation inhibitors such as heparin, hirudin and antithrombin III the DP reaction was inhibited, suggesting that the precipitation zone represents coagulation.	dp	92-94	serpin family C member 1	Homo sapiens	71-87
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
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.	tryptophanyl	69-81	serpin family C member 1	Homo sapiens	101-113
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
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
316698-0	1979	Carboxy terminal fragment of human alpha-1-antitrypsin from hydroxylamine cleavage: homology with antithrombin III.	Hydroxylamine	60-73	serpin family C member 1	Homo sapiens	98-114
527591-1	1979	Tryptophanyl residues of bovine antithrombin were modified with N-bromosuccinimide at near-neutral pH.	tryptophanyl	0-12	serpin family C member 1	Homo sapiens	32-44
527591-1	1979	Tryptophanyl residues of bovine antithrombin were modified with N-bromosuccinimide at near-neutral pH.	Bromosuccinimide	64-82	serpin family C member 1	Homo sapiens	32-44
527591-4	1979	Modification of an average of about one tryptophanyl residue per protein molecule did not affect antithrombin activity measured in the absence of heparin, but decreased the activity assayed in the presence of heparin to about half the value given by unmodified antithrombin.	tryptophanyl	40-52	serpin family C member 1	Homo sapiens	261-273
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
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.	tryptophanyl	98-110	serpin family C member 1	Homo sapiens	123-135
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
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
118968-5	1979	Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid.	Glucosamine	99-110	serpin family C member 1	Homo sapiens	32-48
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
118968-2	1979	Human, porcine, rabbit, and rat antithrombin III have been purified by affinity chromatography using heparin-agarose.	Sepharose	109-116	serpin family C member 1	Homo sapiens	32-48
118968-5	1979	Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid.	Hexoses	91-97	serpin family C member 1	Homo sapiens	32-48
161807-2	1979	The antitrypsin, antiplasmin and antithrombin activities of bis(amidinobenzylidene)- and bis(amidinobenzyl)cycloalkanones are not markedly affected if the amidino group is substituted by an uncharged residue (H, OCH3, Cl, Br, NO2).	bis(amidinobenzylidene)	60-83	serpin family C member 1	Homo sapiens	33-45
161807-2	1979	The antitrypsin, antiplasmin and antithrombin activities of bis(amidinobenzylidene)- and bis(amidinobenzyl)cycloalkanones are not markedly affected if the amidino group is substituted by an uncharged residue (H, OCH3, Cl, Br, NO2).	bis(amidinobenzyl)cycloalkanones	89-121	serpin family C member 1	Homo sapiens	33-45
161807-2	1979	The antitrypsin, antiplasmin and antithrombin activities of bis(amidinobenzylidene)- and bis(amidinobenzyl)cycloalkanones are not markedly affected if the amidino group is substituted by an uncharged residue (H, OCH3, Cl, Br, NO2).	amidino	64-71	serpin family C member 1	Homo sapiens	33-45
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
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
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
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
160589-0	1979	Effects of PGI2 on the inactivation of thrombin, factor Xa, and plasmin by antithrombin-III and heparin.	Epoprostenol	11-15	serpin family C member 1	Homo sapiens	75-91
223567-0	1979	Effect of polyanetholesulphonic acid and xylan sulphate on antithrombin III activity.	polyanetholesulphonic acid	10-36	serpin family C member 1	Homo sapiens	59-75
223567-0	1979	Effect of polyanetholesulphonic acid and xylan sulphate on antithrombin III activity.	xylan sulphate	41-55	serpin family C member 1	Homo sapiens	59-75
316999-7	1979	The molecular weight estimated on SDS electrophoresis for AT-III and alpha 1-AT was 63,000 and 50,000, respectively.	Sodium Dodecyl Sulfate	34-37	serpin family C member 1	Homo sapiens	58-64
469001-1	1979	To clarify the action of dextran sulphate, a heparin analogue, in the clotting of fibrinogen by thrombin, determinations were carried out on the clotting activity, the release of fibrinopeptides from fibrinogen, and the hydrolytic activity of thrombin against a peptide chromogenic substrate in the absence or presence of antithrombin III (heparin cofactor).	Dextran Sulfate	25-41	serpin family C member 1	Homo sapiens	322-338
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
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
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
89015-5	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
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
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
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
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
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
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
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
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
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
531528-4	1979	A negative correlation was found between AT-III and serum creatinine and between AT-III and serum albumin.	Creatinine	58-68	serpin family C member 1	Homo sapiens	41-47
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
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
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.	Disaccharides	139-152	serpin family C member 1	Homo sapiens	215-227
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.	dodecasaccharide	156-172	serpin family C member 1	Homo sapiens	215-227
743219-6	1978	The probability that any randomly chosen dodecasaccharide sequence in heparin should bind to antithrombin was calculated to 0.022.	dodecasaccharide	41-57	serpin family C member 1	Homo sapiens	93-105
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
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
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
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
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
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
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
710412-5	1978	The binding of either fraction to antithrombin was found to result in an increase of the tryptophan fluorescence of the protein.	Tryptophan	89-99	serpin family C member 1	Homo sapiens	34-46
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
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
500822-4	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.	TFF2 protein, human	170-172	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.	porcine heparin	58-73	serpin family C member 1	Homo sapiens	95-107
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
489712-7	1979	3) Transferrin, antithrombin III, prothrombin, and plasminogen showed marked increases after administration of danazol and during pregnancy.	Danazol	111-118	serpin family C member 1	Homo sapiens	16-32
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
120212-0	1979	Chromatography of heparin on sepharose-lysine: molecular size fractionation and its relevance to thrombin and antithrombin III binding.	sepharose-lysine	29-45	serpin family C member 1	Homo sapiens	110-126
508327-0	1979	The effects of phospholipid and factor Va on the inhibition of factor Xa by antithrombin III.	Phospholipids	15-27	serpin family C member 1	Homo sapiens	76-92
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
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
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
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
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
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.	copolymer	33-42	serpin family C member 1	Homo sapiens	4-16
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
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
473117-6	1979	The heparin part of the copolymer was responsible for antithrombin III adsorption and for decrease of factor V activity.	copolymer	24-33	serpin family C member 1	Homo sapiens	54-70
420768-4	1979	The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment.	Sodium Dodecyl Sulfate	65-87	serpin family C member 1	Homo sapiens	12-24
420768-4	1979	The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment.	nadodso4	89-97	serpin family C member 1	Homo sapiens	12-24
420768-4	1979	The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment.	nadodso4	107-115	serpin family C member 1	Homo sapiens	12-24
420768-4	1979	The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment.	Hydroxylamine	156-169	serpin family C member 1	Homo sapiens	12-24
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
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
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
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
216717-0	1979	Measurement of antithrombin III in healthy subjects studied before and after taking aspirin and dipyridamole.	Aspirin	84-91	serpin family C member 1	Homo sapiens	15-31
216717-0	1979	Measurement of antithrombin III in healthy subjects studied before and after taking aspirin and dipyridamole.	Dipyridamole	96-108	serpin family C member 1	Homo sapiens	15-31
483282-0	1979	Enhancement of antithrombin III activity by carrageenans.	Carrageenan	44-56	serpin family C member 1	Homo sapiens	15-31
462917-5	1979	It consists of the following steps: (a) partial purification by precipitation of impurities with 20% polyethylene glycol (PEG) 4000; (b) isolation of AT III from the PEG supernatant by batch adsorption and elution on heparin-Sepharose at a ratio corresponding to 45 vol of plasma or 80 vol of 10% Fr.	Polyethylene Glycols	166-169	serpin family C member 1	Homo sapiens	150-156
708377-0	1978	Effect of heparin on thrombin inactivation by antithrombin-III.	Heparin	10-17	serpin family C member 1	Homo sapiens	46-62
118968-5	1979	Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid.	Neuraminic Acids	116-131	serpin family C member 1	Homo sapiens	32-48
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
118968-7	1979	The total carbohydrate contents were 17, 16, 14, and 15% for human, porcine, rabbit, and rat antithrombin III, respectively.	Carbohydrates	10-22	serpin family C member 1	Homo sapiens	93-109
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
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
118968-13	1979	Human, porcine, and rabbit antithrombin III have a histidine residue at the amino-terminus, while rat antithrombin III contains an amino-terminal asparagine residue.	Asparagine	146-156	serpin family C member 1	Homo sapiens	102-118
698151-2	1978	Quinestrol therapy was associated with increased levels of factors VII and IX and decreased antithrombin activity on the sixth postpartum day, and increased factor IX and plasminogen levels on the fourteenth postpartum day.	Quinestrol	0-10	serpin family C member 1	Homo sapiens	92-104
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
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
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
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.	Quinuclidinyl Benzilate	136-138	serpin family C member 1	Homo sapiens	45-51
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.	Quinuclidinyl Benzilate	136-138	serpin family C member 1	Homo sapiens	57-63
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.	H-Pro-Phe-OH	139-146	serpin family C member 1	Homo sapiens	45-51
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.	H-Pro-Phe-OH	139-146	serpin family C member 1	Homo sapiens	57-63
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.	Arginine	147-150	serpin family C member 1	Homo sapiens	45-51
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.	Arginine	147-150	serpin family C member 1	Homo sapiens	57-63
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.	polysulphate	13-25	serpin family C member 1	Homo sapiens	70-86
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
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.	5--6 arginine	16-29	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.	5--6 arginine	16-29	serpin family C member 1	Homo sapiens	204-220
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.	1,2-cyclohexanedione	56-76	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	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
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	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.	Sepharose	160-169	serpin family C member 1	Homo sapiens	43-59
652506-0	1978	[Changes in antithrombin III during treatment with heparin].	Heparin	51-58	serpin family C member 1	Homo sapiens	12-28
618863-8	1978	Although it remains to be established whether the inhibitory actions of antithrombin III are affected by glucosylceramide, the relative amounts which are bound suggest that antithrombin III may be a significant carrier of the glycolipid.	Glycolipids	226-236	serpin family C member 1	Homo sapiens	72-88
618863-8	1978	Although it remains to be established whether the inhibitory actions of antithrombin III are affected by glucosylceramide, the relative amounts which are bound suggest that antithrombin III may be a significant carrier of the glycolipid.	Glycolipids	226-236	serpin family C member 1	Homo sapiens	173-189
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
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
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
73931-0	1977	Effect of heparin and warfarin on antithrombin III.	Heparin	10-17	serpin family C member 1	Homo sapiens	34-50
73931-0	1977	Effect of heparin and warfarin on antithrombin III.	Warfarin	22-30	serpin family C member 1	Homo sapiens	34-50
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
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.	Ellagic Acid	176-188	serpin family C member 1	Homo sapiens	83-95
148659-2	1977	Antitrypsin, antiplasmin and antithrombin effect of 2-amino-6-alkoxy- and aralkoxynaphthalenes].	2-amino-6-alkoxy- and aralkoxynaphthalenes	52-94	serpin family C member 1	Homo sapiens	29-41
353657-0	1977	[Electrophoretic mobility of antithrombin III in an agarose gel with heparin.	Sepharose	52-59	serpin family C member 1	Homo sapiens	29-45
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
353657-2	1977	The electrophoretic mobility of several forms of antithrombin III in an agarose gel has been compared with the mobility in a gel containing heparin.	Sepharose	72-79	serpin family C member 1	Homo sapiens	49-65
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
353657-5	1977	A purified antithrombin III, prepared by affinity chromatography, contained an immunoreactive material of higher molecular size which has no activity and a higher mobility in agarose gel.	Sepharose	175-182	serpin family C member 1	Homo sapiens	11-27
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
353657-6	1977	When heparin is incorporated in the agarose plate, the electrophoretic mobility of this polymerized antithrombin III is not modified.	Sepharose	36-43	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
601748-0	1977	Heparin-like effect of polymethacrylic acid on the reaction between thrombin and antithrombin-III.	polymethacrylic acid	23-43	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
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
72924-0	1977	Heparin-induced decrease in circulating antithrombin-III.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-56
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
24016-0	1977	Quenching of tryptophan fluorescence in human antithrombin III by iodide ion.	Tryptophan	13-23	serpin family C member 1	Homo sapiens	46-62
24016-0	1977	Quenching of tryptophan fluorescence in human antithrombin III by iodide ion.	Iodides	66-72	serpin family C member 1	Homo sapiens	46-62
24016-1	1977	Iodide is an efficient quencher of antithrombin III intrinsic tryptophan fluorescence.	Iodides	0-6	serpin family C member 1	Homo sapiens	35-51
24016-1	1977	Iodide is an efficient quencher of antithrombin III intrinsic tryptophan fluorescence.	Tryptophan	62-72	serpin family C member 1	Homo sapiens	35-51
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
24016-4	1977	The binding of heparin to antithrombin III influences the number of solvent-exposed tryptophan residues.	Tryptophan	84-94	serpin family C member 1	Homo sapiens	26-42
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
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
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
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.	A73025	81-87	serpin family C member 1	Homo sapiens	191-207
71399-0	1977	Heparin-induced decrease in circulating antithrombin-III.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-56
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
570737-0	1978	Inhibition of thrombin by antithrombin III in the presence of certain glycosaminoglycans found in the mammalian aorta.	Glycosaminoglycans	70-88	serpin family C member 1	Homo sapiens	26-42
705689-3	1978	At III levels measured with six methods in 36 people: 10 healthy controls, 10 women taking a progestagen Lynestrenol and 16 women taking a combined oestrogen-progestagen contraceptive pill.	Lynestrenol	105-116	serpin family C member 1	Homo sapiens	0-6
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
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
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.	Sepharose	98-107	serpin family C member 1	Homo sapiens	6-22
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.	Sepharose	151-160	serpin family C member 1	Homo sapiens	6-22
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.	deae a	228-234	serpin family C member 1	Homo sapiens	6-22
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.	sephadex	238-246	serpin family C member 1	Homo sapiens	6-22
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.	Sepharose	263-270	serpin family C member 1	Homo sapiens	6-22
705690-2	1978	The hydrolytic activity of urokinase (plasminogen activator from urine) on acetyl-glycyl-L-lysine methylester acetate (Ac-gly-lys-OMeAc) was inhibited by antithrombin III in a slow time-dependent manner.	acetyl-glycyl-l-lysine methylester acetate	75-117	serpin family C member 1	Homo sapiens	154-170
705690-2	1978	The hydrolytic activity of urokinase (plasminogen activator from urine) on acetyl-glycyl-L-lysine methylester acetate (Ac-gly-lys-OMeAc) was inhibited by antithrombin III in a slow time-dependent manner.	ac-gly-lys-omeac	119-135	serpin family C member 1	Homo sapiens	154-170
656463-0	1978	The increase in human antithrombin III tryptophan fluorescence produced by heparin.	Tryptophan	39-49	serpin family C member 1	Homo sapiens	22-38
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
149555-4	1978	The extent of plasmin-antithrombin-(heparin) complex formation was studied by intravenous injection of iodine-labelled antithrombin (5-20 muCi) and quantitation of the amount of antithrombin bound to plasmin.	Iodine	103-109	serpin family C member 1	Homo sapiens	119-131
149555-4	1978	The extent of plasmin-antithrombin-(heparin) complex formation was studied by intravenous injection of iodine-labelled antithrombin (5-20 muCi) and quantitation of the amount of antithrombin bound to plasmin.	Iodine	103-109	serpin family C member 1	Homo sapiens	119-131
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
638885-3	1978	Exercise on a treadmill induced similar changes in both groups, but during the use of Demulen the levels of fibrinogen and plasminogen were higher, antithrombin level was lower, and the recalcified clotting and dilute whole blood lysis times were shorter in group 2 than in the corresponding samples obtained from the nonpill users.	SC-11800 EE	86-93	serpin family C member 1	Homo sapiens	148-160
662621-5	1978	The various aspects of this disorder discovered by Egeberg are reviewed: early onset, in several members of the same family, or recurrent thrombo-embolic problems, accompanied by a decrease in functional activity of one of the principal inhibitors of thrombin (AT III), with autosomal dominant transmission and treatment based upon anti-vitamin K agents.	Vitamin K	337-346	serpin family C member 1	Homo sapiens	261-267
74632-0	1978	Heparin-induced decrease in circulating antithrombin III.	Heparin	0-7	serpin family C member 1	Homo sapiens	40-56
618863-2	1978	Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1.	Acetylglucosamine	62-81	serpin family C member 1	Homo sapiens	6-22
618863-2	1978	Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1.	Mannose	83-90	serpin family C member 1	Homo sapiens	6-22
618863-2	1978	Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1.	Galactose	92-101	serpin family C member 1	Homo sapiens	6-22
618863-2	1978	Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1.	N-Acetylneuraminic Acid	107-118	serpin family C member 1	Homo sapiens	6-22
618863-5	1978	Antithrombin III isolated by different procedures was also found to contain glucose in an approximately equimolar ratio with N-acetylglucosamine.	Glucose	76-83	serpin family C member 1	Homo sapiens	0-16
618863-5	1978	Antithrombin III isolated by different procedures was also found to contain glucose in an approximately equimolar ratio with N-acetylglucosamine.	Acetylglucosamine	125-144	serpin family C member 1	Homo sapiens	0-16
618863-8	1978	Although it remains to be established whether the inhibitory actions of antithrombin III are affected by glucosylceramide, the relative amounts which are bound suggest that antithrombin III may be a significant carrier of the glycolipid.	Glucosylceramides	105-121	serpin family C member 1	Homo sapiens	72-88
735880-8	1978	Prophylactic treatment, preferably oral anticoagulants and/or dextran, is recommended for all persons with a low AT III concentration in any situation known to increase the predisposition to thrombosis.	Dextrans	62-69	serpin family C member 1	Homo sapiens	113-119
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
742337-1	1978	(A clinico-pharmacological study of the relationship between antithrombin-III activity and steroid cholestasis).	Steroids	91-98	serpin family C member 1	Homo sapiens	61-77
742337-2	1978	The relationship between steroid cholestasis and antithrombin-III activity were examined in users of oral contraceptives (Infecundin or Bisecurin) and in patients receiving anabolic hormone therapy (Nerobol).	Steroids	25-32	serpin family C member 1	Homo sapiens	49-65
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
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
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
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
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
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.	Sepharose	52-59	serpin family C member 1	Homo sapiens	115-121
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
872292-7	1977	In the high salt system the relative contributions of antithrombin III  to Xa neutralization in human and rabbit plasma are different.	Salts	12-16	serpin family C member 1	Homo sapiens	54-70
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
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
560216-5	1977	Heparin methyl ester is more potent than heparinylglycine in activating antithrombin III, as exhibited by its immediate effect on the thrombin-fibrinogen reaction.	heparin methyl ester	0-20	serpin family C member 1	Homo sapiens	72-88
560216-5	1977	Heparin methyl ester is more potent than heparinylglycine in activating antithrombin III, as exhibited by its immediate effect on the thrombin-fibrinogen reaction.	heparinylglycine	41-57	serpin family C member 1	Homo sapiens	72-88
560216-6	1977	However, heparinylglycine is the more effective of the two, in increasing the rate of thrombin deactivation by antithrombin III.	heparinylglycine	9-25	serpin family C member 1	Homo sapiens	111-127
560216-8	1977	In contrast, N-sulfates are critical for the interaction of heparin with antithrombin III.	n-sulfates	13-23	serpin family C member 1	Homo sapiens	73-89
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
142314-0	1977	The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin.	Sepharose	80-89	serpin family C member 1	Homo sapiens	44-60
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
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.	Lysine	99-105	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
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
12845-6	1977	Heparin and antithrombin III not only neutralized the thrombogenic materials present in the thrombogenic concentrate, but also inhibited the de novo generation of coagulant enzymes during incubation with calcium.	Calcium	204-211	serpin family C member 1	Homo sapiens	12-28
853045-4	1977	After contact with plasma, the copolymer lost part of its antithrombin activity which could be restored by a high ionic-strength medium.	copolymer	31-40	serpin family C member 1	Homo sapiens	58-70
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
65284-2	1977	The labelled antithrombin III has a high specific activity (5.75 units/mg) and displayed a single band on SDS-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	106-109	serpin family C member 1	Homo sapiens	13-29
65284-2	1977	The labelled antithrombin III has a high specific activity (5.75 units/mg) and displayed a single band on SDS-polyacrylamide gel electrophoresis.	polyacrylamide	110-124	serpin family C member 1	Homo sapiens	13-29
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
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
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
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
65182-0	1977	Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence.	Tryptophan	75-85	serpin family C member 1	Homo sapiens	28-44
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
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
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
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
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
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
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
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
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.	Calcium	62-69	serpin family C member 1	Homo sapiens	25-37
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.	Calcium	62-69	serpin family C member 1	Homo sapiens	121-133
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.	Magnesium Chloride	73-91	serpin family C member 1	Homo sapiens	25-37
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.	Magnesium Chloride	73-91	serpin family C member 1	Homo sapiens	121-133
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
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
869991-1	1977	The nature of platelet antithrombin was elucidated by comparison of thrombin binding and antithrombin activities of intact platelets and by purification of antithrombin from platelet lysates using glycerol osmotic lysis, ethanol precipitation and Sephadex gel filtration techniques.	Glycerol	197-205	serpin family C member 1	Homo sapiens	23-35
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
869991-1	1977	The nature of platelet antithrombin was elucidated by comparison of thrombin binding and antithrombin activities of intact platelets and by purification of antithrombin from platelet lysates using glycerol osmotic lysis, ethanol precipitation and Sephadex gel filtration techniques.	Ethanol	221-228	serpin family C member 1	Homo sapiens	23-35
869991-1	1977	The nature of platelet antithrombin was elucidated by comparison of thrombin binding and antithrombin activities of intact platelets and by purification of antithrombin from platelet lysates using glycerol osmotic lysis, ethanol precipitation and Sephadex gel filtration techniques.	sephadex	247-255	serpin family C member 1	Homo sapiens	23-35
869991-5	1977	However, the PGE1 treatment produced slight (less than 30%) but significant decrease of antithrombin activity of intact platelets, whereas the binding of thrombin to platelets was not affected by PGE1 treatment.	Alprostadil	13-17	serpin family C member 1	Homo sapiens	88-100
830556-0	1977	Interaction of heparin with thrombin and antithrombin III.	Heparin	15-22	serpin family C member 1	Homo sapiens	41-57
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
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.	Sepharose	137-144	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.	Sepharose	137-144	serpin family C member 1	Homo sapiens	18-24
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.	Sepharose	115-122	serpin family C member 1	Homo sapiens	43-49
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
402327-4	1977	The method permits a rapid quantitation of AT-III from serum, citrated plasma and EDTA plasma, and a positive correlation was observed between these values and those obtained by single radial immunodiffusion (SRI).	Edetic Acid	82-86	serpin family C member 1	Homo sapiens	43-49
982357-0	1976	Studies on human plasma antithrombin isolated on heparin gel.	Heparin	49-56	serpin family C member 1	Homo sapiens	24-36
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
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
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
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.	Ellagic Acid	262-274	serpin family C member 1	Homo sapiens	83-95
974107-0	1976	The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III.	Caprylates	73-82	serpin family C member 1	Homo sapiens	92-108
974107-1	1976	The binding of 1-anilino-8-naphthalenesulfonate to human antithrombin III was studied by fluorescence enhancement of the fluorophor and fluorescence quenching of the protein emission.	1-anilino-8-naphthalenesulfonate	15-47	serpin family C member 1	Homo sapiens	57-73
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.	1-anilino-8-naphthalenesulfonate	17-49	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.	1-anilino-8-naphthalenesulfonate	17-49	serpin family C member 1	Homo sapiens	176-188
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
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
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
974107-0	1976	The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III.	1-anilino-8-naphthalenesulfonate	15-47	serpin family C member 1	Homo sapiens	92-108
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
974107-0	1976	The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III.	Salicylates	58-68	serpin family C member 1	Homo sapiens	92-108
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
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
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
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
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
1036800-5	1976	In vitro, abnormal III was seen: however an enhanced antithrombin III activity in vitro was not found with carbenicillin and various penicillin derivatives.	Penicillins	133-143	serpin family C member 1	Homo sapiens	53-69
982345-0	1976	Inhibition of the activated Cls subunit of the first component of complement by antithrombin III in the presence of heparin.	Chlorine	28-31	serpin family C member 1	Homo sapiens	80-96
989640-5	1976	Ethinyl oestradiol treatment resulted in much more widespread changes with marked increases in coagulation factors VII, VIII, IX and X, decreased levels of antithrombin and dramatic increases in circulating plasminogen levels and euglobulin lysis activity.	Ethinyl Estradiol	0-18	serpin family C member 1	Homo sapiens	156-168
61631-1	1976	Antithrombin III, purified to homogeneity according to polyacrylamide gel disc electrophoresis and immunoelectrophoresis, inhibited the activity of purified factor IXa and Xa, whereas factor VII was not inhibited either in the active or in the native form.	polyacrylamide	55-69	serpin family C member 1	Homo sapiens	0-16
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
968810-0	1976	Effect of calcium phosphate on thrombin and on its sensitivity to heparin and antithrombin-III.	calcium phosphate	10-27	serpin family C member 1	Homo sapiens	78-94
1273513-5	1976	The antithrombin clotting time is shown to be inversely related to the level of circulating serine procoagulants, directly related to the level of antithrombin, and results from a procoagulant-antithrombin inter-molecular reaction.	Serine	92-98	serpin family C member 1	Homo sapiens	4-16
1247522-8	1976	These occur in position 2 which is occupied by Gly, Arg, and Trp in human, bovine, and horse, respectively; position 6 which has a deletion in human antithrombin III; and position 8 where Ile in human and horse antithrombin III has been replaced by Val in the bovine preparation.	Valine	249-252	serpin family C member 1	Homo sapiens	211-227
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
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
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
1273513-5	1976	The antithrombin clotting time is shown to be inversely related to the level of circulating serine procoagulants, directly related to the level of antithrombin, and results from a procoagulant-antithrombin inter-molecular reaction.	Serine	92-98	serpin family C member 1	Homo sapiens	147-159
1273513-5	1976	The antithrombin clotting time is shown to be inversely related to the level of circulating serine procoagulants, directly related to the level of antithrombin, and results from a procoagulant-antithrombin inter-molecular reaction.	Serine	92-98	serpin family C member 1	Homo sapiens	147-159
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
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).	Sodium Dodecyl Sulfate	150-172	serpin family C member 1	Homo sapiens	243-255
52896-0	1975	Effect of anabolic steroids on plasma antithrombin III.	Steroids	19-27	serpin family C member 1	Homo sapiens	38-54
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
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.	Sepharose	136-143	serpin family C member 1	Homo sapiens	17-36
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.	Polyethylene Glycols	148-167	serpin family C member 1	Homo sapiens	17-36
53066-4	1975	End group analysis of human antithrombin II/III shows histidine as the N-terminal amino acid.	Histidine	54-63	serpin family C member 1	Homo sapiens	28-47
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
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
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
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
52896-3	1975	In distinct contrast to the oral contraceptives, five of the six 17-alpha-alkylated anabolic steroids studied produced increased plasma Antithrombin III levels and five produced decreased levels of plasma alpha2-macroglobulin.	Steroids	93-101	serpin family C member 1	Homo sapiens	136-152
47704-14	1975	Ether extraction of plasma reduces antithrombin III activity.	Ether	0-5	serpin family C member 1	Homo sapiens	35-51
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
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
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.	Sepharose	42-49	serpin family C member 1	Homo sapiens	89-95
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
1201212-2	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.	Sepharose	207-214	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
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
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.	Sepharose	232-239	serpin family C member 1	Homo sapiens	61-67
1154312-2	1975	When agarose was applied in the first phase of the crossed immunoelectrophoresis, the normal and the pathological AT-III revealed identical electrophoretic mobility.	Sepharose	5-12	serpin family C member 1	Homo sapiens	114-120
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
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.	Sepharose	37-44	serpin family C member 1	Homo sapiens	129-135
53064-1	1975	A new rapid method for assaying total antithrombin activity has been developed based on the inactivation of thrombin incorporated into an agarose gel, during the radial diffusion of plasma in the gel.	Sepharose	138-145	serpin family C member 1	Homo sapiens	38-50
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
1115795-0	1975	Action of heparin on thrombin-antithrombin reaction.	Heparin	10-17	serpin family C member 1	Homo sapiens	30-42
47704-18	1975	Antithrombin III neutralizes the activity of prethrombin-E and thrombin-E; consequently, an active histidine center found in the B1 chain of thrombin is not essential for the binding of antithrombin.	Histidine	99-108	serpin family C member 1	Homo sapiens	0-16
4436339-0	1974	Antithrombin activity of a polyelectrolyte synthesized from cis-1,4-polyisoprene.	1,4-polyisoprene	60-80	serpin family C member 1	Homo sapiens	0-12
4423843-0	1974	The rivanol method for the quantitative determination of antithrombin III in plasma.	Ethacridine	4-11	serpin family C member 1	Homo sapiens	57-73
4633781-0	1973	[Behavior of the progessive antithrombin during long-term anticoagulant therapy (Vitamin K antagonists)].	Vitamin K	81-90	serpin family C member 1	Homo sapiens	28-40
4450303-0	1974	A simple 2-step isolation procedure for human antithrombin II/III and its biological activity after insolubilization to agarose.	Sepharose	120-127	serpin family C member 1	Homo sapiens	46-65
4790174-0	1973	[Experimental fibrinogenopathy after reaction of human fibrinogen with beta propiolactone: antithrombin activity, effect on platelet aggregation and function and on fibrin stabilization phase].	Propiolactone	71-89	serpin family C member 1	Homo sapiens	91-103
4631013-0	1972	Inactivation of antithrombin 3 by fatty acids.	Fatty Acids	34-45	serpin family C member 1	Homo sapiens	16-28
5019894-0	1972	[Blood antithrombin activity in intact and adrenalectomized animals during administration of catecholamines and corticosteroids].	Catecholamines	93-107	serpin family C member 1	Homo sapiens	7-19
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
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
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
5944879-0	1966	The influence of calcium on the binding of antithrombin by antithrombin inhibitor.	Calcium	17-24	serpin family C member 1	Homo sapiens	43-55
5643308-0	1968	Protamine, polybrene and the antithrombin action of heparin.	Heparin	52-59	serpin family C member 1	Homo sapiens	29-41
5944879-0	1966	The influence of calcium on the binding of antithrombin by antithrombin inhibitor.	Calcium	17-24	serpin family C member 1	Homo sapiens	59-71
5857034-1	1965	Some preliminary findings on antithrombin mechanisms under the influence of methylene blue].	Methylene Blue	76-90	serpin family C member 1	Homo sapiens	29-41
5865614-0	1965	[On the increase of antithrombin levels during coumarin therapy].	coumarin	47-55	serpin family C member 1	Homo sapiens	20-32
14347404-0	1965	[ELEVATION OF THE ANTITHROMBIN CONTENT OF THE BLOOD DURING COUMARIN THERAPY].	coumarin	59-67	serpin family C member 1	Homo sapiens	18-30
5844087-0	1965	Rise of blood antithrombin level during coumarin therapy.	coumarin	40-48	serpin family C member 1	Homo sapiens	14-26
14258688-2	1964	ACTION OF BLOOD PLATELETS AND THEIR PHOSPHOLIPID SUBSTITUTES ON THE ANTITHROMBIN ACTIVITY OF HEPARIN].	Phospholipids	36-48	serpin family C member 1	Homo sapiens	68-80
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
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
14458319-0	1961	The antithrombin activity of glucuronic esters of bilirubin.	glucuronic	29-39	serpin family C member 1	Homo sapiens	4-16
14458319-0	1961	The antithrombin activity of glucuronic esters of bilirubin.	Esters	40-46	serpin family C member 1	Homo sapiens	4-16
14458319-0	1961	The antithrombin activity of glucuronic esters of bilirubin.	Bilirubin	50-59	serpin family C member 1	Homo sapiens	4-16
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
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
13341284-0	1956	[Plasmatic cofactor of heparin and its relations with antithrombin].	Heparin	23-30	serpin family C member 1	Homo sapiens	54-66
14390722-0	1955	Studies on the antithrombin and heparin cofactor activities of a fraction adsorbed from plasma by aluminum hydroxide.	Aluminum Hydroxide	98-116	serpin family C member 1	Homo sapiens	15-27
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
13243272-0	1955	[Thrombin time and antithrombin power of human plasma in the presence of heparin and some synthetic heparinoids].	Heparinoids	100-111	serpin family C member 1	Homo sapiens	19-31
13198841-0	1954	The antithrombin activity of heparin.	Heparin	29-36	serpin family C member 1	Homo sapiens	4-16
13060907-0	1953	[Plasma content of accelerator and antithrombin active substance in dicumarol induced prothrombinemia].	Dicumarol	68-77	serpin family C member 1	Homo sapiens	35-47
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
13122496-2	1953	An evaluation of true plasma antithrombin titers with particular reference to the Kay test and alpha-tocopherol-calcium gluconate prophylaxis.	alpha-Tocopherol	95-111	serpin family C member 1	Homo sapiens	29-41
14945138-0	1952	[The antithrombin effect of heparin.	Heparin	28-35	serpin family C member 1	Homo sapiens	5-17
14782864-0	1950	Determination of serum prothrombin with a two-stage method, using alcohol to block antithrombin activity.	Alcohols	66-73	serpin family C member 1	Homo sapiens	83-95
15391885-0	1949	Effect of ultrafiltration and carbon dioxide on antithrombin activity of fresh and stored human plasma.	Carbon Dioxide	30-44	serpin family C member 1	Homo sapiens	48-60
20265749-0	1947	Variations in prothrombin and antithrombin following the administration of dicumarol.	Dicumarol	75-84	serpin family C member 1	Homo sapiens	30-42
32040256-0	2021	Antithrombin III as predictive indicator of survival in IPF patients treated with Nintedanib: a preliminary study.	nintedanib	82-92	serpin family C member 1	Homo sapiens	0-16
34017838-3	2021	The experimental results showed that PLA-combined Fe3O4-GO-ASA nanobubbles could effectively improve the antithrombin parameters of PT, TT, APTT, and INR, and significantly inhibit thrombosis when the composite nanobubbles with a concentration of 80 mg mL-1 interacted with the rabbit blood.	fe3o4-go-asa	50-62	serpin family C member 1	Homo sapiens	105-117
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
32040256-3	2021	A previous proteomic analysis of serum of IPF patients before and after one year of Nintedanib treatment showed differential protein expression of antithrombin III.	nintedanib	84-94	serpin family C member 1	Homo sapiens	147-163
32040256-5	2021	METHODS: Serum levels of ATIII were measured by ELISA in 14 IPF patients before and after one year of Nintedanib treatment.	nintedanib	102-112	serpin family C member 1	Homo sapiens	25-30
32040256-10	2021	The results of this preliminary study suggest, that ATIII has potential as a biomarker of IPF severity and in predicting answer to Nintedanib therapy.	nintedanib	131-141	serpin family C member 1	Homo sapiens	52-57
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.	pentasaccharide	29-44	serpin family C member 1	Homo sapiens	84-96
33924175-1	2021	Antithrombin (AT) is a natural anticoagulant that interacts with activated proteases of the coagulation system and with heparan sulfate proteoglycans (HSPG) on the surface of cells.	Heparitin Sulfate	120-135	serpin family C member 1	Homo sapiens	0-12
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.	Fondaparinux	45-57	serpin family C member 1	Homo sapiens	84-96
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.	Fondaparinux	59-63	serpin family C member 1	Homo sapiens	84-96
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
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
33756075-4	2021	We found that substitutions with hydrophobic amino acids in the loop region possessed significantly enhanced antithrombin activity, up to 3-fold higher than the native TBA.	tba	168-171	serpin family C member 1	Homo sapiens	109-121
33917853-1	2021	Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin.	Serine	23-29	serpin family C member 1	Homo sapiens	0-12
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
33187852-0	2021	Successful Antithrombin Administration in Andexanet Alfa-Associated Heparin Resistance.	Heparin	68-75	serpin family C member 1	Homo sapiens	11-23
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
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.	Vitamin K	119-128	serpin family C member 1	Homo sapiens	20-32
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
32536326-0	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
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
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
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
32650697-3	2021	Antithrombin is administered to potentiate heparin"s effects.	Heparin	43-50	serpin family C member 1	Homo sapiens	0-12
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
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
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
33387876-0	2021	SERPINC1 novel mutation (c.637C > T p. Gln213Ter) in a cerebral venous sinus thrombosis case and treatment with agatroban.	agatroban	112-121	serpin family C member 1	Homo sapiens	0-8
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
33176060-9	2021	In addition to the chain length, the type and extent of sulfation of glycosaminoglycans influenced the ability of skeletal muscle myosin to neutralize the polysaccharide"s ability to enhance antithrombin"s activity.	Polysaccharides	155-169	serpin family C member 1	Homo sapiens	191-203
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	13-22	serpin family C member 1	Homo sapiens	84-92
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	13-22	serpin family C member 1	Homo sapiens	145-153
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	185-194	serpin family C member 1	Homo sapiens	145-153
33169829-6	2021	Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds.	Disulfides	185-194	serpin family C member 1	Homo sapiens	145-153
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
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
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
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
33176060-6	2021	Skeletal muscle myosin also reduced the inhibition of factor Xa and thrombin by antithrombin in the presence of heparan sulfate.	Heparitin Sulfate	112-127	serpin family C member 1	Homo sapiens	80-92
33176060-9	2021	In addition to the chain length, the type and extent of sulfation of glycosaminoglycans influenced the ability of skeletal muscle myosin to neutralize the polysaccharide"s ability to enhance antithrombin"s activity.	Glycosaminoglycans	69-87	serpin family C member 1	Homo sapiens	191-203
33367661-0	2021	The Effect of Direct Oral Anticoagulants on Antithrombin Activity Testing Is Abolished by DOAC-Stop in Venous Thromboembolism Patients.	1-(4-acetyl-2,5-dimethoxyphenyl)-2-aminopropane	90-94	serpin family C member 1	Homo sapiens	44-56
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
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
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
33157292-1	2021	Nafamostat, a serine proteinase inhibitor with various actions including antithrombin, antiplasmin, and antitrypsin effects, has been used in clinical practice to treat disseminated intravascular coagulation (DIC) and pancreatitis.	nafamostat	0-10	serpin family C member 1	Homo sapiens	73-85
33390937-11	2020	This study is the first report of administering argatroban and titrating to its appropriate dose in the patient with valve thrombosis, antithrombin deficiency, and HT after mechanical thrombectomy for acute ischemic stroke.	argatroban	48-58	serpin family C member 1	Homo sapiens	135-147
33105321-0	2021	Chronic application of low-dose aspirin affects multiple parameters of three blood cellular types and antithrombin activity: A 1: 1: 1 Propensity Score Matching Analysis.	Aspirin	32-39	serpin family C member 1	Homo sapiens	102-114
33105321-6	2021	A dose-dependent relationship was observed between aspirin and decreased HPR incidence (PAA < 0.001, PADP < 0.01, respectively), decreased monocyte ratio (P = 0.052), increased antithrombin activity (P < 0.001), and increased platelet distribution width (P < 0.05).	Aspirin	51-58	serpin family C member 1	Homo sapiens	177-189
33105321-8	2021	Our finding demonstrated that aspirin exerts its antithrombotic effects at least by antiplatelet function, enhancing antithrombin activity and suppressing monocytes in vivo.	Aspirin	30-37	serpin family C member 1	Homo sapiens	117-129
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.	Warfarin	109-117	serpin family C member 1	Homo sapiens	55-57
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
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
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.	3-o sulfate	4-15	serpin family C member 1	Homo sapiens	182-194
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.	-glcns3s6s- monosaccharide	25-51	serpin family C member 1	Homo sapiens	182-194
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
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.	heparan sulfate glycosaminoglycans	67-101	serpin family C member 1	Homo sapiens	182-194
32745482-0	2020	Novel SERPINC1 missense mutation (Cys462Tyr) causes disruption of the 279Cys-462Cys disulfide bond and leads to type I hereditary antithrombin deficiency.	279cys	70-76	serpin family C member 1	Homo sapiens	6-14
32745482-0	2020	Novel SERPINC1 missense mutation (Cys462Tyr) causes disruption of the 279Cys-462Cys disulfide bond and leads to type I hereditary antithrombin deficiency.	Disulfides	84-93	serpin family C member 1	Homo sapiens	6-14
32745482-10	2020	CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family.	279cys	75-81	serpin family C member 1	Homo sapiens	14-22
32745482-10	2020	CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family.	279cys	75-81	serpin family C member 1	Homo sapiens	111-113
32745482-10	2020	CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family.	Disulfides	89-98	serpin family C member 1	Homo sapiens	14-22
32745482-10	2020	CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family.	Disulfides	89-98	serpin family C member 1	Homo sapiens	111-113
33419227-0	2021	N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function.	Nitrogen	0-1	serpin family C member 1	Homo sapiens	35-47
33419227-3	2021	Antithrombin, a serpin with four potential N-glycosylation sites, plays a pivotal role in hemostasis, wherein its deficiency significantly increases thrombotic risk.	Nitrogen	43-44	serpin family C member 1	Homo sapiens	0-12
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
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
33312433-10	2020	The activity of AT III and PC differed significantly between the two groups from postoperative day 1 to postoperative day 5 (P < 0.05), showing a moderate drop in activity of AT III and PC in the desflurane treatment group and a dramatic drop in the control group.	Desflurane	196-206	serpin family C member 1	Homo sapiens	16-22
33312433-10	2020	The activity of AT III and PC differed significantly between the two groups from postoperative day 1 to postoperative day 5 (P < 0.05), showing a moderate drop in activity of AT III and PC in the desflurane treatment group and a dramatic drop in the control group.	Desflurane	196-206	serpin family C member 1	Homo sapiens	175-181
33237165-9	2020	The stages of NHL were: I (21%), II (18,4%), III (26,3%), and IV (34,2%), but KS were found only at III (40%) and IV (60%) stages.	Potassium	78-80	serpin family C member 1	Homo sapiens	97-103
33146178-0	2020	Visualizing antithrombin-binding 3-O-sulfated heparan sulfate motifs on cell surfaces.	Heparitin Sulfate	46-61	serpin family C member 1	Homo sapiens	12-24
33146178-1	2020	To map the cellular topography of the rare 3-O-sulfated structural motif of heparan sulfate (HS), we constructed quantum dot-based probes for antithrombin and FGF2, which reveal widely different distribution of the targeted HS motifs.	Heparitin Sulfate	93-95	serpin family C member 1	Homo sapiens	142-154
33196311-4	2020	We give illustrative examples of benefit-risk evaluations using 4 treatment interventions including sodium glucose cotransporter 2 inhibitors in patients with type 2 diabetes; a direct antithrombin agent, dabigatran, for reducing stroke and systemic embolism in patients with nonvalvular atrial fibrillation; transcatheter aortic valve replacement in patients with symptomatic severe aortic valve stenosis; and antiplatelet agents vorapaxar and prasugrel for reducing cardiovascular events in patients at high cardiovascular risk.	Dabigatran	205-215	serpin family C member 1	Homo sapiens	185-197
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
32761495-6	2020	The level of ATIII was significantly negatively correlated with the levels of neutrophils, ferritin, LDH, total bilirubin, IL2R, IL6 and IL8 (p < 0.05).	Bilirubin	112-121	serpin family C member 1	Homo sapiens	13-18
32020514-7	2020	In vitro purification and characterization of variant AT showed significant decrease in fluorescence emission intensity, decreased bis-ANS fluorescence emission, changes in secondary structure and presence of polymerized AT in patient"s plasma as assessed by fluorescence, circular dichroism and transmission electron microscopy respectively.	5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)	131-138	serpin family C member 1	Homo sapiens	54-56
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
32791278-0	2020	Antithrombin III-mediated blood coagulation inhibitory activity of chitosan sulfate derivatized with different functional groups.	chitosan sulfate	67-83	serpin family C member 1	Homo sapiens	0-16
32791278-2	2020	The beneficial structural properties and high availability of the sulfate group in ChS1 led to greater anticoagulant activity through both the intrinsic and common pathways with antithrombin III (AT III)-mediated inhibition, particularly involving coagulation factors FXa and FIIa.	Sulfates	66-73	serpin family C member 1	Homo sapiens	178-194
32791278-2	2020	The beneficial structural properties and high availability of the sulfate group in ChS1 led to greater anticoagulant activity through both the intrinsic and common pathways with antithrombin III (AT III)-mediated inhibition, particularly involving coagulation factors FXa and FIIa.	Sulfates	66-73	serpin family C member 1	Homo sapiens	196-202
33083465-9	2020	Antithrombin III activity and body temperature 10 minutes after tourniquet release were significantly lower in the DEX group than in the CON group.	Dexmedetomidine	115-118	serpin family C member 1	Homo sapiens	0-16
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
32841498-0	2020	Impact of exogenous antithrombin on low molecular weight heparin anti-Xa activity assays in a pediatric and young adult leukemia and lymphoma cohort with variable antithrombin levels.	Heparin, Low-Molecular-Weight	36-64	serpin family C member 1	Homo sapiens	20-32
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
32515841-0	2020	Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid.	Iduronic Acid	73-86	serpin family C member 1	Homo sapiens	18-30
32515841-0	2020	Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid.	Glucuronic Acid	112-127	serpin family C member 1	Homo sapiens	18-30
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
32515841-1	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.	pentasaccharide	68-83	serpin family C member 1	Homo sapiens	31-43
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.	Trisaccharides	104-117	serpin family C member 1	Homo sapiens	31-43
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.	Glucuronic Acid	138-153	serpin family C member 1	Homo sapiens	31-43
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.	Glucuronic Acid	155-159	serpin family C member 1	Homo sapiens	31-43
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.	Polysaccharides	225-239	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
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.	Glucuronic Acid	90-94	serpin family C member 1	Homo sapiens	166-178
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.	idoa2s	110-116	serpin family C member 1	Homo sapiens	166-178
32515841-5	2020	Interestingly, two IdoA2S units, both present in a 1C4 - 2S0 equilibrium in the unbound saccharide, respectively shift to full 2S0 and full 1C4 upon binding to antithrombin, providing the best illustration of the critical role of iduronic acid conformational flexibility in biological systems.	Iduronic Acid	230-243	serpin family C member 1	Homo sapiens	160-172
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
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
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
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
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
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
33134780-6	2020	Results: TM-alpha administration did not prolong activated partial thromboplastin time but significantly decreased thrombin-antithrombin complex levels compared with heparin treatment.	tm-alpha	9-17	serpin family C member 1	Homo sapiens	124-136
33134780-7	2020	TM-alpha administration reduced consumption of endogenous anticoagulants such as antithrombin and protein C by DIC, compared with the heparin group.	tm-alpha	0-8	serpin family C member 1	Homo sapiens	81-93
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
32452976-15	2020	Age, disease state, and extracorporeal life support should be taken into consideration when administering antithrombin concentrate.	concentrate	119-130	serpin family C member 1	Homo sapiens	106-118
32422680-1	2020	Antithrombin (AT) is a serine protease inhibitor that regulates the activity of coagulation proteases of both intrinsic and extrinsic pathways.	Serine	23-29	serpin family C member 1	Homo sapiens	0-12
32905087-1	2020	Mannose phosphate isomerase deficiency-congenital disorder of glycosylation (MPI-CDG; formerly named CDG type 1b) is characterized by the clinical triad of hepatopathy, protein-losing enteropathy, and hyperinsulinemic hypoglycemia in combination with coagulation disorder (thrombophilia, depletion of antithrombin, proteins C and S, factor XI).	Mannosephosphates	0-17	serpin family C member 1	Homo sapiens	301-313
32905087-1	2020	Mannose phosphate isomerase deficiency-congenital disorder of glycosylation (MPI-CDG; formerly named CDG type 1b) is characterized by the clinical triad of hepatopathy, protein-losing enteropathy, and hyperinsulinemic hypoglycemia in combination with coagulation disorder (thrombophilia, depletion of antithrombin, proteins C and S, factor XI).	mpi-cdg	77-84	serpin family C member 1	Homo sapiens	301-313
32380829-9	2020	We expect that the tuning of plasmonic coupling at 3D level can open up new routes to design high performance SERS substrates for wide applications.	sers	110-114	serpin family C member 1	Homo sapiens	48-53
32523095-8	2020	When the targets of nintedanib (VEGFR, FGFR and PDGFR) were added, enrichment analysis extracted molecular pathways and process networks involved in cell differentiation (haptoglobin and albumin), coagulation (antithrombin III), epithelial mesenchymal transition, cell proliferation and transmigration.	nintedanib	20-30	serpin family C member 1	Homo sapiens	210-226
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
32194043-0	2020	Structural alteration in hypochlorous acid modified antithrombin indicates generation of neo-epitopes.	Hypochlorous Acid	25-42	serpin family C member 1	Homo sapiens	52-64
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
32347711-6	2020	The extent of sulfation of the minimal-length binder (hexamer) is relatively modest yet persistent, consistent with the notion of six sulfate groups being both essential and sufficient for antithrombin binding.	Sulfates	134-141	serpin family C member 1	Homo sapiens	189-201
32347711-8	2020	Molecular dynamics simulations confirm the existence of favorable electrostatic interactions between the high charge-density saccharide residues flanking the "canonical" antithrombin-binding hexasaccharide and the positive patch on the surface of the overall negatively charged protein.	Carbohydrates	125-135	serpin family C member 1	Homo sapiens	170-182
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
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
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
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
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
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
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
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
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
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
32300539-1	2020	We report the case of a 35-year-old pregnant woman (gravida 3, para 1) with antithrombin deficiency who was successfully treated with apixaban.	apixaban	134-142	serpin family C member 1	Homo sapiens	76-88
31885188-3	2020	Although transitory AT deficiencies and congenital disorders of the N-glycosylation pathways (CDG) have been recently reported as causes of AT deficiency, the current AT clinical screening still only includes anti-FXa activity.	Nitrogen	68-69	serpin family C member 1	Homo sapiens	140-142
32397894-3	2020	In the manufacturing process of fractionated antithrombin from plasma, heat treatment, citrate, and freeze drying speed up the transformation of native antithrombin to latent antithrombin.	Citric Acid	87-94	serpin family C member 1	Homo sapiens	45-57
32397894-3	2020	In the manufacturing process of fractionated antithrombin from plasma, heat treatment, citrate, and freeze drying speed up the transformation of native antithrombin to latent antithrombin.	Citric Acid	87-94	serpin family C member 1	Homo sapiens	152-164
32397894-3	2020	In the manufacturing process of fractionated antithrombin from plasma, heat treatment, citrate, and freeze drying speed up the transformation of native antithrombin to latent antithrombin.	Citric Acid	87-94	serpin family C member 1	Homo sapiens	152-164
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
32347711-8	2020	Molecular dynamics simulations confirm the existence of favorable electrostatic interactions between the high charge-density saccharide residues flanking the "canonical" antithrombin-binding hexasaccharide and the positive patch on the surface of the overall negatively charged protein.	hexasaccharide	191-205	serpin family C member 1	Homo sapiens	170-182
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
32039550-6	2020	RESULTS: Our data confirmed the overestimation of apixaban and rivaroxaban levels by the antithrombin-supplemented anti-Xa method (Berichrom).	apixaban	50-58	serpin family C member 1	Homo sapiens	89-101
32039550-6	2020	RESULTS: Our data confirmed the overestimation of apixaban and rivaroxaban levels by the antithrombin-supplemented anti-Xa method (Berichrom).	Rivaroxaban	63-74	serpin family C member 1	Homo sapiens	89-101
32194638-10	2020	This novel mutation resulted in a substitution of arginine by tryptophan, leading to antithrombin resistance (ATR).	Arginine	50-58	serpin family C member 1	Homo sapiens	85-97
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
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
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
32194638-10	2020	This novel mutation resulted in a substitution of arginine by tryptophan, leading to antithrombin resistance (ATR).	Tryptophan	62-72	serpin family C member 1	Homo sapiens	85-97
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
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
31986476-0	2020	Supplementation with antithrombin III ex vivo optimizes enoxaparin responses in critically injured patients.	Enoxaparin	56-66	serpin family C member 1	Homo sapiens	21-37
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
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
31850760-8	2020	Moreover, molecular docking illustrates the mechanism for the antithrombin activity of PfCN.	pfcn	87-91	serpin family C member 1	Homo sapiens	62-74
31766871-5	2020	Approach and Results: We observed that ellagic acid and long-chain polyphosphates activated the coagulation system in FXI-deficient plasma, as could be demonstrated by measurement of thrombin generation, FIXa-AT (antithrombin), and FXa-AT complex levels, suggesting an FXI bypass route of FIX activation.	Ellagic Acid	39-51	serpin family C member 1	Homo sapiens	213-225
31766871-5	2020	Approach and Results: We observed that ellagic acid and long-chain polyphosphates activated the coagulation system in FXI-deficient plasma, as could be demonstrated by measurement of thrombin generation, FIXa-AT (antithrombin), and FXa-AT complex levels, suggesting an FXI bypass route of FIX activation.	Polyphosphates	67-81	serpin family C member 1	Homo sapiens	213-225
31471127-2	2020	Soon it was found that: 1) thrombin inactivation by UFH was associated with the formation of molecular complexes between antithrombin and the activated forms of factor X (FXa) and thrombin, 2) low-molecular-weight fractions of UFH lose their antithrombin activity while still interacting with FXa, 3) a pentasaccharide sequence of UHF increases FXa (but not thrombin) inactivation by antithrombin.	pentasaccharide	303-318	serpin family C member 1	Homo sapiens	121-133
30913107-3	2020	aXa correlated with heparin (r = 0.97) and antithrombin (r = 0.98) but was unaffected by other parameters.	axa	0-3	serpin family C member 1	Homo sapiens	43-55
32010265-7	2020	ATIII expression was a predictor of AKI nondevelopment [Area under the curve (AUC)-Receiving operator characteristic (ROC)=0.729; sensitivity, 0.700; specificity, 0.714], and the ATIII/Creatine ratio was also a predictor of AKI nondevelopment (AUC-ROC=0.971; sensitivity, 0.900; specificity, 1).	Creatine	185-193	serpin family C member 1	Homo sapiens	0-5
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
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).	argatroban	470-480	serpin family C member 1	Homo sapiens	44-56
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).	bivalirudin	482-493	serpin family C member 1	Homo sapiens	44-56
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).	dabigatran	495-505	serpin family C member 1	Homo sapiens	44-56
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).	rivaroxaban	534-545	serpin family C member 1	Homo sapiens	44-56
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).	apixaban	547-555	serpin family C member 1	Homo sapiens	44-56
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).	edoxaban	557-565	serpin family C member 1	Homo sapiens	44-56
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).	betrixaban	575-585	serpin family C member 1	Homo sapiens	44-56
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
32002903-5	2020	In addition, many plasma proteins such as antithrombin III, superoxide dismutase, C1 inhibitor, and growth factors and cytokines bind to heparan sulfate and by this scenario contribute to the establishment of an anticoagulant and anti-inflammatory endothelial surface.	Heparitin Sulfate	137-152	serpin family C member 1	Homo sapiens	42-58
32152974-0	2020	Formulation and Characterization of Antithrombin Perfluorocarbon Nanoparticles.	Fluorocarbons	49-64	serpin family C member 1	Homo sapiens	36-48
32835836-9	2020	Multiple regression analysis adjusted for age, body-mass index, and fibrinogen levels showed that anti-FXa activity, antithrombin activity, and FVIII activity determined Ks, while anti-FXa activity, plasminogen activator inhibitor-1 level, and presence of right ventricular dysfunction determined CLT.	Potassium	170-172	serpin family C member 1	Homo sapiens	117-129
31747245-4	2019	Constructing an array with TAMRA-modified DNA aptamers that bind to different sites of human thrombin provides fluorescence fingerprints that reflect a reduction of the exposed surface area of thrombin upon complexation with antithrombin III, even in the presence of human serum.	tamra	27-32	serpin family C member 1	Homo sapiens	225-241
31662433-5	2019	Although ATIII has N-glycans and a hydrophobic core, we found that its quality control depended solely on free thiol content.	Sulfhydryl Compounds	111-116	serpin family C member 1	Homo sapiens	9-14
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
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
31662433-6	2019	Mutagenesis of all six Cys residues in ATIII to Ala resulted in its efficient secretion even though the product was not natively folded.	cysteinylcysteine	23-26	serpin family C member 1	Homo sapiens	39-44
31662433-6	2019	Mutagenesis of all six Cys residues in ATIII to Ala resulted in its efficient secretion even though the product was not natively folded.	alanyl-alanyl-alanyl-alanine	48-51	serpin family C member 1	Homo sapiens	39-44
31662433-7	2019	ATIII variants with free thiols were retained in the ER but not degraded.	Sulfhydryl Compounds	25-31	serpin family C member 1	Homo sapiens	0-5
31423004-0	2019	A Comparison of the Oligosaccharide Structures of Antithrombin Derived from Plasma and Recombinant Using POTELLIGENT  Technology.	Oligosaccharides	20-35	serpin family C member 1	Homo sapiens	50-62
31423004-1	2019	Human antithrombin (AT) has two isoforms of which the predominant alpha-form is glycosylated on all four possible glycosylation sites and the lower abundant beta-isoform lacks the oligosaccharide on Asn135.	Oligosaccharides	180-195	serpin family C member 1	Homo sapiens	6-18
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
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
31283067-13	2019	TEG combined with detection of AT-III and D-Dimer levels can distinguish patient with RSA from those with normal fertility and highly possibly predict the occurrence of RSA.	rabbit sperm membrane autoantigen	86-89	serpin family C member 1	Homo sapiens	31-37
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
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
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.	Carbohydrates	135-140	serpin family C member 1	Homo sapiens	165-177
31572449-3	2019	Hence, in the present study, we conducted a case-control study to further evaluate the association between the variant rs2227589 with antithrombin deficiency in pulmonary embolism (PTE).	poly(thienyl ethylene oxide butyl sulfonate)	181-184	serpin family C member 1	Homo sapiens	134-146
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
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
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
30939369-6	2019	Increasing the magnesite dosage from 0.83 to 3.33 g L-1 promoted the phosphorus recovery efficiency from 2.2% to 78.3% at 3 d, which was attributed to sufficient Mg2+ supply.	magnesium carbonate	15-24	serpin family C member 1	Homo sapiens	119-125
30939369-6	2019	Increasing the magnesite dosage from 0.83 to 3.33 g L-1 promoted the phosphorus recovery efficiency from 2.2% to 78.3% at 3 d, which was attributed to sufficient Mg2+ supply.	Phosphorus	69-79	serpin family C member 1	Homo sapiens	119-125
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
30322332-2	2019	PEG-Asp also lowers antithrombin (AT) levels.	pegaspargase	0-7	serpin family C member 1	Homo sapiens	20-32
31147454-0	2019	Trehalose: is it a potential inhibitor of antithrombin polymerization?	Trehalose	0-9	serpin family C member 1	Homo sapiens	42-54
31147454-7	2019	Rep (2019) 5, 39] studies the role of trehalose in the prevention of the polymerization of antithrombin, which belongs to the serpin superfamily.	Trehalose	38-47	serpin family C member 1	Homo sapiens	91-103
31147454-9	2019	The authors demonstrate that trehalose is able to prevent the in vitro polymerization of antithrombin, under conditions in which it usually tends to polymerize, and demonstrate it by using different techniques.	Trehalose	29-38	serpin family C member 1	Homo sapiens	89-101
31147454-10	2019	However, the binding site of trehalose in antithrombin should be defined by site-directed mutagenesis.	Trehalose	29-38	serpin family C member 1	Homo sapiens	42-54
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
30860622-11	2019	CONCLUSIONS: Apixaban concentrations were well correlated with PT (%), antithrombin, and dRVVT confirm test.	apixaban	13-21	serpin family C member 1	Homo sapiens	71-83
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
30873657-12	2019	Acetazolamide improved prothrombin time, factor X, and antithrombin.	Acetazolamide	0-13	serpin family C member 1	Homo sapiens	55-67
30262570-10	2019	The 5-year event-free survival was 80.9+-2.2% among patients assigned to antithrombin compared to 85.9+-2.0% in the unfractionated heparin group (P=0.06), and 86.2+-2.0% in the enoxaparin group (P=0.10).	Enoxaparin	177-187	serpin family C member 1	Homo sapiens	73-85
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
30886063-0	2019	Deciphering the role of trehalose in hindering antithrombin polymerization.	Trehalose	24-33	serpin family C member 1	Homo sapiens	47-59
30886063-4	2019	Here, we screened small molecules to find potential leads that can reduce AT polymer formation.	Polymers	77-84	serpin family C member 1	Homo sapiens	74-76
30886063-5	2019	We identified simple sugar molecules that successfully blocked polymer formation without a significant loss of normal activity of AT under specific buffer and temperature conditions.	Sugars	21-26	serpin family C member 1	Homo sapiens	130-132
30886063-6	2019	Of these, trehalose proved to be most promising as it showed a marked decrease in the bead like polymeric structures of AT shown by electron microscopic analysis.	Trehalose	10-19	serpin family C member 1	Homo sapiens	120-122
30886063-7	2019	A circular dichroism (CD) analysis indicated alteration in the secondary structure profile and an increased thermal stability of AT in the presence of trehalose.	Trehalose	151-160	serpin family C member 1	Homo sapiens	129-131
30886063-8	2019	Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose.	Guanidine	0-23	serpin family C member 1	Homo sapiens	60-62
30886063-8	2019	Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose.	Guanidine	25-31	serpin family C member 1	Homo sapiens	60-62
30886063-8	2019	Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose.	Trehalose	129-138	serpin family C member 1	Homo sapiens	60-62
30886063-9	2019	A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic.	1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid	42-92	serpin family C member 1	Homo sapiens	269-271
30886063-9	2019	A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic.	1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid	42-92	serpin family C member 1	Homo sapiens	284-286
30886063-9	2019	A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic.	5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)	94-101	serpin family C member 1	Homo sapiens	269-271
30886063-9	2019	A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic.	5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate)	94-101	serpin family C member 1	Homo sapiens	284-286
30886063-9	2019	A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic.	Trehalose	114-123	serpin family C member 1	Homo sapiens	269-271
30886063-9	2019	A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic.	Trehalose	114-123	serpin family C member 1	Homo sapiens	284-286
31090040-8	2019	Both baseline and nadir AT levels were significantly lower in severe than in mild and moderate AHB.	nadir	18-23	serpin family C member 1	Homo sapiens	24-26
31090040-9	2019	Moreover, the concentration of AT negatively correlated with INR, aspartate aminotransferase, and total and conjugated bilirubin levels.	Bilirubin	119-128	serpin family C member 1	Homo sapiens	31-33
31090040-10	2019	Interestingly, nadir AT levels positively correlated with the duration of hospitalization.	nadir	15-20	serpin family C member 1	Homo sapiens	21-23
30845788-4	2019	Possible inter-species differences in the GAG-binding sites on antithrombin III, heparanase, and chemokines of the CCL and CXCL families were examined by sequence alignments, molecular modelling and assessment of surface electrostatic potentials to determine if one species of laboratory animal is likely to result in more clinically relevant data than another.	Glycosaminoglycans	42-45	serpin family C member 1	Homo sapiens	63-79
30794399-2	2019	Thus, complexes between antithrombin and anti-VEGF RNA aptamers with single dithiophosphate moieties and thrombin and VEGF, respectively, display equilibrium dissociation constants KD of ca.	dithiophosphate	76-91	serpin family C member 1	Homo sapiens	24-36
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
30660948-0	2019	Monitoring of heparins in antithrombin-deficient patients.	Heparin	14-22	serpin family C member 1	Homo sapiens	26-38
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
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
30660948-6	2019	RESULTS: Mean anti-Xa activity with LWMH was 0.55 IU/mL (0.30-0.74) (recovery 69%, 38-93%) in antithrombin-deficient subjects and 0.82 (0.71-0.89) IU/mL in controls (recovery 103%, 89-111%).	lwmh	36-40	serpin family C member 1	Homo sapiens	94-106
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
30660948-9	2019	Antithrombin activity correlated with anti-Xa activity of UFH (R = 0.77) and LMWH (R = 0.66).	Heparin, Low-Molecular-Weight	77-81	serpin family C member 1	Homo sapiens	0-12
30660948-12	2019	Standard LWMH- or UFH-doses are likely to lead to under treatment in antithrombin-deficient individuals.	lwmh	9-13	serpin family C member 1	Homo sapiens	69-81
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
30791534-4	2019	The most negatively charged surface and the maximum binding ability towards antithrombin III were found for the heparinized PU with the lowest amount of aryl azide/anchor sites.	Polyurethanes	124-126	serpin family C member 1	Homo sapiens	76-92
30791534-4	2019	The most negatively charged surface and the maximum binding ability towards antithrombin III were found for the heparinized PU with the lowest amount of aryl azide/anchor sites.	aryl azide	153-163	serpin family C member 1	Homo sapiens	76-92
30545931-0	2019	MPI-CDG with transient hypoglycosylation and antithrombin deficiency.	mpi-cdg	0-7	serpin family C member 1	Homo sapiens	45-57
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
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
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
30618231-5	2019	At 3 d after I/R injury, NPcurcumin inhibited the increase in MMP-9, attenuated the decrease in occludin and zona occluden-1, and maintained BBB integrity.	npcurcumin	25-35	serpin family C member 1	Homo sapiens	0-6
31069723-8	2019	Positive correlations between total cholesterol and APTT and between triglyceride and APTT and ATIII were found in the poorly controlled PGDM group.	Triglycerides	69-81	serpin family C member 1	Homo sapiens	95-100
31069723-8	2019	Positive correlations between total cholesterol and APTT and between triglyceride and APTT and ATIII were found in the poorly controlled PGDM group.	9-hydroxy-11,15-dioxo-2,3,18,19-tetranorprost-5-ene-1,20-dioic acid	137-141	serpin family C member 1	Homo sapiens	95-100
30431449-2	2019	We encountered a case of inherited type I AT deficiency and identified the causative mutation; a novel c.7430A&gt;G missense mutation in the SERPINC1 gene in which tyrosine was substituted for cysteine at the 292nd amino acid.	Tyrosine	164-172	serpin family C member 1	Homo sapiens	141-149
30431449-2	2019	We encountered a case of inherited type I AT deficiency and identified the causative mutation; a novel c.7430A&gt;G missense mutation in the SERPINC1 gene in which tyrosine was substituted for cysteine at the 292nd amino acid.	Cysteine	193-201	serpin family C member 1	Homo sapiens	141-149
30174468-1	2018	Fitusiran is an RNA interference therapeutic that targets antithrombin (AT) in the liver and interferes with AT translation by binding and degrading messenger RNA-AT, thereby silencing AT gene expression and preventing AT synthesis.	Givosiran	0-9	serpin family C member 1	Homo sapiens	58-70
32821443-7	2019	Conclusion: Both ATIII and pentoxifylline treatments had positive effects on fibrinogen, FDP, D-Dimer, AT III activity and DIC scores in patients with Gram-negative sepsis who developed DIC.	Pentoxifylline	27-41	serpin family C member 1	Homo sapiens	103-109
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.	Alkynes	36-42	serpin family C member 1	Homo sapiens	153-169
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
29173042-0	2018	Antithrombin conformational modulation by D-myo-inositol 3,4,5,6-tetrakisphosphate (TMI), a novel scaffold for the development of antithrombotic agents.	D-myo-inositol 3,4,5,6-tetrakisphosphate	42-82	serpin family C member 1	Homo sapiens	0-12
29173042-0	2018	Antithrombin conformational modulation by D-myo-inositol 3,4,5,6-tetrakisphosphate (TMI), a novel scaffold for the development of antithrombotic agents.	4-tolyl isocyanate	84-87	serpin family C member 1	Homo sapiens	0-12
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.	Glycosaminoglycans	104-122	serpin family C member 1	Homo sapiens	0-12
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
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.	Heparitin Sulfate	138-153	serpin family C member 1	Homo sapiens	0-12
29173042-3	2018	Recently, a new compound, named TMI, was discovered in our group with nanomolar affinity to antithrombin, and shown to be able to induce a partial activation of antithrombin.	4-tolyl isocyanate	32-35	serpin family C member 1	Homo sapiens	92-104
29173042-3	2018	Recently, a new compound, named TMI, was discovered in our group with nanomolar affinity to antithrombin, and shown to be able to induce a partial activation of antithrombin.	4-tolyl isocyanate	32-35	serpin family C member 1	Homo sapiens	161-173
30319401-0	2018	Dexamethasone Preconditioning in Cardiac Procedures Reduces Decreased Antithrombin Activity and Is Associated to Beneficial Outcomes: Role of Endothelium.	Dexamethasone	0-13	serpin family C member 1	Homo sapiens	70-82
30077924-0	2018	Isolation of recombinant human antithrombin isoforms by Cellufine Sulfate affinity chromatography.	cellufine sulfate	56-73	serpin family C member 1	Homo sapiens	31-43
30808215-0	2019	The Antithrombin Effect of Ankaferd Hemostat (ABS) Is Related to the High Iron Content of the Medicine.	Iron	74-78	serpin family C member 1	Homo sapiens	4-16
31030756-5	2019	Low antithrombin III levels in blood circulation also affects the efficacy of Fondaparinux.	Fondaparinux	78-90	serpin family C member 1	Homo sapiens	4-20
30574006-4	2018	It remains controversial as to which anticoagulation therapy, defined as antithrombin or antiplatelet therapy, is better for patients with CS and a PFO.	Cesium	139-141	serpin family C member 1	Homo sapiens	73-85
30774881-4	2019	Through an experimental and computational approach using fluorescence polarization, ITC, docking and molecular dynamics simulations we investigate the binding of these functionalized GAG derivatives to ten representative regulatory proteins including IL-8, IL-10, BMP-2, sclerostin, TIMP-3, CXCL-12, TGF-beta, FGF-1, FGF-2, and AT-III, and we establish structure-activity relationships for GAG recognition.	Glycosaminoglycans	183-186	serpin family C member 1	Homo sapiens	328-334
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
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
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
29999301-1	2018	Factor Xa (fXa) inhibition by antithrombin (AT) enabled by heparin or heparan sulfate is critical for controlling blood coagulation.	Heparitin Sulfate	70-85	serpin family C member 1	Homo sapiens	30-42
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
29526957-6	2018	Rivaroxaban (15 mg) was continued for 6 months with no recurrence, indicating the efficacy of this factor Xa inhibitor for the treatment and prevention of VTE in patients with antithrombin deficiency.	Rivaroxaban	0-11	serpin family C member 1	Homo sapiens	176-188
29733637-7	2018	The anticoagulant action of copolymers is probably mediated by antithrombin, but it differs from that of unfractionated heparin.	copolymers	28-38	serpin family C member 1	Homo sapiens	63-75
30181723-0	2018	Effect of Exogenous Antithrombin Administration on Anti-Xa Levels in Infants Treated With Enoxaparin.	Enoxaparin	90-100	serpin family C member 1	Homo sapiens	20-32
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
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.	Enoxaparin	143-153	serpin family C member 1	Homo sapiens	46-62
30181723-8	2018	The median dose of antithrombin III was 50 units/kg and was administered when patients were receiving a median enoxaparin dose of 1.71 mg/kg.	Enoxaparin	111-121	serpin family C member 1	Homo sapiens	19-35
30181723-10	2018	CONCLUSIONS: These results demonstrated that administration of exogenous antithrombin III to infants who were being treated with enoxaparin results in a significant increase in anti-Xa levels.	Enoxaparin	129-139	serpin family C member 1	Homo sapiens	73-89
30181723-12	2018	However, antithrombin III supplementation could be considered a potential option for patients who are unable to adequately achieve therapeutic anti-Xa levels with enoxaparin alone.	Enoxaparin	163-173	serpin family C member 1	Homo sapiens	9-25
29353463-0	2018	Protective effect of a newly developed fucose-deficient recombinant antithrombin against histone-induced endothelial damage.	Fucose	39-45	serpin family C member 1	Homo sapiens	68-80
29353463-2	2018	In the present study, we sought to evaluate the protective effects of a newly developed fucose-deficient recombinant antithrombin.	Fucose	88-94	serpin family C member 1	Homo sapiens	117-129
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
29466798-13	2018	After multivariable analysis, ATIII activity &lt;75% remained a significant independent predictor of CIN (OR 2.207,95%CI [1.29-3.777]; P=0.004) as well as baseline serum creatinine (OR 1.009,95%CI [1.001-1.016]; P=0.026).	Creatinine	170-180	serpin family C member 1	Homo sapiens	30-35
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
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
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.	pentasaccharide	112-127	serpin family C member 1	Homo sapiens	59-71
29561141-2	2018	Three basic residues of antithrombin, Lys114, Lys125, and Arg129, have been shown to be hotspots for binding the pentasaccharide, but the molecular basis for such hotspot binding has been unclear.	pentasaccharide	113-128	serpin family C member 1	Homo sapiens	24-36
29561141-5	2018	Rapid kinetic studies showed that the hotspot residue mutations progressively abrogated the ability of the pentasaccharide to bind productively to native antithrombin and to conformationally activate the serpin by engaging the hotspot residues in an induced-fit interaction.	pentasaccharide	107-122	serpin family C member 1	Homo sapiens	154-166
29561141-6	2018	Examination of the antithrombin-pentasaccharide complex structure revealed that the hotspot residues form two adjoining binding pockets for critical sulfates of the pentasaccharide that structurally link these residues.	pentasaccharide	32-47	serpin family C member 1	Homo sapiens	19-31
29561141-6	2018	Examination of the antithrombin-pentasaccharide complex structure revealed that the hotspot residues form two adjoining binding pockets for critical sulfates of the pentasaccharide that structurally link these residues.	pentasaccharide	165-180	serpin family C member 1	Homo sapiens	19-31
29561141-7	2018	Together, these findings demonstrate that cooperative interactions of Lys114, Lys125, and Arg129 are critical for the productive induced-fit binding of the heparin pentasaccharide to antithrombin that allosterically activates the anticoagulant function of the serpin.	IC 831423	156-179	serpin family C member 1	Homo sapiens	183-195
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
29573524-2	2018	These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA).	pentasaccharide	102-117	serpin family C member 1	Homo sapiens	72-84
29573524-2	2018	These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA).	2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose	127-133	serpin family C member 1	Homo sapiens	72-84
29573524-2	2018	These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA).	6s-glca	137-144	serpin family C member 1	Homo sapiens	72-84
29573524-2	2018	These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA).	N-sulfo-D-glucosamine	145-150	serpin family C member 1	Homo sapiens	72-84
29573524-2	2018	These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA).	3,6s-idoa2s-glcns	151-168	serpin family C member 1	Homo sapiens	72-84
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
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
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
28888219-10	2018	CONCLUSIONS: Residual plasma rivaroxaban at the trough steady state may explain the antithrombin effect of rivaroxaban in patients with nonvalvular atrial fibrillation.	Rivaroxaban	29-40	serpin family C member 1	Homo sapiens	84-96
28888219-10	2018	CONCLUSIONS: Residual plasma rivaroxaban at the trough steady state may explain the antithrombin effect of rivaroxaban in patients with nonvalvular atrial fibrillation.	Rivaroxaban	107-118	serpin family C member 1	Homo sapiens	84-96
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
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
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
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
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
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
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
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
28602126-7	2017	Normalized LAC ratio was positively correlated with D-dimer, fibrinogen, and procoagulant activity of coagulating factor VIII, and negatively correlated with antithrombin activity, respectively ( P &lt; .01).	Lactose	11-14	serpin family C member 1	Homo sapiens	158-170
28961453-1	2017	INTRODUCTION: Antithrombin resistance (ATR) prothrombinemia is an inherited thrombophilic disorder caused by missense mutations in prothrombin gene (F2) at Arg596 of the sodium-binding region.	Sodium	170-176	serpin family C member 1	Homo sapiens	14-26
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
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
28617415-9	2017	Antithrombin-III levels and transferrin-glycosylation showed significant improvement, and increase in galactosylation and whole glycan content.	Polysaccharides	128-134	serpin family C member 1	Homo sapiens	0-16
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
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.	3-o	68-71	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.	3-o	68-71	serpin family C member 1	Homo sapiens	22-27
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.	Glucosamine	93-104	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.	Glucosamine	93-104	serpin family C member 1	Homo sapiens	22-27
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
29031112-4	2017	After exhaustively digesting LMWHs with the mixture of heparinase I, II and III, almost all the resulting oligosaccharide building blocks, including the three 3-O-sulfated tetrasaccharides derived from the ATIII-binding site, were resolved by CE separation.	tetrasaccharides	172-188	serpin family C member 1	Homo sapiens	206-211
29031112-7	2017	The peak assignment was further confirmed by analysis of the high ATIII affinity fractions, which contains much high 3-O-sulfated tetrasaccharides.	3-o-sulfated tetrasaccharides	117-146	serpin family C member 1	Homo sapiens	66-71
29031112-8	2017	With the method, the molar percentage of the ATIII-binding site of enoxaparin from different batches and different manufactures were measured and compared.	Enoxaparin	67-77	serpin family C member 1	Homo sapiens	45-50
28760491-0	2017	Effects of tibolone on fibrinogen and antithrombin III: A systematic review and meta-analysis of controlled trials.	tibolone	11-19	serpin family C member 1	Homo sapiens	38-54
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
28760491-1	2017	Tibolone is a synthetic steroid with estrogenic, androgenic and progestogenic activity, but the evidence regarding its effects on fibrinogen and antithrombin III (ATIII) has not been conclusive.	tibolone	0-8	serpin family C member 1	Homo sapiens	145-161
28760491-1	2017	Tibolone is a synthetic steroid with estrogenic, androgenic and progestogenic activity, but the evidence regarding its effects on fibrinogen and antithrombin III (ATIII) has not been conclusive.	tibolone	0-8	serpin family C member 1	Homo sapiens	163-168
28760491-2	2017	We assessed the impact of tibolone on fibrinogen and ATIII through a systematic review and meta-analysis of available randomized controlled trials (RCTs).	tibolone	26-34	serpin family C member 1	Homo sapiens	53-58
28760491-3	2017	The search included PUBMED, Web of Science, Scopus, and Google Scholar (up to January 31st, 2016) to identify controlled clinical studies investigating the effects of oral tibolone treatment on fibrinogen and ATIII.	tibolone	172-180	serpin family C member 1	Homo sapiens	209-214
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
28304137-8	2017	At 225 ng/mL apixaban, the median percentage increase in antithrombin level was 31% when measured with the Liquid Antithrombin  reagent and 44% with the Innovance Antithrombin  reagent.	apixaban	13-21	serpin family C member 1	Homo sapiens	57-69
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
30279820-8	2017	The present case suggests that rivaroxaban is a direct Factor Xa inhibitor and does not require cofactors such as antithrombin-III, thus it is suitable for anticoagulation therapy in patients with low antithrombin-III activity.&gt;.	Rivaroxaban	31-42	serpin family C member 1	Homo sapiens	201-217
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, Low-Molecular-Weight	93-97	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
28794370-5	2017	The present case illustrates the effectiveness of rivaroxaban in preventing thromboembolisms due to surgery, even in very elderly patients with antithrombin deficiency.	Rivaroxaban	50-61	serpin family C member 1	Homo sapiens	144-156
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
28485404-10	2017	Finally, we also obtained confirmatory results extending previous findings implicating AUTS2, SGOL1 and SERPINC1 genes in alcohol consumption traits in non-Hispanic whites.	Alcohols	122-129	serpin family C member 1	Homo sapiens	104-112
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
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
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
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
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, Low-Molecular-Weight	192-196	serpin family C member 1	Homo sapiens	45-57
28691885-2	2017	Fitusiran, an investigational RNA interference (RNAi) therapy that targets antithrombin (encoded by SERPINC1), is in development to address these and other limitations.	Givosiran	0-9	serpin family C member 1	Homo sapiens	75-87
28691885-2	2017	Fitusiran, an investigational RNA interference (RNAi) therapy that targets antithrombin (encoded by SERPINC1), is in development to address these and other limitations.	Givosiran	0-9	serpin family C member 1	Homo sapiens	100-108
28691885-12	2017	CONCLUSIONS: Once-monthly subcutaneous administration of fitusiran resulted in dose-dependent lowering of the antithrombin level and increased thrombin generation in participants with hemophilia A or B who did not have inhibitory alloantibodies.	Givosiran	57-66	serpin family C member 1	Homo sapiens	110-122
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
28317410-0	2017	Sex hormone-binding globulin and antithrombin III activity in women with oral ultra-low-dose estradiol.	Estradiol	93-102	serpin family C member 1	Homo sapiens	33-49
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
28219627-5	2017	Our data demonstrated ATIII significantly attenuated the elevation of serum creatinine, blood urea nitrogen, and renal histological injury.	Creatinine	76-86	serpin family C member 1	Homo sapiens	22-27
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
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
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
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
28481865-12	2017	4) HES significantly decreased antithrombin activity (AT: A) of the anticoagulant system with increasing HR vs. baseline and RL.	Hydroxyethyl Starch Derivatives	3-6	serpin family C member 1	Homo sapiens	31-43
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
28340300-7	2017	We identified a novel octasaccharide that interacts with antithrombin and displays anti factor Xa activity.	Octasaccharide	22-36	serpin family C member 1	Homo sapiens	57-69
30046692-10	2017	A deeper intronic mutation (c.1154-14G&gt;A), identified in three unrelated patients with traces of disulphide dimers of antithrombin in plasma, created a cryptic splicing site that might generate a variant with 4 additional in frame residues according to in silico predictions.	disulphide	100-110	serpin family C member 1	Homo sapiens	121-133
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
28229167-7	2017	The corresponding mutations in SERPINC1 (anti-thrombin III) at position 456 (Gly456Arg) and SERPINI1 (neuroserpin) at position 392 (Gly392Glu) caused an anti-thrombin deficiency and severe dementia due to intracellular retention of the polymers.	Polymers	236-244	serpin family C member 1	Homo sapiens	31-39
28007564-0	2017	Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants.	3-o-sulfated tetrasaccharides	39-68	serpin family C member 1	Homo sapiens	70-82
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
28772696-0	2017	Effect of Immobilized Antithrombin III on the Thromboresistance of Polycarbonate Urethane.	polycarbonate urethane	67-89	serpin family C member 1	Homo sapiens	22-38
28303970-9	2017	The decrease in the strong electronegative charge of terminal glycans may modulate hemostatic protein-protein interactions, which in combination with a strong prothrombotic situation, such as antithrombin deficiency, could increase the risk of thrombosis.	Polysaccharides	62-69	serpin family C member 1	Homo sapiens	192-204
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
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, Low-Molecular-Weight	31-35	serpin family C member 1	Homo sapiens	153-165
28282887-3	2017	In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin).	pentasaccharide	96-111	serpin family C member 1	Homo sapiens	70-82
28282887-3	2017	In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin).	Heparin, Low-Molecular-Weight	165-169	serpin family C member 1	Homo sapiens	70-82
28282887-3	2017	In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin).	Enoxaparin	215-225	serpin family C member 1	Homo sapiens	70-82
28219627-5	2017	Our data demonstrated ATIII significantly attenuated the elevation of serum creatinine, blood urea nitrogen, and renal histological injury.	Urea	94-98	serpin family C member 1	Homo sapiens	22-27
28219627-5	2017	Our data demonstrated ATIII significantly attenuated the elevation of serum creatinine, blood urea nitrogen, and renal histological injury.	Nitrogen	99-107	serpin family C member 1	Homo sapiens	22-27
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
28243911-2	2017	Antithrombin activity of dextran sulfate with a molecular weight of 20 kDa reached 12.6-15.3 U/mg.	Dextran Sulfate	25-40	serpin family C member 1	Homo sapiens	0-12
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	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	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
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
27783482-0	2017	An Asymmetric Runaway Domain Swap Antithrombin Dimer as a Key Intermediate for Polymerization Revealed by Hydrogen/Deuterium-Exchange Mass Spectrometry.	Hydrogen	106-114	serpin family C member 1	Homo sapiens	34-46
27783482-0	2017	An Asymmetric Runaway Domain Swap Antithrombin Dimer as a Key Intermediate for Polymerization Revealed by Hydrogen/Deuterium-Exchange Mass Spectrometry.	Deuterium	115-124	serpin family C member 1	Homo sapiens	34-46
27783482-6	2017	Here, we show how hydrogen/deuterium-exchange mass spectrometry (HDX-MS) provides detailed insight into the structural dynamics of each subunit in a polymerization-competent antithrombin dimer.	Hydrogen	18-26	serpin family C member 1	Homo sapiens	174-186
27783482-6	2017	Here, we show how hydrogen/deuterium-exchange mass spectrometry (HDX-MS) provides detailed insight into the structural dynamics of each subunit in a polymerization-competent antithrombin dimer.	Deuterium	27-36	serpin family C member 1	Homo sapiens	174-186
27783482-9	2017	The local subunit-specific deuterium uptake of this polymerization-competent dimer strongly supports a beta4A-beta5A beta-hairpin runaway domain swap mechanism for antithrombin polymerization.	Deuterium	27-36	serpin family C member 1	Homo sapiens	164-176
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
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
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, Low-Molecular-Weight	138-142	serpin family C member 1	Homo sapiens	34-46
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
27810279-0	2016	Synthesis and characterisation of magnetised Dacron-heparin composite employed for antithrombin affinity purification.	Polyethylene Terephthalates	45-51	serpin family C member 1	Homo sapiens	83-95
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
27810279-9	2016	Human plasma antithrombin activity was reduced by approximately 20% in the presence of the 1.0M NaCl fraction, and this eluate was able to prolong coagulation time (aPTT) using both preparations.	Sodium Chloride	96-100	serpin family C member 1	Homo sapiens	13-25
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
27862941-7	2016	Antithrombin action therefore requires a minimum length of seven sugar units next to the pentasaccharide whereas anti-factor Xa action does not.	Sugars	65-70	serpin family C member 1	Homo sapiens	0-12
27862941-7	2016	Antithrombin action therefore requires a minimum length of seven sugar units next to the pentasaccharide whereas anti-factor Xa action does not.	pentasaccharide	89-104	serpin family C member 1	Homo sapiens	0-12
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
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
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
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
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
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
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
27611497-3	2016	In this study, we report the effects of dFG-3 (Mw ~14kDa) on the catalysis rates of factor IIa (FIIa), factor Xa (FXa) and factor IXa (FIXa) inhibition by antithrombin (AT), and the kinetic of the interactions between coagulation proteases or inhibitors and dFG-3 were also studied using biolayer interferometry (BLI) technology.	1,3-Diphenylguanidine	40-43	serpin family C member 1	Homo sapiens	155-167
27611497-3	2016	In this study, we report the effects of dFG-3 (Mw ~14kDa) on the catalysis rates of factor IIa (FIIa), factor Xa (FXa) and factor IXa (FIXa) inhibition by antithrombin (AT), and the kinetic of the interactions between coagulation proteases or inhibitors and dFG-3 were also studied using biolayer interferometry (BLI) technology.	1,3-Diphenylguanidine	258-261	serpin family C member 1	Homo sapiens	155-167
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
27701728-9	2016	Warfarin-induced skin necrosis is a rare but serious complication that can be prevented by routine screening for protein C, protein S or antithrombin deficiencies or for the presence of antiphospholipid antibodies before beginning warfarin therapy.	Warfarin	0-8	serpin family C member 1	Homo sapiens	137-149
27324768-8	2016	Independent covariates related to significant decreases of linezolid concentrations included higher weight, creatinine clearance rates, and fibrinogen and antithrombin concentrations, lower concentrations of lactate, and the presence of acute respiratory distress syndrome (ARDS).	Linezolid	59-68	serpin family C member 1	Homo sapiens	155-167
27214821-11	2016	Moreover, intermittent antithrombin deficiency and hypoglycosylation was recorded in five out of these eight patients, all associated with moderate alcohol intake.	Alcohols	148-155	serpin family C member 1	Homo sapiens	23-35
27214821-14	2016	An aberrant N-glycosylation causing a recessive or transient antithrombin deficiency is a new form of thrombophilia.	Nitrogen	12-13	serpin family C member 1	Homo sapiens	61-73
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
27441845-0	2016	Correction: Identification of Regulatory Mutations in SERPINC1 Affecting Vitamin D Response Elements Associated with Antithrombin Deficiency.	Vitamin D	73-82	serpin family C member 1	Homo sapiens	54-62
27098529-9	2016	In conclusion, p.Val30Glu by affecting the cleavage of antithrombin"s signal peptide, results in a mature protein lacking the N-terminal dipeptide with no functional consequences in normal conditions, but that increases the sensitivity to be folded intracellularly into polymers, facilitating transient antithrombin deficiency and the subsequent risk of thrombosis.	Dipeptides	137-146	serpin family C member 1	Homo sapiens	55-67
27098529-9	2016	In conclusion, p.Val30Glu by affecting the cleavage of antithrombin"s signal peptide, results in a mature protein lacking the N-terminal dipeptide with no functional consequences in normal conditions, but that increases the sensitivity to be folded intracellularly into polymers, facilitating transient antithrombin deficiency and the subsequent risk of thrombosis.	Dipeptides	137-146	serpin family C member 1	Homo sapiens	303-315
26989842-4	2016	We developed a capillary zone electrophoresis method, based on a neutral polyethylene oxide-coated capillary and a buffer close to physiological conditions, enabling the separation of more than eight forms of AT.	Polyethylene Glycols	73-91	serpin family C member 1	Homo sapiens	209-211
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
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
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
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
27322195-7	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.	lys125alaantithrombin	116-137	serpin family C member 1	Homo sapiens	48-60
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
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
27010094-7	2016	Genetic analysis revealed a single-base substitution (C&gt;T) at the codon 359 (Arg to STOP) in the 5th exon portion of the antithrombin gene, heterozygote.	Arginine	80-83	serpin family C member 1	Homo sapiens	124-136
27222580-6	2016	ATIII has three disulfide bonds, two near the N terminus and one near the C terminus.	Disulfides	16-25	serpin family C member 1	Homo sapiens	0-5
27222580-7	2016	Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state.	Disulfides	74-83	serpin family C member 1	Homo sapiens	15-20
27222580-7	2016	Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state.	Disulfides	139-148	serpin family C member 1	Homo sapiens	15-20
27222580-7	2016	Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state.	Disulfides	185-195	serpin family C member 1	Homo sapiens	15-20
27222580-9	2016	N-linked glycans and carbohydrate-binding molecular chaperones contribute to the efficient folding and secretion of functional ATIII.	n-linked glycans	0-16	serpin family C member 1	Homo sapiens	127-132
27222580-9	2016	N-linked glycans and carbohydrate-binding molecular chaperones contribute to the efficient folding and secretion of functional ATIII.	Carbohydrates	21-33	serpin family C member 1	Homo sapiens	127-132
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
26747427-1	2016	The structure of the N-linked oligosaccharides attached to antithrombin (AT) has been shown to affect its anticoagulant activity and pharmacokinetics.	n-linked oligosaccharides	21-46	serpin family C member 1	Homo sapiens	59-71
27053426-7	2016	Antithrombin inactivation of thrombin was impaired in the presence of the sulfated coumarins suggesting that allosteric partial inhibition arises from catalytic dysfunction of the active site.	Coumarins	83-92	serpin family C member 1	Homo sapiens	0-12
27088203-7	2016	The patient had a steroid-dependent submicroscopic glomerulonephritis with a severe episode of nephrotic syndrome associated with centralization of circulation, proteinuria 40.9 g/day, deep hypoproteinemia (albumin=1.2 g/dl), hyperlipidemia, hypercoagulable state (antithrombin activity 29%), polycythemia (Hb=21.1 g/dl, HTC=60%).	Steroids	18-25	serpin family C member 1	Homo sapiens	265-277
27102510-4	2016	In Phase III trials, rivaroxaban, apixaban, edoxaban (antifactor Xa agents), and dabigatran (an antithrombin agent) were noninferior and probably safer than conventional anticoagulation therapy (low-molecular-weight heparin followed by vitamin K antagonists).	Dabigatran	81-91	serpin family C member 1	Homo sapiens	96-108
27003919-0	2016	Identification of Regulatory Mutations in SERPINC1 Affecting Vitamin D Response Elements Associated with Antithrombin Deficiency.	Vitamin D	61-70	serpin family C member 1	Homo sapiens	42-50
27003919-7	2016	The relevance of the vitamin D pathway on the regulation of SERPINC1 was confirmed in a cell model.	Vitamin D	21-30	serpin family C member 1	Homo sapiens	60-68
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
26797521-2	2016	Although another plasma serpin with an Arg-Ser reactive centre, antithrombin (AT), has been shown to inhibit factor VIIa (FVIIa), no published data are available with respect to FVIIa inhibition by API M358R.	Arginine	39-42	serpin family C member 1	Homo sapiens	64-76
26797521-2	2016	Although another plasma serpin with an Arg-Ser reactive centre, antithrombin (AT), has been shown to inhibit factor VIIa (FVIIa), no published data are available with respect to FVIIa inhibition by API M358R.	Serine	43-46	serpin family C member 1	Homo sapiens	64-76
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.	tetrasaccharide	49-64	serpin family C member 1	Homo sapiens	254-270
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
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.	Enoxaparin	120-130	serpin family C member 1	Homo sapiens	254-270
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.	3-o-sulfated tetrasaccharide	197-225	serpin family C member 1	Homo sapiens	254-270
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
27003919-8	2016	Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium.	paricalcitol	25-37	serpin family C member 1	Homo sapiens	100-108
27003919-8	2016	Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium.	paricalcitol	25-37	serpin family C member 1	Homo sapiens	124-136
27003919-8	2016	Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium.	Vitamin D	41-50	serpin family C member 1	Homo sapiens	100-108
27003919-9	2016	This study shows further evidence of the transcriptional regulation of SERPINC1 by vitamin D and first describes the functional and pathological relevance of mutations affecting VDRE of this gene.	Vitamin D	83-92	serpin family C member 1	Homo sapiens	71-79
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
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.	pentasaccharide	89-104	serpin family C member 1	Homo sapiens	140-152
26510969-11	2016	Edoxaban impairs the assessment of lupus anticoagulant, protein S (clotting method), APC-R, antithrombin (FXa-based assay) and measurement of clotting factor activity.	edoxaban	0-8	serpin family C member 1	Homo sapiens	92-104
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
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
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
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
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
26581031-5	2016	BACKGROUND: Antithrombin III (AT)beta is an isoform of AT that lacks the post-translational carbohydrate modification at Asn135.	Carbohydrates	92-104	serpin family C member 1	Homo sapiens	12-28
26584351-2	2016	METHODS: Polymer particles were incubated in (1) EDTA-plasma (10 mM) to monitor the adsorption of 20 selected proteins; (2) lepirudin-anticoagulated plasma to evaluate contact system activation, monitored by the formation of complexes between the generated proteases factor[F]XIIa, FXIa and kallikrein and the serpins C1-inhibitor [C1INH] and antithrombin [AT]; (3) lepirudin-anticoagulated whole blood to determine cytokine release.	Polymers	9-16	serpin family C member 1	Homo sapiens	343-355
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
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
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
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
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
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
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
26686866-2	2016	The molecule is a recombinant protein analog of factor Xa that binds to Factor Xa inhibitors and antithrombin:LMWH complex but does not trigger prothrombotic activity.	Heparin, Low-Molecular-Weight	110-114	serpin family C member 1	Homo sapiens	97-109
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
26554332-5	2016	Chorioallantoic membrane assay (CAM) shows that antiangiogenic activity of latent and oxidized AT are better than thalidomide, a potent antiangiogenic drug.	Thalidomide	114-125	serpin family C member 1	Homo sapiens	95-97
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
26674994-7	2016	Compared to the PMMA group, the BCC group exhibited significantly lower levels of arterial pressure, pulmonary artery pressure, blood oxygen pressure, blood carbon dioxide pressure, blood bicarbonate, base excess, antithrombin III and D-dimer.	bcc	32-35	serpin family C member 1	Homo sapiens	214-230
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
26280926-10	2015	These results were further confirmed by orthogonal analytical techniques, including NMR, which revealed compositional differences of oligosaccharides both in low- and high-affinity antithrombin fractions of enoxaparin.	Oligosaccharides	133-149	serpin family C member 1	Homo sapiens	181-193
26280926-10	2015	These results were further confirmed by orthogonal analytical techniques, including NMR, which revealed compositional differences of oligosaccharides both in low- and high-affinity antithrombin fractions of enoxaparin.	Enoxaparin	207-217	serpin family C member 1	Homo sapiens	181-193
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
26340667-8	2015	The comparison of the glycosidic linkage torsion angle values in solution with the antithrombin-pentasaccharide complex also indicates that the pentasaccharide conformation changes upon binding to antithrombin III.	pentasaccharide	96-111	serpin family C member 1	Homo sapiens	197-213
26340667-8	2015	The comparison of the glycosidic linkage torsion angle values in solution with the antithrombin-pentasaccharide complex also indicates that the pentasaccharide conformation changes upon binding to antithrombin III.	pentasaccharide	144-159	serpin family C member 1	Homo sapiens	197-213
26340667-9	2015	The data supports the assumption that the protein selects the more populated (2)S0 conformer of heparin pentasaccharide and, consequently, the binding process of heparin pentasaccharide with antithrombin III is energetically more favorable than formerly expected.	IC 831423	96-119	serpin family C member 1	Homo sapiens	191-207
26340667-9	2015	The data supports the assumption that the protein selects the more populated (2)S0 conformer of heparin pentasaccharide and, consequently, the binding process of heparin pentasaccharide with antithrombin III is energetically more favorable than formerly expected.	IC 831423	162-185	serpin family C member 1	Homo sapiens	191-207
26115461-0	2015	Investigating changes in the gas-phase conformation of Antithrombin III upon binding of Arixtra using traveling wave ion mobility spectrometry (TWIMS).	Fondaparinux	88-95	serpin family C member 1	Homo sapiens	55-71
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
26115461-4	2015	Arixtra is the smallest synthetic Hp containing the specific pentasaccharide sequence required to bind with ATIII.	Fondaparinux	0-7	serpin family C member 1	Homo sapiens	108-113
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
26115461-4	2015	Arixtra is the smallest synthetic Hp containing the specific pentasaccharide sequence required to bind with ATIII.	pentasaccharide	61-76	serpin family C member 1	Homo sapiens	108-113
26115461-5	2015	Here we report the first travelling wave ion mobility mass spectrometry (TWIMS) investigation of the conformational changes in ATIII induced by its interaction with Arixtra.	Fondaparinux	165-172	serpin family C member 1	Homo sapiens	127-132
26115461-6	2015	Native electrospray ionization mass spectrometry allowed the gentle transfer of the native topology of ATIII and ATIII-Arixtra complex.	Fondaparinux	119-126	serpin family C member 1	Homo sapiens	113-118
26115461-7	2015	IM measurements of ATIII and ATIII-Arixtra complex showed a single structure, with well-defined collisional cross section (CCS) values.	Fondaparinux	35-42	serpin family C member 1	Homo sapiens	29-34
26115461-8	2015	An average 3.6% increase in CCS of ATIII occurred as a result of its interaction with Arixtra, which agrees closely with the theoretical estimation of the change in CCS based on protein crystal structures.	Fondaparinux	86-93	serpin family C member 1	Homo sapiens	35-40
26115461-10	2015	A Hp oligosaccharide whose structure is similar to Arixtra but missing the 3-O sulfo group on the central glucosamine residue showed a dramatic decrease in binding affinity towards ATIII, but no change in the mobility behavior of the complex, consistent with prior studies that suggested that 3-O sulfation affects the equilibrium constant for binding to ATIII, but not the mode of interaction.	hp oligosaccharide	2-20	serpin family C member 1	Homo sapiens	181-186
26115461-10	2015	A Hp oligosaccharide whose structure is similar to Arixtra but missing the 3-O sulfo group on the central glucosamine residue showed a dramatic decrease in binding affinity towards ATIII, but no change in the mobility behavior of the complex, consistent with prior studies that suggested that 3-O sulfation affects the equilibrium constant for binding to ATIII, but not the mode of interaction.	hp oligosaccharide	2-20	serpin family C member 1	Homo sapiens	355-360
26115461-11	2015	In contrast, nonspecific binding by a Hp tetrasaccharide showed more complex mobility behavior, suggesting more promiscuous interactions with ATIII.	hp tetrasaccharide	38-56	serpin family C member 1	Homo sapiens	142-147
26115461-12	2015	The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding.	Fondaparinux	56-63	serpin family C member 1	Homo sapiens	50-55
26115461-12	2015	The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding.	Fondaparinux	56-63	serpin family C member 1	Homo sapiens	50-55
26115461-12	2015	The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding.	Fondaparinux	122-129	serpin family C member 1	Homo sapiens	40-45
26115461-12	2015	The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding.	Fondaparinux	122-129	serpin family C member 1	Homo sapiens	50-55
26115461-12	2015	The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding.	Fondaparinux	122-129	serpin family C member 1	Homo sapiens	50-55
26250112-7	2015	The comparative structural analyses indicated that neither the stability, nor the topology of the G4s, but the different localization of the two benzene rings of the linker was responsible for the loss of the antithrombin activity for TBA-bs13.	thrombin aptamer	235-238	serpin family C member 1	Homo sapiens	209-221
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
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
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
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).	Heparitin Sulfate	260-275	serpin family C member 1	Homo sapiens	6-18
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).	pentasaccharides	296-312	serpin family C member 1	Homo sapiens	6-18
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).	ps	314-316	serpin family C member 1	Homo sapiens	6-18
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
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
26186963-7	2015	RESULTS: High salt concentrations specifically restricted the pentassacharide-induced activation of antithrombin to the beta glycoform.	Salts	14-18	serpin family C member 1	Homo sapiens	100-112
26186963-7	2015	RESULTS: High salt concentrations specifically restricted the pentassacharide-induced activation of antithrombin to the beta glycoform.	pentassacharide	62-77	serpin family C member 1	Homo sapiens	100-112
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
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.	baysilon	24-46	serpin family C member 1	Homo sapiens	63-75
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
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.	polydopamine	133-145	serpin family C member 1	Homo sapiens	63-75
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
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".	polydopamine	139-151	serpin family C member 1	Homo sapiens	62-74
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".	polydopamine	153-156	serpin family C member 1	Homo sapiens	62-74
26082359-10	2015	Multiple regression analyses indicated that HCY level was negatively correlated with AT-III (beta = -0.199, P = 0.011) and positively correlated with age (beta = 0.217, P = 0.04), female gender (beta = 5.667, P = 0.001) and TM (beta = 2.341, P = 0.003).	Homocysteine	44-47	serpin family C member 1	Homo sapiens	85-91
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
26232351-0	2015	Extracellular histone H3 levels are inversely correlated with antithrombin levels and platelet counts and are associated with mortality in sepsis patients.	HS 3	22-24	serpin family C member 1	Homo sapiens	62-74
26232351-6	2015	H3 levels are positively correlated with lactate dehydrogenase (LDH) activity (Spearman"s rho=0.49, P&lt;0.001), and negatively correlated with antithrombin levels (rho=-0.34, P=0.027) and platelet counts (rho=-0.33, P=0.031).	HS 3	0-2	serpin family C member 1	Homo sapiens	144-156
26232351-7	2015	CONCLUSIONS: We conclude that circulating H3 levels correlate with mortality in sepsis patients and inversely correlate with antithrombin levels and platelet counts.	HS 3	42-44	serpin family C member 1	Homo sapiens	125-137
26059252-1	2015	The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers.	pentasaccharide	199-214	serpin family C member 1	Homo sapiens	158-174
26059252-1	2015	The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers.	pentasaccharide	199-214	serpin family C member 1	Homo sapiens	176-181
26059252-1	2015	The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers.	tetraethylene glycol	223-243	serpin family C member 1	Homo sapiens	158-174
26059252-1	2015	The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers.	tetraethylene glycol	223-243	serpin family C member 1	Homo sapiens	176-181
26059252-10	2015	In conclusion, GLP-1 peptides conjugated to an ATIII binding carrier pentasaccharide have a substantially prolonged bioactive profile compatible for possible once-weekly treatment of type 2 diabetes in humans.	pentasaccharide	69-84	serpin family C member 1	Homo sapiens	47-52
25869030-0	2015	Successful treatment with rivaroxaban of an extended superficial vein thrombosis in a patient with acquired antithrombin deficiency due to Peg-asparaginase treatment.	Rivaroxaban	26-37	serpin family C member 1	Homo sapiens	108-120
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
29123765-13	2016	The thrombin-antithrombin complex may be useful for monitoring the plasma dabigatran level.	Dabigatran	74-84	serpin family C member 1	Homo sapiens	13-25
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
25585615-5	2015	The results revealed that the antithrombin activity of the boronophenylalanine-modified hirudin to human thrombin was more enhanced than that of rHirudin.	4-boronophenylalanine	59-78	serpin family C member 1	Homo sapiens	30-42
25585615-5	2015	The results revealed that the antithrombin activity of the boronophenylalanine-modified hirudin to human thrombin was more enhanced than that of rHirudin.	rhirudin	145-153	serpin family C member 1	Homo sapiens	30-42
26023895-6	2015	Further studies revealed that the reactivity of FIXa-G317R and FIXa-G317E with antithrombin has been impaired 10- and 13-fold, respectively, in the absence and 166- and 500-fold, respectively, in the presence of pentasaccharide.	pentasaccharide	212-227	serpin family C member 1	Homo sapiens	79-91
25851619-2	2015	Hemophilia B prophylaxis targets plasma FIX levels &gt; 1% but neglects extravascular FIX, which colocalizes with antithrombin-heparan sulfate.	Heparitin Sulfate	127-142	serpin family C member 1	Homo sapiens	114-126
25851619-9	2015	Dual mutations in the heparin exosite or combined mutations in both exosites synergistically reduced the inhibition rate for antithrombin-heparin.	heparin exosite	22-37	serpin family C member 1	Homo sapiens	125-137
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
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
25921251-0	2015	High-resolution probing heparan sulfate-antithrombin interaction on a single endothelial cell surface: single-molecule AFM studies.	Heparitin Sulfate	24-39	serpin family C member 1	Homo sapiens	40-52
25921251-1	2015	Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT).	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	179-191
25921251-1	2015	Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT).	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	193-195
25921251-1	2015	Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT).	Heparitin Sulfate	17-19	serpin family C member 1	Homo sapiens	179-191
25921251-1	2015	Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT).	Heparitin Sulfate	17-19	serpin family C member 1	Homo sapiens	193-195
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
25553275-5	2015	RESULTS: The procoagulant factors II, VII, IX, X, and XI and anticoagulant factors protein C and protein S showed significant correlations with triglyceride, and the procoagulant factors II, V, VII, IX, X, XI, and XII and anticoagulant factors antithrombin and protein C correlated with total cholesterol.	Triglycerides	144-156	serpin family C member 1	Homo sapiens	244-256
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
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
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
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.	argatroban	193-203	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.	argatroban	193-203	serpin family C member 1	Homo sapiens	144-146
25600805-6	2015	Other serpins, including antithrombin III and pigment epithelium-derived factor, were also degraded by heparan sulfate.	Heparitin Sulfate	103-118	serpin family C member 1	Homo sapiens	25-41
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
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
25325940-2	2015	One example, the extensively studied heparin pentasaccharide sequence-which binds antithrombin-III, inducing a conformational change that increases its serpin protease activity by 1,000-fold-is unique in that no other specific GAG-protein structure-function relations have been described to the same degree.	IC 831423	37-60	serpin family C member 1	Homo sapiens	82-98
25325940-2	2015	One example, the extensively studied heparin pentasaccharide sequence-which binds antithrombin-III, inducing a conformational change that increases its serpin protease activity by 1,000-fold-is unique in that no other specific GAG-protein structure-function relations have been described to the same degree.	Glycosaminoglycans	227-230	serpin family C member 1	Homo sapiens	82-98
25325941-3	2015	However, only 3-O sulfonated heparin pentasaccharide units have been proven to bind to antithrombin and elicit an anticoagulant response.	IC 831423	29-52	serpin family C member 1	Homo sapiens	87-99
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
25687119-6	2015	Furthermore, Bothrops jararaca antithrombin is more effective in preventing acute inflammation induced by carrageenan when compared to human antithrombin.	Carrageenan	106-117	serpin family C member 1	Homo sapiens	31-43
25231101-10	2015	The presence of dabigatran caused an overestimation of the antithrombin level when measured with a thrombin-based activity assay and the presence of rivaroxaban an overestimation of the antithrombin level when measured with a FXa-based assay.	Dabigatran	16-26	serpin family C member 1	Homo sapiens	59-71
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
25466848-7	2015	Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression.	Retinoids	0-9	serpin family C member 1	Homo sapiens	112-114
25466848-7	2015	Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression.	Dexamethasone	36-49	serpin family C member 1	Homo sapiens	112-114
25466848-7	2015	Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression.	Cortisone	51-60	serpin family C member 1	Homo sapiens	112-114
25466848-7	2015	Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression.	Methylprednisolone	65-83	serpin family C member 1	Homo sapiens	112-114
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.	heparan sulfate (hs) 3-	0-23	serpin family C member 1	Homo sapiens	88-104
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
25485983-1	2014	The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: alpha and beta, with four and three N-glycans, respectively.	N-[3-(Trimethoxysilyl)propyl]aniline	55-59	serpin family C member 1	Homo sapiens	63-75
25485983-1	2014	The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: alpha and beta, with four and three N-glycans, respectively.	n-glycans	190-199	serpin family C member 1	Homo sapiens	63-75
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
25331949-3	2014	Mutations of antithrombin Tyr(253) and His(319) exosite residues produced massive 10-200-fold losses in reactivity with factors Xa and IXa in both unactivated and heparin-activated states, indicating that these residues made critical attractive interactions with protease independent of heparin activation.	Tyrosine	26-29	serpin family C member 1	Homo sapiens	13-25
25331949-3	2014	Mutations of antithrombin Tyr(253) and His(319) exosite residues produced massive 10-200-fold losses in reactivity with factors Xa and IXa in both unactivated and heparin-activated states, indicating that these residues made critical attractive interactions with protease independent of heparin activation.	exosite	48-55	serpin family C member 1	Homo sapiens	13-25
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.	exosite	35-42	serpin family C member 1	Homo sapiens	67-79
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
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
25307422-3	2014	MGO has been shown to inhibit ATIII activity in vitro, however the mechanism of inhibition is incompletely understood.	Pyruvaldehyde	0-3	serpin family C member 1	Homo sapiens	30-35
25396040-5	2014	Soc., 2013, 135, 167 - 173) to a piperidinone-piperidine chemotype 1 indicated specific derivatives were candidates to perturb a protein-protein interface in the alpha-antithrombin dimer; those particular derivatives of 1 were prepared and tested.	2-piperidone	33-45	serpin family C member 1	Homo sapiens	168-180
25396040-5	2014	Soc., 2013, 135, 167 - 173) to a piperidinone-piperidine chemotype 1 indicated specific derivatives were candidates to perturb a protein-protein interface in the alpha-antithrombin dimer; those particular derivatives of 1 were prepared and tested.	piperidine	46-56	serpin family C member 1	Homo sapiens	168-180
25307422-4	2014	As such, we designed this study to investigate the kinetics and mechanism of MGO-mediated ATIII inhibition.	Pyruvaldehyde	77-80	serpin family C member 1	Homo sapiens	90-95
25307422-5	2014	METHODS: MGO-mediated ATIII inhibition was confirmed using inverse experiments detecting activity of the ATIII targets thrombin and factor Xa.	Pyruvaldehyde	9-12	serpin family C member 1	Homo sapiens	22-27
25307422-5	2014	METHODS: MGO-mediated ATIII inhibition was confirmed using inverse experiments detecting activity of the ATIII targets thrombin and factor Xa.	Pyruvaldehyde	9-12	serpin family C member 1	Homo sapiens	105-110
25307422-6	2014	Fluorogenic assays were performed in both PBS and plasma after incubation of ATIII with MGO, at molar ratios comparable to those observed in the plasma of diabetic patients.	Pyruvaldehyde	88-91	serpin family C member 1	Homo sapiens	77-82
25307422-7	2014	LC-coupled tandem mass spectrometry was utilized to investigate the exact mechanism of MGO-mediated ATIII inhibition.	Pyruvaldehyde	87-90	serpin family C member 1	Homo sapiens	100-105
25307422-8	2014	RESULTS AND CONCLUSIONS: MGO concentration-dependently attenuated inhibition of thrombin and factor Xa by ATIII in PBS-based assays, both in the presence and absence of heparin.	Pyruvaldehyde	25-28	serpin family C member 1	Homo sapiens	106-111
25307422-9	2014	In addition, MGO concentration-dependently inhibited ATIII activity in a plasma-based system, to the level of plasma completely deficient in ATIII, again both in the presence and absence of heparin.	Pyruvaldehyde	13-16	serpin family C member 1	Homo sapiens	53-58
25307422-9	2014	In addition, MGO concentration-dependently inhibited ATIII activity in a plasma-based system, to the level of plasma completely deficient in ATIII, again both in the presence and absence of heparin.	Pyruvaldehyde	13-16	serpin family C member 1	Homo sapiens	141-146
25307422-10	2014	Results from LC-MS/MS experiments revealed that MGO covalently adducts the active site Arg 393 of ATIII through two distinct glyoxalation mechanisms.	Pyruvaldehyde	48-51	serpin family C member 1	Homo sapiens	98-103
25307422-10	2014	Results from LC-MS/MS experiments revealed that MGO covalently adducts the active site Arg 393 of ATIII through two distinct glyoxalation mechanisms.	Arginine	87-90	serpin family C member 1	Homo sapiens	98-103
25307422-11	2014	We posit that active site adduction is the mechanism of MGO-mediated inhibition of ATIII, and thus contributes to the underlying pathophysiology of the diabetic hypercoagulable state and complications thereof.	Pyruvaldehyde	56-59	serpin family C member 1	Homo sapiens	83-88
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
23698186-1	2014	Valsartan is known to inhibit platelet activity in both in vitro and ex vivo clinical setting, whereas aliskiren in vitro modulates antithrombin-III in plasma.	aliskiren	103-112	serpin family C member 1	Homo sapiens	132-148
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
24711209-8	2014	In addition, antithrombin constituted ~40% of the total adsorbed plasma protein concentration on the EPA-heparin surfaces.	Eicosapentaenoic Acid	101-104	serpin family C member 1	Homo sapiens	13-25
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
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
25361933-6	2014	The uHcy/Cr ratio correlated more closely with protein C, antithrombin III, TNF-alpha, and NOx levels than did sHcy concentrations.	Chromium	9-11	serpin family C member 1	Homo sapiens	58-74
25145542-0	2014	Antithrombin-binding oligosaccharides: structural diversities in a unique function?	Oligosaccharides	21-37	serpin family C member 1	Homo sapiens	0-12
25145542-3	2014	Moreover, the position of the pentasaccharide along the chain as well as the structure of the neighbor units affects the affinity to antithrombin.	pentasaccharide	30-45	serpin family C member 1	Homo sapiens	133-145
25145542-4	2014	The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin.	Oligosaccharides	197-213	serpin family C member 1	Homo sapiens	176-188
25145542-4	2014	The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin.	Oligosaccharides	197-213	serpin family C member 1	Homo sapiens	258-270
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
25130453-10	2014	At 3-D imaging and dissection, the DAEM was found to be an extension of the metacarpophalangeal joint capsule.	daem	35-39	serpin family C member 1	Homo sapiens	0-6
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).	Tinzaparin	148-158	serpin family C member 1	Homo sapiens	49-55
24920241-0	2014	Outstanding effects on antithrombin activity of modified TBA diastereomers containing an optically pure acyclic nucleotide analogue.	tba	57-60	serpin family C member 1	Homo sapiens	23-35
24979180-1	2014	CONTEXT: The results of studies among patients with antithrombin deficiency have suggested that the use of warfarin will increase the level of antithrombin.	Warfarin	107-115	serpin family C member 1	Homo sapiens	52-64
24979180-1	2014	CONTEXT: The results of studies among patients with antithrombin deficiency have suggested that the use of warfarin will increase the level of antithrombin.	Warfarin	107-115	serpin family C member 1	Homo sapiens	143-155
24979180-2	2014	OBJECTIVE: To reevaluate the effect of warfarin on antithrombin levels using an automated amidolytic method in current use.	Warfarin	39-47	serpin family C member 1	Homo sapiens	51-63
24979180-3	2014	DESIGN: Antithrombin levels were measured in patients who were receiving warfarin for atrial fibrillation and were compared with antithrombin levels in preoperative patients who had not received warfarin.	Warfarin	73-81	serpin family C member 1	Homo sapiens	8-20
24979180-4	2014	RESULTS: Patients receiving warfarin had a mean antithrombin level of 100.40% (range, 81%-153%).	Warfarin	28-36	serpin family C member 1	Homo sapiens	48-60
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
24801362-7	2014	The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms.	Salts	199-203	serpin family C member 1	Homo sapiens	86-98
24801362-7	2014	The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms.	Salts	199-203	serpin family C member 1	Homo sapiens	151-163
24801362-7	2014	The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms.	Salts	199-203	serpin family C member 1	Homo sapiens	151-163
24375987-0	2014	Retrospective evaluation of antithrombin III supplementation in neonates and infants receiving enoxaparin for treatment of thrombosis.	Enoxaparin	95-105	serpin family C member 1	Homo sapiens	28-44
24375987-5	2014	PROCEDURE: This retrospective study compared time to therapeutic anti-Xa levels in patients &lt;1 year of age receiving enoxaparin with AT3 (Group 1) and without AT3 (Group 2) for treatment of thrombosis.	Enoxaparin	120-130	serpin family C member 1	Homo sapiens	136-139
24561026-3	2014	Activated AT also inhibits thrombin by forming a stable ternary complex of AT, thrombin, and a polysaccharide (requires at least an 18-mer/octadeca-mer polysaccharide).	Polysaccharides	152-166	serpin family C member 1	Homo sapiens	10-12
24561026-3	2014	Activated AT also inhibits thrombin by forming a stable ternary complex of AT, thrombin, and a polysaccharide (requires at least an 18-mer/octadeca-mer polysaccharide).	Polysaccharides	152-166	serpin family C member 1	Homo sapiens	75-77
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
24616065-2	2014	The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue.	IC 831423	81-104	serpin family C member 1	Homo sapiens	40-46
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
24770491-7	2014	The antithrombin (AT) binding affinities of a GlcA2S- and an IdoA2S-hexasaccharide were determined by affinity co-electrophoresis.	2-O-sulfo-beta-D-glucuronic acid	46-52	serpin family C member 1	Homo sapiens	4-16
24770491-7	2014	The antithrombin (AT) binding affinities of a GlcA2S- and an IdoA2S-hexasaccharide were determined by affinity co-electrophoresis.	idoa2s-hexasaccharide	61-82	serpin family C member 1	Homo sapiens	4-16
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
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
24824609-0	2014	Role of the C-sheet in the maturation of N-glycans on antithrombin: functional relevance of pleiotropic mutations.	n-glycans	41-50	serpin family C member 1	Homo sapiens	54-66
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
24824609-12	2014	Our results suggest the C-sheet of antithrombin as a new region that is relevant for proper maturation of the N-glycans.	n-glycans	110-119	serpin family C member 1	Homo sapiens	35-47
24561026-0	2014	Isolation of a pure octadecasaccharide with antithrombin activity from an ultra-low-molecular-weight heparin.	octadecasaccharide	20-38	serpin family C member 1	Homo sapiens	44-56
24561026-2	2014	Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine.	pentasaccharide	87-102	serpin family C member 1	Homo sapiens	27-39
24561026-2	2014	Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine.	pentasaccharide	87-102	serpin family C member 1	Homo sapiens	41-43
24561026-2	2014	Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine.	pentasaccharide	87-102	serpin family C member 1	Homo sapiens	72-74
24561026-2	2014	Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine.	glucosamine 3-O-sulfate	124-148	serpin family C member 1	Homo sapiens	27-39
24561026-2	2014	Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine.	glucosamine 3-O-sulfate	124-148	serpin family C member 1	Homo sapiens	41-43
24561026-2	2014	Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine.	glucosamine 3-O-sulfate	124-148	serpin family C member 1	Homo sapiens	72-74
24561026-3	2014	Activated AT also inhibits thrombin by forming a stable ternary complex of AT, thrombin, and a polysaccharide (requires at least an 18-mer/octadeca-mer polysaccharide).	Polysaccharides	95-109	serpin family C member 1	Homo sapiens	10-12
24616065-2	2014	The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue.	3,6-o	127-132	serpin family C member 1	Homo sapiens	40-46
24616065-2	2014	The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue.	glucosamine 2-sulfate	142-160	serpin family C member 1	Homo sapiens	40-46
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
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).	Enoxaparin	132-142	serpin family C member 1	Homo sapiens	49-55
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).	pentasaccharide	177-192	serpin family C member 1	Homo sapiens	49-55
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).	Fondaparinux	198-210	serpin family C member 1	Homo sapiens	49-55
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).	Fondaparinux	212-219	serpin family C member 1	Homo sapiens	49-55
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
24632519-7	2014	P-beads bound LPS dissolved in antithrombin III (AT III) solution which is a strong inhibitor of activated factors C and B as well as the clotting enzyme in the LAL assay; the inhibitory effect of AT III was completely reversed upon washing the P-beads with 25% acetonitrile.	acetonitrile	262-274	serpin family C member 1	Homo sapiens	31-47
24632519-7	2014	P-beads bound LPS dissolved in antithrombin III (AT III) solution which is a strong inhibitor of activated factors C and B as well as the clotting enzyme in the LAL assay; the inhibitory effect of AT III was completely reversed upon washing the P-beads with 25% acetonitrile.	acetonitrile	262-274	serpin family C member 1	Homo sapiens	49-55
24632519-7	2014	P-beads bound LPS dissolved in antithrombin III (AT III) solution which is a strong inhibitor of activated factors C and B as well as the clotting enzyme in the LAL assay; the inhibitory effect of AT III was completely reversed upon washing the P-beads with 25% acetonitrile.	acetonitrile	262-274	serpin family C member 1	Homo sapiens	197-203
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
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.	Fondaparinux	0-12	serpin family C member 1	Homo sapiens	78-94
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.	Fondaparinux	0-12	serpin family C member 1	Homo sapiens	96-102
24361527-3	2014	Sulfation at the C3 position of glucosamine is a relatively rare, yet biologically significant modification, initially described as a key determinant for binding and activation of antithrombin and later for infection by type I herpes simplex virus.	Glucosamine	32-43	serpin family C member 1	Homo sapiens	180-192
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.	pentasaccharide	48-63	serpin family C member 1	Homo sapiens	78-94
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
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.	pentasaccharide	48-63	serpin family C member 1	Homo sapiens	96-102
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
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
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
23460104-9	2014	The novel oral anticoagulants (NOAC) dabigatran etexilat (Pradaxa ), rivaroxaban (Xarelto ) and apixaban (Eliquis ), also known as "direct" anticoagulants, act independently from antithrombin by inhibiting thrombin, as in the case of dabigatran, or by inhibiting factor Xa, as in the case of rivaroxaban and apixaban.	apixaban	96-104	serpin family C member 1	Homo sapiens	179-191
23460104-9	2014	The novel oral anticoagulants (NOAC) dabigatran etexilat (Pradaxa ), rivaroxaban (Xarelto ) and apixaban (Eliquis ), also known as "direct" anticoagulants, act independently from antithrombin by inhibiting thrombin, as in the case of dabigatran, or by inhibiting factor Xa, as in the case of rivaroxaban and apixaban.	Dabigatran	37-47	serpin family C member 1	Homo sapiens	179-191
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
24339381-3	2014	We have discovered that exosite-targeting antithrombin aptamers enhance the activity of thrombin toward a small peptide substrate, Sar(N-methylglycine)-Pro-Arg-paranitroanilide, and that the activation of the enzyme by these aptamers is strongly inhibited by their complementary DNAs.	exosite	24-31	serpin family C member 1	Homo sapiens	42-54
24339381-3	2014	We have discovered that exosite-targeting antithrombin aptamers enhance the activity of thrombin toward a small peptide substrate, Sar(N-methylglycine)-Pro-Arg-paranitroanilide, and that the activation of the enzyme by these aptamers is strongly inhibited by their complementary DNAs.	(n-methylglycine)-pro-arg-paranitroanilide	134-176	serpin family C member 1	Homo sapiens	42-54
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
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).	pentasaccharide	101-116	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).	pentasaccharide	101-116	serpin family C member 1	Homo sapiens	170-176
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
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
24735089-0	2014	Surface modification of polydimethylsiloxane with a covalent antithrombin-heparin complex to prevent thrombosis.	baysilon	24-44	serpin family C member 1	Homo sapiens	61-73
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
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.	baysilon	46-66	serpin family C member 1	Homo sapiens	95-107
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.	baysilon	68-72	serpin family C member 1	Homo sapiens	95-107
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
24735089-1	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.	Polyethylene Glycols	145-164	serpin family C member 1	Homo sapiens	95-107
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.	Polyethylene Glycols	166-169	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.	pentasaccharide	100-115	serpin family C member 1	Homo sapiens	51-63
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
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.	4-Hydroxy-trans-aconitic acid	41-44	serpin family C member 1	Homo sapiens	51-63
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
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
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
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.	Heparitin Sulfate	151-166	serpin family C member 1	Homo sapiens	14-26
23820940-8	2013	ETP ratios were higher in patients than in controls and were directly correlated with platelet counts and inversely with the plasma levels of free protein S, protein C and antithrombin.	etp	0-3	serpin family C member 1	Homo sapiens	172-184
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
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	212-224
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.	IC 831423	255-278	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.	IC 831423	255-278	serpin family C member 1	Homo sapiens	212-224
24068708-7	2013	These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role.	Tyrosine	189-192	serpin family C member 1	Homo sapiens	34-46
24068708-7	2013	These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role.	Tyrosine	189-192	serpin family C member 1	Homo sapiens	121-133
24068708-7	2013	These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role.	Alanine	201-204	serpin family C member 1	Homo sapiens	34-46
24068708-7	2013	These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role.	Alanine	201-204	serpin family C member 1	Homo sapiens	121-133
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
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.	Heparitin Sulfate	168-183	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
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.	Nitrogen	93-94	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
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
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.	Zinc	130-132	serpin family C member 1	Homo sapiens	63-75
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
24142738-0	2013	Pharmacokinetic and pharmacodynamic properties of batifiban coadministered with antithrombin agents in Chinese healthy volunteers.	batifiban	50-59	serpin family C member 1	Homo sapiens	80-92
24142738-2	2013	To observe whether antithrombin agents affect the pharmacokinetic and pharmacodynamic properties of batifiban in combination therapy and optimize clinical administration dosage of batifiban, an open-label and parallel study was conducted.	batifiban	100-109	serpin family C member 1	Homo sapiens	19-31
24142738-3	2013	Thirty healthy subjects were randomly divided into three groups, which were sequentially treated with batifiban alone, or oral coadministration of clopidogrel, aspirin and UFH, or batifiban coadministered with these antithrombin agents.	batifiban	180-189	serpin family C member 1	Homo sapiens	216-228
23911501-8	2013	This contributes to the better preservation of the ATIII pentasaccharide binding sequence, which results in a high Anti-Xa/Anti-IIa ratio (1.86).	pentasaccharide	57-72	serpin family C member 1	Homo sapiens	51-56
23843463-0	2013	Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties.	heparin dodecasaccharide	0-24	serpin family C member 1	Homo sapiens	40-52
23843463-0	2013	Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties.	pentasaccharides	61-77	serpin family C member 1	Homo sapiens	40-52
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
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)).	pentasaccharide	133-148	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)).	nac	168-171	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)).	glcua	176-181	serpin family C member 1	Homo sapiens	4-16
24074654-7	2013	CONCLUSIONS: Introduction of routine ATIII administration was associated with decreases in FFP, platelet, and PRBC exposure in neonates with CDH and decreases in PRBC transfusions in neonates without CDH during the first three days of ECMO support.	prbc	110-114	serpin family C member 1	Homo sapiens	37-42
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
23752481-0	2013	Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots.	mn-doped	97-105	serpin family C member 1	Homo sapiens	50-62
23752481-0	2013	Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots.	Zinc	106-109	serpin family C member 1	Homo sapiens	50-62
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
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.	aziridine	132-149	serpin family C member 1	Homo sapiens	82-94
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.	mn-doped	157-165	serpin family C member 1	Homo sapiens	82-94
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.	Zinc	166-169	serpin family C member 1	Homo sapiens	82-94
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.	pei-mn-zns	171-181	serpin family C member 1	Homo sapiens	82-94
23752481-0	2013	Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots.	aziridine	72-89	serpin family C member 1	Homo sapiens	50-62
24164039-2	2013	The methodology of an anti-factor Xa assay is that LMWH is added to a known amount of excess factor Xa and excess antithrombin.	Heparin, Low-Molecular-Weight	51-55	serpin family C member 1	Homo sapiens	114-126
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
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
23840401-8	2013	HOCl-altered isolated proteins antithrombin III and human serum albumin, taken as representative examples of the whole pool of plasma proteins, were both able to exert the same activity of binding to gp120 and inhibition of viral proliferation.	Hypochlorous Acid	0-4	serpin family C member 1	Homo sapiens	31-47
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
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
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
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
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
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
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
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
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
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
23581397-6	2013	METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain.	Diacetyl	56-71	serpin family C member 1	Homo sapiens	24-26
23581397-6	2013	METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain.	1,4-diselenophene-1,4-diketone	75-83	serpin family C member 1	Homo sapiens	24-26
23581397-6	2013	METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain.	Arginine	121-129	serpin family C member 1	Homo sapiens	24-26
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.	Diacetyl	23-34	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.	Diacetyl	23-34	serpin family C member 1	Homo sapiens	79-81
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
23581397-10	2013	CONCLUSIONS: AT-BD appears to be as efficient as protamine to neutralize UFH in vivo but could be more largely used because it also reverses fondaparinux and LMWH.	UFH	73-76	serpin family C member 1	Homo sapiens	13-15
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
23705025-5	2013	This validation study suggested LARGE, a gene encoding a protein with xylosyltransferase and glucuronyltransferase activities that forms heparin-like linear polysaccharides, as a potential modulator of antithrombin based on the significant association of one SNPs, rs762057, with anti-FXa activity, particularly after adjustment for age, sex and SERPINC1 rs2227589 genotype, all factors influencing antithrombin levels (p = 0.02).	Polysaccharides	157-172	serpin family C member 1	Homo sapiens	202-214
23705025-5	2013	This validation study suggested LARGE, a gene encoding a protein with xylosyltransferase and glucuronyltransferase activities that forms heparin-like linear polysaccharides, as a potential modulator of antithrombin based on the significant association of one SNPs, rs762057, with anti-FXa activity, particularly after adjustment for age, sex and SERPINC1 rs2227589 genotype, all factors influencing antithrombin levels (p = 0.02).	Polysaccharides	157-172	serpin family C member 1	Homo sapiens	346-354
23705025-5	2013	This validation study suggested LARGE, a gene encoding a protein with xylosyltransferase and glucuronyltransferase activities that forms heparin-like linear polysaccharides, as a potential modulator of antithrombin based on the significant association of one SNPs, rs762057, with anti-FXa activity, particularly after adjustment for age, sex and SERPINC1 rs2227589 genotype, all factors influencing antithrombin levels (p = 0.02).	Polysaccharides	157-172	serpin family C member 1	Homo sapiens	399-411
22978318-0	2013	Half-life prolongation of therapeutic proteins by conjugation to ATIII-binding pentasaccharides: a first-in-human study of CarboCarrier  insulin.	pentasaccharides	79-95	serpin family C member 1	Homo sapiens	65-70
22978318-1	2013	AIM: Conjugation to antithrombin III ATIII-binding pentasaccharides has been proposed as a novel method to extend the half-life of therapeutic proteins.	pentasaccharides	51-67	serpin family C member 1	Homo sapiens	37-42
22978318-12	2013	The elimination half-life of the molecule was clearly extended compared with endogenous insulin, indicating that conjugation to ATIII-binding pentasaccharides is a viable approach to extend the half-life of therapeutic proteins in humans.	pentasaccharides	142-158	serpin family C member 1	Homo sapiens	128-133
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
23016581-6	2013	The native form of antithrombin binds with high affinity to vascular heparan sulfate proteoglycans containing a specific pentasaccharide sequence and it is this cofactor interaction that activates antithrombin to maximal rate of thrombin inhibition.	pentasaccharide	121-136	serpin family C member 1	Homo sapiens	19-31
23016581-6	2013	The native form of antithrombin binds with high affinity to vascular heparan sulfate proteoglycans containing a specific pentasaccharide sequence and it is this cofactor interaction that activates antithrombin to maximal rate of thrombin inhibition.	pentasaccharide	121-136	serpin family C member 1	Homo sapiens	197-209
23016581-7	2013	Upon inhibitory complex formation with target proteinases the antithrombin undergoes stressed to relaxed transformation and lose their high affinity for pentasacchride.	pentasacchride	153-167	serpin family C member 1	Homo sapiens	62-74
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
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
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
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
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
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
23219177-12	2013	In conclusion, prasugrel, when given after bivalirudin as the intraprocedural antithrombin agent for patients with acute coronary syndrome undergoing PCI, is as safe and effective as clopidogrel.	Prasugrel Hydrochloride	15-24	serpin family C member 1	Homo sapiens	78-90
23329795-0	2013	Emerging applications of argatroban in the management of systemic malignancies: potential benefits besides its primary role as an antithrombin agent.	argatroban	25-35	serpin family C member 1	Homo sapiens	130-142
23083208-0	2013	An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence.	heparin octasaccharide	32-54	serpin family C member 1	Homo sapiens	11-23
23083208-0	2013	An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence.	glucosamine 3-O-sulfate	74-98	serpin family C member 1	Homo sapiens	11-23
23083208-0	2013	An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence.	pentasaccharide	113-128	serpin family C member 1	Homo sapiens	11-23
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.	n-sulfated glucosamine	21-43	serpin family C member 1	Homo sapiens	129-141
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
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.	Heparitin Sulfate	93-108	serpin family C member 1	Homo sapiens	129-141
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.	pentasaccharide	150-165	serpin family C member 1	Homo sapiens	129-141
23083208-4	2013	The molecular conformation of the octasaccharide-antithrombin complex has been determined by NMR experiments and docking/energy minimization.	Octasaccharide	34-48	serpin family C member 1	Homo sapiens	49-61
23083208-5	2013	The presence of the second 3-O-sulfated glucosamine in the octasaccharide induced more than one order of magnitude increase in affinity to antithrombin compared to the pentasaccharide AGA*IA.	glucosamine 3-O-sulfate	27-51	serpin family C member 1	Homo sapiens	139-151
23083208-5	2013	The presence of the second 3-O-sulfated glucosamine in the octasaccharide induced more than one order of magnitude increase in affinity to antithrombin compared to the pentasaccharide AGA*IA.	Octasaccharide	59-73	serpin family C member 1	Homo sapiens	139-151
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
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
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
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.	Polyurethanes	0-12	serpin family C member 1	Homo sapiens	30-42
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	274-277	serpin family C member 1	Homo sapiens	41-43
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	274-277	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	274-277	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	274-277	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	303-306	serpin family C member 1	Homo sapiens	41-43
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	303-306	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	303-306	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Arginine	303-306	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Serine	350-353	serpin family C member 1	Homo sapiens	41-43
23388336-4	2013	The cells were induced by IPTG to express AT-III.	Isopropyl Thiogalactoside	26-30	serpin family C member 1	Homo sapiens	42-48
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Serine	350-353	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Serine	350-353	serpin family C member 1	Homo sapiens	120-122
23578459-6	2013	RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T &gt; G or AT-c.134G &gt; A and c.342T &gt; G. Homology modeling showed that the mutation (AT-c.342T &gt; G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s.	Serine	350-353	serpin family C member 1	Homo sapiens	120-122
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
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
23010574-0	2012	Potentiation of anti-angiogenic activity of heparin by blocking the ATIII-interacting pentasaccharide unit and increasing net anionic charge.	pentasaccharide	86-101	serpin family C member 1	Homo sapiens	68-73
23010574-5	2012	This study showed that the conjugation of sodium taurocholates selectively blocked interaction with antithrombin III (ATIII) while enhancing the binding with VEGF.	Sodium	42-48	serpin family C member 1	Homo sapiens	100-116
23010574-5	2012	This study showed that the conjugation of sodium taurocholates selectively blocked interaction with antithrombin III (ATIII) while enhancing the binding with VEGF.	Sodium	42-48	serpin family C member 1	Homo sapiens	118-123
23010574-7	2012	Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding.	Taurocholic Acid	73-92	serpin family C member 1	Homo sapiens	178-183
23010574-7	2012	Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding.	Prednisolone	151-158	serpin family C member 1	Homo sapiens	178-183
23010574-7	2012	Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding.	pentasaccharide	192-207	serpin family C member 1	Homo sapiens	178-183
23010574-7	2012	Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding.	Heparin, Low-Molecular-Weight	216-220	serpin family C member 1	Homo sapiens	178-183
23010574-7	2012	Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding.	Sulfates	292-299	serpin family C member 1	Homo sapiens	178-183
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
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
22641607-0	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.	Polyethylene Glycols	63-81	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
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
22905983-9	2012	The molecular target for LMWH/ssLMWH was confirmed by supplementing FIX/antithrombin-depleted plasma with 90 nm recombinant FIX possessing mutations in the heparin-binding exosite.	Heparin, Low-Molecular-Weight	25-29	serpin family C member 1	Homo sapiens	72-84
22905983-9	2012	The molecular target for LMWH/ssLMWH was confirmed by supplementing FIX/antithrombin-depleted plasma with 90 nm recombinant FIX possessing mutations in the heparin-binding exosite.	sslmwh	30-36	serpin family C member 1	Homo sapiens	72-84
22905983-11	2012	CONCLUSIONS: Therapeutic LMWH concentrations inhibit plasma thrombin generation via antithrombin-independent interaction with the FIXa heparin-binding exosite.	Heparin, Low-Molecular-Weight	25-29	serpin family C member 1	Homo sapiens	84-96
22204993-7	2012	Antithrombin increased to the normal level on day 1 in the antithrombin group but on day 7 in the gabexate mesilate group.	Gabexate	98-115	serpin family C member 1	Homo sapiens	0-12
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
22819492-0	2012	Effect of antithrombin III on glycoprotein Ib/IX/V activation in human platelets: suppression of thromboxane A2 generation.	Thromboxane A2	97-111	serpin family C member 1	Homo sapiens	10-26
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
22535529-4	2012	Sequencing analysis of SERPINC1 gene of three families revealed that Family I had double novel missense mutations (c.134G &gt; A&amp;c.342T &gt; G), Family II had a nonsense mutation (c.770G &gt; A) while Family III had a frameshift mutation (c.800-803del).	Adenosine Monophosphate	129-132	serpin family C member 1	Homo sapiens	23-31
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
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.	Zinc	50-56	serpin family C member 1	Homo sapiens	167-179
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
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.	Zinc	90-96	serpin family C member 1	Homo sapiens	160-172
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
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
22758787-12	2012	The mutant antithrombin, with a molecular weight of 59 kDa, had a proteolytic cleavage at W49 but maintained the N-terminal disulphide bonds, and was conformationally sensitive.	disulphide	124-134	serpin family C member 1	Homo sapiens	11-23
22542983-9	2012	DISCUSSION: Tranexamic acid associated to direct anti-Xa (antithrombin-independent) oral anticoagulants was effective in reducing postoperative blood loss, improving hemoglobinemia at 5 days and reducing transfusion rates.	Tranexamic Acid	12-27	serpin family C member 1	Homo sapiens	58-70
22819492-2	2012	In the present study, we investigated the effect of antithrombin-III (AT-III), an anticoagulant, on the ristocetin-induced glycoprotein Ib/IX/V activation in human platelets.	Ristocetin	104-114	serpin family C member 1	Homo sapiens	52-68
22819492-2	2012	In the present study, we investigated the effect of antithrombin-III (AT-III), an anticoagulant, on the ristocetin-induced glycoprotein Ib/IX/V activation in human platelets.	Ristocetin	104-114	serpin family C member 1	Homo sapiens	70-76
22819492-3	2012	AT-III inhibited ristocetin-stimulated platelet aggregation.	Ristocetin	17-27	serpin family C member 1	Homo sapiens	0-6
22819492-4	2012	The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III.	Ristocetin	4-14	serpin family C member 1	Homo sapiens	138-144
22819492-4	2012	The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III.	11-dehydro-txb	37-51	serpin family C member 1	Homo sapiens	138-144
22819492-4	2012	The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III.	txa	79-82	serpin family C member 1	Homo sapiens	138-144
22819492-5	2012	AT-III also reduced the ristocetin-stimulated secretion of platelet-derived growth factor (PDGF)-AB.	Ristocetin	24-34	serpin family C member 1	Homo sapiens	0-6
22819492-7	2012	AT-III reduced the binding of SZ2, a monoclonal antibody to the sulfated sequence in the alpha-chain of glycoprotein Ib, to the ristocetin-stimulated platelets.	Ristocetin	128-138	serpin family C member 1	Homo sapiens	0-6
22819492-8	2012	These results strongly suggest that AT-III reduced ristocetin-stimulated release of sCD40 ligand due to inhibiting TXA(2) production in human platelets.	Ristocetin	51-61	serpin family C member 1	Homo sapiens	36-42
22819492-8	2012	These results strongly suggest that AT-III reduced ristocetin-stimulated release of sCD40 ligand due to inhibiting TXA(2) production in human platelets.	Thromboxane A2	115-121	serpin family C member 1	Homo sapiens	36-42
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.	Glycosaminoglycans	87-104	serpin family C member 1	Homo sapiens	127-139
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
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
22498748-11	2012	The presence of a fully functional beta-glycoform together with the activity retained by these variants helps to explain the viability of homozygous and the milder thrombotic risk of heterozygous patients with these specific antithrombin mutations.	glycoform	40-49	serpin family C member 1	Homo sapiens	225-237
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
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
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
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
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
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
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
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
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
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
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
22742452-3	2012	We screened a large database in silico to find alternative molecules and predicted d-myo-inositol 3,4,5,6-tetrakisphosphate (TMI) to strongly interact with antithrombin.	D-myo-inositol 3,4,5,6-tetrakisphosphate	83-123	serpin family C member 1	Homo sapiens	156-168
22742452-3	2012	We screened a large database in silico to find alternative molecules and predicted d-myo-inositol 3,4,5,6-tetrakisphosphate (TMI) to strongly interact with antithrombin.	4-tolyl isocyanate	125-128	serpin family C member 1	Homo sapiens	156-168
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.	4-tolyl isocyanate	88-91	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	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.	4-tolyl isocyanate	0-3	serpin family C member 1	Homo sapiens	13-25
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.	4-tolyl isocyanate	0-3	serpin family C member 1	Homo sapiens	86-98
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
22742452-7	2012	Our in silico screen identified a new, non-polysaccharide scaffold able to interact with the heparin binding domain of antithrombin.	Polysaccharides	43-57	serpin family C member 1	Homo sapiens	119-131
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
22481271-8	2012	Under moderate stress, coexpression of WT and conformational variants in HEK-EBNA cells increased the intracellular retention of antithrombin and the formation of disulfide-linked polymers, which correlated with impaired secretion and reduction of anticoagulant activity in the medium.	N-tert-Butyl-N-ethylnitrosamine	77-81	serpin family C member 1	Homo sapiens	129-141
22481271-8	2012	Under moderate stress, coexpression of WT and conformational variants in HEK-EBNA cells increased the intracellular retention of antithrombin and the formation of disulfide-linked polymers, which correlated with impaired secretion and reduction of anticoagulant activity in the medium.	Disulfides	163-172	serpin family C member 1	Homo sapiens	129-141
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
22534775-7	2012	However, the assay with the addition of exogenous antithrombin detected falsely high concentrations of rivaroxaban even in plasma samples from controls who had not taken rivaroxaban (intercept values using the high calibrator set and the low calibrator set: +26.49 ng/ml and +13.71 ng/ml, respectively).	Rivaroxaban	103-114	serpin family C member 1	Homo sapiens	50-62
22864323-1	2012	Warfarin sodium is an antithrombin agent used in patients with prosthetic valve and atrial fibrillation.	Warfarin	0-15	serpin family C member 1	Homo sapiens	22-34
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
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
22353523-9	2012	ATIII is correlated with 13 of 14 other clinical tests, including albumin, bilirubin, prothrombin time, rapid turnover proteins, HGF, ICGR15 and others.	Bilirubin	75-84	serpin family C member 1	Homo sapiens	0-5
21835782-9	2012	We also designed a synthetic path to prepare a nonasaccharide with an antithrombin-binding affinity of 3 nM.	Nonasaccharide Glc4Xyl3Gal2	47-61	serpin family C member 1	Homo sapiens	70-82
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
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.	Glycosaminoglycans	34-52	serpin family C member 1	Homo sapiens	66-78
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.	pentasaccharide	92-107	serpin family C member 1	Homo sapiens	66-78
22315264-9	2012	Fondaparinux, a synthetic pentasaccharide, catalyzes the inhibition of factor Xa, but not thrombin, in an antithrombin-dependent fashion.	pentasaccharide	26-41	serpin family C member 1	Homo sapiens	106-118
22149666-0	2012	Modification of polyurethane surface with an antithrombin-heparin complex for blood contact: influence of molecular weight of polyethylene oxide used as a linker/spacer.	Polyurethanes	16-28	serpin family C member 1	Homo sapiens	45-57
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
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.	N-hydroxysuccinimide	136-156	serpin family C member 1	Homo sapiens	3-15
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.	N-hydroxysuccinimide	158-161	serpin family C member 1	Homo sapiens	3-15
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
22161774-0	2012	Heparin-coated colloidal mesoporous silica nanoparticles efficiently bind to antithrombin as an anticoagulant drug-delivery system.	mesoporous	25-35	serpin family C member 1	Homo sapiens	77-89
22161774-0	2012	Heparin-coated colloidal mesoporous silica nanoparticles efficiently bind to antithrombin as an anticoagulant drug-delivery system.	Silicon Dioxide	36-42	serpin family C member 1	Homo sapiens	77-89
21819239-7	2012	In this review, the pharmacology of warfarin and the pharmacology of the newly developed oral anti-Xa and antithrombin agents are discussed.	Warfarin	36-44	serpin family C member 1	Homo sapiens	106-118
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
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
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.	pentasaccharide	145-160	serpin family C member 1	Homo sapiens	195-207
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.	pentasaccharide	250-265	serpin family C member 1	Homo sapiens	88-100
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.	pentasaccharide	250-265	serpin family C member 1	Homo sapiens	195-207
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
22149018-1	2012	OBJECTIVE: Recent findings suggest that cerebral edema is a characteristic finding on magnetic resonance imaging in women with eclampsia and that pregnancy-induced antithrombin deficiency (PIATD) may reflect enhanced vascular permeability and may allow the retention of excess water in the interstitial space.	Water	277-282	serpin family C member 1	Homo sapiens	164-176
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
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.	Heparitin Sulfate	37-52	serpin family C member 1	Homo sapiens	16-28
23152789-4	2012	The availability of multiple co-crystal structures facilitates a structural analysis that challenges the long-held belief that the GAG binding sites in antithrombin and thrombin are essentially similar with high solvent exposure and shallow surface characteristics.	Glycosaminoglycans	131-134	serpin family C member 1	Homo sapiens	152-164
23152789-9	2012	Cavity analyses suggest the presence of a reasonably sized bifurcated cavity in antithrombin that facilitates a firm "hand-shake" with H/HS, but with thrombin, a weaker "high-five".	Hydrogen	137-139	serpin family C member 1	Homo sapiens	80-92
23152789-10	2012	Tightly bound water molecules were predicted to be localized in the pentasaccharide binding pocket of antithrombin, but absent in thrombin.	Water	14-19	serpin family C member 1	Homo sapiens	102-114
23152789-10	2012	Tightly bound water molecules were predicted to be localized in the pentasaccharide binding pocket of antithrombin, but absent in thrombin.	pentasaccharide	68-83	serpin family C member 1	Homo sapiens	102-114
22900053-6	2012	However, concomitant administration of an antithrombin activator or direct factor Xa inhibitor and direct thrombin inhibitor proved to be a particularly effective combination for controlling the procoagulant effects of hALPCs both in vitro and in vivo.	halpcs	219-225	serpin family C member 1	Homo sapiens	42-54
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
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
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
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
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
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
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
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
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
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
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
21325262-5	2011	Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys).	Cytosine	115-123	serpin family C member 1	Homo sapiens	25-33
21325262-5	2011	Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys).	Cytosine	115-123	serpin family C member 1	Homo sapiens	192-200
21325262-5	2011	Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys).	Thymine	127-134	serpin family C member 1	Homo sapiens	25-33
21325262-5	2011	Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys).	Thymine	127-134	serpin family C member 1	Homo sapiens	192-200
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
21799398-0	2011	Peroperative effects of fresh frozen plasma and antithrombin III on heparin sensitivity and coagulation during nitroglycerine infusion in coronary artery bypass surgery.	Nitroglycerin	111-125	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
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
21799398-9	2011	ATIII administration increases heparin sensitivity and decreases heparin requirements compared with FFP in patients undergoing CABGS with peroperative NTG infusion.	Nitroglycerin	151-154	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
21799398-10	2011	ATIII may be preferred to FFP in patients with heparin resistance due to NTG infusion undergoing CABGS.	Nitroglycerin	73-76	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.	Hydrogen	14-22	serpin family C member 1	Homo sapiens	126-138
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
21875153-4	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.	Hydrogen	116-124	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
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.	Arginine	131-134	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.	Arginine	142-145	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.	Hydrogen	163-171	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
21875153-5	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.	Lysine	225-228	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.	Lysine	236-239	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.	Hydrogen	254-262	serpin family C member 1	Homo sapiens	54-59
21875153-6	2011	In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions.	pentasaccharide	35-50	serpin family C member 1	Homo sapiens	22-34
21875153-6	2011	In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions.	Lysine	59-62	serpin family C member 1	Homo sapiens	22-34
21875153-6	2011	In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions.	Proline	68-71	serpin family C member 1	Homo sapiens	22-34
21875153-6	2011	In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions.	Lysine	79-82	serpin family C member 1	Homo sapiens	22-34
21875153-6	2011	In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions.	Hydrogen	102-110	serpin family C member 1	Homo sapiens	22-34
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
22097175-12	2011	Urinary excretion of Hcy significantly increases, in comparison to control, and correlates with serum AT III level.	Homocysteine	21-24	serpin family C member 1	Homo sapiens	102-108
21866963-3	2011	The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2).	cdse	60-64	serpin family C member 1	Homo sapiens	23-35
21866963-3	2011	The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2).	Zinc	65-68	serpin family C member 1	Homo sapiens	23-35
21866963-3	2011	The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2).	Adenosine Triphosphate	139-142	serpin family C member 1	Homo sapiens	23-35
21866963-3	2011	The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2).	Adenosine Triphosphate	139-142	serpin family C member 1	Homo sapiens	23-35
21866963-3	2011	The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2).	Luminol	377-384	serpin family C member 1	Homo sapiens	23-35
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.	asn135-linked oligosaccharide	14-43	serpin family C member 1	Homo sapiens	64-66
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.	asn135-linked oligosaccharide	14-43	serpin family C member 1	Homo sapiens	176-178
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
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
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.	Polysaccharides	96-110	serpin family C member 1	Homo sapiens	64-66
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
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.	Polysaccharides	146-152	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.	Polysaccharides	146-152	serpin family C member 1	Homo sapiens	188-190
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
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
21751805-1	2011	The observed salt dependence of charged ligand binding to polyelectrolytes, such as proteins to DNA or antithrombin to heparin, is often interpreted by means of the "oligolysine model."	Salts	13-17	serpin family C member 1	Homo sapiens	103-115
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
21866614-20	2004	UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide.	Glycosaminoglycans	34-52	serpin family C member 1	Homo sapiens	87-103
21866614-20	2004	UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide.	pentasaccharide	112-127	serpin family C member 1	Homo sapiens	87-103
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.	Parathion	11-16	serpin family C member 1	Homo sapiens	106-122
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
21297450-1	2011	The effect of protamine sulfate on factor Xa (FXa) and the factor Xa-antithrombin complex was studied via SDS-PAGE and Western blot analysis.	Sodium Dodecyl Sulfate	106-109	serpin family C member 1	Homo sapiens	69-81
21655672-8	2011	The AT assay dependent on thrombin activity was not influenced by rivaroxaban, whereas the AT levels dependent on factor Xa activity were significantly increased by rivaroxaban.	Rivaroxaban	165-176	serpin family C member 1	Homo sapiens	91-93
21655682-0	2011	Massive muscle haematoma three months after starting vitamin K antagonist therapy for deep-vein thrombosis in an antithrombin deficient patient: another case of factor IX propeptide mutation.	Vitamin K	53-62	serpin family C member 1	Homo sapiens	113-125
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.	Sodium Dodecyl Sulfate	31-53	serpin family C member 1	Homo sapiens	0-12
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.	Sodium Dodecyl Sulfate	55-58	serpin family C member 1	Homo sapiens	0-12
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
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.	Tryptophan	255-265	serpin family C member 1	Homo sapiens	0-12
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.	pentasaccharide	89-104	serpin family C member 1	Homo sapiens	0-12
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
21297455-0	2011	Functionality of fondaparinux (pentasaccharide) depends on clinical antithrombin levels.	pentasaccharide	31-46	serpin family C member 1	Homo sapiens	68-80
21297455-1	2011	Fondaparinux (Arixtra) is an antithrombin (AT)-dependent synthetic inhibitor of factor Xa (FXa).	Fondaparinux	0-12	serpin family C member 1	Homo sapiens	29-41
21297455-5	2011	For 0.2-1.5 mug/ml fondaparinux (plasma concentrations achieved with dosages for prophylaxis and treatment of venous thromboembolism) and AT levels of 0.5 U/ml there was 20% loss of activity and with 0.25 U/ml AT there was a 45% loss of activity compared to 1 U/ml AT.	Fondaparinux	19-31	serpin family C member 1	Homo sapiens	210-212
21297455-5	2011	For 0.2-1.5 mug/ml fondaparinux (plasma concentrations achieved with dosages for prophylaxis and treatment of venous thromboembolism) and AT levels of 0.5 U/ml there was 20% loss of activity and with 0.25 U/ml AT there was a 45% loss of activity compared to 1 U/ml AT.	Fondaparinux	19-31	serpin family C member 1	Homo sapiens	210-212
21297455-10	2011	With AT levels below 30% of normal induced by anti-AT antibodies, there was a 60% in-vivo reduction in the antithrombotic activity of fondaparinux (ED50 75 vs. 240 mug/kg).	Fondaparinux	134-146	serpin family C member 1	Homo sapiens	5-7
21297455-10	2011	With AT levels below 30% of normal induced by anti-AT antibodies, there was a 60% in-vivo reduction in the antithrombotic activity of fondaparinux (ED50 75 vs. 240 mug/kg).	Fondaparinux	134-146	serpin family C member 1	Homo sapiens	51-53
21297455-1	2011	Fondaparinux (Arixtra) is an antithrombin (AT)-dependent synthetic inhibitor of factor Xa (FXa).	Fondaparinux	14-21	serpin family C member 1	Homo sapiens	29-41
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.	Calcium	58-65	serpin family C member 1	Homo sapiens	191-203
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
21138266-6	2011	The following structure-activity relationships were found: 3-O-rutinosides (10, 13) were direct inhibitors of FXa, while 7-O-rutinosides (7, 8) showed inhibition of FXa by ATIII activation.	7-o-rutinosides	121-136	serpin family C member 1	Homo sapiens	172-177
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
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
20557984-0	2011	[Antithrombin homozygous type II HBS deficiency (99Leu-Phe) associated with recurrent arterial thrombosis].	99leu-phe	49-58	serpin family C member 1	Homo sapiens	1-13
21103660-3	2011	Dabigatran was added to plasma from healthy subjects in the concentration range 0-1,000 mug/l and analysed using several reagents for activated thromboplastin time (APTT), prothrombin time (PT), fibrinogen, antithrombin, and activated protein C resistance.	Dabigatran	0-10	serpin family C member 1	Homo sapiens	207-219
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
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
21028827-0	2010	Effects on molecular conformation and anticoagulant activities of 1,6-anhydrosugars at the reducing terminal of antithrombin-binding octasaccharides isolated from low-molecular-weight heparin enoxaparin.	1,6-anhydrosugars	66-83	serpin family C member 1	Homo sapiens	112-124
20946166-4	2011	MATERIALS AND METHODS: Rivaroxaban was added to plasma from healthy subjects in the concentration range 0-1000 mug L(-1) and analyzed using different reagents for activated partial thromboplastin time (APTT), prothrombin time (PT), antithrombin, fibrinogen and activated protein C (APC) resistance assays.	Rivaroxaban	23-34	serpin family C member 1	Homo sapiens	232-244
21568083-7	2011	RESULTS: Short-term use (3 months) of both tibolone and CCHT had a detrimental effect on antithrombin, protein C and protein S levels (decreased), and even more so in the group treated with CCHT.	tibolone	43-51	serpin family C member 1	Homo sapiens	89-101
21568083-7	2011	RESULTS: Short-term use (3 months) of both tibolone and CCHT had a detrimental effect on antithrombin, protein C and protein S levels (decreased), and even more so in the group treated with CCHT.	ccht	56-60	serpin family C member 1	Homo sapiens	89-101
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
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
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.	pentasaccharide	80-95	serpin family C member 1	Homo sapiens	12-24
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
20816747-1	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.	heparan sulfate glycosaminoglycans	115-149	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.	pentasaccharide	51-66	serpin family C member 1	Homo sapiens	153-165
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
20816747-3	2010	Here we present kinetic evidence for similar induced-fit mechanisms of pentasaccharide binding to native and latent antithrombins and kinetic simulations which together support a three-step mechanism of allosteric activation of native antithrombin involving two successive conformational changes.	pentasaccharide	71-86	serpin family C member 1	Homo sapiens	116-128
20816747-5	2010	The observation that variant antithrombins that cannot undergo the second conformational change bind the pentasaccharide like latent antithrombin and are partially activated suggests that both conformational changes contribute to allosteric activation, in agreement with a recently proposed model of allosteric activation.	pentasaccharide	105-120	serpin family C member 1	Homo sapiens	29-41
19825921-4	2010	Fondaparinux is a synthetic pentasaccharide that binds to antithrombin and potentiates inhibition of factor Xa.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	58-70
21028827-0	2010	Effects on molecular conformation and anticoagulant activities of 1,6-anhydrosugars at the reducing terminal of antithrombin-binding octasaccharides isolated from low-molecular-weight heparin enoxaparin.	octasaccharides	133-148	serpin family C member 1	Homo sapiens	112-124
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
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
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.	Heparitin Sulfate	67-82	serpin family C member 1	Homo sapiens	12-24
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
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.	heparan sulfate pentasaccharide	33-64	serpin family C member 1	Homo sapiens	68-80
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
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
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
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
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
21572750-9	2010	Idrabiotaparinux is an indirect inhibitor of Xa as it accelerates the activity of antithrombin.	idrabiotaparinux	0-16	serpin family C member 1	Homo sapiens	82-94
20660032-10	2010	Mean serum Ca and P significantly increased compared to baseline, whereas serum Mg decreased at 3 d.	Magnesium	80-82	serpin family C member 1	Homo sapiens	93-99
20660032-11	2010	1,25-Dihydroxyvitamin D significantly increased from 46.8 +- 18.9 to 97.8 +- 38.3 pg/ml at 3 d (P &lt; 0.001) and to 59.5 +- 27.3 pg/ml at 60 d (P &lt; 0.05).	1,25-dihydroxyvitamin D	0-23	serpin family C member 1	Homo sapiens	88-94
21507819-1	2010	UNLABELLED: Fondaparinux, a pentasaccharide which selectively binds to antithrombin III, has negligible to no cross-reactivity with heparin-induced thrombocytopenia (HIT) antibodies in in vitro studies.	Fondaparinux	12-24	serpin family C member 1	Homo sapiens	71-87
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).	danaparoid	54-64	serpin family C member 1	Homo sapiens	145-157
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).	Fondaparinux	66-78	serpin family C member 1	Homo sapiens	145-157
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
20443661-1	2010	OBJECTIVE: This retrospective study was performed to characterize the laboratory features and water metabolism of women with pregnancy-induced antithrombin deficiency (PIATD).	Water	94-99	serpin family C member 1	Homo sapiens	143-155
21507819-1	2010	UNLABELLED: Fondaparinux, a pentasaccharide which selectively binds to antithrombin III, has negligible to no cross-reactivity with heparin-induced thrombocytopenia (HIT) antibodies in in vitro studies.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	71-87
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
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
20531960-6	2010	The anti-Xa agent rivaroxaban and the antithrombin agent dabigatran are already available for the prophylaxis of venous thromboembolism in some countries.	Dabigatran	57-67	serpin family C member 1	Homo sapiens	38-50
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
22282689-2	2010	This antithrombotic and antithrombin activity is of great pharmacologic interest and makes sulodexide a suitable drug for the prophylaxis and treatment of arterial and venous peripheral diseases.	glucuronyl glucosamine glycan sulfate	91-101	serpin family C member 1	Homo sapiens	24-36
20184328-0	2010	Inhibitory properties of the P1 Tyr variant of antithrombin.	Tyrosine	32-35	serpin family C member 1	Homo sapiens	47-59
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
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
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
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
20014840-6	2010	The three oxidation states present in the range of water stability are At(-I), At(+I), and At(+III) and exist as At(-), At(+), and AtO(+), respectively, in the 1-2 pH range.	Water	51-56	serpin family C member 1	Homo sapiens	91-98
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
19805567-5	2010	We report on the development of long-lasting enfuvirtide conjugates by the use of the site-specific conjugation of enfuvirtide to an antithrombin-binding carrier pentasaccharide (CP) through polyethylene glycol (PEG) linkers of various lengths.	pentasaccharide	162-177	serpin family C member 1	Homo sapiens	133-145
19805567-5	2010	We report on the development of long-lasting enfuvirtide conjugates by the use of the site-specific conjugation of enfuvirtide to an antithrombin-binding carrier pentasaccharide (CP) through polyethylene glycol (PEG) linkers of various lengths.	Polyethylene Glycols	191-210	serpin family C member 1	Homo sapiens	133-145
19805567-5	2010	We report on the development of long-lasting enfuvirtide conjugates by the use of the site-specific conjugation of enfuvirtide to an antithrombin-binding carrier pentasaccharide (CP) through polyethylene glycol (PEG) linkers of various lengths.	Polyethylene Glycols	212-215	serpin family C member 1	Homo sapiens	133-145
22111528-1	2010	Idraparinux is a polymethylated synthetic pentasaccharide that binds to antithrombin with high affinity.	idraparinux	0-11	serpin family C member 1	Homo sapiens	72-84
22111528-1	2010	Idraparinux is a polymethylated synthetic pentasaccharide that binds to antithrombin with high affinity.	synthetic pentasaccharide	32-57	serpin family C member 1	Homo sapiens	72-84
22282689-1	2010	Sulodexide is a highly purified glycosaminoglycan containing a combination of heparan sulfate with affinity for antithrombin III and dermatan sulfate with affinity for heparin cofactor II.	glucuronyl glucosamine glycan sulfate	0-10	serpin family C member 1	Homo sapiens	112-128
20229677-11	2010	One case (0.62%) of DVT propagation into the vena cava occurred in a woman with antithrombin deficiency treated with LMWH.	Heparin, Low-Molecular-Weight	117-121	serpin family C member 1	Homo sapiens	80-92
19899825-5	2010	Additionally, we characterized alterations in the glycan structures of vitronectin (Asn-169, 242) and antithrombin III (Asn-225) that were identified in HCC patient plasma.	Asparagine	120-123	serpin family C member 1	Homo sapiens	102-118
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
19715676-0	2009	Role of P2 glycine in determining the specificity of antithrombin reaction with coagulation proteases.	Glycine	11-18	serpin family C member 1	Homo sapiens	53-65
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
19967150-9	2009	Similar to heparin, the ability of sulfated galactan to potentiate FXa inhibition by antithrombin is calcium-dependent.	Calcium	101-108	serpin family C member 1	Homo sapiens	85-97
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
19818773-1	2009	Allosteric activation of antithrombin as a rapid inhibitor of factors IXa and Xa requires binding of a high-affinity heparin pentasaccharide.	IC 831423	117-140	serpin family C member 1	Homo sapiens	25-37
19818773-2	2009	The currently-accepted mechanism involves removal of a constraint on the antithrombin reactive center loop (RCL) so that the proteinase can simultaneously engage both the P1 arginine and an exosite at Y253.	Arginine	174-182	serpin family C member 1	Homo sapiens	73-85
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
19843180-3	2009	We have evaluated the functional and conformational effects on antithrombin of citrullination, a post-translational modification catalyzed by peptidylarginine deiminase (PAD), which changes arginine to citrulline.	Arginine	150-158	serpin family C member 1	Homo sapiens	63-75
19843180-3	2009	We have evaluated the functional and conformational effects on antithrombin of citrullination, a post-translational modification catalyzed by peptidylarginine deiminase (PAD), which changes arginine to citrulline.	Citrulline	202-212	serpin family C member 1	Homo sapiens	63-75
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
19573895-5	2009	We incubated in vitro plasma and purified antithrombin and human hepatoma cells (HepG2) with methyl-glyoxal and glucose.	Pyruvaldehyde	93-107	serpin family C member 1	Homo sapiens	42-54
19837548-1	2009	We present the case of a 73-year-old man, operated on for paralyzing sciatica, who displayed acute postoperative respiratory distress and intra-alveolar haemorrhage following the administration of dabigatran etexilate, a new oral antithrombin used in the prevention of venous thromboembolism.	Dabigatran	197-217	serpin family C member 1	Homo sapiens	230-242
19631608-0	2009	Antithrombin III suppresses ADP-induced platelet granule secretion: inhibition of HSP27 phosphorylation.	Adenosine Diphosphate	28-31	serpin family C member 1	Homo sapiens	0-16
19631608-4	2009	In the present study, we investigated the relationship between AT-III and the ADP-induced platelet granule secretion.	Adenosine Diphosphate	78-81	serpin family C member 1	Homo sapiens	63-69
19631608-5	2009	The ADP-induced secretion of platelet-derived growth factor (PDGF)-AB and serotonin (5-HT) were significantly suppressed by AT-III.	Adenosine Diphosphate	4-7	serpin family C member 1	Homo sapiens	124-130
19631608-5	2009	The ADP-induced secretion of platelet-derived growth factor (PDGF)-AB and serotonin (5-HT) were significantly suppressed by AT-III.	Serotonin	74-83	serpin family C member 1	Homo sapiens	124-130
19631608-8	2009	AT-III markedly attenuated the ADP-induced phosphorylation levels of p44/p42 MAPK and p38 MAPK.	Adenosine Diphosphate	31-34	serpin family C member 1	Homo sapiens	0-6
19631608-9	2009	Furthermore, the ADP-induced HSP27 phosphorylation was suppressed by AT-III.	Adenosine Diphosphate	17-20	serpin family C member 1	Homo sapiens	69-75
19631608-10	2009	These results strongly suggest that AT-III directly acts on platelets and suppresses ADP-induced platelet granule secretion due to inhibiting HSP27 phosphorylation via p44/p42 MAPK and p38 MAPK.	Adenosine Diphosphate	85-88	serpin family C member 1	Homo sapiens	36-42
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
19888512-2	2009	De novo chemical synthesis of the corresponding pentasaccharide as well as simplified analogues has provided very specific, antithrombin-mediated inhibitors of factor Xa with various pharmacokinetic profiles.	pentasaccharide	48-63	serpin family C member 1	Homo sapiens	124-136
19888512-4	2009	Because of the very specific binding to antithrombin the pharmacokinetics of pentasaccharides can be predicted and transferred to other molecules covalently bound to them.	pentasaccharides	77-93	serpin family C member 1	Homo sapiens	40-52
19888516-7	2009	The fucosylated chondroitin sulfate inhibits thrombin by heparin cofactor II, whereas sulfated fucan inhibits thrombin by both antithrombin and heparin cofactor II.	fucan	95-100	serpin family C member 1	Homo sapiens	127-139
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
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
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
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.	heparan sulfate glycosaminoglycans	12-46	serpin family C member 1	Homo sapiens	83-95
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.	pentasaccharide	127-142	serpin family C member 1	Homo sapiens	83-95
19661062-2	2009	To elucidate the role of the 3-O-sulfo group in the activation mechanism, we compared the effects of deleting the 3-O-sulfo group or mutating the Lys(114) binding partner of this group on antithrombin-pentasaccharide interactions by equilibrium binding and rapid kinetic analyses.	pentasaccharide	201-216	serpin family C member 1	Homo sapiens	188-200
19661062-3	2009	Binding studies over a wide range of ionic strength and pH showed that loss of the 3-O-sulfo group caused a massive approximately 60% loss in binding energy for the antithrombin-pentasaccharide interaction due to the disruption of a cooperative network of ionic and nonionic interactions.	3-o-sulfo	83-92	serpin family C member 1	Homo sapiens	165-177
19661062-3	2009	Binding studies over a wide range of ionic strength and pH showed that loss of the 3-O-sulfo group caused a massive approximately 60% loss in binding energy for the antithrombin-pentasaccharide interaction due to the disruption of a cooperative network of ionic and nonionic interactions.	pentasaccharide	178-193	serpin family C member 1	Homo sapiens	165-177
19661062-4	2009	Despite this affinity loss, the 3-O-desulfonated pentasaccharide retained the ability to induce tryptophan fluorescence changes and to enhance factor Xa reactivity in antithrombin, indicative of normal conformational activation.	3-o-desulfonated pentasaccharide	32-64	serpin family C member 1	Homo sapiens	167-179
19661062-5	2009	Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin.	Parathion	50-55	serpin family C member 1	Homo sapiens	131-143
19661062-5	2009	Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin.	Parathion	50-55	serpin family C member 1	Homo sapiens	207-219
19661062-5	2009	Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin.	pentasaccharide	95-110	serpin family C member 1	Homo sapiens	131-143
19661062-5	2009	Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin.	pentasaccharide	95-110	serpin family C member 1	Homo sapiens	207-219
19661062-6	2009	By contrast, mutation of Lys(114) solely affected the preferential interaction of the pentasaccharide with activated antithrombin.	Lysine	25-28	serpin family C member 1	Homo sapiens	117-129
19661062-6	2009	By contrast, mutation of Lys(114) solely affected the preferential interaction of the pentasaccharide with activated antithrombin.	pentasaccharide	86-101	serpin family C member 1	Homo sapiens	117-129
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	3-o-sulfo	36-45	serpin family C member 1	Homo sapiens	124-136
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	3-o-sulfo	36-45	serpin family C member 1	Homo sapiens	208-220
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	3-o-sulfo	36-45	serpin family C member 1	Homo sapiens	208-220
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	IC 831423	86-109	serpin family C member 1	Homo sapiens	124-136
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	IC 831423	86-109	serpin family C member 1	Homo sapiens	208-220
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	IC 831423	86-109	serpin family C member 1	Homo sapiens	208-220
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	Lysine	165-168	serpin family C member 1	Homo sapiens	124-136
19661062-7	2009	These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state.	Lysine	241-244	serpin family C member 1	Homo sapiens	124-136
19414859-1	2009	Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chondroitin sulfate with antithrombin-independent antithrombotic properties.	holothurian glycosaminoglycan	14-43	serpin family C member 1	Homo sapiens	92-104
19414859-1	2009	Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chondroitin sulfate with antithrombin-independent antithrombotic properties.	dhg	45-48	serpin family C member 1	Homo sapiens	92-104
19414859-1	2009	Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chondroitin sulfate with antithrombin-independent antithrombotic properties.	Chondroitin Sulfates	67-86	serpin family C member 1	Homo sapiens	92-104
19861246-10	2009	CONCLUSION: DHPLC allows automated and rapid high-throughput detection of AT- III gene mutation and polymorphisms in the clinical setting and prenatal diagnosis.	dhplc	12-17	serpin family C member 1	Homo sapiens	74-81
19573895-5	2009	We incubated in vitro plasma and purified antithrombin and human hepatoma cells (HepG2) with methyl-glyoxal and glucose.	Glucose	112-119	serpin family C member 1	Homo sapiens	42-54
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
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
19172319-5	2009	However, detailed comparison of our modeled structure of ZPI/FXa with that of AT3/FXa points to differences in interaction specificity at the reactive center and in the stability of the inhibitory complex, due to the presence of a tyrosine residue at the P1 position in ZPI, instead of the P1 arginine residue in AT3.	Tyrosine	231-239	serpin family C member 1	Homo sapiens	78-81
19389385-5	2009	While oversulfated chondroitin sulfate binds tightly to antithrombin III, unlike heparin, OSCS does not induce antithrombin III to undergo the conformational change required for its inactivation of thrombin and factor Xa.	Chondroitin Sulfates	19-38	serpin family C member 1	Homo sapiens	56-72
19172319-5	2009	However, detailed comparison of our modeled structure of ZPI/FXa with that of AT3/FXa points to differences in interaction specificity at the reactive center and in the stability of the inhibitory complex, due to the presence of a tyrosine residue at the P1 position in ZPI, instead of the P1 arginine residue in AT3.	Arginine	293-301	serpin family C member 1	Homo sapiens	78-81
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
19497853-0	2009	Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function.	Lignin	64-71	serpin family C member 1	Homo sapiens	15-27
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
19690236-3	2009	RESULTS: Heptest clotting time was shorter at any given fondaparinux concentration in the antithrombin-deficient samples, indicating less anticoagulant effect than in the group with normal antithrombin levels.	Fondaparinux	56-68	serpin family C member 1	Homo sapiens	90-102
19690236-9	2009	Higher levels of antithrombin lead to an exaggerated effect of fondaparinux on Heptest.	Fondaparinux	63-75	serpin family C member 1	Homo sapiens	17-29
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
19497853-0	2009	Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function.	Lignin	64-71	serpin family C member 1	Homo sapiens	123-135
19497853-1	2009	Antithrombin, a major regulator of coagulation and angiogenesis, is known to interact with several natural sulfated polysaccharides.	Polysaccharides	116-131	serpin family C member 1	Homo sapiens	0-12
19497853-6	2009	Fluorescence binding studies indicate that sulfated DHPs bind to antithrombin with micromolar affinity under physiological conditions.	dhps	52-56	serpin family C member 1	Homo sapiens	65-77
19497853-7	2009	Salt dependence of binding affinity indicates that the antithrombin-sulfated DHP interaction involves a massive 80-87% non-ionic component to the free energy of binding.	Salts	0-4	serpin family C member 1	Homo sapiens	55-67
19497853-8	2009	Competitive binding studies with heparin pentasaccharide, epicatechin sulfate, and full-length heparin indicate that sulfated DHPs bind to both the pentasaccharide-binding site and extended heparin-binding site of antithrombin.	IC 831423	33-56	serpin family C member 1	Homo sapiens	214-226
19497853-8	2009	Competitive binding studies with heparin pentasaccharide, epicatechin sulfate, and full-length heparin indicate that sulfated DHPs bind to both the pentasaccharide-binding site and extended heparin-binding site of antithrombin.	dhps	126-130	serpin family C member 1	Homo sapiens	214-226
19497853-11	2009	Enzyme inhibition studies indicate that only one of the three sulfated DHPs studied is a potent inhibitor of free factor VIIa in the presence of antithrombin.	dhps	71-75	serpin family C member 1	Homo sapiens	145-157
19497853-12	2009	Overall, the chemo-enzymatic origin and antithrombin binding properties of sulfated DHPs present novel opportunities for potent and selective modulation of the serpin function, especially for inhibiting the initiation phase of hemostasis.	dhps	84-88	serpin family C member 1	Homo sapiens	40-52
19386495-1	2009	An efficient [DEF+GH] route was developed to the synthesis of Idraparinux, which is a fully O-sulfated, O-methylated mimic of the unique Antithrombin III binding domain of heparin.	idraparinux	62-73	serpin family C member 1	Homo sapiens	137-153
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
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.	Polysaccharides	66-72	serpin family C member 1	Homo sapiens	172-188
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.	Polysaccharides	189-195	serpin family C member 1	Homo sapiens	172-188
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
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
19422445-0	2009	Dexamethasone induces a heat-stress response that ameliorates the conformational consequences on antithrombin of L-asparaginase treatment.	Dexamethasone	0-13	serpin family C member 1	Homo sapiens	97-109
19422445-3	2009	OBJECTIVES: We have investigated the effect of two corticoids, dexamethasone and prednisone, on the conformational consequences of L-ASP treatment on antithrombin.	Dexamethasone	63-76	serpin family C member 1	Homo sapiens	150-162
19422445-6	2009	RESULTS: In all models, L-ASP alone or in combination with prednisone caused the intracellular retention of antithrombin associated with a severe deficiency.	Prednisone	59-69	serpin family C member 1	Homo sapiens	108-120
19422445-8	2009	CONCLUSIONS: These results suggest a protective effect of dexamethasone on the conformational consequences of L-ASP on antithrombin as a result of exacerbated HSR and UPR that help to explain the reduced risk of thrombosis reported in patients that follow this scheme of treatment.	Dexamethasone	58-71	serpin family C member 1	Homo sapiens	119-131
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.	Glucuronic Acid	0-13	serpin family C member 1	Homo sapiens	70-82
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.	Iduronic Acid	18-29	serpin family C member 1	Homo sapiens	70-82
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.	Disaccharides	41-54	serpin family C member 1	Homo sapiens	70-82
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.	pentasaccharide	91-106	serpin family C member 1	Homo sapiens	70-82
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
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.	sulfate esters	139-153	serpin family C member 1	Homo sapiens	70-82
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.	sodium sulfonatomethyl	186-208	serpin family C member 1	Homo sapiens	70-82
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
18996625-5	2009	Activator IAS(5) containing 5,6-disulfated tetrahydroisoquinoline and 3,4,5-trisulfated phenyl rings was found to bind antithrombin at pH 7.4 with an affinity comparable to the reference trisaccharide DEF.	5,6-disulfated tetrahydroisoquinoline	28-65	serpin family C member 1	Homo sapiens	119-131
18996625-5	2009	Activator IAS(5) containing 5,6-disulfated tetrahydroisoquinoline and 3,4,5-trisulfated phenyl rings was found to bind antithrombin at pH 7.4 with an affinity comparable to the reference trisaccharide DEF.	3,4,5-trisulfated	70-87	serpin family C member 1	Homo sapiens	119-131
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
19425011-0	2009	Capillary electrophoretic study of small, highly sulfated, non-sugar molecules interacting with antithrombin.	Sugars	63-68	serpin family C member 1	Homo sapiens	96-108
19425011-3	2009	Scatchard analysis of the interaction of three tetrahydroisoquinoline-based polysulfated molecules with AT results in monophasic profiles with affinities in the range of 40-60 microM in 20 mM sodium phosphate buffer, pH 7.4.	1,2,3,4-tetrahydroisoquinoline	47-69	serpin family C member 1	Homo sapiens	104-106
19425011-3	2009	Scatchard analysis of the interaction of three tetrahydroisoquinoline-based polysulfated molecules with AT results in monophasic profiles with affinities in the range of 40-60 microM in 20 mM sodium phosphate buffer, pH 7.4.	sodium phosphate	192-208	serpin family C member 1	Homo sapiens	104-106
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
19320820-9	2009	CONCLUSIONS: The interaction of AT with syndecan-4 is required for its prostacyclin-dependent protective effect through a PTX-sensitive and non-S1P(1)-related G(i)-protein coupled receptor.	Epoprostenol	71-83	serpin family C member 1	Homo sapiens	32-34
19275167-1	2009	The recently arising antithrombin drug, angiomax, was successfully conjugated with a 5"-amino oligonucleotide through click chemistry.	5"-amino oligonucleotide	85-109	serpin family C member 1	Homo sapiens	21-33
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.	3-o	16-19	serpin family C member 1	Homo sapiens	107-123
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.	sulfated	20-28	serpin family C member 1	Homo sapiens	107-123
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.	Glucosamine	29-40	serpin family C member 1	Homo sapiens	107-123
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
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.	Heparitin Sulfate	64-79	serpin family C member 1	Homo sapiens	107-123
19327165-5	2009	RESULTS: Upon normalization of serum testosterone there was an improvement of hyperglycemia, a decrease of leukocytes and of fibrinogen levels, an increase of antithrombin III activity and of tissue oxygen pressure.	Testosterone	37-49	serpin family C member 1	Homo sapiens	159-175
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
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
19049827-1	2009	Antithrombin was purified from Bothrops jararaca plasma by affinity chromatography using HiTrap Heparin HP column, and its molecular weight, amino-terminal sequence, carbohydrate content, isoelectric point, inhibition of bovine thrombin, and immunological properties were studied and compared with previously described antithrombins.	Carbohydrates	166-178	serpin family C member 1	Homo sapiens	0-12
19049827-2	2009	B. jararaca antithrombin is a single-chain glycoprotein with a total carbohydrate content of 18%.	Carbohydrates	69-81	serpin family C member 1	Homo sapiens	12-24
19170587-4	2009	Rivaroxaban is a small molecule directed at active sites, and the agent mechanistically differs from traditional anticoagulants, such as heparins and fondaparinux, in that its activity is independent of antithrombin and its ability to inhibit prothrombinase bound factor Xa.	Rivaroxaban	0-11	serpin family C member 1	Homo sapiens	203-215
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
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.	Arginine	113-121	serpin family C member 1	Homo sapiens	107-112
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.	Tyrosine	39-42	serpin family C member 1	Homo sapiens	73-85
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.	Glutamic Acid	51-54	serpin family C member 1	Homo sapiens	73-85
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
19010776-5	2009	Mutation of Arg-150 in factor Xa, which interacts with the exosite residues in heparin-activated antithrombin, abrogated the ability of the engineered exosites in alpha1PI to promote factor Xa inhibition.	Arginine	12-15	serpin family C member 1	Homo sapiens	97-109
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.	Serine	193-199	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.	Serine	193-199	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.	Serine	193-199	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	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
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
19689280-5	2009	Lastly, the short unique pentasaccharidic sequence which is crucial for heparin"s activity and has been recently synthesized as Fondaparinux, only acts via the formation of the high affinity ternary complex with ATIII-factor Xa.	Fondaparinux	128-140	serpin family C member 1	Homo sapiens	212-217
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
18698082-7	2008	A reduced dexamethasone related increase of antithrombin and protein S, and subsequent decline below normal levels after introduction of asparaginase, may result in a hypercoagulable state, contributing to development of symptomatic osteonecrosis.	Dexamethasone	10-23	serpin family C member 1	Homo sapiens	44-56
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	33-36	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	33-36	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	33-36	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.	Lysine	53-59	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.	Lysine	53-59	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.	Lysine	53-59	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.	Arginine	113-121	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.	Arginine	113-121	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
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.	pentasaccharide	11-26	serpin family C member 1	Homo sapiens	82-94
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
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
19035835-3	2008	Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin.	pentasaccharide	73-88	serpin family C member 1	Homo sapiens	28-40
19035835-4	2008	Rapid kinetic studies demonstrated that this pentasaccharide induced a conformational change also in latent and cleaved antithrombin.	pentasaccharide	45-60	serpin family C member 1	Homo sapiens	120-132
19035835-5	2008	The binding affinities of these antithrombin forms for the pentasaccharide, as compared to native antithrombin, were approximately 30-fold lower due to two to three fewer ionic interactions, resulting in less stable conformationally altered states.	pentasaccharide	59-74	serpin family C member 1	Homo sapiens	32-44
19035835-5	2008	The binding affinities of these antithrombin forms for the pentasaccharide, as compared to native antithrombin, were approximately 30-fold lower due to two to three fewer ionic interactions, resulting in less stable conformationally altered states.	pentasaccharide	59-74	serpin family C member 1	Homo sapiens	98-110
19035835-6	2008	Affinities of latent and cleaved antithrombin for longer heparin chains, containing the pentasaccharide sequence, were 2-fold lower than for the pentasaccharide itself.	pentasaccharide	88-103	serpin family C member 1	Homo sapiens	33-45
19035835-6	2008	Affinities of latent and cleaved antithrombin for longer heparin chains, containing the pentasaccharide sequence, were 2-fold lower than for the pentasaccharide itself.	pentasaccharide	145-160	serpin family C member 1	Homo sapiens	33-45
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.	pentasaccharide	100-115	serpin family C member 1	Homo sapiens	43-55
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
19035835-8	2008	These findings contribute to delineating the mechanism by which heparin or heparan sulfate mediates antiangiogenic activity of antithrombin.	Heparitin Sulfate	75-90	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
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
18761723-0	2008	Heparan sulfates from arteries and veins differ in their antithrombin-mediated anticoagulant activity.	Heparitin Sulfate	0-16	serpin family C member 1	Homo sapiens	57-69
18669628-1	2008	Anticoagulant heparan sulfate proteoglycans bind and activate antithrombin by virtue of a specific 3-O-sulfated pentasaccharide.	3-o-sulfated pentasaccharide	99-127	serpin family C member 1	Homo sapiens	62-74
18669628-8	2008	Heparan sulfate chains were fractionated according to their affinity for antithrombin, and their structure was analyzed by 1H NMR and MS/MS.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	73-85
18669628-10	2008	These antithrombin-binding chains contain more than 6% 3-O-sulfated glucosamine residues, convey an anticoagulant activity of 2.5 IU/ml to human follicular fluid, and have an anti-Factor Xa specific activity of 167 IU/mg.	Glucosamine	68-79	serpin family C member 1	Homo sapiens	6-18
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
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
18691229-9	2008	Beriplex P/N showed the greatest capacity for thrombin inhibition, a reflection of the observed high levels of the coagulation inhibitors protein C, protein S, protein Z, and small amounts of antithrombin III and heparin in this product.	beriplex p	0-10	serpin family C member 1	Homo sapiens	192-208
18691229-9	2008	Beriplex P/N showed the greatest capacity for thrombin inhibition, a reflection of the observed high levels of the coagulation inhibitors protein C, protein S, protein Z, and small amounts of antithrombin III and heparin in this product.	Nitrogen	11-12	serpin family C member 1	Homo sapiens	192-208
18558097-7	2008	Finally, the antithrombin-alpha-thrombin covalent complex dissociates from the polysaccharide chain.	Polysaccharides	79-93	serpin family C member 1	Homo sapiens	13-25
18640975-0	2008	Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction.	octasaccharides	21-36	serpin family C member 1	Homo sapiens	0-12
18640975-0	2008	Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction.	pentasaccharide	74-89	serpin family C member 1	Homo sapiens	0-12
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)).	pentasaccharide	126-141	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)).	Glucosamine	161-165	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)).	Glucuronic Acid	177-181	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)).	idoua	196-201	serpin family C member 1	Homo sapiens	100-112
18558097-4	2008	Our results indicate the following: 1) both the sulfated galactan and heparin potentiate protease inactivation by antithrombin at similar molar concentrations, however they differ markedly in the molecular size required for their activities; 2) this galactan interacts predominantly with exosite II on alpha-thrombin and, similar to heparin, catalyzes the formation of a covalent complex between antithrombin and the protease; 3) the sulfated galactan has a higher affinity for alpha-thrombin than for antithrombin.	Galactans	57-65	serpin family C member 1	Homo sapiens	114-126
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
18558097-4	2008	Our results indicate the following: 1) both the sulfated galactan and heparin potentiate protease inactivation by antithrombin at similar molar concentrations, however they differ markedly in the molecular size required for their activities; 2) this galactan interacts predominantly with exosite II on alpha-thrombin and, similar to heparin, catalyzes the formation of a covalent complex between antithrombin and the protease; 3) the sulfated galactan has a higher affinity for alpha-thrombin than for antithrombin.	Galactans	57-65	serpin family C member 1	Homo sapiens	396-408
18558097-4	2008	Our results indicate the following: 1) both the sulfated galactan and heparin potentiate protease inactivation by antithrombin at similar molar concentrations, however they differ markedly in the molecular size required for their activities; 2) this galactan interacts predominantly with exosite II on alpha-thrombin and, similar to heparin, catalyzes the formation of a covalent complex between antithrombin and the protease; 3) the sulfated galactan has a higher affinity for alpha-thrombin than for antithrombin.	Galactans	57-65	serpin family C member 1	Homo sapiens	396-408
18558097-5	2008	We propose that the preferred pathway of sulfated galactan-induced inactivation of alpha-thrombin by antithrombin starts with the polysaccharide binding to the protease through a high-affinity interaction.	Galactans	50-58	serpin family C member 1	Homo sapiens	101-113
18558097-5	2008	We propose that the preferred pathway of sulfated galactan-induced inactivation of alpha-thrombin by antithrombin starts with the polysaccharide binding to the protease through a high-affinity interaction.	Polysaccharides	130-144	serpin family C member 1	Homo sapiens	101-113
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
18695376-4	2008	RECENT FINDINGS: Fondaparinux is a synthetic pentasaccharide, which binds to antithrombin, thereby indirectly inhibiting factor Xa.	pentasaccharide	45-60	serpin family C member 1	Homo sapiens	77-89
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
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.	ba-peg	41-47	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.	ba-peg	41-47	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
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
18433074-0	2008	Conjugation of ATIII-binding pentasaccharides to extend the half-life of proteins: long-acting insulin.	pentasaccharides	29-45	serpin family C member 1	Homo sapiens	15-20
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.	iminodisuccinic acid	0-31	serpin family C member 1	Homo sapiens	178-190
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.	idoa2s	33-39	serpin family C member 1	Homo sapiens	178-190
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
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.	Polysaccharides	119-133	serpin family C member 1	Homo sapiens	178-190
18570058-8	2008	We found an increase in AT-III in men receiving E(2) which may be related to gonadal steroid withdrawal, but no significant differences in other inflammatory or clotting factor parameters.	Steroids	85-92	serpin family C member 1	Homo sapiens	24-30
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
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
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.	Glycosaminoglycans	34-52	serpin family C member 1	Homo sapiens	66-78
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.	pentasaccharide	92-107	serpin family C member 1	Homo sapiens	66-78
18574264-8	2008	Fondaparinux, a synthetic pentasaccharide, catalyzes the inhibition of factor Xa, but not thrombin, in an antithrombin-dependent fashion.	pentasaccharide	26-41	serpin family C member 1	Homo sapiens	106-118
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
18447601-1	2008	BACKGROUND: Idraparinux is a synthetic pentasaccharide that binds to antithrombin with high affinity.	pentasaccharide	39-54	serpin family C member 1	Homo sapiens	69-81
18541230-0	2008	Protective effects of antithrombin on puromycin aminonucleoside nephrosis in rats.	Puromycin	38-47	serpin family C member 1	Homo sapiens	22-34
18541230-1	2008	We investigated the effects of antithrombin, a plasma inhibitor of coagulation factors, in rats with puromycin aminonucleoside-induced nephrosis, which is an experimental model of human nephrotic syndrome.	Puromycin Aminonucleoside	101-126	serpin family C member 1	Homo sapiens	31-43
18541230-4	2008	Treatment with antithrombin attenuated the puromycin aminonucleoside-induced hematological abnormalities.	Puromycin Aminonucleoside	43-68	serpin family C member 1	Homo sapiens	15-27
18541230-7	2008	In addition, antithrombin treatment markedly suppressed puromycin aminonucleoside-induced apoptosis of renal tubular epithelial cells.	Puromycin Aminonucleoside	56-81	serpin family C member 1	Homo sapiens	13-25
18273869-7	2008	Antithrombin deficiency correlated with underlying malignancy, donor HLA-mismatch, and TBI, whereas decreased PC activity demonstrated a trend of association with lack of T-cell depletion and TBI.	Thioacetazone	87-90	serpin family C member 1	Homo sapiens	0-12
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
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.	Sepharose	182-189	serpin family C member 1	Homo sapiens	58-70
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
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.	Tryptophan	106-116	serpin family C member 1	Homo sapiens	60-72
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
18184032-1	2008	Fondaparinux is a synthetic pentasaccharide that inhibits thrombin formation and thrombus development via selective antithrombin mediated inhibition of factor Xa.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	116-128
18720820-7	2008	The result showed that the resonance scattering intensity at 491 nm (I(RS)) is linear to the AT-III concentration in the range of 62.5 to 850 ng x mL(-1), under the optimum conditions of 0.30 mL goat-anti-human AT-III antibody, 30 mg x mL(-1) polyethelene glycol-6000, being incubated at 37 degrees C for 15 min, the voltage at 400 V, and the excitation and emission slit width both at 5.0 nm.	polyethelene glycol-6000	243-267	serpin family C member 1	Homo sapiens	93-99
18345636-8	2008	Binding characteristics of the neutral resins for the natural anticoagulants protein C and antithrombin showed remarkable differences, with weak binding of antithrombin but strong removal of protein C, not only for the anion exchanger, but also for neutral polymers of the large pore size range.	Polymers	257-265	serpin family C member 1	Homo sapiens	91-103
18393915-3	2008	Fondaparinux is a relative new pharmacological agent that selectively binds to antithrombin, and represents a new class of synthetic selective inhibitors of activated factor X. Eleven percent of the fondaparinux-related English language literature, between 2001 and 2007, refers to orthopaedic trauma, and was the sample assessed for this critical analysis review.	Fondaparinux	0-12	serpin family C member 1	Homo sapiens	79-91
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.	oligo	73-78	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.	tyrosine O-sulfate	79-95	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.	oligo	150-155	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.	tyrosine O-sulfate	156-172	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
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.	hexasaccharide	238-252	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.	5-diphosphomevalonic acid	253-256	serpin family C member 1	Homo sapiens	183-190
18160297-4	2008	Moreover, we found longer oligo(tyrosine sulfate) has higher binding affinity to hAT III (123-139).	tyrosine O-sulfate	32-48	serpin family C member 1	Homo sapiens	81-88
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
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
18195690-0	2008	Inhibition of proteasome by bortezomib causes intracellular aggregation of hepatic serpins and increases the latent circulating form of antithrombin.	Bortezomib	28-38	serpin family C member 1	Homo sapiens	136-148
18195690-13	2008	Finally, bortezomib had only minor effects on the mature circulating antithrombin, with increased amounts of latent antithrombin in plasma.	Bortezomib	9-19	serpin family C member 1	Homo sapiens	116-128
18260648-0	2008	Characterization of heparin oligosaccharides binding specifically to antithrombin III using mass spectrometry.	heparin oligosaccharides	20-44	serpin family C member 1	Homo sapiens	69-85
18260648-4	2008	Here we describe a hydrophobic trapping assay for screening a library of heparin hexasaccharides for binders to antithrombin III (ATIII).	heparin hexasaccharides	73-96	serpin family C member 1	Homo sapiens	112-128
18260648-4	2008	Here we describe a hydrophobic trapping assay for screening a library of heparin hexasaccharides for binders to antithrombin III (ATIII).	heparin hexasaccharides	73-96	serpin family C member 1	Homo sapiens	130-135
18260648-8	2008	The specificity of the hexasaccharides binding ATIII was confirmed by assaying their ability to enhance ATIII-mediated inhibition of Factor Xa in vitro.	hexasaccharides	23-38	serpin family C member 1	Homo sapiens	47-52
18260648-8	2008	The specificity of the hexasaccharides binding ATIII was confirmed by assaying their ability to enhance ATIII-mediated inhibition of Factor Xa in vitro.	hexasaccharides	23-38	serpin family C member 1	Homo sapiens	104-109
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
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
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
17909966-2	2008	A specific pentasaccharide in heparinoids activates antithrombin III, resulting in inactivation of factor Xa and-when additional saccharides are present-inactivation of factor IIa.	pentasaccharide	11-26	serpin family C member 1	Homo sapiens	52-68
17909966-2	2008	A specific pentasaccharide in heparinoids activates antithrombin III, resulting in inactivation of factor Xa and-when additional saccharides are present-inactivation of factor IIa.	Heparinoids	30-41	serpin family C member 1	Homo sapiens	52-68
18278163-6	2008	They share a common mechanism of action together with the endogenous antithrombotic heparan sulfate, i.e. the catalysis of the antithrombin-mediated inhibition of factor Xa.	Heparitin Sulfate	84-99	serpin family C member 1	Homo sapiens	127-139
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
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
18065202-7	2008	RESULTS: The levels of hemostatic variables did not change significantly throughout the study in the isoflavone group; however, the isoflavone group showed a statistically significant reduction in plasma concentration of prothrombin fragments 1 plus 2; both groups showed a statistically significant reduction in antithrombin, protein C, and free protein S levels.	Isoflavones	132-142	serpin family C member 1	Homo sapiens	313-325
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
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
17584894-6	2007	SDS-PAGE showed that OTR4120 induced the formation of covalently linked complexes between antithrombin III or heparin cofactor II and thrombin.	Sodium Dodecyl Sulfate	0-3	serpin family C member 1	Homo sapiens	90-106
22275964-9	2008	Antithrombin-III showed a 4% borderline significant reduction in the fenretinide arm relative to placebo, irrespective of the HRT administration route (p = 0.055).	Fenretinide	69-80	serpin family C member 1	Homo sapiens	0-16
18206177-0	2008	Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine.	Acrolein	38-46	serpin family C member 1	Homo sapiens	0-12
18206177-0	2008	Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine.	Homocysteine	51-63	serpin family C member 1	Homo sapiens	0-12
18206177-0	2008	Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine.	Thiolactone	64-75	serpin family C member 1	Homo sapiens	0-12
18206177-0	2008	Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine.	Cysteine	55-63	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	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
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.	Lysine	157-160	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.	Acrolein	192-200	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.	Acrolein	192-200	serpin family C member 1	Homo sapiens	236-248
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.	homocysteine thiolactone	204-228	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.	homocysteine thiolactone	204-228	serpin family C member 1	Homo sapiens	236-248
18206177-4	2008	When we incubated human antithrombin with increasing concentrations of acrolein (0-2 mmol/L) over a short period of time (0-4 h), a time and concentration dependent loss of activity was apparent (IC(50)=0.25 mmol/L).	Acrolein	71-79	serpin family C member 1	Homo sapiens	24-36
18206177-7	2008	When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost.	Acrolein	40-48	serpin family C member 1	Homo sapiens	5-17
18206177-7	2008	When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost.	Acrolein	40-48	serpin family C member 1	Homo sapiens	85-97
18206177-7	2008	When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost.	Cysteine	53-61	serpin family C member 1	Homo sapiens	5-17
18206177-7	2008	When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost.	Cysteine	53-61	serpin family C member 1	Homo sapiens	85-97
18560242-1	2008	BACKGROUND/AIMS: Argatroban, a hepatically metabolized direct thrombin inhibitor, is approved for use in heparin-induced thrombocytopenia (HIT; several countries) and in antithrombin-deficient patients undergoing hemodialysis (Japan).	argatroban	17-27	serpin family C member 1	Homo sapiens	170-182
18560242-3	2008	METHODS: A literature search identified 34 publications (12 prospective studies, 4 retrospective studies, 18 anecdotal reports) that together described 644 argatroban-treated patients (446 with HIT, 82 with antithrombin deficiency) with varying degrees of renal function.	argatroban	156-166	serpin family C member 1	Homo sapiens	207-219
18560242-9	2008	CONCLUSION: Current literature suggests that argatroban is well tolerated and provides adequate anticoagulation in patients with renal dysfunction or failure, including individuals with HIT or antithrombin deficiency where anticoagulant options are limited.	argatroban	45-55	serpin family C member 1	Homo sapiens	193-205
17996279-5	2008	Pentasaccharides are synthetic drugs that accelerate the interaction between factor Xa and antithrombin but selectively inhibit factor Xa activity.	pentasaccharides	0-16	serpin family C member 1	Homo sapiens	91-103
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
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
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
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
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
17875649-4	2007	Equilibrium binding of NBD-labeled antithrombins to S195A proteases showed that exosites generated by conformationally activating antithrombin with a heparin pentasaccharide enhanced the affinity of the serpin for S195A factor Xa minimally 100-fold.	IC 831423	150-173	serpin family C member 1	Homo sapiens	35-47
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
18663937-1	2007	For the first time it is proved, that patients with an acute virus myocarditis have statistically confirmed authentic reduction in quantity of thrombocytes, extention of parameters of a activated partial thrombin time, reduction in concentration of a heparin-antithrombin III (AT-III) complex against suppressed enzyme of antiradical protection - superoxide dismutase and it has led to activization of a malonic dialdehyde in erythrocytes, thrombocytes and blood serum.	Malondialdehyde	404-422	serpin family C member 1	Homo sapiens	251-275
17621651-0	2007	Macroscopic thrombus formation on angioplasty equipment following antithrombin therapy with enoxaparin.	Enoxaparin	92-102	serpin family C member 1	Homo sapiens	66-78
17621651-2	2007	We evaluated the incidence and consequences of periprocedural macroscopic thrombus formation on PCI equipment following antithrombin therapy with enoxaparin.	Enoxaparin	146-156	serpin family C member 1	Homo sapiens	120-132
17621651-3	2007	Between April 2003 and December 2004, all patients undergoing cardiac catheterization following antithrombin therapy with enoxaparin were evaluated.	Enoxaparin	122-132	serpin family C member 1	Homo sapiens	96-108
17621651-11	2007	Percutaneous coronary intervention following antithrombin therapy with enoxaparin is associated with a 5% incidence of macroscopic thrombus formation on PCI equipment.	Enoxaparin	71-81	serpin family C member 1	Homo sapiens	45-57
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
17879089-0	2007	Comparison of planar SDS-PAGE, CGE-on-a-chip, and MALDI-TOF mass spectrometry for analysis of the enzymatic de-N-glycosylation of antithrombin III and coagulation factor IX with PNGase F. Three different analytical techniques (planar SDS-PAGE, CGE-on-a-chip and MALDI-TOF-MS) applied for determination of the molecular weight of intact and partly and completely de-N-glycosylated human serum glycoproteins (antithrombin III and coagulation factor IX) have been compared.	Sodium Dodecyl Sulfate	234-237	serpin family C member 1	Homo sapiens	130-146
17577134-8	2007	Decreases in antithrombin III, platelet count and fibrinogen levels, prolongation of prothrombin time, and increases in the plasma fibrin degradation products were significantly suppressed by the administration of methylprednisolone.	Methylprednisolone	214-232	serpin family C member 1	Homo sapiens	13-29
17890948-1	2007	Fondaparinux is a new anticoagulant that interacts with antithrombin III and activated coagulation factor X resulting in an inhibition of the coagulation system.	Fondaparinux	0-12	serpin family C member 1	Homo sapiens	56-72
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
17709798-7	2007	Tamoxifen increased IGFBP-3 and lowered antithrombin-III, C reactive protein, and mammographic density, with greater effects of 5 mg/day.	Tamoxifen	0-9	serpin family C member 1	Homo sapiens	40-56
17884631-7	2007	We discovered that polysaccharides without the iduronic acid residue displayed strong binding affinity to antithrombin and high anti-Xa and anti-IIa activities.	Polysaccharides	19-34	serpin family C member 1	Homo sapiens	106-118
17884631-7	2007	We discovered that polysaccharides without the iduronic acid residue displayed strong binding affinity to antithrombin and high anti-Xa and anti-IIa activities.	Iduronic Acid	47-60	serpin family C member 1	Homo sapiens	106-118
17907113-5	2007	Pioglitazone significantly (p &lt; or = 0.001) decreased circulating levels of von Willebrand factor (-9.7%, -9.4%) and plasminogen activator inhibitor-1 (-16.8 ng/ml, -12.3 ng/ml), and increased levels of antithrombin-III (+1.3 mg/dL, +1.5 mg/dL) after six and 12 months, respectively.	Pioglitazone	0-12	serpin family C member 1	Homo sapiens	206-222
17323934-0	2007	High affinity interaction between a synthetic, highly negatively charged pentasaccharide and alpha- or beta-antithrombin is predominantly due to nonionic interactions.	pentasaccharide	73-88	serpin family C member 1	Homo sapiens	108-120
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
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
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
17536781-0	2007	Frontal analysis capillary electrophoresis hyphenated to electrospray ionization mass spectrometry for the characterization of the antithrombin/heparin pentasaccharide complex.	pentasaccharide	152-167	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.	pentasaccharide	103-118	serpin family C member 1	Homo sapiens	73-85
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.	pentasaccharide	103-118	serpin family C member 1	Homo sapiens	135-147
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
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
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.	pentasaccharide	52-67	serpin family C member 1	Homo sapiens	31-43
17546440-7	2007	The synthetic, selective antithrombin-binding pentasaccharide fondaparinux has been successfully used in prophylaxis for the prevention of thrombosis in highest risk patients.	pentasaccharide	46-61	serpin family C member 1	Homo sapiens	25-37
17047995-3	2007	Thus, anticoagulant treatment with melagatran is of special interest in neonatal patients, whose plasma is relatively deficient in antithrombin.	melagatran	35-45	serpin family C member 1	Homo sapiens	131-143
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.	Enoxaparin	0-10	serpin family C member 1	Homo sapiens	110-126
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
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, Low-Molecular-Weight	46-50	serpin family C member 1	Homo sapiens	110-126
17600038-8	2007	CONCLUSIONS: When compared with UFH, enoxaparin was associated with superior efficacy as adjunctive antithrombin therapy among &gt;49 000 patients across the ACS spectrum.	Enoxaparin	37-47	serpin family C member 1	Homo sapiens	100-112
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
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
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
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
17478454-7	2007	Plasma selenium was positively correlated with minimum platelet count, minimum plasma antithrombin activity, and protein C activity.	Selenium	7-15	serpin family C member 1	Homo sapiens	86-98
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.	Sulfhydryl Compounds	0-5	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	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
17323934-1	2007	Idraparinux is a synthetic O-sulfated, O-methylated pentasaccharide that binds tightly to antithrombin (AT) and thereby specifically and efficiently induces the inactivation of the procoagulant protease, factor Xa.	idraparinux	0-11	serpin family C member 1	Homo sapiens	90-102
17323934-1	2007	Idraparinux is a synthetic O-sulfated, O-methylated pentasaccharide that binds tightly to antithrombin (AT) and thereby specifically and efficiently induces the inactivation of the procoagulant protease, factor Xa.	pentasaccharide	52-67	serpin family C member 1	Homo sapiens	90-102
17156824-6	2007	Compared with the low-dose HT group those treated with tibolone showed more pronounced decreases in factor VII, less reduction of antithrombin and protein C and even increased levels in protein S and tissue factor pathway inhibitor.	tibolone	55-63	serpin family C member 1	Homo sapiens	130-142
17364989-7	2007	In conclusion, the lower risk of severe acute GVHD in the CBT group may have been related to the smaller decrease of AT-3 after transplantation.	N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE	58-61	serpin family C member 1	Homo sapiens	117-121
17364989-6	2007	The AT-3 level after engraftment was significantly higher in the CBT group than in the BMT group and it did not fail along with the elevation of elastase in the CBT group (p &lt; 0.01 by the Mann-Whitney U-test vs. the BMT group).	N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE	65-68	serpin family C member 1	Homo sapiens	4-8
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
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
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, Low-Molecular-Weight	84-88	serpin family C member 1	Homo sapiens	130-142
17229412-5	2007	The example of interactions between heparin and antithrombin III illustrates how such a complex mechanism as the regulation of blood coagulation by a specific pentasaccharide can be dissected through the combined use of dedicated carbohydrate chemistry and structural glycobiology.	pentasaccharide	159-174	serpin family C member 1	Homo sapiens	48-64
17229412-5	2007	The example of interactions between heparin and antithrombin III illustrates how such a complex mechanism as the regulation of blood coagulation by a specific pentasaccharide can be dissected through the combined use of dedicated carbohydrate chemistry and structural glycobiology.	Carbohydrates	230-242	serpin family C member 1	Homo sapiens	48-64
17600391-9	2007	In the case of pregnancy, antithrombin concentrate is often used around the time of birth when LMWH may increase the risk of post-partum haemorrhage.	Heparin, Low-Molecular-Weight	95-99	serpin family C member 1	Homo sapiens	26-38
18333219-8	2007	The postoperative level of AT-III in the control group was significantly lower than in the steroid group (ANOVA p &lt; 0.01).	Steroids	91-98	serpin family C member 1	Homo sapiens	27-33
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
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
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
17167048-1	2007	Antithrombin (AT) inhibition of coagulation enzymes is catalyzed by unfractionated heparin (UFH) and other heparinoids.	Heparinoids	107-118	serpin family C member 1	Homo sapiens	0-12
17297193-4	2007	Also not previously reported is the use of bivaluridin as the periprocedural antithrombin agent during and after high-risk aortic valvuloplasty.	bivaluridin	43-54	serpin family C member 1	Homo sapiens	77-89
17966105-0	2007	[The insufficiency of low molecular weight heparin (LMWH) prophylaxis in patients with hereditary antithrombin (AT) deficiency].	Heparin, Low-Molecular-Weight	52-56	serpin family C member 1	Homo sapiens	98-110
17477084-7	2007	RESULTS: After 2-months therapy with simvastatin in patients with hlp II it was observed significantly decrease of activity of factor X (20.94 +/- 19.04 vs. 9.44 +/- 7.31 mU/mL), thrombin generation (79.62 +/- 36.68 vs. 67.99 +/- 37.69 U/mL), clot bound thrombin (49.73 +/- 21.17 vs. 37.08 +/- 26.10 U/mL) and increase of antithrombin III activity (13.03 +/- 6.11 vs. 20.64 +/- 4.18 U/mL).	Simvastatin	37-48	serpin family C member 1	Homo sapiens	322-338
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
17200767-1	2007	Fondaparinux is a synthetic pentasaccharide consisting of the minimal sequence of heparin which interacts with antithrombin (AT).	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	111-123
17270255-1	2007	INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action.	Dermatan Sulfate	14-30	serpin family C member 1	Homo sapiens	131-143
17270255-1	2007	INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action.	Dermatan Sulfate	32-34	serpin family C member 1	Homo sapiens	131-143
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
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
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
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
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
17040907-0	2006	Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains.	Heparitin Sulfate	39-54	serpin family C member 1	Homo sapiens	15-27
17040907-0	2006	Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains.	Heparitin Sulfate	39-54	serpin family C member 1	Homo sapiens	221-233
17040907-0	2006	Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains.	Heparitin Sulfate	251-266	serpin family C member 1	Homo sapiens	15-27
17040907-0	2006	Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains.	Heparitin Sulfate	251-266	serpin family C member 1	Homo sapiens	221-233
17040907-8	2006	Moreover, the inability of native antithrombin to bind this co-receptor implies that native and conformationally altered forms of antithrombin differentially bind proangiogenic heparan sulfate domains.	Heparitin Sulfate	177-192	serpin family C member 1	Homo sapiens	130-142
16624472-2	2006	Two sesquiterpenolides of similar structures (atractylenolide I, AT-I; atractylenolide III, AT-III) were isolated from dried rhizome of Atractylodes ovata.	sesquiterpenolides	4-22	serpin family C member 1	Homo sapiens	92-98
16796563-0	2006	Conformational transitions induced in heparin octasaccharides by binding with antithrombin III.	heparin octasaccharides	38-61	serpin family C member 1	Homo sapiens	78-94
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
17043951-6	2006	Anticoagulant heparan sulfate proteoglycans (aHSPG), like heparin, possess a pentasaccharide sequence which binds and activates antithrombin III.	pentasaccharide	77-92	serpin family C member 1	Homo sapiens	128-144
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
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
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
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
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
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.	Alanine	166-169	serpin family C member 1	Homo sapiens	53-65
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.	Glutamic Acid	173-176	serpin family C member 1	Homo sapiens	53-65
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
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
16954536-3	2006	ATH was produced using Schiff base/Amadori rearrangement by incubating antithrombin with unfractionated heparin for 14 d at 40 degrees C. ATH was then digested using Proteinase K, and the heparin-peptide was reacted with NaIO4/NaBH4/mild acid to degrade the heparin moiety.	Schiff Bases	23-34	serpin family C member 1	Homo sapiens	71-83
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
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
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
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
16940049-0	2006	Disruption of a tight cluster surrounding tyrosine 131 in the native conformation of antithrombin III activates it for factor Xa inhibition.	Tyrosine	42-50	serpin family C member 1	Homo sapiens	85-101
16940049-2	2006	This study focused on tyrosine 131, which is located at the helix D-sheet A interface, adjacent to the ATIII pentasaccharide and heparin cofactor-binding sites and some 17A away from the RCL insertion.	Tyrosine	22-30	serpin family C member 1	Homo sapiens	103-108
16940049-2	2006	This study focused on tyrosine 131, which is located at the helix D-sheet A interface, adjacent to the ATIII pentasaccharide and heparin cofactor-binding sites and some 17A away from the RCL insertion.	pentasaccharide	109-124	serpin family C member 1	Homo sapiens	103-108
16940049-3	2006	Crystallographic structures show that the Tyr(131) ring is buried in native ATIII and then becomes exposed when pentasaccharide binds to the inhibitor and activates it.	Tyrosine	42-45	serpin family C member 1	Homo sapiens	76-81
16940049-3	2006	Crystallographic structures show that the Tyr(131) ring is buried in native ATIII and then becomes exposed when pentasaccharide binds to the inhibitor and activates it.	pentasaccharide	112-127	serpin family C member 1	Homo sapiens	76-81
16940049-4	2006	This change suggested that Tyr(131) might serve as a switch for ATIII conformational activation.	Tyrosine	27-30	serpin family C member 1	Homo sapiens	64-69
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.	Tyrosine	16-19	serpin family C member 1	Homo sapiens	114-126
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.	Tyrosine	16-19	serpin family C member 1	Homo sapiens	305-310
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.	Asparagine	25-28	serpin family C member 1	Homo sapiens	114-126
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.	Asparagine	25-28	serpin family C member 1	Homo sapiens	305-310
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.	Leucine	34-37	serpin family C member 1	Homo sapiens	114-126
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.	Leucine	34-37	serpin family C member 1	Homo sapiens	305-310
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.	Leucine	43-46	serpin family C member 1	Homo sapiens	114-126
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.	Leucine	43-46	serpin family C member 1	Homo sapiens	305-310
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.	Serine	52-55	serpin family C member 1	Homo sapiens	114-126
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.	Serine	52-55	serpin family C member 1	Homo sapiens	305-310
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.	Tyrosine	208-216	serpin family C member 1	Homo sapiens	114-126
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.	Tyrosine	208-216	serpin family C member 1	Homo sapiens	305-310
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
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
17174877-6	2006	CASE REPORT: We present a case of recurrent acute in-stent thrombosis in a patient with mild antithrombin III (AT) deficiency despite the combined administration of clopidogrel and aspirin.	Clopidogrel	165-176	serpin family C member 1	Homo sapiens	93-109
17174877-6	2006	CASE REPORT: We present a case of recurrent acute in-stent thrombosis in a patient with mild antithrombin III (AT) deficiency despite the combined administration of clopidogrel and aspirin.	Aspirin	181-188	serpin family C member 1	Homo sapiens	93-109
16938875-8	2006	We demonstrated the specificity of the antithrombin III functionalized sensor for the physiologically active pentasaccharide sequence.	pentasaccharide	109-124	serpin family C member 1	Homo sapiens	39-55
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
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
16837886-11	2006	Oral E(2) with NETA reduced antithrombin III (P &lt; 0.001) and protein C (P &lt; 0.001) activity.	Norethindrone Acetate	15-19	serpin family C member 1	Homo sapiens	28-44
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
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.	Enoxaparin	125-135	serpin family C member 1	Homo sapiens	262-274
16672689-0	2006	Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin-independent mechanism.	holothurian glycosaminoglycan	14-43	serpin family C member 1	Homo sapiens	105-117
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
16672689-1	2006	Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chrondroitin sulfate that possesses antithrombin-independent antithrombotic properties and inhibits factor X activation by the intrinsic tenase complex (factor IXa-factor VIIIa).	holothurian glycosaminoglycan	14-43	serpin family C member 1	Homo sapiens	103-115
16672689-1	2006	Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chrondroitin sulfate that possesses antithrombin-independent antithrombotic properties and inhibits factor X activation by the intrinsic tenase complex (factor IXa-factor VIIIa).	dhg	45-48	serpin family C member 1	Homo sapiens	103-115
16672689-1	2006	Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chrondroitin sulfate that possesses antithrombin-independent antithrombotic properties and inhibits factor X activation by the intrinsic tenase complex (factor IXa-factor VIIIa).	chrondroitin sulfate	67-87	serpin family C member 1	Homo sapiens	103-115
16711739-2	2006	Only the twisted boat conformation allowed the biologically active pentasaccharide unit of heparin (DEFGH) to bind to antithrombin.	pentasaccharide	67-82	serpin family C member 1	Homo sapiens	118-130
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.	exosite	98-105	serpin family C member 1	Homo sapiens	58-70
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
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
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
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
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
16685318-1	2006	BACKGROUND: Subcutaneous enoxaparin is increasingly employed as the antithrombin of choice in non-ST elevation myocardial infarction and in conjunction with various fibrinolytic regimens in acute ST elevation myocardial infarction (STEMI).	Enoxaparin	25-35	serpin family C member 1	Homo sapiens	68-80
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
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
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
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
16618121-0	2006	Pentasaccharide enhances the inactivation of factor Xa by antithrombin by promoting the assembly of a Michaelis-type intermediate complex.	pentasaccharide	0-15	serpin family C member 1	Homo sapiens	58-70
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
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.	corline heparin	49-64	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.	corline heparin	49-64	serpin family C member 1	Homo sapiens	40-42
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
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
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
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
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
16442510-0	2006	Thrombin inhibition by antithrombin in the presence of oversulfated dermatan sulfates.	Dermatan Sulfate	68-85	serpin family C member 1	Homo sapiens	23-35
16442510-2	2006	DSS1 and DSS2 both enhanced the rate at which antithrombin (AT) inactivates thrombin according to a concentration dependent manner.	dss2	9-13	serpin family C member 1	Homo sapiens	46-58
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.	Vitamin K	44-53	serpin family C member 1	Homo sapiens	11-23
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
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
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
16290930-2	2006	A naphthylsulfonamide analogue showed excellent antithrombin activity.	naphthylsulfonamide	2-21	serpin family C member 1	Homo sapiens	48-60
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
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
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
16310443-9	2005	Systemic oxygen saturation correlated positively with the levels of anticoagulants (protein C, protein S, antithrombin III) and procoagulants (factors II, V, VII, and X) (all with p&lt;0.05, r=0.33 to 0.61).	Oxygen	9-15	serpin family C member 1	Homo sapiens	106-122
16475045-6	2006	Fondaparinux is a synthetic pentasaccharide, which binds to antithrombin, thereby indirectly selectively inhibiting factor Xa.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	60-72
16310167-5	2006	Surface plasmon resonance was used to measure the interaction of each member of this polysaccharide library with antithrombin III (ATIII), to afford structural information on sulfo groups required for this HP/HS-protein interaction.	Polysaccharides	85-99	serpin family C member 1	Homo sapiens	113-129
16310167-5	2006	Surface plasmon resonance was used to measure the interaction of each member of this polysaccharide library with antithrombin III (ATIII), to afford structural information on sulfo groups required for this HP/HS-protein interaction.	Polysaccharides	85-99	serpin family C member 1	Homo sapiens	131-136
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
16337041-5	2006	RESULTS: After 1 week of treatment, a significant increase of ATIII (p &lt; 0.05), fV (p &lt; 0.01) and vWF (p &lt; 0.05) was found in the control group, but not in atorvastatin-treated group.	Atorvastatin	165-177	serpin family C member 1	Homo sapiens	62-67
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
16394262-3	2006	Heparan sulfate enables growth factor function and modifies enzyme/inhibitor functions, such as antithrombin III and heparin cofactor II.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	96-112
16192735-4	2006	Those women receiving intranasal estradiol showed a mild increment in plasminogen activator inhibitor-1 (PAI-I) (from 6.8 +/- 3.5 to 9.6 +/- 3.9 U/ml, p &lt; 0.01); however, fibrinogen, factor VII-tissue factor complex (VIIa-rTF), antithrombin III (ATIII), protein C (PC) activity, protein S (PS) activity, plasminogen (PLG), and tissue-type plasminogen activator antigen (t-PA) were unchanged.	Estradiol	33-42	serpin family C member 1	Homo sapiens	249-254
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
17124098-8	2006	Fondaparinux is a synthetic pentasaccharide, which binds to antithrombin, thereby indirectly selectively inhibiting factor Xa.	pentasaccharide	28-43	serpin family C member 1	Homo sapiens	60-72
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
17323590-1	2006	The antithrombin binding sequence of heparin, a pentasaccharide, has been synthesized as fondaparinux, an indirect, selective, and reversible factor Xa inhibitor.	pentasaccharide	48-63	serpin family C member 1	Homo sapiens	4-16
16260789-4	2005	By selecting appropriate enzymatic modification steps, an inactive precursor has been converted to the heparan sulfate having three distinct biological activities, associated with binding to antithrombin, fibroblast growth factor-2, and herpes simplex virus envelope glycoprotein D. Because the recombinant sulfotransferases are expressed in bacteria, and the method uses a low cost sulfo donor, it can be readily utilized to synthesize large quantities of anticoagulant heparin drug or other biologically active heparan sulfates.	Heparitin Sulfate	103-118	serpin family C member 1	Homo sapiens	191-203
16344381-11	2005	These data suggest that LMWH should be the preferred antithrombin in this setting.	Heparin, Low-Molecular-Weight	24-28	serpin family C member 1	Homo sapiens	53-65
16305899-12	2005	International normalized ratio (p = 0.03) and antithrombin III (p = 0.04) levels were elevated during CPB in the CCPB group, most likely owing to differences of the intraoperative anticoagulation management.	ccpb	113-117	serpin family C member 1	Homo sapiens	46-62
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
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.	Polyethylene Glycols	86-89	serpin family C member 1	Homo sapiens	5-10
16109780-3	2005	Fondaparinux, a synthetic anticoagulant modeled after the antithrombin-binding pentasaccharide, is believed to be nonimmunogenic.	pentasaccharide	79-94	serpin family C member 1	Homo sapiens	58-70
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
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
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
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
16128566-0	2005	Importance of tryptophan 49 of antithrombin in heparin binding and conformational activation.	Tryptophan	14-24	serpin family C member 1	Homo sapiens	31-43
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
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.	Tryptophan	0-10	serpin family C member 1	Homo sapiens	17-29
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
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
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
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
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.	pentasaccharide	113-128	serpin family C member 1	Homo sapiens	55-67
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
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
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
16078853-0	2005	Mechanism of poly(acrylic acid) acceleration of antithrombin inhibition of thrombin: implications for the design of novel heparin mimics.	carbopol 940	13-31	serpin family C member 1	Homo sapiens	48-60
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
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
16078853-2	2005	Our recent study of the antithrombin-activating properties of a carboxylic acid-based polymer, poly(acrylic acid) (PAA), demonstrated a surprisingly high acceleration in thrombin inhibition (Monien, B. H.; Desai, U. R. J. Med.	carboxylic acid-based polymer	64-93	serpin family C member 1	Homo sapiens	24-36
16078853-2	2005	Our recent study of the antithrombin-activating properties of a carboxylic acid-based polymer, poly(acrylic acid) (PAA), demonstrated a surprisingly high acceleration in thrombin inhibition (Monien, B. H.; Desai, U. R. J. Med.	carbopol 940	95-113	serpin family C member 1	Homo sapiens	24-36
16078853-2	2005	Our recent study of the antithrombin-activating properties of a carboxylic acid-based polymer, poly(acrylic acid) (PAA), demonstrated a surprisingly high acceleration in thrombin inhibition (Monien, B. H.; Desai, U. R. J. Med.	carbopol 940	115-118	serpin family C member 1	Homo sapiens	24-36
16078853-6	2005	Competitive binding studies with low-affinity heparin and a heparin tetrasaccharide suggest that PAA binds antithrombin in both the pentasaccharide- and the extended heparin-binding sites, and these results are corroborated by molecular modeling.	heparin tetrasaccharide	60-83	serpin family C member 1	Homo sapiens	107-119
16078853-6	2005	Competitive binding studies with low-affinity heparin and a heparin tetrasaccharide suggest that PAA binds antithrombin in both the pentasaccharide- and the extended heparin-binding sites, and these results are corroborated by molecular modeling.	carbopol 940	97-100	serpin family C member 1	Homo sapiens	107-119
16078853-6	2005	Competitive binding studies with low-affinity heparin and a heparin tetrasaccharide suggest that PAA binds antithrombin in both the pentasaccharide- and the extended heparin-binding sites, and these results are corroborated by molecular modeling.	pentasaccharide	132-147	serpin family C member 1	Homo sapiens	107-119
16078853-7	2005	The salt-dependence of the K(D) of the PAA-antithrombin interaction shows the formation of five ionic interactions.	Salts	4-8	serpin family C member 1	Homo sapiens	43-55
16078853-9	2005	A bell-shaped profile of the observed rate constant for antithrombin inhibition of thrombin as a function of PAA concentration was observed, suggesting that inhibition proceeds through the "bridging" mechanism.	carbopol 940	109-112	serpin family C member 1	Homo sapiens	56-68
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
16277716-12	2005	Low antithrombin concentrations before certoparin were independently correlated with underdosing of certoparin.	certoparin	100-110	serpin family C member 1	Homo sapiens	4-16
16202731-6	2005	Compared with placebo, raloxifene 60 mg decreased total protein S (-8.2%, P = .009) after 4 weeks and antithrombin (-6.0%, P = .034) and fibrinogen (-18.1%, P = .007) after 12 weeks.	Raloxifene Hydrochloride	23-33	serpin family C member 1	Homo sapiens	102-114
16145710-1	2005	The glycan structures of the major and more than ten minor populated isoforms of antithrombin (AT) were determined after separation of the isoforms by IEF using IPG strips.	Polysaccharides	4-10	serpin family C member 1	Homo sapiens	81-93
16145710-1	2005	The glycan structures of the major and more than ten minor populated isoforms of antithrombin (AT) were determined after separation of the isoforms by IEF using IPG strips.	2-Isopropoxyethanol	161-164	serpin family C member 1	Homo sapiens	81-93
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
16085538-4	2005	Fondaparinux is a novel synthetic heparin pentasaccharide capable of inhibiting factor Xa via the action of antithrombin (AT) but devoid of anti-factor IIa (thrombin) activity.	IC 831423	34-57	serpin family C member 1	Homo sapiens	108-120
16102051-2	2005	Novel parenteral agents include synthetic analogs of the pentasaccharide sequence of heparin that mediates its interaction with antithrombin.	pentasaccharide	57-72	serpin family C member 1	Homo sapiens	128-140
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
15967359-0	2005	QCM-FIA with PGMA coating for dynamic interaction study of heparin and antithrombin III.	polyglycidyl methacrylate	13-17	serpin family C member 1	Homo sapiens	71-87
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).	polyglycidyl methacrylate	68-95	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).	polyglycidyl methacrylate	68-95	serpin family C member 1	Homo sapiens	354-360
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).	pgma) polymer	97-110	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).	pgma) polymer	97-110	serpin family C member 1	Homo sapiens	354-360
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
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, Low-Molecular-Weight	25-29	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, Low-Molecular-Weight	25-29	serpin family C member 1	Homo sapiens	83-88
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
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, Low-Molecular-Weight	318-322	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, Low-Molecular-Weight	318-322	serpin family C member 1	Homo sapiens	83-88
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, Low-Molecular-Weight	318-322	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, Low-Molecular-Weight	318-322	serpin family C member 1	Homo sapiens	83-88
15970714-0	2005	Antithrombin efficiency is maintained in vitro in human plasma following dilution with hydroxyethyl starches.	hydroxyethyl starches	87-108	serpin family C member 1	Homo sapiens	0-12
16022574-2	2005	It is a chemically synthesised pentasaccharide mimicking the site of heparin that binds to antithrombin.	pentasaccharide	31-46	serpin family C member 1	Homo sapiens	91-103
16013610-1	2005	The paper presents data on the primary structure of the glycan variants present in human antithrombin (AT) isoforms obtained from a plasma pool.	Polysaccharides	56-62	serpin family C member 1	Homo sapiens	89-101
16013610-1	2005	The paper presents data on the primary structure of the glycan variants present in human antithrombin (AT) isoforms obtained from a plasma pool.	Polysaccharides	56-62	serpin family C member 1	Homo sapiens	103-105
16013610-8	2005	In total, the variability in the carbohydrate structure of plasma derived AT appears as being quite limited.	Carbohydrates	33-45	serpin family C member 1	Homo sapiens	74-76
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
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
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
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
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
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).	pentasaccharide	100-115	serpin family C member 1	Homo sapiens	58-74
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).	sr123781	188-196	serpin family C member 1	Homo sapiens	58-74
16142016-5	2005	Furthermore, repaglinide administration resulted in a significant decrease in fasting plasma free fatty acids, fibrinogen, thrombin-antithrombin complex and reaction product of malondialdehyde with thiobarbituric acid (TBARS) levels, in absence of significant difference in fasting plasma insulin levels.	repaglinide	13-24	serpin family C member 1	Homo sapiens	132-144
16142016-8	2005	At time 120" of meal test, repaglinide vs glimepiride administration was associated with a significant decline in plasma triglycerides, free fatty acids, fibrinogen, Plasminogen Activator Inhibitor-1, plasmin-alpha(2)-antiplasmin complex, thrombin-antithrombin complex, TBARS levels and increase in plasma HDL-cholesterol levels.	repaglinide	27-38	serpin family C member 1	Homo sapiens	248-260
15957976-2	2005	It is one of a group of glycosaminoglycan compounds that accelerate the inactivation of factor Xa by inducing a conformational change in antithrombin.	Glycosaminoglycans	24-41	serpin family C member 1	Homo sapiens	137-149
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, Low-Molecular-Weight	26-30	serpin family C member 1	Homo sapiens	0-12
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
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.	Enoxaparin	204-214	serpin family C member 1	Homo sapiens	0-12
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
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).	Citric Acid	124-131	serpin family C member 1	Homo sapiens	39-55
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
15882280-6	2005	Moreover, after adjustment for antithrombin-III levels and illness severity score, the relative risk of hemorrhage with citrate anticoagulation was significantly lower than that with heparin (relative risk of 0.14; 95% CI 0.02 to 0.96, P= 0.05).	Citric Acid	120-127	serpin family C member 1	Homo sapiens	31-47
16052399-5	2005	Eight women with pregnancy-induced antithrombin deficiency, including three women with gestational thrombocytopenia, were significantly more likely to develop perinatal elevations of AST, lactate dehydrogenase, serum creatinine, fibrin/fibrinogen degradation products, and D-dimer than were those without pregnancy-induced antithrombin deficiency.	Creatinine	217-227	serpin family C member 1	Homo sapiens	35-47
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Heparitin Sulfate	97-113	serpin family C member 1	Homo sapiens	63-75
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Heparitin Sulfate	97-113	serpin family C member 1	Homo sapiens	148-160
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Superoxides	199-215	serpin family C member 1	Homo sapiens	63-75
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Superoxides	199-215	serpin family C member 1	Homo sapiens	148-160
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Adenosine Diphosphate	262-283	serpin family C member 1	Homo sapiens	63-75
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Adenosine Diphosphate	262-283	serpin family C member 1	Homo sapiens	148-160
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Adenosine Triphosphate	288-310	serpin family C member 1	Homo sapiens	63-75
15968398-3	2005	In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets.	Adenosine Triphosphate	288-310	serpin family C member 1	Homo sapiens	148-160
15968398-4	2005	Adenosine triphosphate-induced platelet aggregation is reduced after treatment of platelets with antithrombin, which is reversed by blockade of syndecan-4.	Adenosine Triphosphate	0-22	serpin family C member 1	Homo sapiens	97-109
15968398-5	2005	We further observed that antithrombin limits CD40 ligand expression in adenosine diphosphate-activated platelets and inhibits the shedding of syndecan-4 from activated platelets.	Adenosine Diphosphate	71-92	serpin family C member 1	Homo sapiens	25-37
15968398-7	2005	We suggest that antithrombin might exert beneficial effects in disseminated intravascular coagulation by reducing platelet activation, observed as inhibited CD40 ligand expression, syndecan-4 shedding, and adenosine diphosphate- and adenosine triphosphate-release from activated platelets with subsequent inhibition of neutrophil respiratory burst.	Adenosine Diphosphate	206-227	serpin family C member 1	Homo sapiens	16-28
15968398-7	2005	We suggest that antithrombin might exert beneficial effects in disseminated intravascular coagulation by reducing platelet activation, observed as inhibited CD40 ligand expression, syndecan-4 shedding, and adenosine diphosphate- and adenosine triphosphate-release from activated platelets with subsequent inhibition of neutrophil respiratory burst.	triphosphoric acid	243-255	serpin family C member 1	Homo sapiens	16-28
15968411-0	2005	Inihibition of cytokine response by methylprednisolone attenuates antithrombin reduction following hepatic resection.	Methylprednisolone	36-54	serpin family C member 1	Homo sapiens	66-78
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
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
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
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.	Iduronic Acid	181-194	serpin family C member 1	Homo sapiens	119-125
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
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.	Enoxaparin	141-151	serpin family C member 1	Homo sapiens	53-65
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
16124953-9	2005	A nonsignificant trend toward higher rates of major bleeding was seen at 7 days for enoxaparin-treated patients, in both the overall safety population and the population of patients who did not receive antithrombin treatment before randomization, but there was no difference in blood transfusions.	Enoxaparin	84-94	serpin family C member 1	Homo sapiens	202-214
15787598-4	2005	The formation of polymers results in the failure to secrete mutants of other members of the serpin superfamily: antithrombin, C1 inhibitor and alpha1-antichymotrypsin, to cause a plasma deficiency that results in the clinical syndromes of thrombosis, angio-oedema and emphysema respectively.	Polymers	17-25	serpin family C member 1	Homo sapiens	112-124
16161915-11	2005	Both simvastatin and atorvastatin markedly increased AT III (87%, 98%) in comparison to the initial values.	Simvastatin	5-16	serpin family C member 1	Homo sapiens	53-59
15878740-5	2005	Minor amounts of particular a heparan sulfate (&lt; 5% of the total arterial glycosaminoglycans) with high anticoagulant activity were also observed, as assessed by its retention on an antithrombin-affinity column.	Heparitin Sulfate	30-45	serpin family C member 1	Homo sapiens	185-197
15878740-8	2005	One is based on antithrombin activation by the heparan sulfate expressed by the endothelial cells.	Heparitin Sulfate	47-62	serpin family C member 1	Homo sapiens	16-28
16161915-11	2005	Both simvastatin and atorvastatin markedly increased AT III (87%, 98%) in comparison to the initial values.	Atorvastatin	21-33	serpin family C member 1	Homo sapiens	53-59
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
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
15698795-4	2005	Most per-sulfated flavonoids studied are activators of antithrombin for accelerated inhibition of factor Xa, a key enzyme of the blood coagulation cascade.	Flavonoids	18-28	serpin family C member 1	Homo sapiens	55-67
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
15804733-8	2005	Raloxifene decreased the levels of fibrinogen, from 354.7 to 302.0 g/l (p = 0.009) and the levels of antithrombin III, from 102.4 to 98.5% (p = 0.039).	Raloxifene Hydrochloride	0-10	serpin family C member 1	Homo sapiens	101-117
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
15664348-4	2005	The purity of the AT III from this one-step purification is 93% as measured by SDS-PAGE and the protein recovery yield is about 90%.	Sodium Dodecyl Sulfate	79-82	serpin family C member 1	Homo sapiens	18-24
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
15699163-7	2005	Fondaparinux, which is identical with the antithrombin III-binding pentasaccharide in heparin, did not bind to LBP or alter LBP function.	pentasaccharide	67-82	serpin family C member 1	Homo sapiens	42-58
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
15757405-8	2005	They include anti-Xa inhibitors, such as pentasaccharide, and antithrombin inhibitors, such as ximelagatran.	ximelagatran	95-107	serpin family C member 1	Homo sapiens	62-74
15749837-1	2005	Dermatan sulfate mediates the blood coagulation cascade by binding to heparin cofactor II and potentiating the antithrombin activity.	Dermatan Sulfate	0-16	serpin family C member 1	Homo sapiens	111-123
15652173-7	2005	The antithrombin-mediated anti-factor Xa activity of human liver heparan sulfate, however, was much lower than porcine intestinal (pharmaceutical) heparin but was comparable to standard porcine intestinal heparan sulfate.	Heparitin Sulfate	65-80	serpin family C member 1	Homo sapiens	4-16
16156690-1	2005	Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin.	Fondaparinux	0-19	serpin family C member 1	Homo sapiens	108-120
16156690-1	2005	Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin.	Fondaparinux	21-33	serpin family C member 1	Homo sapiens	108-120
16156690-1	2005	Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin.	pentasaccharide	59-74	serpin family C member 1	Homo sapiens	108-120
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
15743473-0	2005	Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis.	Hyaluronic Acid	30-45	serpin family C member 1	Homo sapiens	14-26
15743473-5	2005	Various glycosaminoglycans, including HA, chondroitin sulfate, keratan sulfate, heparin, and heparan, were incubated with human antithrombin III in vitro.	Glycosaminoglycans	8-26	serpin family C member 1	Homo sapiens	128-144
15743473-7	2005	HA concentrations ranging from 250 to 1000 mug/ml significantly blocked the ability of antithrombin to inhibit thrombin in the presence of Ca2+ or Fe3+, and chondroitin A, B and C also reduced this ability under the same conditions but to a lesser extent.	ferric sulfate	147-151	serpin family C member 1	Homo sapiens	87-99
15715496-0	2005	Antithrombin activation by nonsulfated, non-polysaccharide organic polymer.	Polysaccharides	44-58	serpin family C member 1	Homo sapiens	0-12
15715496-1	2005	Accelerated antithrombin inhibition of procoagulant enzymes has been exclusively achieved with polysulfated polysaccharides.	Polysaccharides	108-123	serpin family C member 1	Homo sapiens	12-24
15715496-2	2005	We reasoned that antithrombin activation should be possible with nonsulfated activators based only on carboxylic acid groups.	Carboxylic Acids	102-117	serpin family C member 1	Homo sapiens	17-29
15715496-3	2005	As a proof of the principle, linear poly(acrylic acid)s were found to bind to antithrombin and accelerate inhibition of factor Xa and thrombin.	carbopol 940	36-55	serpin family C member 1	Homo sapiens	78-90
15715496-4	2005	Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators.	Sulfates	58-65	serpin family C member 1	Homo sapiens	86-98
15715496-4	2005	Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators.	Sulfates	58-65	serpin family C member 1	Homo sapiens	217-229
15715496-4	2005	Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators.	carboxylate	199-210	serpin family C member 1	Homo sapiens	86-98
15715496-4	2005	Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators.	carboxylate	199-210	serpin family C member 1	Homo sapiens	217-229
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	15-22	serpin family C member 1	Homo sapiens	33-45
15604328-11	2005	CONCLUSION: Atorvastatin did not change the maximum hyperaemic flow, although it decreased plasma concentrations of antithrombin III, protein C, factor V, tPA, and PAI-1 in patients with heart failure.	Atorvastatin	12-24	serpin family C member 1	Homo sapiens	116-132
15634277-5	2005	The mutation also significantly decreases (i) the catalytic activity of thrombin with a 9-fold reduction in catalytic efficiency of the mutant toward S-2238; (ii) the interaction with benzamidine; (iii) the rate of inhibition by TLCK and antithrombin; and (iv) the rate of hydrolysis of macromolecular substrates (fibrinogen, protein C).	benzamidine	184-195	serpin family C member 1	Homo sapiens	238-250
16218489-4	2005	This is the case of fondaparinux, a pentasaccharide which can interact with antithrombin, thus inhibiting factor Xa.	pentasaccharide	36-51	serpin family C member 1	Homo sapiens	76-88
15608477-8	2005	AT III levels were positively correlated with plasma total cholesterol levels, plasma low density lipoprotein cholesterol levels, plasma triglycerides and D-dimer levels.	Cholesterol	59-70	serpin family C member 1	Homo sapiens	0-6
15608477-8	2005	AT III levels were positively correlated with plasma total cholesterol levels, plasma low density lipoprotein cholesterol levels, plasma triglycerides and D-dimer levels.	Triglycerides	137-150	serpin family C member 1	Homo sapiens	0-6
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
16293985-6	2005	However, the complete loss of thrombin-induced VEGF production upon treatment with argatroban, a derivative of arginine and a potent anticoagulant/antithrombin agent, supports the notion that argatroban serves as a useful therapeutic tool for thrombin-associated pathologic conditions.	argatroban	83-93	serpin family C member 1	Homo sapiens	147-159
16293985-6	2005	However, the complete loss of thrombin-induced VEGF production upon treatment with argatroban, a derivative of arginine and a potent anticoagulant/antithrombin agent, supports the notion that argatroban serves as a useful therapeutic tool for thrombin-associated pathologic conditions.	argatroban	192-202	serpin family C member 1	Homo sapiens	147-159
15567452-0	2005	Pharmacokinetics of UH and LMWH are similar with respect to antithrombin activity.	Heparin, Low-Molecular-Weight	27-31	serpin family C member 1	Homo sapiens	60-72
16521916-5	2005	Statistically significant relationship of AT III activity with age (Spearman"s rho=-0.23; p=0.002), trigliceride level (rho=0.17; p=0.03), Geriatric Depression Scale (rho=-0.17; p=0.03) and Instrumental Activities of Daily Living scale (rho=0.16; p=0.03) was found.	trigliceride	100-112	serpin family C member 1	Homo sapiens	42-48
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
15792676-8	2005	CONCLUSIONS: The correlation between TEG and PT, APTT and antithrombin level supports its value in providing a global measure of haemostasis.	triethylene glycol	37-40	serpin family C member 1	Homo sapiens	58-70
15935830-1	2005	We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103.	Methionine	205-215	serpin family C member 1	Homo sapiens	41-53
15935830-1	2005	We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103.	Methionine	205-215	serpin family C member 1	Homo sapiens	55-57
15935830-1	2005	We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103.	Methionine	217-220	serpin family C member 1	Homo sapiens	41-53
15935830-1	2005	We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103.	Methionine	217-220	serpin family C member 1	Homo sapiens	55-57
15578742-0	2004	Exact molecular mass determination of various forms of native and de-N-glycosylated human plasma-derived antithrombin by means of electrospray ionization ion trap mass spectrometry.	Nitrogen	69-70	serpin family C member 1	Homo sapiens	105-117
15543318-0	2004	Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems.	Oligosaccharides	34-50	serpin family C member 1	Homo sapiens	54-66
15567465-7	2005	For both high and low coagulant challenges, clotting times increased and prothrombin fragment 1.2 and thrombin-antithrombin (TAT) formation decreased with melagatran in a concentration-dependent fashion in umbilical cord and adult plasma.	melagatran	155-165	serpin family C member 1	Homo sapiens	111-123
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
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
15543318-2	2004	The abilities of three synthetic oligosaccharides to accelerate antithrombin inhibition of ten clotting or fibrinolytic proteinases were compared with those of unfractionated, fractionated high-affinity and low-molecular-weight heparins.	Oligosaccharides	33-49	serpin family C member 1	Homo sapiens	64-76
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.	Polyurethanes	30-32	serpin family C member 1	Homo sapiens	102-118
15486847-5	2004	Although the presence of persistent antibody to phospholipids was the most common abnormal finding in the laboratory, evaluation of thrombophilia, cases of low levels of proteins C and S and antithrombin III, and elevated levels of factor VIII and homocysteine were also identified.	Phospholipids	48-61	serpin family C member 1	Homo sapiens	191-207
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.	Polyurethanes	41-43	serpin family C member 1	Homo sapiens	102-118
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.	Phosphorus	5-6	serpin family C member 1	Homo sapiens	102-118
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
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
15456490-7	2004	Interestingly, FXIa(WT) and FXIa-Glu555 cleave the small tripeptide substrate S-2366 with comparable k(cat)s. Modeling indicates that the side chain of Glu555 significantly alters the electrostatic charge around the active site, and would sterically interfere with the interaction between the FXIa S2" site and the P2" residues on factor IX and antithrombin.	tripeptide K-26	57-67	serpin family C member 1	Homo sapiens	345-357
17491674-11	2004	The activity of ATIII was significantly lower in men with CAF/GF ratio &gt;or= 1.17, as compared to those with CAF/GF &lt; 1.17 (105.10 +/- 10.02 vs. 113.42 +/- 10.72 %, p &lt; 0.05).	Leu-Thr	119-121	serpin family C member 1	Homo sapiens	16-21
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.	pentasaccharide	9-24	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.	pentasaccharide	9-24	serpin family C member 1	Homo sapiens	262-274
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
15325299-10	2004	We also focused our attention on di- and tetrasaccharidic species containing the 3-O-sulfated glucosamines taken as markers of the active sites for antithrombin III.	Glucosamine	94-106	serpin family C member 1	Homo sapiens	148-164
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
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
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.	Glycosaminoglycans	34-52	serpin family C member 1	Homo sapiens	66-78
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.	pentasaccharide	85-100	serpin family C member 1	Homo sapiens	66-78
15543318-6	2004	A synthetic hexadecasaccharide, containing both the pentasaccharide sequence and a proteinase binding site, exerts its anticoagulant effect by accelerating antithrombin inactivation of both thrombin and factor Xa to rate constants of approximately 10(6) - 10(7) M(-1).s(-1), although thrombin appears to be the more important target.	hexadecasaccharide	12-30	serpin family C member 1	Homo sapiens	156-168
15543318-6	2004	A synthetic hexadecasaccharide, containing both the pentasaccharide sequence and a proteinase binding site, exerts its anticoagulant effect by accelerating antithrombin inactivation of both thrombin and factor Xa to rate constants of approximately 10(6) - 10(7) M(-1).s(-1), although thrombin appears to be the more important target.	pentasaccharide	52-67	serpin family C member 1	Homo sapiens	156-168
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.	pentasaccharides	62-78	serpin family C member 1	Homo sapiens	29-41
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
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
15311268-2	2004	We report the crystal structure of the rate-determining encounter complex formed between antithrombin, anhydrothrombin and an optimal synthetic 16-mer oligosaccharide.	16-mer oligosaccharide	144-166	serpin family C member 1	Homo sapiens	89-101
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.	16-mer oligosaccharide	4-26	serpin family C member 1	Homo sapiens	134-146
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.	pentasaccharide	102-117	serpin family C member 1	Homo sapiens	134-146
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
15311268-6	2004	The protein-protein and protein-oligosaccharide interactions together explain the basis for heparin activation of antithrombin as a thrombin inhibitor.	Oligosaccharides	32-47	serpin family C member 1	Homo sapiens	114-126
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
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
15311269-2	2004	Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans.	Glycosaminoglycans	146-164	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
15311269-4	2004	Here we present the crystal structure at a resolution of 2.5 A of the ternary complex between antithrombin, thrombin and a heparin mimetic (SR123781).	sr123781	140-148	serpin family C member 1	Homo sapiens	94-106
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.	pentasaccharide	69-84	serpin family C member 1	Homo sapiens	149-161
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
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, Low-Molecular-Weight	139-143	serpin family C member 1	Homo sapiens	149-161
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
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
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
15326828-6	2004	Pharmaceutic research has developed new drugs, some of which are already on the market, such as fondaparinux, a pentasaccharide that can interact with antithrombin, thus inhibiting factor Xa.	pentasaccharide	112-127	serpin family C member 1	Homo sapiens	151-163
15355575-0	2004	Determination of the stabilizer sucrose in a plasma-derived antithrombin process solution by hydrophilic interaction chromatography with evaporative light-scattering detection.	Sucrose	32-39	serpin family C member 1	Homo sapiens	60-72
15355575-3	2004	A process sample of antithrombin (Atenativ) from Octapharma AB (Stockholm, Sweden) containing 20% sucrose is analyzed.	Sucrose	98-105	serpin family C member 1	Homo sapiens	20-32
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
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.	Enoxaparin	65-75	serpin family C member 1	Homo sapiens	106-118
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
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
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
15219196-0	2004	Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin.	1-Carboxyglutamic Acid	12-38	serpin family C member 1	Homo sapiens	116-128
15219196-0	2004	Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin.	Calcium	87-94	serpin family C member 1	Homo sapiens	116-128
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
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
15219196-8	2004	These results support a theory that mutating individual Gla residues in FXa alters the calcium-induced conformational changes in the Gla region and affects the antithrombin-heparin inhibition reaction.	Glutamic Acid	56-59	serpin family C member 1	Homo sapiens	160-172
15219196-8	2004	These results support a theory that mutating individual Gla residues in FXa alters the calcium-induced conformational changes in the Gla region and affects the antithrombin-heparin inhibition reaction.	Calcium	87-94	serpin family C member 1	Homo sapiens	160-172
15372880-1	2004	A new assay based on using an original chromogenic substrate (z-Ala-Ala-Arg-pNa) and designed for the determination of antithrombin III is described in the paper.	z-ala-ala-arg	62-75	serpin family C member 1	Homo sapiens	119-135
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
15060080-1	2004	Heparan sulfate interacts with antithrombin, a protease inhibitor, to regulate blood coagulation.	Heparitin Sulfate	0-15	serpin family C member 1	Homo sapiens	31-43
15317404-3	2004	Fondaparinux, a new, synthetic pentasaccharide, binds to antithrombin III and potentiates antithrombin III"s inhibition of factor Xa.	pentasaccharide	31-46	serpin family C member 1	Homo sapiens	57-73
15317404-3	2004	Fondaparinux, a new, synthetic pentasaccharide, binds to antithrombin III and potentiates antithrombin III"s inhibition of factor Xa.	pentasaccharide	31-46	serpin family C member 1	Homo sapiens	90-106
15199558-0	2004	A synthetic antithrombin III binding pentasaccharide is now a drug!	pentasaccharide	37-52	serpin family C member 1	Homo sapiens	12-28
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.	pentasaccharide	51-66	serpin family C member 1	Homo sapiens	107-123
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.	pentasaccharide	51-66	serpin family C member 1	Homo sapiens	125-131
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
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
15199558-5	2004	The resulting antithrombotic drug arixtra, which went on the market in the USA and Europe in 2002, shows superior antithrombotic activity and brings about AT-III-mediated activity against factor Xa exclusively.	Fondaparinux	34-41	serpin family C member 1	Homo sapiens	155-161
15199558-6	2004	Structure-based design has subsequently led to analogues with longer-lasting activity, such as idraparinux, as well as novel conjugates and long oligosaccharides with specific anti-Xa and antithrombin activities.	Oligosaccharides	145-161	serpin family C member 1	Homo sapiens	188-200
15060080-3	2004	This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin.	Phosphoadenosine Phosphosulfate	54-91	serpin family C member 1	Homo sapiens	235-247
15060080-3	2004	This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin.	Glucosamine	118-129	serpin family C member 1	Homo sapiens	235-247
15060080-3	2004	This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin.	3-o-sulfo glucosamine	150-171	serpin family C member 1	Homo sapiens	235-247
15060080-3	2004	This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin.	Heparitin Sulfate	216-231	serpin family C member 1	Homo sapiens	235-247
15186640-6	2004	We believe that malabsorption of vitamin K dependent proteins C, S and antithrombin due to bariatric surgery predisposed the patient to purpura fulminans and disseminated intravascular coagulation.	Vitamin K	33-42	serpin family C member 1	Homo sapiens	71-83
15164384-1	2004	Antithrombin (AT), the most important coagulation serine proteases inhibitor, plays an important role in maintaining the hemostatic balance.	Serine	50-56	serpin family C member 1	Homo sapiens	0-12
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
15140129-0	2004	Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis.	Disulfides	71-80	serpin family C member 1	Homo sapiens	35-47
15140129-11	2004	The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop.	Disulfides	69-78	serpin family C member 1	Homo sapiens	13-25
15140129-11	2004	The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop.	Disulfides	69-78	serpin family C member 1	Homo sapiens	102-114
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
14996843-0	2004	Antithrombin-mediated anticoagulant activity of sulfated polysaccharides: different mechanisms for heparin and sulfated galactans.	Polysaccharides	57-72	serpin family C member 1	Homo sapiens	0-12
14996843-7	2004	4) Possibly, it is the bulk structure of the sulfated galactan, and not a specific minor component as in heparin, that determines its interaction with antithrombin.	Galactans	54-62	serpin family C member 1	Homo sapiens	151-163
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
14996843-14	2004	The conformational activation of antithrombin and the consequent formation of a covalent complex with thrombin appear to be less important for the anticoagulant activity of sulfated galactan than for heparin.	Galactans	182-190	serpin family C member 1	Homo sapiens	33-45
14996843-15	2004	Our results demonstrate that the paradigm of heparin-antithrombin interaction cannot be extended to other sulfated polysaccharides.	Polysaccharides	115-130	serpin family C member 1	Homo sapiens	53-65
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
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
15162900-10	2004	Direct thrombin inhibitors, such as argatroban, seem to be suitable alternatives for acute anticoagulation in patients with antithrombin deficiency.	argatroban	36-46	serpin family C member 1	Homo sapiens	124-136
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, Low-Molecular-Weight	122-126	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
15931699-1	2004	AIM: To analyse the correlation between coagulation tests (PT APTT fibrinogen, D-dimer) and albumin with AT-II in DHF as well to find the formula to calculate AT-III with the parameter of coagulation tests and albumin.	dhf	114-117	serpin family C member 1	Homo sapiens	159-165
15210403-13	2004	In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity.	Heparin, Low-Molecular-Weight	18-22	serpin family C member 1	Homo sapiens	157-169
15210403-13	2004	In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity.	Dalteparin	24-34	serpin family C member 1	Homo sapiens	157-169
15210403-13	2004	In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity.	Enoxaparin	36-46	serpin family C member 1	Homo sapiens	157-169
15210403-13	2004	In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity.	Nadroparin	48-58	serpin family C member 1	Homo sapiens	157-169
15931699-5	2004	RESULTS: A significant correlation was found between PT and AT-III (r= -0.631; p=0.000), between D-dimer and AT-III (r= -0.337; p=0.021) and between albumin and AT-III (r= 0.291; p-0.045).	Platinum	53-55	serpin family C member 1	Homo sapiens	60-66
15931699-8	2004	PT, D-dimer and AT-III were correlated with the grading severity of the DHF.	dhf	72-75	serpin family C member 1	Homo sapiens	16-22
15168893-1	2004	Clinical practice over the past decade has evolved to include new agents, LMWH and synthetic polysaccharides, that bind to and enhance the activity of antithrombin similar to UFH.	Heparin, Low-Molecular-Weight	74-78	serpin family C member 1	Homo sapiens	151-163
15168893-1	2004	Clinical practice over the past decade has evolved to include new agents, LMWH and synthetic polysaccharides, that bind to and enhance the activity of antithrombin similar to UFH.	Polysaccharides	93-108	serpin family C member 1	Homo sapiens	151-163
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
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
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
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
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
15005625-1	2004	A unique pentasaccharide fragment of high-affinity heparin activates antithrombin (AT) to enhance its rate of complex formation with factor Xa (FXa) by 200-300-fold.	pentasaccharide	9-24	serpin family C member 1	Homo sapiens	69-81
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
15171962-1	2004	Argatroban represents the first antithrombin agent that was approved for clinical use.	argatroban	0-10	serpin family C member 1	Homo sapiens	32-44
15259286-0	2004	Low-dose oral combination of 17beta-estradiol and norethisterone acetate in postmenopausal women decreases factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1.	Estradiol	29-45	serpin family C member 1	Homo sapiens	131-143
15259286-0	2004	Low-dose oral combination of 17beta-estradiol and norethisterone acetate in postmenopausal women decreases factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1.	Norethindrone Acetate	50-72	serpin family C member 1	Homo sapiens	131-143
15259286-5	2004	RESULTS: The two low doses of E2-NETA induced significantly lower plasma levels of factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1 (PAI-1), compared with placebo treatmen CONCLUSIONS: Low-dose E2 (1 mg) in combination with NETA resulted in favorable changes of factor VII activity and fibrinogen, compared with placebo.	e2-neta	30-37	serpin family C member 1	Homo sapiens	107-119
15259286-5	2004	RESULTS: The two low doses of E2-NETA induced significantly lower plasma levels of factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1 (PAI-1), compared with placebo treatmen CONCLUSIONS: Low-dose E2 (1 mg) in combination with NETA resulted in favorable changes of factor VII activity and fibrinogen, compared with placebo.	Norethindrone Acetate	33-37	serpin family C member 1	Homo sapiens	107-119
14694355-7	2004	Specifically mutant alleles of antithrombin, C1-inhibitor and alpha(1)-antichymotrypsin have been reported that favour the spontaneous formation of polymers and the retention of protein within hepatocytes.	Polymers	148-156	serpin family C member 1	Homo sapiens	31-43
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
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
14705167-12	2004	synthetic non-sugar antithrombin activators.	Sugars	14-19	serpin family C member 1	Homo sapiens	20-32
14623882-0	2004	The influence of hinge region residue Glu-381 on antithrombin allostery and metastability.	Glutamic Acid	38-41	serpin family C member 1	Homo sapiens	49-61
14623882-1	2004	Antithrombin becomes an efficient inhibitor of factor Xa and thrombin by binding a specific pentasaccharide sequence found on a small fraction of the heparan sulfate proteoglycans lining the microvaculature.	pentasaccharide	92-107	serpin family C member 1	Homo sapiens	0-12
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
14759471-3	2004	In our case, due to the poor reversibility of the antithrombin agents, argatroban was chosen as a heparin substitute due to its short half-life and its anticoagulation assessment using the activated clotting time (ACT).	argatroban	71-81	serpin family C member 1	Homo sapiens	50-62
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
15000687-2	2004	Heparin and pentosan polysulfate stabilized antithrombin III; this resulted in decrease in ultrasonic-induced formation of the aggregate and latent forms.	Pentosan Sulfuric Polyester	12-32	serpin family C member 1	Homo sapiens	44-60
15171962-3	2004	Unlike the other antithrombin drugs, such as hirudins and hirulogs, argatroban is a reversible antithrombin agent and therefore exhibits a considerably different pharmacological profile.	argatroban	68-78	serpin family C member 1	Homo sapiens	17-29
15171962-3	2004	Unlike the other antithrombin drugs, such as hirudins and hirulogs, argatroban is a reversible antithrombin agent and therefore exhibits a considerably different pharmacological profile.	argatroban	68-78	serpin family C member 1	Homo sapiens	95-107
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
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
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
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
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.	Polysaccharides	161-175	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	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
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).	pentasaccharide	43-58	serpin family C member 1	Homo sapiens	124-136
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.	IC 831423	336-359	serpin family C member 1	Homo sapiens	94-106
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).	Sugars	88-93	serpin family C member 1	Homo sapiens	124-136
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
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
14730971-10	2004	Together, these findings show that N-terminal residues of antithrombin make markedly different contributions to the energetics and dynamics of binding of the pentasaccharide ligand to the native and activated conformational states of the inhibitor that could not have been predicted from the X-ray structure.	pentasaccharide	158-173	serpin family C member 1	Homo sapiens	58-70
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
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).	Iduronic Acid	18-31	serpin family C member 1	Homo sapiens	214-230
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).	Glycosaminoglycans	43-61	serpin family C member 1	Homo sapiens	214-230
15233593-1	2004	Fondaparinux sodium (Arixtra; fondaparinux) is the first of a new class of synthetic pentasaccharide anticoagulants that bind to antithrombin and inhibit the action of factor Xa.	Fondaparinux	0-19	serpin family C member 1	Homo sapiens	129-141
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).	Glycosaminoglycans	63-66	serpin family C member 1	Homo sapiens	214-230
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).	Dermatan Sulfate	76-92	serpin family C member 1	Homo sapiens	214-230
15233593-1	2004	Fondaparinux sodium (Arixtra; fondaparinux) is the first of a new class of synthetic pentasaccharide anticoagulants that bind to antithrombin and inhibit the action of factor Xa.	Fondaparinux	21-28	serpin family C member 1	Homo sapiens	129-141
15233593-1	2004	Fondaparinux sodium (Arixtra; fondaparinux) is the first of a new class of synthetic pentasaccharide anticoagulants that bind to antithrombin and inhibit the action of factor Xa.	pentasaccharide	85-100	serpin family C member 1	Homo sapiens	129-141