PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
31637210-1	2019	Serpin family D member 1 (SERPIND1) belongs to the serine protease inhibitor family.	cholecystokinin C-terminal flanking peptide	51-57	serpin family D member 1	Homo sapiens	0-24
31637210-1	2019	Serpin family D member 1 (SERPIND1) belongs to the serine protease inhibitor family.	cholecystokinin C-terminal flanking peptide	51-57	serpin family D member 1	Homo sapiens	26-34
31637210-9	2019	The addition of the PI3K/AKT pathway inhibitor LY294002 to SERPIND1-overexpressing cells could reverse the promoting effect of SERPIND1 on the malignant biological behavior of ovarian cancer cells.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	47-55	serpin family D member 1	Homo sapiens	59-67
31637210-9	2019	The addition of the PI3K/AKT pathway inhibitor LY294002 to SERPIND1-overexpressing cells could reverse the promoting effect of SERPIND1 on the malignant biological behavior of ovarian cancer cells.	2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one	47-55	serpin family D member 1	Homo sapiens	127-135
30716452-1	2019	OBJECTIVES: The objective of this randomized controlled trial was to assess the influence of use of posts as well as the type of posterior tooth (premolars vs molars) for the treatment with lithium disilicate (LS2) partial crowns.	Lithium	190-197	serpin family D member 1	Homo sapiens	210-213
30853210-11	2019	RESULTS: DTA and XRD analysis revealed that the transformation of the lithium silicate (LS) phase to the LS2 phase was completed for IPS e.max and Initial LiSi Press ingots while for Celtra Press ingots it was not.	aluminum lithium silicate	70-86	serpin family D member 1	Homo sapiens	105-108
30853210-11	2019	RESULTS: DTA and XRD analysis revealed that the transformation of the lithium silicate (LS) phase to the LS2 phase was completed for IPS e.max and Initial LiSi Press ingots while for Celtra Press ingots it was not.	leucylserine	88-90	serpin family D member 1	Homo sapiens	105-108
31247951-6	2019	We report protein-specific N-glycosylation patterns, including a correlation of core fucosylated structures with immunoglobulin G (IgG) levels, and of trisialylated, trigalactosylated, and triantennary structures with heparin cofactor 2 (SERPIND2).	Nitrogen	27-28	serpin family D member 1	Homo sapiens	218-236
31275456-12	2019	Concerning rs6831280, ANCOVA found BMDs at LS 2-4 (L2-4) and total hip (TH) among the study subjects suffering from SOP with GA genotype were lower than in those carrying GG or AA (P-L2-4 = 0.004 and P-TH = 0.027, respectively).	ancova	22-28	serpin family D member 1	Homo sapiens	43-49
30611633-3	2019	Here, we present a series of N-alkylated styrylquinolinium dyes named Ls-1, Ls-2 and Ls-3 with varying side groups at the chain end.	n-alkylated styrylquinolinium	29-58	serpin family D member 1	Homo sapiens	76-80
30611633-6	2019	Furthermore, confocal fluorescence images and MTT assays indicated dye Ls-2 could pass through membrane and enter the living HepG2 cells with low cytotoxicity.	monooxyethylene trimethylolpropane tristearate	46-49	serpin family D member 1	Homo sapiens	71-75
29551381-2	2018	PURPOSE: The purpose of this in vitro study was to investigate the shear bond strength (SBS) between zirconia core and lithium disilicate (LS2) veneered ceramic after surface pretreatments.	Lithium	119-126	serpin family D member 1	Homo sapiens	139-142
31165103-1	2019	PURPOSE: To investigate the tensile bond strength of silane-containing universal adhesives and self-etch glass-ceramic primer to lithium disilicate glass ceramics (LS2).	Silanes	53-59	serpin family D member 1	Homo sapiens	164-167
31165103-1	2019	PURPOSE: To investigate the tensile bond strength of silane-containing universal adhesives and self-etch glass-ceramic primer to lithium disilicate glass ceramics (LS2).	Lithium	129-136	serpin family D member 1	Homo sapiens	164-167
31165103-10	2019	CONCLUSION: Additional silanization of HF-etched LS2 statistically signficantly improved the tensile bond strength of the silane-containing universal adhesive (Scotchbond Universal).	Silanes	122-128	serpin family D member 1	Homo sapiens	49-52
30150759-7	2018	Second, 13 differentially expressed genes associated with energy and O2 consumption processes under soil flooding had lower transcript levels in LS1 than those in LS2, which might contribute to better energy-/O2-saving abilities and behaviours in flood-tolerant LS1 than those in flood-susceptible LS2 under hypoxic stress.	Oxygen	69-71	serpin family D member 1	Homo sapiens	163-166
30150759-7	2018	Second, 13 differentially expressed genes associated with energy and O2 consumption processes under soil flooding had lower transcript levels in LS1 than those in LS2, which might contribute to better energy-/O2-saving abilities and behaviours in flood-tolerant LS1 than those in flood-susceptible LS2 under hypoxic stress.	Oxygen	69-71	serpin family D member 1	Homo sapiens	298-301
29551381-14	2018	CONCLUSIONS: The bond strength between zirconia and veneering LS2 was significantly increased by application of silica-containing glass-ceramic liner but was decreased with airborne-particle abrasion.	Silicon Dioxide	112-118	serpin family D member 1	Homo sapiens	62-65
30302438-11	2018	Lithium disilicate (LS2) occlusal onlays were used to stabilize the VDO, and anterior LS2 and feldspathic veneers, combined with direct composite restorations, were executed to reach the planned minimally invasive result.	Lithium	0-7	serpin family D member 1	Homo sapiens	20-23
27301751-1	2016	Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma.	Heparin	15-22	serpin family D member 1	Homo sapiens	92-96
28729537-1	2017	Crystalline lithium disilicate (Li2Si2O5, LS2) materials, which have excellent mechanical properties with high transparency, should be obtained efficiently through the crystallization of supercooled liquid composed of LS2.	li2si2o5	32-40	serpin family D member 1	Homo sapiens	218-221
28093860-0	2017	Monolithic implant-supported lithium disilicate (LS2) crowns in a complete digital workflow: A prospective clinical trial with a 2-year follow-up.	Lithium	29-36	serpin family D member 1	Homo sapiens	49-52
28093860-2	2017	PURPOSE: The aim of this prospective clinical trial was to analyze the treatment concept of monolithic lithium disilicate (LS2) single-unit restorations in a complete digital workflow.	Lithium	103-110	serpin family D member 1	Homo sapiens	123-126
28124818-0	2017	A Hexasaccharide Containing Rare 2-O-Sulfate-Glucuronic Acid Residues Selectively Activates Heparin Cofactor II.	hexasaccharide	2-16	serpin family D member 1	Homo sapiens	92-111
28124818-0	2017	A Hexasaccharide Containing Rare 2-O-Sulfate-Glucuronic Acid Residues Selectively Activates Heparin Cofactor II.	2-o-sulfate	33-44	serpin family D member 1	Homo sapiens	92-111
28124818-0	2017	A Hexasaccharide Containing Rare 2-O-Sulfate-Glucuronic Acid Residues Selectively Activates Heparin Cofactor II.	Glucuronic Acid	45-60	serpin family D member 1	Homo sapiens	92-111
28124818-2	2017	Using a computational strategy on a library of 46 656 heparan sulfate hexasaccharides we identified a rare sequence consisting of consecutive glucuronic acid 2-O-sulfate residues as selectively targeting HCII.	heparan sulfate hexasaccharides	54-85	serpin family D member 1	Homo sapiens	204-208
28124818-2	2017	Using a computational strategy on a library of 46 656 heparan sulfate hexasaccharides we identified a rare sequence consisting of consecutive glucuronic acid 2-O-sulfate residues as selectively targeting HCII.	glucuronic acid 2-o-sulfate	142-169	serpin family D member 1	Homo sapiens	204-208
28124818-6	2017	This group of rare designed hexasaccharides will help understand HCII function.	hexasaccharides	28-43	serpin family D member 1	Homo sapiens	65-69
27783757-2	2016	This study evaluated the performance, usefulness, and operational suitability of the Digene Hybrid Capture II (HCII) CT-ID DNA-test as an opportunistic screening tool to detect C. trachomatis in the public health system in Manaus, Amazonas State.	aluminum hydroxide, magnesium hydroxide, drug combination	85-91	serpin family D member 1	Homo sapiens	111-115
27301751-1	2016	Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma.	Heparin	24-27	serpin family D member 1	Homo sapiens	92-96
26076831-1	2015	BACKGROUND: Elucidating the microstructural responses of the lithium disilicate system like the popular IPS e.max  CAD (LS2), made specifically for computer-aided design and computer-aided manufacturing (CAD-CAM), as a temperature-dependent system unravels new ways to enhance material properties and performance.	Lithium	61-68	serpin family D member 1	Homo sapiens	120-123
27430660-10	2016	Finally, SERPIND1 (HCII) was validated at the protein level by immunohistochemistry in 107 paraffin-embedded ovarian tissues.	Paraffin	91-99	serpin family D member 1	Homo sapiens	9-17
27430660-10	2016	Finally, SERPIND1 (HCII) was validated at the protein level by immunohistochemistry in 107 paraffin-embedded ovarian tissues.	Paraffin	91-99	serpin family D member 1	Homo sapiens	19-23
29638072-7	2016	It was found that LS2 tablets containing spherically granulated dibasic calcium phosphate and magnesium aluminometasilicate exhibit the best dissolution profile and mechanical properties while tablets composed only with Neusilin  US2 was characterized by the smallest size and mass with preserved good mechanical properties and furosemide dissolution.	dibasic	64-71	serpin family D member 1	Homo sapiens	18-21
29638072-7	2016	It was found that LS2 tablets containing spherically granulated dibasic calcium phosphate and magnesium aluminometasilicate exhibit the best dissolution profile and mechanical properties while tablets composed only with Neusilin  US2 was characterized by the smallest size and mass with preserved good mechanical properties and furosemide dissolution.	calcium phosphate	72-89	serpin family D member 1	Homo sapiens	18-21
25130770-7	2015	We further showed that HCII could up-regulate cancer cell migration through the activation of PI3K, which acts upstream of Rac1 and Cdc42, and this effect could be blocked by heparin.	Heparin	175-182	serpin family D member 1	Homo sapiens	23-27
25130770-8	2015	We suggest that HCII is a novel metastasis enhancer and may be used as a prognostic predictor for heparin treatment in NSCLC.	Heparin	98-105	serpin family D member 1	Homo sapiens	16-20
23915851-4	2013	RESULTS: Those with the ESR1 Crs1884054 allele were found to have a lower BMD at LS2-4/Lateral view (p = 0.005 and permutated p = 0.046), and those with the ESR1 haplotype Trs2234693-Ars922996 had a higher risk for low BMD also at LS2-4/Lat (OR = 1.8, 95% CI = 1.1-2.9).	crs1884054	29-39	serpin family D member 1	Homo sapiens	81-86
25268825-4	2014	Variation of nano-sized PS sphere number within the interstitial voids formed between neighbouring macro-sized spheres enabled the reproducible fabrication of LS2 and LS6 structures, which contain 1 and 3 nano-spheres respectively in each interstitial void.	Polystyrenes	24-26	serpin family D member 1	Homo sapiens	159-162
24950623-6	2014	We found HCII remain nested in the largest intron of phosphatidylinositol (PI) 4-kinase (PIK4CA) gene (genetic variants of this gene cause schizophrenia) at the origin of vertebrates, dated about 500MY old.	Phosphatidylinositols	53-73	serpin family D member 1	Homo sapiens	9-13
25104919-3	2014	The current work benchmarks the SCC-DFTB/MM method against more accurate DFT/MM by simulating PT in a synthetic leucine-serine channel (LS2), which emulates the structure and function of biomolecular proton channels.	dftb	36-40	serpin family D member 1	Homo sapiens	136-139
25104919-3	2014	The current work benchmarks the SCC-DFTB/MM method against more accurate DFT/MM by simulating PT in a synthetic leucine-serine channel (LS2), which emulates the structure and function of biomolecular proton channels.	Platinum	94-96	serpin family D member 1	Homo sapiens	136-139
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	86-105
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	107-111
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	86-105
22987196-1	2013	Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II (HCII) to enhance thrombin inhibition.	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	107-111
22857008-1	2012	CONTEXT: Neolignans are usually dimers formed by oxidative coupling of allyl and propenyl phenols, and the neolignan analogue, 2-phenoxy-1-phenylethanone (LS-2) is a promising antimycobacterial compound showing very weak cytotoxicity in mammalian cells and lack of acute toxicity in murine models.	Lignans	9-19	serpin family D member 1	Homo sapiens	155-159
22857008-1	2012	CONTEXT: Neolignans are usually dimers formed by oxidative coupling of allyl and propenyl phenols, and the neolignan analogue, 2-phenoxy-1-phenylethanone (LS-2) is a promising antimycobacterial compound showing very weak cytotoxicity in mammalian cells and lack of acute toxicity in murine models.	Lignans	107-116	serpin family D member 1	Homo sapiens	155-159
22857008-1	2012	CONTEXT: Neolignans are usually dimers formed by oxidative coupling of allyl and propenyl phenols, and the neolignan analogue, 2-phenoxy-1-phenylethanone (LS-2) is a promising antimycobacterial compound showing very weak cytotoxicity in mammalian cells and lack of acute toxicity in murine models.	2-phenoxy-1-phenylethanone	127-153	serpin family D member 1	Homo sapiens	155-159
22857008-3	2012	MATERIALS AND METHODS: Hepatocytes were treated with LS-2 from 0.05 up to 1 mM, for 24 and 48 h, and reduced glutathione (GSH), lipid peroxidation and cytochrome P450 enzyme (CYP450) activity were assayed.	Glutathione	109-120	serpin family D member 1	Homo sapiens	53-57
21805439-6	2011	In particular, HCII binds many glycosaminoglycans (GAGs) such as heparin and heparin sulfate as well as several different polyanions to enhance its inhibition of thrombin.	Glycosaminoglycans	31-49	serpin family D member 1	Homo sapiens	15-19
21854223-3	2012	Polymeric microparticles containing the synthetic analogue of neolignan, 1-phenyl-2-phenoxiethanone (LS-2), were obtained by a method of emulsification and solvent evaporation and chemically characterized.	Lignans	62-71	serpin family D member 1	Homo sapiens	101-105
21854223-3	2012	Polymeric microparticles containing the synthetic analogue of neolignan, 1-phenyl-2-phenoxiethanone (LS-2), were obtained by a method of emulsification and solvent evaporation and chemically characterized.	1-phenyl-2-phenoxiethanone	73-99	serpin family D member 1	Homo sapiens	101-105
22206940-1	2012	Thrombin inactivation by heparin cofactor II (HCII) is accelerated by ternary complex formation with heparin.	Heparin	25-32	serpin family D member 1	Homo sapiens	46-50
22206940-8	2012	These studies demonstrate that binding of HCII to the thrombin heparin complex is dramatically enhanced compared with heparin binding alone and that exosite I is still available for ligand or HCII binding when both heparin binding sites on thrombin are saturated.	Heparin	63-70	serpin family D member 1	Homo sapiens	42-46
21805439-6	2011	In particular, HCII binds many glycosaminoglycans (GAGs) such as heparin and heparin sulfate as well as several different polyanions to enhance its inhibition of thrombin.	Heparin	65-72	serpin family D member 1	Homo sapiens	15-19
21805439-6	2011	In particular, HCII binds many glycosaminoglycans (GAGs) such as heparin and heparin sulfate as well as several different polyanions to enhance its inhibition of thrombin.	Heparitin Sulfate	77-92	serpin family D member 1	Homo sapiens	15-19
21805439-7	2011	Distinctly, HCII is able to use the GAG dermatan sulfate for accelerated thrombin inhibition.	gag dermatan sulfate	36-56	serpin family D member 1	Homo sapiens	12-16
21805439-10	2011	Additionally, pharmaceuticals are being developed that use the dermatan sulfate activation of HCII for anticoagulation.	Dermatan Sulfate	63-79	serpin family D member 1	Homo sapiens	94-98
19414859-2	2009	Heparin cofactor II (HCII)-dependent and -independent mechanisms for DHG inhibition of plasma thrombin generation were evaluated.	dhg	69-72	serpin family D member 1	Homo sapiens	0-19
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Heparin	63-70	serpin family D member 1	Homo sapiens	84-88
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	182-198	serpin family D member 1	Homo sapiens	63-82
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	182-198	serpin family D member 1	Homo sapiens	84-88
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	200-202	serpin family D member 1	Homo sapiens	63-82
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Dermatan Sulfate	200-202	serpin family D member 1	Homo sapiens	84-88
20670608-7	2010	Second-order rate constants for thrombin inactivation by recombinant and deglycosylated HCII were comparable, at optimal GAG concentrations that were lower than those for plasma HCII, consistent with its weaker GAG binding.	Glycosaminoglycans	121-124	serpin family D member 1	Homo sapiens	88-92
20670608-7	2010	Second-order rate constants for thrombin inactivation by recombinant and deglycosylated HCII were comparable, at optimal GAG concentrations that were lower than those for plasma HCII, consistent with its weaker GAG binding.	Glycosaminoglycans	211-214	serpin family D member 1	Homo sapiens	88-92
20670608-8	2010	This weaker binding may be attributed to interference of the Asn(169)N-glycan with the HCII heparin-binding site.	Asparagine	61-64	serpin family D member 1	Homo sapiens	87-91
20670608-8	2010	This weaker binding may be attributed to interference of the Asn(169)N-glycan with the HCII heparin-binding site.	n-glycan	69-77	serpin family D member 1	Homo sapiens	87-91
20053992-5	2010	SOS bound HCII with K(D) 1.45 +/- 0.30 mm, and this binding was tightened in the T.SOS.HCII complex, characterized by K(complex) of approximately 0.20 microm.	sucrose octasulfate	0-3	serpin family D member 1	Homo sapiens	10-14
20053992-5	2010	SOS bound HCII with K(D) 1.45 +/- 0.30 mm, and this binding was tightened in the T.SOS.HCII complex, characterized by K(complex) of approximately 0.20 microm.	sucrose octasulfate	0-3	serpin family D member 1	Homo sapiens	87-91
20053992-9	2010	Thrombin generation in plasma was suppressed by SOS, both in HCII-dependent and -independent processes.	sucrose octasulfate	48-51	serpin family D member 1	Homo sapiens	61-65
20053992-10	2010	The ex vivo HCII-dependent process may utilize the proposed model and suggests a potential for oversulfated disaccharides in controlling HCII-regulated thrombin generation.	Disaccharides	108-121	serpin family D member 1	Homo sapiens	12-16
20053992-10	2010	The ex vivo HCII-dependent process may utilize the proposed model and suggests a potential for oversulfated disaccharides in controlling HCII-regulated thrombin generation.	Disaccharides	108-121	serpin family D member 1	Homo sapiens	137-141
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Glycosaminoglycans	144-162	serpin family D member 1	Homo sapiens	63-82
20670608-1	2010	Irreversible inactivation of alpha-thrombin (T) by the serpin, heparin cofactor II (HCII), is accelerated by ternary complex formation with the glycosaminoglycans (GAGs) heparin and dermatan sulfate (DS).	Glycosaminoglycans	144-162	serpin family D member 1	Homo sapiens	84-88
20053992-0	2010	Sucrose octasulfate selectively accelerates thrombin inactivation by heparin cofactor II.	sucrose octasulfate	0-19	serpin family D member 1	Homo sapiens	69-88
20053992-1	2010	Inactivation of thrombin (T) by the serpins heparin cofactor II (HCII) and antithrombin (AT) is accelerated by a heparin template between the serpin and thrombin exosite II.	Heparin	44-51	serpin family D member 1	Homo sapiens	65-69
20053992-3	2010	Sucrose octasulfate (SOS) accelerated thrombin inactivation by HCII but not AT by 2000-fold.	sucrose octasulfate	0-19	serpin family D member 1	Homo sapiens	63-67
20053992-3	2010	Sucrose octasulfate (SOS) accelerated thrombin inactivation by HCII but not AT by 2000-fold.	sucrose octasulfate	21-24	serpin family D member 1	Homo sapiens	63-67
19414859-2	2009	Heparin cofactor II (HCII)-dependent and -independent mechanisms for DHG inhibition of plasma thrombin generation were evaluated.	dhg	69-72	serpin family D member 1	Homo sapiens	21-25
17890822-11	2007	INTERPRETATION & CONCLUSION: The main utility of HC-II is in the triage of patients with cytology smear diagnosis of ASC-US, ASC-H or L-SIL, for referral to colposcopic examination.	Adenosine Monophosphate	16-19	serpin family D member 1	Homo sapiens	53-58
18971786-2	2008	BACKGROUND: HCII inhibits thrombin activity by binding to dermatan sulfate and has been shown to be a novel and independent risk factor for atherosclerosis.	Dermatan Sulfate	58-74	serpin family D member 1	Homo sapiens	12-16
19456182-1	2009	Lignosulfonic acid (LS1) and partially desulfonated lignosulfonic acid (LS2) were oxidatively deposited on a preactivated glassy carbon (GC) electrode, giving rise to redox active films showing three distinct redox couples at midpeak potentials (E degrees ") of 0.22, 0.44, and 0.53 V (vs Ag/AgCl in 0.1 M H(2)SO(4)).	LIGNOSULFONIC ACID	52-70	serpin family D member 1	Homo sapiens	72-75
19456182-1	2009	Lignosulfonic acid (LS1) and partially desulfonated lignosulfonic acid (LS2) were oxidatively deposited on a preactivated glassy carbon (GC) electrode, giving rise to redox active films showing three distinct redox couples at midpeak potentials (E degrees ") of 0.22, 0.44, and 0.53 V (vs Ag/AgCl in 0.1 M H(2)SO(4)).	Carbon	129-135	serpin family D member 1	Homo sapiens	72-75
19456182-1	2009	Lignosulfonic acid (LS1) and partially desulfonated lignosulfonic acid (LS2) were oxidatively deposited on a preactivated glassy carbon (GC) electrode, giving rise to redox active films showing three distinct redox couples at midpeak potentials (E degrees ") of 0.22, 0.44, and 0.53 V (vs Ag/AgCl in 0.1 M H(2)SO(4)).	silver chloride	292-296	serpin family D member 1	Homo sapiens	72-75
19456182-4	2009	In neutral electrolytes, the LS1- and LS2-modified electrodes behaved as anionic coatings, showing an increase in the charge transfer resistance (R(ct)) for the ferrocyanide/ferricyanide redox couple.	hexacyanoferrate II	161-173	serpin family D member 1	Homo sapiens	38-41
19456182-4	2009	In neutral electrolytes, the LS1- and LS2-modified electrodes behaved as anionic coatings, showing an increase in the charge transfer resistance (R(ct)) for the ferrocyanide/ferricyanide redox couple.	hexacyanoferrate III	174-186	serpin family D member 1	Homo sapiens	38-41
19456182-11	2009	On the other hand, the relative enhancement of this constant caused by the presence of Mg(2+) ions was much higher for LS1-based electrodes than for LS2-based electrodes.	magnesium ion	87-93	serpin family D member 1	Homo sapiens	149-152
18262463-3	2008	The Digene Hybrid Capture II (hcII) assay is the only FDA approved method used in conjunction with cytology for HPV screening of women older than 30.	aluminum hydroxide, magnesium hydroxide, drug combination	4-10	serpin family D member 1	Homo sapiens	30-34
16202803-1	2005	In the present study, a hydrophilic bifunctional polymeric resin (LS-2) with sulfonic groups was synthesized, and the adsorption performance of three aniline compounds, aniline, 4-methylaniline, and 4-nitroaniline onto LS-2 was compared with that on the commercial Amberlite XAD-4.	aniline	150-157	serpin family D member 1	Homo sapiens	66-70
15869786-8	2006	HCII-IIa complexes of all P1 variants were stable in the absence of heparin, but those of the L444K and L444R variants released active IIa over time with heparin.	Heparin	68-75	serpin family D member 1	Homo sapiens	0-4
15869786-8	2006	HCII-IIa complexes of all P1 variants were stable in the absence of heparin, but those of the L444K and L444R variants released active IIa over time with heparin.	Heparin	154-161	serpin family D member 1	Homo sapiens	0-4
15869786-11	2006	This is the first description of HCII-IIa complexes of transient stability forming in the absence of heparin, and may explain the extent to which the reactive centre loop of HCII differs from that of AT.	Heparin	101-108	serpin family D member 1	Homo sapiens	33-37
16450897-8	2005	The same strong differences in sensitivity were observed when both the PCR and HC II methods were studied on the same Papanicolaou stained glass slides, whereas on unstained slides no significant difference was found.	papanicolaou	118-130	serpin family D member 1	Homo sapiens	79-84
16450897-9	2005	CONCLUSION: The results demonstrate that Papanicolaou staining of a cervical smear significantly decreases the sensitivity of an HPV test performed with the HC II method, whereas the PCR method is less affected.	papanicolaou	41-53	serpin family D member 1	Homo sapiens	157-162
16650906-1	2007	BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor.	Dermatan Sulfate	82-98	serpin family D member 1	Homo sapiens	12-31
16650906-1	2007	BACKGROUND: Heparin cofactor II (HCII) could inactivate thrombin after binding to dermatan sulfate at injured arterial walls, and has been shown to be a novel and independent antiatherosclerotic factor.	Dermatan Sulfate	82-98	serpin family D member 1	Homo sapiens	33-37
17222891-4	2007	All these glycosaminoglycans (GAGs) also inhibited thrombin-induced aggregation of washed platelets in the presence of antithrombin (AT) or heparin cofactor II (HCII) but not in their absence.	Glycosaminoglycans	10-28	serpin family D member 1	Homo sapiens	161-165
17222891-6	2007	In the presence of HCII, DSb, a slightly oversulfated DS, had the highest inhibitory effect, whereas heparin and DSd, the most oversulfated derivative, had lower potencies in this case.	1,2-di-(4-sulfamidophenyl)-4-butylpyrazolidine-3,5-dione	25-28	serpin family D member 1	Homo sapiens	19-23
17222891-6	2007	In the presence of HCII, DSb, a slightly oversulfated DS, had the highest inhibitory effect, whereas heparin and DSd, the most oversulfated derivative, had lower potencies in this case.	Dermatan Sulfate	25-27	serpin family D member 1	Homo sapiens	19-23
17222891-7	2007	These data suggest that the inhibition of thrombin-induced platelet aggregation by the oversulfated DS derivatives is related to their ability to potentiate thrombin inactivation by AT or HCII.	Dermatan Sulfate	100-102	serpin family D member 1	Homo sapiens	188-192
16624894-0	2006	N-Acetylgalactosamine 4,6-O-sulfate residues mediate binding and activation of heparin cofactor II by porcine mucosal dermatan sulfate.	n-acetylgalactosamine 4,6-o-sulfate	0-35	serpin family D member 1	Homo sapiens	79-98
16624894-0	2006	N-Acetylgalactosamine 4,6-O-sulfate residues mediate binding and activation of heparin cofactor II by porcine mucosal dermatan sulfate.	Dermatan Sulfate	118-134	serpin family D member 1	Homo sapiens	79-98
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	64-83
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	85-89
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	64-83
16624894-1	2006	Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	85-89
16624894-2	2006	A hexasaccharide consisting of three l-iduronic acid 2-O-sulfate (IdoA2SO3)-->N-acetyl-D-galactosamine 4-O-sulfate (GalNAc4SO3) subunits was previously isolated from porcine skin DS and shown to bind HCII with high affinity.	hexasaccharide	2-16	serpin family D member 1	Homo sapiens	203-207
16624894-3	2006	DS from porcine intestinal mucosa has a much lower content of this disaccharide but activates HCII with potency similar to that of porcine skin DS.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	94-98
16624894-4	2006	Therefore, we sought to characterize oligosaccharides from porcine mucosal DS that interact with HCII.	Oligosaccharides	37-53	serpin family D member 1	Homo sapiens	97-101
16624894-4	2006	Therefore, we sought to characterize oligosaccharides from porcine mucosal DS that interact with HCII.	Dermatan Sulfate	75-77	serpin family D member 1	Homo sapiens	97-101
16624894-7	2006	We found that the smallest oligosaccharides able to bind HCII were hexasaccharides.	Oligosaccharides	27-43	serpin family D member 1	Homo sapiens	57-61
16624894-7	2006	We found that the smallest oligosaccharides able to bind HCII were hexasaccharides.	hexasaccharides	67-82	serpin family D member 1	Homo sapiens	57-61
16624894-10	2006	Decasaccharides and dodecasaccharides containing one or two GalNAc4,6SO3 residues stimulated thrombin inhibition by HCII and prolonged the clotting time of normal but not HCII-depleted human plasma.	decasaccharides	0-15	serpin family D member 1	Homo sapiens	116-120
16624894-10	2006	Decasaccharides and dodecasaccharides containing one or two GalNAc4,6SO3 residues stimulated thrombin inhibition by HCII and prolonged the clotting time of normal but not HCII-depleted human plasma.	dodecasaccharides	20-37	serpin family D member 1	Homo sapiens	116-120
16624894-10	2006	Decasaccharides and dodecasaccharides containing one or two GalNAc4,6SO3 residues stimulated thrombin inhibition by HCII and prolonged the clotting time of normal but not HCII-depleted human plasma.	dodecasaccharides	20-37	serpin family D member 1	Homo sapiens	171-175
16624894-10	2006	Decasaccharides and dodecasaccharides containing one or two GalNAc4,6SO3 residues stimulated thrombin inhibition by HCII and prolonged the clotting time of normal but not HCII-depleted human plasma.	galnac4	60-67	serpin family D member 1	Homo sapiens	116-120
16624894-10	2006	Decasaccharides and dodecasaccharides containing one or two GalNAc4,6SO3 residues stimulated thrombin inhibition by HCII and prolonged the clotting time of normal but not HCII-depleted human plasma.	6so3	68-72	serpin family D member 1	Homo sapiens	116-120
16624894-11	2006	These data support the hypothesis that modification of IdoA-->GalNAc4SO3 subunits in the DS polymer by either 2-O-sulfation of IdoA or 6-O-sulfation of GalNAc can generate molecules with HCII-binding sites and anticoagulant activity.	galnac4so3	65-75	serpin family D member 1	Homo sapiens	190-194
16624894-11	2006	These data support the hypothesis that modification of IdoA-->GalNAc4SO3 subunits in the DS polymer by either 2-O-sulfation of IdoA or 6-O-sulfation of GalNAc can generate molecules with HCII-binding sites and anticoagulant activity.	Dermatan Sulfate	92-94	serpin family D member 1	Homo sapiens	190-194
16624894-11	2006	These data support the hypothesis that modification of IdoA-->GalNAc4SO3 subunits in the DS polymer by either 2-O-sulfation of IdoA or 6-O-sulfation of GalNAc can generate molecules with HCII-binding sites and anticoagulant activity.	N-acetylgalactosaminuronic acid	65-71	serpin family D member 1	Homo sapiens	190-194
16339402-0	2006	Placental dermatan sulfate: isolation, anticoagulant activity, and association with heparin cofactor II.	Dermatan Sulfate	10-26	serpin family D member 1	Homo sapiens	84-103
16339402-4	2006	Dermatan sulfate (DS) specifically activates HCII and is abundant in the placenta, but the locations of DS and HCII in the placenta have not been determined.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	45-49
16339402-4	2006	Dermatan sulfate (DS) specifically activates HCII and is abundant in the placenta, but the locations of DS and HCII in the placenta have not been determined.	Dermatan Sulfate	18-20	serpin family D member 1	Homo sapiens	45-49
16339402-6	2006	DS isolated from human placenta contains disaccharides implicated in activation of HCII and has anticoagulant activity similar to that of mucosal DS.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	83-87
16339402-6	2006	DS isolated from human placenta contains disaccharides implicated in activation of HCII and has anticoagulant activity similar to that of mucosal DS.	Disaccharides	41-54	serpin family D member 1	Homo sapiens	83-87
16339402-8	2006	HCII colocalizes with DS in the walls of fetal blood vessels and is also present in syncytiotrophoblast cells.	Dermatan Sulfate	22-24	serpin family D member 1	Homo sapiens	0-4
16339402-9	2006	Our data suggest that DS is in a position to activate HCII in the fetal blood vessels or in the stroma of placental villi after injury to the syncytiotrophoblast layer and thereby inhibit fibrin generation in the placenta.	Dermatan Sulfate	22-24	serpin family D member 1	Homo sapiens	54-58
16202803-2	2005	The uptake of the aniline compounds on LS-2 is a procedure of coexistence of physisorption and chemisorption and obeys the pseudo-second order rate equation, while the uptake of the compounds on XAD-4 is merely a physical adsorption and follows the pseudo-first order rate equation.	aniline	18-25	serpin family D member 1	Homo sapiens	39-43
16202803-4	2005	Dynamic adsorption and desorption studies for aniline on LS-2 show that the breakthrough adsorption capacity and the total adsorption capacity are 0.96 and 1.24 mmol per milliliter resin, respectively.	aniline	46-53	serpin family D member 1	Homo sapiens	57-61
15297491-8	2004	For the 161 patients with HBV DNA levels detectable by the Digene HC II assay, the HBV DNA levels obtained by the Digene HC II assay and by the COBAS-AM assay showed an excellent correlation (r = 0.95; P < 0.001).	aluminum hydroxide, magnesium hydroxide, drug combination	59-65	serpin family D member 1	Homo sapiens	66-71
15315969-7	2004	Furthermore, the invertebrate dermatan sulfates, which have higher charge densities than mammalian dermatan sulfate, slightly prolonged the thrombotic occlusion time of HCII(-/-) mice.	Dermatan Sulfate	30-47	serpin family D member 1	Homo sapiens	169-173
15315969-7	2004	Furthermore, the invertebrate dermatan sulfates, which have higher charge densities than mammalian dermatan sulfate, slightly prolonged the thrombotic occlusion time of HCII(-/-) mice.	Dermatan Sulfate	30-46	serpin family D member 1	Homo sapiens	169-173
15371417-4	2004	In this report we investigate the heparin binding properties of HCII and conclude that binding is nonspecific with a minimal heparin length of 13 monosaccharide units required and affinity critically dependent on ionic strength.	Monosaccharides	146-160	serpin family D member 1	Homo sapiens	64-68
15371417-5	2004	Rapid kinetics of heparin binding indicate an induced fit mechanism that involves a conformational change in HCII.	Heparin	18-25	serpin family D member 1	Homo sapiens	109-113
15371417-6	2004	Thus, HCII binds to heparin in a manner analogous to the interaction of AT with low affinity heparin.	Heparin	20-27	serpin family D member 1	Homo sapiens	6-10
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Heparin	29-36	serpin family D member 1	Homo sapiens	74-78
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Heparin	99-106	serpin family D member 1	Homo sapiens	74-78
15371417-7	2004	A fully allosteric 2000-fold heparin activation of thrombin inhibition by HCII is demonstrated for heparin chains up to 26 monosaccharide units in length.	Monosaccharides	123-137	serpin family D member 1	Homo sapiens	74-78
15371417-8	2004	We conclude that the heparin-binding mechanism of HCII is closely analogous to that of AT and that the induced fit mechanism suggests the potential design or discovery of specific HCII agonists.	Heparin	21-28	serpin family D member 1	Homo sapiens	50-54
15371417-8	2004	We conclude that the heparin-binding mechanism of HCII is closely analogous to that of AT and that the induced fit mechanism suggests the potential design or discovery of specific HCII agonists.	Heparin	21-28	serpin family D member 1	Homo sapiens	180-184
15511233-3	2004	Using a disulfide cross-linking strategy, we demonstrate that at least three different sites (positions 52, 54 and 68) within the N terminus may be tethered in a reformable manner to position 195 in the loop region between helix D and strand s2A of the HCII molecule, suggesting that the N-terminal domain may interact with the inhibitor scaffold in a permissive manner.	Disulfides	8-17	serpin family D member 1	Homo sapiens	253-257
15511233-6	2004	Treatment with dithiothreitol and iodoacetamide restores activity towards alpha-thrombin, suggesting that release of the N terminus of HCII is an important component of the multistep interaction between the inhibitor and alpha-thrombin.	Dithiothreitol	15-29	serpin family D member 1	Homo sapiens	135-139
15511233-6	2004	Treatment with dithiothreitol and iodoacetamide restores activity towards alpha-thrombin, suggesting that release of the N terminus of HCII is an important component of the multistep interaction between the inhibitor and alpha-thrombin.	Iodoacetamide	34-47	serpin family D member 1	Homo sapiens	135-139
15292227-6	2004	Four mutants (Asp51, Lys52, Lys145/Thr147/Trp148, Asp234) showed normal increased rates of inhibition by HCII-glycosaminoglycans, whereas four mutants (Trp50, Glu202, Glu229, Arg233) remained resistant to inhibition by HCII with glycosaminoglycans.	Glycosaminoglycans	110-128	serpin family D member 1	Homo sapiens	105-109
15292227-8	2004	Collectively, our results support a "double bridge" mechanism for HCII inhibition of thrombin in the presence of glycosaminoglycans, which relies in part on ternary complex formation but is primarily dominated by an allosteric process involving contact of the "hirudin-like" domain of HCII with thrombin exosite-1.	Glycosaminoglycans	113-131	serpin family D member 1	Homo sapiens	66-70
15292227-8	2004	Collectively, our results support a "double bridge" mechanism for HCII inhibition of thrombin in the presence of glycosaminoglycans, which relies in part on ternary complex formation but is primarily dominated by an allosteric process involving contact of the "hirudin-like" domain of HCII with thrombin exosite-1.	Glycosaminoglycans	113-131	serpin family D member 1	Homo sapiens	285-289
15927366-1	2005	In this paper a new bifunctional polymeric resin (LS-2) was synthesized by introducing sulfonic groups onto the surface of the resin during the post-crossing of chloromethyl low crosslinking macroporous poly-styrene resin, and the comparison of the adsorption properties of LS-2 with Amberlite XAD-4 toward aniline and 4-methylaniline in aqueous solutions was made.	sulfonic	87-95	serpin family D member 1	Homo sapiens	50-54
15927366-1	2005	In this paper a new bifunctional polymeric resin (LS-2) was synthesized by introducing sulfonic groups onto the surface of the resin during the post-crossing of chloromethyl low crosslinking macroporous poly-styrene resin, and the comparison of the adsorption properties of LS-2 with Amberlite XAD-4 toward aniline and 4-methylaniline in aqueous solutions was made.	chloromethyl	161-173	serpin family D member 1	Homo sapiens	50-54
15927366-1	2005	In this paper a new bifunctional polymeric resin (LS-2) was synthesized by introducing sulfonic groups onto the surface of the resin during the post-crossing of chloromethyl low crosslinking macroporous poly-styrene resin, and the comparison of the adsorption properties of LS-2 with Amberlite XAD-4 toward aniline and 4-methylaniline in aqueous solutions was made.	Polystyrenes	203-215	serpin family D member 1	Homo sapiens	50-54
15927366-1	2005	In this paper a new bifunctional polymeric resin (LS-2) was synthesized by introducing sulfonic groups onto the surface of the resin during the post-crossing of chloromethyl low crosslinking macroporous poly-styrene resin, and the comparison of the adsorption properties of LS-2 with Amberlite XAD-4 toward aniline and 4-methylaniline in aqueous solutions was made.	aniline	307-314	serpin family D member 1	Homo sapiens	50-54
15927366-1	2005	In this paper a new bifunctional polymeric resin (LS-2) was synthesized by introducing sulfonic groups onto the surface of the resin during the post-crossing of chloromethyl low crosslinking macroporous poly-styrene resin, and the comparison of the adsorption properties of LS-2 with Amberlite XAD-4 toward aniline and 4-methylaniline in aqueous solutions was made.	4-toluidine	319-334	serpin family D member 1	Homo sapiens	50-54
15927366-5	2005	The adsorption for aniline or 4-methylaniline on LS-2 was proved to be an endothermic process and increasing temperature was favorable.	aniline	19-26	serpin family D member 1	Homo sapiens	49-53
15927366-5	2005	The adsorption for aniline or 4-methylaniline on LS-2 was proved to be an endothermic process and increasing temperature was favorable.	4-toluidine	30-45	serpin family D member 1	Homo sapiens	49-53
15927366-6	2005	From the studies on the adsorption thermodynamics, static equilibrium adsorption, and the desorption conditions, an important conclusion can be drawn that the adsorption for aniline or 4-methylaniline on the LS-2 is a coexistence process of physical adsorption and chemical transition.	aniline	174-181	serpin family D member 1	Homo sapiens	208-212
15927366-6	2005	From the studies on the adsorption thermodynamics, static equilibrium adsorption, and the desorption conditions, an important conclusion can be drawn that the adsorption for aniline or 4-methylaniline on the LS-2 is a coexistence process of physical adsorption and chemical transition.	4-toluidine	185-200	serpin family D member 1	Homo sapiens	208-212
15543340-6	2004	Adjusting for the material of the implanted stents (nitinol vs. Wallstents), patients with a high HCII activity had a 0.39-fold reduced risk for instent restenosis (95% CI 0.17 to 0.90, p=0.028), additional adjustment for diabetes mellitus, poor run-off, critical limb ischemia and cumulative length of the stented segment did not alter the observed effect.	nitinol	52-59	serpin family D member 1	Homo sapiens	98-102
15337701-0	2004	Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis.	Glutamic Acid	63-72	serpin family D member 1	Homo sapiens	25-44
15297491-8	2004	For the 161 patients with HBV DNA levels detectable by the Digene HC II assay, the HBV DNA levels obtained by the Digene HC II assay and by the COBAS-AM assay showed an excellent correlation (r = 0.95; P < 0.001).	aluminum hydroxide, magnesium hydroxide, drug combination	114-120	serpin family D member 1	Homo sapiens	121-126
15247982-0	2004	Studies on the effect of calcium in interactions between heparin and heparin cofactor II using surface plasmon resonance.	Calcium	25-32	serpin family D member 1	Homo sapiens	69-88
15247982-2	2004	Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin.	Heparin	128-135	serpin family D member 1	Homo sapiens	0-19
15247982-2	2004	Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin.	Heparin	128-135	serpin family D member 1	Homo sapiens	21-25
15247982-3	2004	The interaction of heparin with HCII has been the focus of many studies using affinity chromatography and fluorescence spectroscopy.	Heparin	19-26	serpin family D member 1	Homo sapiens	32-36
15247982-4	2004	In this study, surface plasmon resonance (SPR) spectroscopy was used to quantitatively measure the interaction of heparin and HCII using a heparin biochip prepared by covalently immobilizing preformed albumin-heparin conjugate.	Heparin	139-146	serpin family D member 1	Homo sapiens	126-130
15247982-4	2004	In this study, surface plasmon resonance (SPR) spectroscopy was used to quantitatively measure the interaction of heparin and HCII using a heparin biochip prepared by covalently immobilizing preformed albumin-heparin conjugate.	Heparin	139-146	serpin family D member 1	Homo sapiens	126-130
15247982-5	2004	HCII contains multiple EF hand domains that represent putative calcium ion binding sites.	Calcium	63-70	serpin family D member 1	Homo sapiens	0-4
15247982-6	2004	The interactions of HCII with heparin, low-molecular-weight heparin, and heparin oligosaccharides (disaccharide, tetrasaccharide, hexasaccharide) were examined in solution competition experiments using SPR.	Heparin	30-37	serpin family D member 1	Homo sapiens	20-24
15247982-6	2004	The interactions of HCII with heparin, low-molecular-weight heparin, and heparin oligosaccharides (disaccharide, tetrasaccharide, hexasaccharide) were examined in solution competition experiments using SPR.	Disaccharides	99-111	serpin family D member 1	Homo sapiens	20-24
15247982-6	2004	The interactions of HCII with heparin, low-molecular-weight heparin, and heparin oligosaccharides (disaccharide, tetrasaccharide, hexasaccharide) were examined in solution competition experiments using SPR.	tetrasaccharide	113-128	serpin family D member 1	Homo sapiens	20-24
15247982-6	2004	The interactions of HCII with heparin, low-molecular-weight heparin, and heparin oligosaccharides (disaccharide, tetrasaccharide, hexasaccharide) were examined in solution competition experiments using SPR.	hexasaccharide	130-144	serpin family D member 1	Homo sapiens	20-24
15247982-7	2004	The results also showed while calcium ions enhanced the heparin/HCII interaction, the activity of heparin-HCII complex against thrombin was not calcium dependent but can be enhanced by the presence of calcium.	Calcium	30-37	serpin family D member 1	Homo sapiens	64-68
15247982-7	2004	The results also showed while calcium ions enhanced the heparin/HCII interaction, the activity of heparin-HCII complex against thrombin was not calcium dependent but can be enhanced by the presence of calcium.	Calcium	30-37	serpin family D member 1	Homo sapiens	106-110
15247982-7	2004	The results also showed while calcium ions enhanced the heparin/HCII interaction, the activity of heparin-HCII complex against thrombin was not calcium dependent but can be enhanced by the presence of calcium.	Calcium	144-151	serpin family D member 1	Homo sapiens	106-110
15247982-7	2004	The results also showed while calcium ions enhanced the heparin/HCII interaction, the activity of heparin-HCII complex against thrombin was not calcium dependent but can be enhanced by the presence of calcium.	Calcium	144-151	serpin family D member 1	Homo sapiens	106-110
15084912-5	2004	Peptide binding studies revealed that the majority of the CII-peptide binding affinity for DR1 and DR4 is controlled by the Phe at 263 and, unexpectedly, the adjacent Lys.	Phenylalanine	124-127	serpin family D member 1	Homo sapiens	58-61
15196911-3	2004	In the presence of glycosaminoglycans, AT and PCI had significantly reduced thrombin inhibition with Toggle-25, but it was only reduced 3-fold for HCII.	Glycosaminoglycans	19-37	serpin family D member 1	Homo sapiens	147-151
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	serpin family D member 1	Homo sapiens	8-27
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	serpin family D member 1	Homo sapiens	29-33
15148272-2	2004	Because heparin cofactor II (HCII) inhibits thrombin actions after binding to dermatan sulfate at injured arterial walls, HCII may negatively regulate thrombin actions in vascular walls.	Dermatan Sulfate	78-94	serpin family D member 1	Homo sapiens	122-126
15084912-5	2004	Peptide binding studies revealed that the majority of the CII-peptide binding affinity for DR1 and DR4 is controlled by the Phe at 263 and, unexpectedly, the adjacent Lys.	Lysine	167-170	serpin family D member 1	Homo sapiens	58-61
12859981-0	2003	Mechanism of activation of heparin cofactor II by calcium spirulan.	spirulan	50-66	serpin family D member 1	Homo sapiens	27-46
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	serpin family D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Heparin	0-7	serpin family D member 1	Homo sapiens	305-309
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 D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Iduronic Acid	18-31	serpin family D member 1	Homo sapiens	305-309
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 D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Glycosaminoglycans	43-61	serpin family D member 1	Homo sapiens	305-309
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 D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Glycosaminoglycans	63-66	serpin family D member 1	Homo sapiens	305-309
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 D member 1	Homo sapiens	284-303
15078125-1	2004	Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin).	Dermatan Sulfate	76-92	serpin family D member 1	Homo sapiens	305-309
15078125-2	2004	Although AT and HCII are structural homologs, only heparin binds to AT, and HCII has different binding sites for heparin and dermatan sulfate.	Heparin	113-120	serpin family D member 1	Homo sapiens	76-80
15078125-2	2004	Although AT and HCII are structural homologs, only heparin binds to AT, and HCII has different binding sites for heparin and dermatan sulfate.	Dermatan Sulfate	125-141	serpin family D member 1	Homo sapiens	76-80
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Heparin	28-35	serpin family D member 1	Homo sapiens	141-145
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Heparin	167-174	serpin family D member 1	Homo sapiens	141-145
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Dermatan Sulfate	179-195	serpin family D member 1	Homo sapiens	141-145
15078125-3	2004	Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains.	Glycosaminoglycans	251-254	serpin family D member 1	Homo sapiens	141-145
15078125-6	2004	Whereas it inactivates the binding site for AT causing a drop of the anticoagulant activity, it enhances the HCII-associated activity of both heparin and dermatan sulfate.	Heparin	142-149	serpin family D member 1	Homo sapiens	109-113
15078125-6	2004	Whereas it inactivates the binding site for AT causing a drop of the anticoagulant activity, it enhances the HCII-associated activity of both heparin and dermatan sulfate.	Dermatan Sulfate	154-170	serpin family D member 1	Homo sapiens	109-113
15115672-7	2004	RESULTS AND CONCLUSIONS: The F450L, P455L, P477L, P477*, and T446* (*=stop codon) mutations reduced HCII secretion 6.6- to 24-fold, while the F402L, A404T, and P407L mutations reduced AT secretion in COS-1 cells 1.7- to 5.2-fold.	carbonyl sulfide	200-203	serpin family D member 1	Homo sapiens	100-104
15204704-11	2004	RESULTS: Of the 14 cantharidin analogues tested, LS-1, LS-2 and LS-5 at concentrations of 3-20 microM showed little or no toxicity, produced elevated levels of H1 and H3 phosphorylation, and effected significant radiosensitization at low radiation dose.	Cantharidin	19-30	serpin family D member 1	Homo sapiens	55-59
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	serpin family D member 1	Homo sapiens	8-27
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	serpin family D member 1	Homo sapiens	29-33
14744972-2	2004	Because heparin cofactor II (HCII) inhibits thrombin action in the presence of dermatan sulfate, which is abundantly present in arterial wall, HCII may affect vascular remodeling by modulating thrombin action.	Dermatan Sulfate	79-95	serpin family D member 1	Homo sapiens	143-147
14747034-0	2004	Efficient treatment of paraffin-embedded cervical tissue for HPV DNA testing by HC-II and PCR assays.	Paraffin	23-31	serpin family D member 1	Homo sapiens	80-85
14747034-3	2004	STUDY DESIGN: the use of HC-II assay with formaldehyde-fixed paraffin-embedded cervical biopsies, for retrospective studies or to support histological findings, was investigated by analysing three different sample treatments.	Formaldehyde	42-54	serpin family D member 1	Homo sapiens	25-30
14747034-3	2004	STUDY DESIGN: the use of HC-II assay with formaldehyde-fixed paraffin-embedded cervical biopsies, for retrospective studies or to support histological findings, was investigated by analysing three different sample treatments.	Paraffin	61-69	serpin family D member 1	Homo sapiens	25-30
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	spirulan	0-16	serpin family D member 1	Homo sapiens	104-123
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	spirulan	0-16	serpin family D member 1	Homo sapiens	125-129
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	spirulan	0-16	serpin family D member 1	Homo sapiens	221-225
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	spirulan	18-23	serpin family D member 1	Homo sapiens	104-123
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	spirulan	18-23	serpin family D member 1	Homo sapiens	125-129
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	spirulan	18-23	serpin family D member 1	Homo sapiens	221-225
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	Polysaccharides	43-57	serpin family D member 1	Homo sapiens	104-123
12859981-1	2003	Calcium spirulan (Ca-SP), a novel sulfated polysaccharide, increases the rate of thrombin inhibition by heparin cofactor II (HCII) more than 1000-fold through a mechanism not requiring the amino-terminal acidic domain of HCII.	Polysaccharides	43-57	serpin family D member 1	Homo sapiens	125-129
12859981-2	2003	Activation of HCII by Ca-SP was molecular-weight dependent.	spirulan	22-27	serpin family D member 1	Homo sapiens	14-18
12859981-3	2003	Furthermore, HD22, an aptamer that binds exosite II of thrombin, produced a concentration-dependent, 15-fold reduction at 5 microM in the rate of thrombin inhibition by HCII with Ca-SP, suggesting that Ca-SP interacts with exosite II of thrombin.	spirulan	179-184	serpin family D member 1	Homo sapiens	169-173
12885634-1	2003	Classical molecular dynamics simulations using the multistate empirical valence bond model for aqueous proton transport were performed to characterize the hydration structure of an excess proton inside a leucine-serine synthetic ion channel, LS2.	Serine	212-218	serpin family D member 1	Homo sapiens	242-245
12859981-3	2003	Furthermore, HD22, an aptamer that binds exosite II of thrombin, produced a concentration-dependent, 15-fold reduction at 5 microM in the rate of thrombin inhibition by HCII with Ca-SP, suggesting that Ca-SP interacts with exosite II of thrombin.	spirulan	202-207	serpin family D member 1	Homo sapiens	169-173
12859981-4	2003	Mutations of Lys173 to Leu (K173L) and Arg189 to Leu (R189L) in the HCII molecule resulted in large decreases in the rate of thrombin inhibition mediated by Ca-SP and in the NaCl concentration needed for elution from Ca-SP-Toyopearl.	spirulan	157-162	serpin family D member 1	Homo sapiens	68-72
12859981-4	2003	Mutations of Lys173 to Leu (K173L) and Arg189 to Leu (R189L) in the HCII molecule resulted in large decreases in the rate of thrombin inhibition mediated by Ca-SP and in the NaCl concentration needed for elution from Ca-SP-Toyopearl.	Sodium Chloride	174-178	serpin family D member 1	Homo sapiens	68-72
12859981-4	2003	Mutations of Lys173 to Leu (K173L) and Arg189 to Leu (R189L) in the HCII molecule resulted in large decreases in the rate of thrombin inhibition mediated by Ca-SP and in the NaCl concentration needed for elution from Ca-SP-Toyopearl.	spirulan	217-222	serpin family D member 1	Homo sapiens	68-72
12859981-6	2003	These results indicate that Ca-SP binds to the positive charges of Lys173 and Arg189 on the HCII molecule.	spirulan	28-33	serpin family D member 1	Homo sapiens	92-96
12859981-7	2003	In the thrombin inhibitory process by HCII, Ca-SP appears to play as a template by binding to both thrombin and HCII.	spirulan	44-49	serpin family D member 1	Homo sapiens	38-42
12859981-7	2003	In the thrombin inhibitory process by HCII, Ca-SP appears to play as a template by binding to both thrombin and HCII.	spirulan	44-49	serpin family D member 1	Homo sapiens	112-116
12149217-8	2002	A drastic decrease (up to 500-fold) of the second-order rate constant pertaining to heparin cofactor II (HCII) interaction, especially in the presence of dermatan sulfate, was found for the FIIa-MT67 compared with FIIa-WT, suggesting a severe impairment of thrombin inhibition by HCII in vivo.	Dermatan Sulfate	154-170	serpin family D member 1	Homo sapiens	84-103
15013278-7	2003	Results of experiments on gel-filtered platelets from humans indicate that the inhibition of thrombin-induced platelet aggregation caused by UFH and LMWH in the presence of AT is more prominent than that caused by DHG with HCII.	dhg	214-217	serpin family D member 1	Homo sapiens	223-227
12818259-9	2003	In HCII depleted PPP, the dose-dependent increase in k" produced by sulodexide was significantly lower than in PPP, while the dose-dependent increase in k" produced by FMH was similar to the increase produced in PPP.	glucuronyl glucosamine glycan sulfate	68-78	serpin family D member 1	Homo sapiens	3-7
12818259-10	2003	CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH.	glucuronyl glucosamine glycan sulfate	45-55	serpin family D member 1	Homo sapiens	113-117
12818259-10	2003	CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH.	Dermatan Sulfate	131-133	serpin family D member 1	Homo sapiens	113-117
12818259-10	2003	CONCLUSIONS: Thrombin inhibition produced by sulodexide is due to the additive effect of its components, namely, HCII catalysis by DS and AT catalysis by FMH.	alpha-fluoromethylhistidine	154-157	serpin family D member 1	Homo sapiens	113-117
12169660-5	2002	HCII inhibits thrombin, the final protease of the coagulation cascade, in a glycosaminoglycan-dependent manner that involves the release of a sequestered hirudin-like N-terminal tail for interaction with thrombin.	Glycosaminoglycans	76-93	serpin family D member 1	Homo sapiens	0-4
12149217-8	2002	A drastic decrease (up to 500-fold) of the second-order rate constant pertaining to heparin cofactor II (HCII) interaction, especially in the presence of dermatan sulfate, was found for the FIIa-MT67 compared with FIIa-WT, suggesting a severe impairment of thrombin inhibition by HCII in vivo.	Dermatan Sulfate	154-170	serpin family D member 1	Homo sapiens	105-109
11856753-0	2002	Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.	Aspartic Acid	0-13	serpin family D member 1	Homo sapiens	60-79
12413592-8	2002	In contrast, HCII does not require Arg(93), Arg(97) and Arg(101) of thrombin exosite-2 and further supports the hypothesis that HCII uses an allosteric process following glycosaminoglycan binding to inhibit thrombin.	Glycosaminoglycans	170-187	serpin family D member 1	Homo sapiens	13-17
12413592-8	2002	In contrast, HCII does not require Arg(93), Arg(97) and Arg(101) of thrombin exosite-2 and further supports the hypothesis that HCII uses an allosteric process following glycosaminoglycan binding to inhibit thrombin.	Glycosaminoglycans	170-187	serpin family D member 1	Homo sapiens	128-132
12095635-0	2002	Contribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibition.	Dermatan Sulfate	84-100	serpin family D member 1	Homo sapiens	49-68
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Heparin	26-33	serpin family D member 1	Homo sapiens	47-51
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Dermatan Sulfate	92-108	serpin family D member 1	Homo sapiens	26-45
12095635-1	2002	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated 1000-fold by heparin or dermatan sulfate.	Dermatan Sulfate	92-108	serpin family D member 1	Homo sapiens	47-51
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Lysine	75-78	serpin family D member 1	Homo sapiens	69-73
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Arginine	88-91	serpin family D member 1	Homo sapiens	69-73
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Heparin	116-123	serpin family D member 1	Homo sapiens	69-73
12095635-5	2002	These results provide evidence that basic residues of the A helix of HCII (Lys(101) and Arg(106)) are necessary for heparin- or dermatan sulfate-accelerated thrombin inhibition.	Dermatan Sulfate	128-144	serpin family D member 1	Homo sapiens	69-73
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Glycosaminoglycans	91-108	serpin family D member 1	Homo sapiens	31-35
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	135-142	serpin family D member 1	Homo sapiens	31-35
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	201-208	serpin family D member 1	Homo sapiens	31-35
11856753-3	2002	Interestingly, D72N/Y73F/D75N rHCII had significantly enhanced thrombin inhibition without glycosaminoglycan (4-fold greater) and with heparin (6-fold greater), showing maximal activity at 2 microg/ml heparin compared with wild-type recombinant HCII (wt-rHCII) with maximal activity at 20 microg/ml heparin.	Heparin	201-208	serpin family D member 1	Homo sapiens	31-35
11856753-9	2002	These results indicate that improved thrombin inhibition in the AR2 HCII mutants is mediated by enhanced interactions between the acidic domain and anion-binding exosite-1 of thrombin and that AR2 may be a "molecular rheostat" to promote thrombin inhibition in the presence of glycosaminoglycans.	Glycosaminoglycans	277-295	serpin family D member 1	Homo sapiens	68-72
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 D member 1	Homo sapiens	22-41
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 D member 1	Homo sapiens	43-47
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	59-66	serpin family D member 1	Homo sapiens	0-4
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	139-146	serpin family D member 1	Homo sapiens	0-4
12413592-5	2002	HCII achieved the same maximum activity in the presence of heparin with both wild-type and R93A/R97A/R101A thrombins; however, the optimum heparin concentration was 20 times greater than the reaction with wild-type thrombin, indicative of a decrease in heparin affinity.	Heparin	139-146	serpin family D member 1	Homo sapiens	0-4
12413592-6	2002	Dermatan sulfate (DSO4)-catalyzed HCII thrombin inhibition was unchanged in R93A/R97A/R101A thrombin compared to wild-type recombinant thrombin.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	34-38
12413592-6	2002	Dermatan sulfate (DSO4)-catalyzed HCII thrombin inhibition was unchanged in R93A/R97A/R101A thrombin compared to wild-type recombinant thrombin.	dso4	18-22	serpin family D member 1	Homo sapiens	34-38
11856753-0	2002	Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.	tyrosine O-sulfate	37-53	serpin family D member 1	Homo sapiens	60-79
11856753-0	2002	Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition.	Glycosaminoglycans	123-140	serpin family D member 1	Homo sapiens	60-79
12003316-1	2002	The present paper deals with a laboratory-scale study of anaerobic treatment of two commercial mixtures (LS2, LT7) of alcohol ethoxylates with 8-14 carbon atoms and 2 and 7 ethoxy groups.	Alcohols	118-125	serpin family D member 1	Homo sapiens	105-108
12003316-1	2002	The present paper deals with a laboratory-scale study of anaerobic treatment of two commercial mixtures (LS2, LT7) of alcohol ethoxylates with 8-14 carbon atoms and 2 and 7 ethoxy groups.	Carbon	148-154	serpin family D member 1	Homo sapiens	105-108
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 D member 1	Homo sapiens	219-238
11751969-5	2002	As predicted based on the crystal structures, the majority of the CII-peptide binding affinity for DR1 and DR4 is controlled by the Phe(263); however, unexpectedly the adjacent Lys(264) also contributed significantly to the binding affinity of the peptide.	Phenylalanine	132-135	serpin family D member 1	Homo sapiens	66-69
11751969-5	2002	As predicted based on the crystal structures, the majority of the CII-peptide binding affinity for DR1 and DR4 is controlled by the Phe(263); however, unexpectedly the adjacent Lys(264) also contributed significantly to the binding affinity of the peptide.	Lysine	177-180	serpin family D member 1	Homo sapiens	66-69
11751969-8	2002	Affinity-enhancing substitutions frequently involved replacement of a negative charge, or Gly or Pro, hallmark amino acids of CII structure.	Glycine	90-93	serpin family D member 1	Homo sapiens	126-129
11751969-8	2002	Affinity-enhancing substitutions frequently involved replacement of a negative charge, or Gly or Pro, hallmark amino acids of CII structure.	Proline	97-100	serpin family D member 1	Homo sapiens	126-129
11583326-1	2001	We compare the relative activities of surface-bound and fluid-phase thrombin and their inhibition by heparin and Intimatan, a novel heparin cofactor II (HCII) agonist.	Heparin	101-108	serpin family D member 1	Homo sapiens	132-151
11583326-1	2001	We compare the relative activities of surface-bound and fluid-phase thrombin and their inhibition by heparin and Intimatan, a novel heparin cofactor II (HCII) agonist.	Heparin	101-108	serpin family D member 1	Homo sapiens	153-157
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 D member 1	Homo sapiens	240-244
11204559-2	2001	To investigate the molecular pathogenesis of our patient, we performed sequencing analysis and expressed recombinant human wild-type and mutant HC II molecules in COS-1 and CHO-K1 cells.	carbonyl sulfide	163-166	serpin family D member 1	Homo sapiens	144-149
11204559-6	2001	Transient transfection, metabolic labeling and pulse-chase experiments followed by immunoprecipitation analysis showed that the recombinant mutant HC II molecules were secreted from COS-1 cells in reduced amounts compared with the wild-type, and that an enhanced intracellular association of the mutant molecules with a chaperone, GRP78/BiP, was observed in CHO-K1 cells.	carbonyl sulfide	182-185	serpin family D member 1	Homo sapiens	147-152
11204559-8	2001	Immunohistochemical staining of the transfected cells revealed that COS-1 cells expressing the mutant HC II molecules were stained mainly in the perinuclear area.	carbonyl sulfide	68-71	serpin family D member 1	Homo sapiens	102-107
10753952-0	2000	Activation of heparin cofactor II by calcium spirulan.	spirulan	37-53	serpin family D member 1	Homo sapiens	14-33
10749870-2	2000	The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall.	Dermatan Sulfate	4-20	serpin family D member 1	Homo sapiens	74-93
10749870-2	2000	The dermatan sulfate chains are known to stimulate thrombin inhibition by heparin cofactor II (HCII), a plasma proteinase inhibitor that has been detected within the artery wall.	Dermatan Sulfate	4-20	serpin family D member 1	Homo sapiens	95-99
11776053-10	2000	GAG inhibited thrombin activity in the presence of HCII with a second order rate constant of 1.14 x 10(7) m-1.min-1, which was 4.6 times higher than that of ATIII.	Glycosaminoglycans	0-3	serpin family D member 1	Homo sapiens	51-55
10749870-7	2000	Affinity coelectrophoresis analysis of a subset of samples demonstrated that increased interaction of proteoglycan with HCII in agarose gels paralleled increased activity in thrombin-HCII inhibition assays.	Sepharose	128-135	serpin family D member 1	Homo sapiens	120-124
10753952-10	2000	These results indicate that Arg(103) in HCII molecule is not critical for the interaction with Ca-SP.	Arginine	28-31	serpin family D member 1	Homo sapiens	40-44
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Polysaccharides	145-160	serpin family D member 1	Homo sapiens	0-19
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Polysaccharides	145-160	serpin family D member 1	Homo sapiens	21-25
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Heparin	176-183	serpin family D member 1	Homo sapiens	0-19
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Heparin	176-183	serpin family D member 1	Homo sapiens	21-25
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Dermatan Sulfate	188-204	serpin family D member 1	Homo sapiens	0-19
10753952-1	2000	Heparin cofactor II (HCII) is a plasma serine protease inhibitor whose ability to inhibit alpha-thrombin is accelerated by a variety of sulfated polysaccharides in addition to heparin and dermatan sulfate.	Dermatan Sulfate	188-204	serpin family D member 1	Homo sapiens	21-25
10753952-2	2000	Previous investigations have indicated that calcium spirulan (Ca-SP), a novel sulfated polysaccharide, enhanced the rate of inhibition of alpha-thrombin by HCII.	spirulan	44-60	serpin family D member 1	Homo sapiens	156-160
10753952-2	2000	Previous investigations have indicated that calcium spirulan (Ca-SP), a novel sulfated polysaccharide, enhanced the rate of inhibition of alpha-thrombin by HCII.	spirulan	62-67	serpin family D member 1	Homo sapiens	156-160
10753952-2	2000	Previous investigations have indicated that calcium spirulan (Ca-SP), a novel sulfated polysaccharide, enhanced the rate of inhibition of alpha-thrombin by HCII.	Polysaccharides	87-101	serpin family D member 1	Homo sapiens	156-160
10753952-3	2000	In this study, we investigated the mechanism of the activation of HCII by Ca-SP.	spirulan	74-79	serpin family D member 1	Homo sapiens	66-70
10753952-4	2000	Interestingly, in the presence of Ca-SP, an N-terminal deletion mutant of HCII (rHCII-Delta74) inhibited alpha-thrombin, as native recombinant HCII (native rHCII) did.	spirulan	34-39	serpin family D member 1	Homo sapiens	74-78
10753952-7	2000	Our results suggested that the anion-binding exosite I of alpha-thrombin was essential for the rapid inhibition reaction by HCII in the presence of Ca-SP and that the N-terminal acidic domain of HCII was not required.	spirulan	148-153	serpin family D member 1	Homo sapiens	124-128
10753952-8	2000	Therefore, we proposed a mechanism by which HCII was activated allosterically by Ca-SP and could interact with the anion-binding exosite I of thrombin not through the N-terminal acidic domain of HCII.	spirulan	81-86	serpin family D member 1	Homo sapiens	44-48
10574918-1	1999	Heparin cofactor II (HCII) is a serpin whose thrombin inhibition activity is accelerated by glycosaminoglycans.	Glycosaminoglycans	92-110	serpin family D member 1	Homo sapiens	0-19
10574918-1	1999	Heparin cofactor II (HCII) is a serpin whose thrombin inhibition activity is accelerated by glycosaminoglycans.	Glycosaminoglycans	92-110	serpin family D member 1	Homo sapiens	21-25
10574918-2	1999	We describe the novel properties of a carboxyl-terminal histidine-tagged recombinant HCII (rHCII-CHis(6)).	Histidine	56-65	serpin family D member 1	Homo sapiens	85-89
10574918-3	1999	Thrombin inhibition by rHCII-CHis(6) was increased >2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin.	Heparin	94-101	serpin family D member 1	Homo sapiens	24-28
10574918-3	1999	Thrombin inhibition by rHCII-CHis(6) was increased >2-fold at approximately 5 microgram/ml heparin compared with wild-type recombinant HCII (wt-rHCII) at 50-100 microgram/ml heparin.	Heparin	177-184	serpin family D member 1	Homo sapiens	24-28
10209287-0	1999	Amino acid residues of heparin cofactor II required for stimulation of thrombin inhibition by sulphated polyanions.	polyanions	104-114	serpin family D member 1	Homo sapiens	23-42
10488098-0	1999	Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.	Heparin	14-21	serpin family D member 1	Homo sapiens	91-110
10488098-0	1999	Comparison of heparin- and dermatan sulfate-mediated catalysis of thrombin inactivation by heparin cofactor II.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	91-110
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	serpin family D member 1	Homo sapiens	38-57
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	serpin family D member 1	Homo sapiens	59-63
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Heparin	0-7	serpin family D member 1	Homo sapiens	124-128
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	serpin family D member 1	Homo sapiens	38-57
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	serpin family D member 1	Homo sapiens	59-63
10488098-1	1999	Heparin and dermatan sulfate activate heparin cofactor II (HCII) comparably, presumably by liberating the amino terminus of HCII to bind to exosite I of thrombin.	Dermatan Sulfate	12-28	serpin family D member 1	Homo sapiens	124-128
10488098-6	1999	Whereas activation of HCII by heparin was chain-length dependent, stimulation by dermatan sulfate was not, suggesting that dermatan sulfate does not utilize a template mechanism to accelerate the inhibitory process.	Heparin	30-37	serpin family D member 1	Homo sapiens	22-26
10488098-7	1999	Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus.	Dermatan Sulfate	40-56	serpin family D member 1	Homo sapiens	98-102
10488098-7	1999	Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus.	Dermatan Sulfate	133-149	serpin family D member 1	Homo sapiens	98-102
10488098-7	1999	Fluorescence spectroscopy revealed that dermatan sulfate evokes greater conformational changes in HCII than heparin, suggesting that dermatan sulfate stimulates HCII by producing more effective displacement of the amino terminus.	Dermatan Sulfate	133-149	serpin family D member 1	Homo sapiens	161-165
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Heparin	82-89	serpin family D member 1	Homo sapiens	0-19
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Heparin	82-89	serpin family D member 1	Homo sapiens	21-25
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Dermatan Sulfate	93-110	serpin family D member 1	Homo sapiens	0-19
10494755-1	1999	Heparin cofactor II (HCII) is a specific inhibitor of thrombin in the presence of heparin or dermatan sulphate.	Dermatan Sulfate	93-110	serpin family D member 1	Homo sapiens	21-25
10209287-3	1999	In this study we determined the concentrations (IC50) of various polyanions required to stimulate thrombin inhibition by native recombinant HCII in comparison with three recombinant HCII variants having decreased affinity for heparin (Lys-173-->Gln), dermatan sulphate (Arg-189-->His), or both heparin and dermatan sulphate (Lys-185-->Asn).	polyanions	65-75	serpin family D member 1	Homo sapiens	140-144
10209287-3	1999	In this study we determined the concentrations (IC50) of various polyanions required to stimulate thrombin inhibition by native recombinant HCII in comparison with three recombinant HCII variants having decreased affinity for heparin (Lys-173-->Gln), dermatan sulphate (Arg-189-->His), or both heparin and dermatan sulphate (Lys-185-->Asn).	Heparin	226-233	serpin family D member 1	Homo sapiens	182-186
10209287-8	1999	These results suggest that, like dermatan sulphate and heparin, other polyanions stimulate HCII primarily by an allosteric mechanism requiring the N-terminal acidic domain.	Dermatan Sulfate	33-50	serpin family D member 1	Homo sapiens	91-95
10209287-8	1999	These results suggest that, like dermatan sulphate and heparin, other polyanions stimulate HCII primarily by an allosteric mechanism requiring the N-terminal acidic domain.	Heparin	55-62	serpin family D member 1	Homo sapiens	91-95
10209287-8	1999	These results suggest that, like dermatan sulphate and heparin, other polyanions stimulate HCII primarily by an allosteric mechanism requiring the N-terminal acidic domain.	polyanions	70-80	serpin family D member 1	Homo sapiens	91-95
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	polyanions	23-33	serpin family D member 1	Homo sapiens	119-138
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	polyanions	23-33	serpin family D member 1	Homo sapiens	140-144
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	61-78	serpin family D member 1	Homo sapiens	119-138
10209287-1	1999	A variety of sulphated polyanions in addition to heparin and dermatan sulphate stimulate the inhibition of thrombin by heparin cofactor II (HCII).	Dermatan Sulfate	61-78	serpin family D member 1	Homo sapiens	140-144
10209287-2	1999	Previous investigations indicated that the binding sites on HCII for heparin and dermatan sulphate overlap but are not identical.	Heparin	69-76	serpin family D member 1	Homo sapiens	60-64
10209287-2	1999	Previous investigations indicated that the binding sites on HCII for heparin and dermatan sulphate overlap but are not identical.	Dermatan Sulfate	81-98	serpin family D member 1	Homo sapiens	60-64
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	33-52
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	54-58
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	intimatan	92-101	serpin family D member 1	Homo sapiens	33-52
10093889-5	1999	For example, we suggest that the heparin cofactor II (HCII) catalysts, dermatan sulfate and Intimatan, inhibit surface-bound thrombin more effectively than heparin/ATIII, thereby inhibiting intimal hyperplasia effectively.	intimatan	92-101	serpin family D member 1	Homo sapiens	54-58
10349131-1	1999	Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate.	Dermatan Sulfate	115-131	serpin family D member 1	Homo sapiens	0-19
10349131-1	1999	Heparin Cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of dermatan sulfate.	Dermatan Sulfate	115-131	serpin family D member 1	Homo sapiens	21-25
10349131-6	1999	In our laboratory, we measured HCII plasmatic levels in the normal Buenos Aires city population and in patients under different clinical conditions, such as sepsis, diabetis, burns, oral anticoagulation and in patients treated with heparin, hyperhomcysteinemia in whom septic and diabetic patients showed decreased values.	Heparin	232-239	serpin family D member 1	Homo sapiens	31-35
10349131-7	1999	HCII thrombin inhibition possibly takes place in extravascular sites where dermatan sulfate is present.	Dermatan Sulfate	75-91	serpin family D member 1	Homo sapiens	0-4
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 D member 1	Homo sapiens	93-112
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	89-96	serpin family D member 1	Homo sapiens	0-19
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	89-96	serpin family D member 1	Homo sapiens	21-25
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	100-116	serpin family D member 1	Homo sapiens	0-19
9843172-1	1998	Heparin cofactor II (HCII) is a serpin that inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	100-116	serpin family D member 1	Homo sapiens	21-25
9641623-8	1998	This study shows that the mechanism by which the dextran derivatives inhibit thrombin is original and is related to preferential interaction with thrombin; this both inhibits the clotting activity of the enzyme and increases the reaction rate of thrombin inhibition by HCII.	Dextrans	49-56	serpin family D member 1	Homo sapiens	269-273
9893056-3	1998	Amino acid analyses indicated that the rhCIIbac was adequately hydroxylated at prolyl residues but underhydroxylated at lysyl residues and underglycosylated compared with tissue-derived hCII, while rhCIIht was hyperhydroxylated and hyperglycosylated at lysyl residues.	Peptide oostatic hormone	79-85	serpin family D member 1	Homo sapiens	40-44
9893056-6	1998	These data indicate that the degree of hydroxylysine glycosylation may play a role in the induction of the arthritogenic response to CII.	Hydroxylysine	39-52	serpin family D member 1	Homo sapiens	133-136
9813026-10	1998	The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin.	Heparin	78-85	serpin family D member 1	Homo sapiens	57-61
9813026-10	1998	The larger effects of the thrombin exosite-I mutants for HCII inhibition with heparin and dermatan sulfate indicate its need for exosite-I, presumably through contact of the "hirudin-like" domain of HCII with exosite-I of thrombin.	Dermatan Sulfate	90-106	serpin family D member 1	Homo sapiens	199-203
9641623-3	1998	We studied both their anticoagulant activity and the catalysis of thrombin (T) inhibition by heparin cofactor II (HCII) and antithrombin (AT) in the presence of these dextran derivatives relative to heparin and dextran sulfate (DXSu).	Heparin	93-100	serpin family D member 1	Homo sapiens	114-118
9641623-4	1998	The anticoagulant activity of CMDBS was due both to direct thrombin inhibition and to catalysis of thrombin inhibition by HCII.	cmdbs	30-35	serpin family D member 1	Homo sapiens	122-126
9353333-5	1997	Purified recombinant meizothrombin and meizothrombin(desF1) were inhibited by HCII in the presence of dermatan sulfate with maximal second-order rate constants of 8 x 10(6) M-1.min-1 and 1.8 x 10(7) M-1.min-1, respectively, but were inhibited less than one-tenth as fast by AT in the presence of heparin.	Dermatan Sulfate	102-118	serpin family D member 1	Homo sapiens	78-82
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	72-79	serpin family D member 1	Homo sapiens	0-19
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	72-79	serpin family D member 1	Homo sapiens	21-25
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	83-99	serpin family D member 1	Homo sapiens	0-19
9485475-1	1998	Heparin cofactor II (HCII) inhibits thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	83-99	serpin family D member 1	Homo sapiens	21-25
9485475-3	1998	We recently observed that heparin induces dissociation of complexes containing thrombin and the reactive site mutant HCII(L444R) to yield active thrombin and cleaved inhibitor (Han, J.	Heparin	26-33	serpin family D member 1	Homo sapiens	117-121
9485475-7	1998	In the current study, we have investigated the mechanism by which heparin induces dissociation of the thrombin-HCII(L444R) complex.	Heparin	66-73	serpin family D member 1	Homo sapiens	111-115
9485475-9	1998	Binding of heparin to HCII(L444R) in the complex also does not appear to be required, since the heparin dose response is unaltered for complexes containing the double mutant HCII(L444R/K173Q), which has decreased affinity for heparin.	Heparin	11-18	serpin family D member 1	Homo sapiens	22-26
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	49-56	serpin family D member 1	Homo sapiens	152-156
9485475-12	1998	Second, a monoclonal IgG that interacts with the heparin-binding site of thrombin mimicks heparin in its ability to induce dissociation of the thrombin-HCII(L444R) complex.	Heparin	90-97	serpin family D member 1	Homo sapiens	152-156
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	83-90	serpin family D member 1	Homo sapiens	24-28
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	165-172	serpin family D member 1	Homo sapiens	24-28
9485475-13	1998	Finally, the complex of HCII(L444R) with thrombin(desPPW), which binds normally to heparin but lacks Pro60BPro60CTrp60D in an insertion loop ("60-loop") between the heparin-binding site and the catalytic site, does not dissociate in the presence of heparin.	Heparin	165-172	serpin family D member 1	Homo sapiens	24-28
9485475-14	1998	These results suggest that binding of heparin to thrombin induces an allosteric effect causing destabilization of the thrombin-HCII(L444R) complex and that the allosteric effect may be mediated by the 60-loop.	Heparin	38-45	serpin family D member 1	Homo sapiens	127-131
9353333-5	1997	Purified recombinant meizothrombin and meizothrombin(desF1) were inhibited by HCII in the presence of dermatan sulfate with maximal second-order rate constants of 8 x 10(6) M-1.min-1 and 1.8 x 10(7) M-1.min-1, respectively, but were inhibited less than one-tenth as fast by AT in the presence of heparin.	Heparin	296-303	serpin family D member 1	Homo sapiens	78-82
9353333-7	1997	When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate.	Dermatan Sulfate	14-30	serpin family D member 1	Homo sapiens	167-171
9353333-7	1997	When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate.	Sodium Dodecyl Sulfate	124-146	serpin family D member 1	Homo sapiens	5-9
9353333-7	1997	When HCII and dermatan sulfate were present continuously during the prothrombinase reaction, meizothrombin was trapped as a sodium dodecyl sulfate-stable complex with HCII and no amidolytic activity could be detected with a thrombin substrate.	Sodium Dodecyl Sulfate	124-146	serpin family D member 1	Homo sapiens	167-171
9306616-4	1997	4) Fucoidan enhanced the interaction of thrombin with both AT-III and heparin cofactor II (HC-II) and it was more effective than unfractionated heparin of LMwt-heparin in enhancing the interaction of HC-II with thrombin.	Heparin	70-77	serpin family D member 1	Homo sapiens	91-96
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 D member 1	Homo sapiens	119-124
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 D member 1	Homo sapiens	243-248
9068899-0	1997	Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative.	Dermatan Sulfate	75-93	serpin family D member 1	Homo sapiens	36-55
9162031-0	1997	Arginine 200 of heparin cofactor II promotes intramolecular interactions of the acidic domain.	Arginine	0-8	serpin family D member 1	Homo sapiens	16-35
9162031-4	1997	Two mutations at a unique HCII residue, Arg200 --> Ala or Glu, were generated by site-directed mutagenesis.	Alanine	54-57	serpin family D member 1	Homo sapiens	26-30
9162031-4	1997	Two mutations at a unique HCII residue, Arg200 --> Ala or Glu, were generated by site-directed mutagenesis.	Glutamic Acid	61-64	serpin family D member 1	Homo sapiens	26-30
9079643-0	1997	Heparin facilitates dissociation of complexes between thrombin and a reactive site mutant (L444R) of heparin cofactor II.	Heparin	0-7	serpin family D member 1	Homo sapiens	101-120
9079643-3	1997	Mutation of leucine 444 to arginine at the P1 position of recombinant HCII (rHCII) increases the rate of inhibition of thrombin approximately 100-fold in the absence of a glycosaminoglycan (Derechin, V. M., Blinder, M. A., and Tollefsen, D. M. (1990) J. Biol.	derechin	190-198	serpin family D member 1	Homo sapiens	70-74
9068899-3	1997	Analysis of the experimental data obtained for DS, DSS1 and DSS2 was performed using a previously described model which allows computation of the dissociation constant (KPS,HC) of the polysaccharide-HC II complex and the rate constant of thrombin inhibition by the polysaccharide-HC II complex (k).	ds	47-49	serpin family D member 1	Homo sapiens	199-204
15622771-0	1997	[The antithrombin action of stichopus japonicus acid mucopolysaccharide (Sjamp) is mediated by heparin cofactor II].	sjamp	73-78	serpin family D member 1	Homo sapiens	95-114
9031720-9	1997	These data indicate that heparin-HC II complex reactivity is greater than that of the heparin-AT complex towards thrombin, whereas heparin affinity is stronger for AT.	Heparin	25-32	serpin family D member 1	Homo sapiens	33-38
9068899-0	1997	Mechanism of thrombin inhibition by heparin cofactor II in the presence of dermatan sulphates, native or oversulphated, and a heparin-like dextran derivative.	Dextrans	139-146	serpin family D member 1	Homo sapiens	36-55
9157603-6	1997	In terms of in vitro anticoagulant activity assessed by use of purified human components, DHGs (DHG, HMW-DHG, and LMW-DHG) had different anti-thrombin activity in the presence of HCII and anti-factor Xase activities, which differences were dependent on the molecular weight.	dhgs	90-94	serpin family D member 1	Homo sapiens	179-183
8995378-0	1997	Heparin promotes proteolytic inactivation by thrombin of a reactive site mutant (L444R) of recombinant heparin cofactor II.	Heparin	0-7	serpin family D member 1	Homo sapiens	103-122
8995378-1	1997	A heparin cofactor II (HCII) mutant with an Arg substituted for Leu444 at the P1 position (L444R-rHCII) was previously found to have altered proteinase specificity (Derechin, V. M., Blinder, M. A., and Tollefsen, D. M. (1990) J. Biol.	derechin	165-173	serpin family D member 1	Homo sapiens	2-21
8995378-1	1997	A heparin cofactor II (HCII) mutant with an Arg substituted for Leu444 at the P1 position (L444R-rHCII) was previously found to have altered proteinase specificity (Derechin, V. M., Blinder, M. A., and Tollefsen, D. M. (1990) J. Biol.	derechin	165-173	serpin family D member 1	Homo sapiens	23-27
9068899-3	1997	Analysis of the experimental data obtained for DS, DSS1 and DSS2 was performed using a previously described model which allows computation of the dissociation constant (KPS,HC) of the polysaccharide-HC II complex and the rate constant of thrombin inhibition by the polysaccharide-HC II complex (k).	dss2	60-64	serpin family D member 1	Homo sapiens	199-204
9068899-5	1997	Knowing that DSS1 has a sulphur content per disaccharide of 7.8%, compared with 11.5% for DSS2, these results indicate that the polysaccharide affinity for HC II is increased only in the case of DSS 2, whereas the oversulphation increases the reactivities towards thrombin of both complexes DSS1-HC II and DSS2-HC II.	dss2	90-94	serpin family D member 1	Homo sapiens	156-161
9068899-5	1997	Knowing that DSS1 has a sulphur content per disaccharide of 7.8%, compared with 11.5% for DSS2, these results indicate that the polysaccharide affinity for HC II is increased only in the case of DSS 2, whereas the oversulphation increases the reactivities towards thrombin of both complexes DSS1-HC II and DSS2-HC II.	Polysaccharides	128-142	serpin family D member 1	Homo sapiens	156-161
9068899-8	1997	The experimental data obtained for CMDBS fit a kinetic model in which the biospecific dextran derivative rapidly forms a complex with thrombin which is more reactive towards HC II than the free protease.	Dextrans	86-93	serpin family D member 1	Homo sapiens	174-179
9157603-6	1997	In terms of in vitro anticoagulant activity assessed by use of purified human components, DHGs (DHG, HMW-DHG, and LMW-DHG) had different anti-thrombin activity in the presence of HCII and anti-factor Xase activities, which differences were dependent on the molecular weight.	dhg	90-93	serpin family D member 1	Homo sapiens	179-183
8885144-0	1996	Active site for heparin cofactor II in low molecular mass dermatan sulfate.	Dermatan Sulfate	58-74	serpin family D member 1	Homo sapiens	16-35
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 D member 1	Homo sapiens	99-118
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 D member 1	Homo sapiens	120-124
8902986-0	1996	A heparin cofactor II mutation (HCII Rimini) combined with factor V Leiden or type I protein C deficiency in two unrelated thrombophilic subjects.	Heparin	2-9	serpin family D member 1	Homo sapiens	32-36
8885144-4	1996	HCII is activated by the oversulfated sequence (IdoA2SO3-GalNAc4SO3)4 or by both the sequences (IdoA2SO3-GalNAc4SO3)n and (IdoA-GalNAc-4,6SO3)n, [n > or = 2].	(idoa2so3-galnac4so3)4	47-69	serpin family D member 1	Homo sapiens	0-4
8885144-4	1996	HCII is activated by the oversulfated sequence (IdoA2SO3-GalNAc4SO3)4 or by both the sequences (IdoA2SO3-GalNAc4SO3)n and (IdoA-GalNAc-4,6SO3)n, [n > or = 2].	idoa2so3-galnac4so3	48-67	serpin family D member 1	Homo sapiens	0-4
8885144-4	1996	HCII is activated by the oversulfated sequence (IdoA2SO3-GalNAc4SO3)4 or by both the sequences (IdoA2SO3-GalNAc4SO3)n and (IdoA-GalNAc-4,6SO3)n, [n > or = 2].	(idoa-galnac-4,6so3	122-141	serpin family D member 1	Homo sapiens	0-4
8885144-10	1996	The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS.	idoa-galnac-4,6so3 disaccharide	56-87	serpin family D member 1	Homo sapiens	31-35
8885144-10	1996	The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS.	Dermatan Sulfate	135-137	serpin family D member 1	Homo sapiens	31-35
8885144-10	1996	The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS.	galnac4so3	200-210	serpin family D member 1	Homo sapiens	31-35
8885144-10	1996	The important influence on the HCII activity of natural IdoA-GalNAc-4,6SO3 disaccharide was confirmed by investigation on oversulfated DS obtained by a limited and selective chemical 6-O-sulfation in GalNAc4SO3 units of DS.	Dermatan Sulfate	220-222	serpin family D member 1	Homo sapiens	31-35
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Serine	32-38	serpin family D member 1	Homo sapiens	0-19
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Heparin	77-84	serpin family D member 1	Homo sapiens	21-25
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Dermatan Sulfate	89-105	serpin family D member 1	Homo sapiens	0-19
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Dermatan Sulfate	89-105	serpin family D member 1	Homo sapiens	21-25
8792767-7	1996	Pretreatment of monolayers with heparitinase I (and of extracellular matrix with HNO2) to degrade heparan sulfate blocked the thrombin-HCII inhibition rate increase.	Nitrous Acid	81-85	serpin family D member 1	Homo sapiens	135-139
8792767-7	1996	Pretreatment of monolayers with heparitinase I (and of extracellular matrix with HNO2) to degrade heparan sulfate blocked the thrombin-HCII inhibition rate increase.	Heparitin Sulfate	98-113	serpin family D member 1	Homo sapiens	135-139
8792767-10	1996	At a concentration of 1 microgram/mL hexuronic acid, high-charge HSPG stimulated a 7-fold thrombin-HCII inhibition rate increase relative to reactions without proteoglycan, whereas low-charge HSPG induced a 2-fold rate increase.	Hexuronic Acids	37-51	serpin family D member 1	Homo sapiens	99-103
8702860-7	1996	This was manifested by an increase in the second order rate constant of activation by thrombin for des-(868-1562)-factor VIII-HCII (12.0 +/- 0.48 x 10(6) M-1 s-1) compared with des-(868-1562)-factor VIII (1.77 +/- 0.21 x 10(6) M-1 s-1).	Diethylstilbestrol	99-102	serpin family D member 1	Homo sapiens	126-130
8792767-1	1996	Heparin cofactor II (HCII) is a potent thrombin inhibitor in the presence of heparin and dermatan sulfate, glycosaminoglycans that accelerate the inhibition reaction.	Heparin	77-84	serpin family D member 1	Homo sapiens	0-19
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Serine	32-38	serpin family D member 1	Homo sapiens	21-25
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	0-19
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	21-25
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Heparin	146-153	serpin family D member 1	Homo sapiens	0-19
8562924-1	1996	Heparin cofactor II (HCII) is a serine proteinase inhibitor in human plasma that rapidly inhibits thrombin in the presence of dermatan sulfate or heparin.	Heparin	146-153	serpin family D member 1	Homo sapiens	21-25
8562924-3	1996	Polymerase chain reaction (PCR)-based sequence analysis showed that the propositus" gene for HCII (HCII Awaji gene) had a thymine insertion after codon (GAT) for Asp88 in exon II, resulting in a frameshift mutation.	Thymine	122-129	serpin family D member 1	Homo sapiens	93-97
8562924-3	1996	Polymerase chain reaction (PCR)-based sequence analysis showed that the propositus" gene for HCII (HCII Awaji gene) had a thymine insertion after codon (GAT) for Asp88 in exon II, resulting in a frameshift mutation.	Thymine	122-129	serpin family D member 1	Homo sapiens	99-103
8815580-3	1996	In conditioned medium, HuH-7 cells constantly produced HC II that was functionally active and formed a complex with thrombin in the presence of dermatan sulfate.	Dermatan Sulfate	144-160	serpin family D member 1	Homo sapiens	55-60
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 D member 1	Homo sapiens	54-73
8845462-4	1996	Using the HC II assay the elimination half-lives (T1/2 el) increased from 1.9 h to 3.3 h with increasing doses of LMW-dermatan sulfate.	lmw-dermatan sulfate	114-134	serpin family D member 1	Homo sapiens	10-15
9112638-1	1996	Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation.	Heparin	114-121	serpin family D member 1	Homo sapiens	0-19
9112638-1	1996	Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation.	Heparin	114-121	serpin family D member 1	Homo sapiens	21-26
9112638-1	1996	Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation.	Glycosaminoglycans	131-149	serpin family D member 1	Homo sapiens	0-19
9112638-1	1996	Heparin cofactor II (HC II) is a plasma glycoprotein which inhibits thrombin but not factor Xa and which requires heparin or other glycosaminoglycans for its activation.	Glycosaminoglycans	131-149	serpin family D member 1	Homo sapiens	21-26
8542607-6	1995	1.2), mainly oversulfated at C-2 of iduronic acid residues, showed comparatively higher anticoagulant activity (in the HC-II mediated thrombin inhibition test).	Iduronic Acid	36-49	serpin family D member 1	Homo sapiens	119-124
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 D member 1	Homo sapiens	69-74
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 D member 1	Homo sapiens	99-104
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 D member 1	Homo sapiens	69-74
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 D member 1	Homo sapiens	99-104
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 D member 1	Homo sapiens	78-83
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 D member 1	Homo sapiens	78-83
7588997-4	1995	However after a 2 min interaction, heparin showed an increase in the HC-II-thrombin interaction at higher concentrations.	Heparin	35-42	serpin family D member 1	Homo sapiens	69-74
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 D member 1	Homo sapiens	41-46
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 D member 1	Homo sapiens	41-46
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 D member 1	Homo sapiens	100-119
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 D member 1	Homo sapiens	205-224
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 D member 1	Homo sapiens	227-246
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 D member 1	Homo sapiens	248-252
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 D member 1	Homo sapiens	227-246
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 D member 1	Homo sapiens	248-252
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 D member 1	Homo sapiens	227-246
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 D member 1	Homo sapiens	248-252
7888673-4	1995	DHG inhibited the amidolytic activity of thrombin in the presence of HCII with a second order rate constant of 1.2 x 10(8) (mol/L)-1 min-1.	dhg	0-3	serpin family D member 1	Homo sapiens	69-73
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 D member 1	Homo sapiens	87-91
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 D member 1	Homo sapiens	150-154
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 D member 1	Homo sapiens	75-79
8091403-0	1994	Relative influence of different disulphate disaccharide clusters on the HCII-mediated inhibition of thrombin by dermatan sulphates of different origins.	disulphate disaccharide	32-55	serpin family D member 1	Homo sapiens	72-76
8091403-2	1994	The effect of the chemical removal of the sulphate groups on the HCII-mediated activity was studied.	Sulfates	42-50	serpin family D member 1	Homo sapiens	65-69
8091403-4	1994	When the content of sequences (IdoA-GalNAc4, 6SO3) is higher than that of sequences (IdoA2SO3-GalNAc4SO3), removal of the sulphate groups from Ido2SO3 reduces the HCII activity less than when the latter sequences prevail.	idoa-galnac4	31-43	serpin family D member 1	Homo sapiens	163-167
8091403-4	1994	When the content of sequences (IdoA-GalNAc4, 6SO3) is higher than that of sequences (IdoA2SO3-GalNAc4SO3), removal of the sulphate groups from Ido2SO3 reduces the HCII activity less than when the latter sequences prevail.	6so3	45-49	serpin family D member 1	Homo sapiens	163-167
8091403-4	1994	When the content of sequences (IdoA-GalNAc4, 6SO3) is higher than that of sequences (IdoA2SO3-GalNAc4SO3), removal of the sulphate groups from Ido2SO3 reduces the HCII activity less than when the latter sequences prevail.	idoa2so3-galnac4so3	85-104	serpin family D member 1	Homo sapiens	163-167
8091403-4	1994	When the content of sequences (IdoA-GalNAc4, 6SO3) is higher than that of sequences (IdoA2SO3-GalNAc4SO3), removal of the sulphate groups from Ido2SO3 reduces the HCII activity less than when the latter sequences prevail.	Sulfates	122-130	serpin family D member 1	Homo sapiens	163-167
8091403-4	1994	When the content of sequences (IdoA-GalNAc4, 6SO3) is higher than that of sequences (IdoA2SO3-GalNAc4SO3), removal of the sulphate groups from Ido2SO3 reduces the HCII activity less than when the latter sequences prevail.	ido2so3	143-150	serpin family D member 1	Homo sapiens	163-167
8091403-5	1994	(IdoA-GalNAc4, 6SO3) cooperates with (IdoA2SO3-GalNAc4SO3) in the activation of the HCII.	idoa-galnac4	1-13	serpin family D member 1	Homo sapiens	84-88
8091403-5	1994	(IdoA-GalNAc4, 6SO3) cooperates with (IdoA2SO3-GalNAc4SO3) in the activation of the HCII.	6so3	15-19	serpin family D member 1	Homo sapiens	84-88
8091403-5	1994	(IdoA-GalNAc4, 6SO3) cooperates with (IdoA2SO3-GalNAc4SO3) in the activation of the HCII.	idoa2so3-galnac4so3	38-57	serpin family D member 1	Homo sapiens	84-88
8017769-1	1994	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Dermatan Sulfate	22-38	serpin family D member 1	Homo sapiens	54-58
8017769-1	1994	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Heparin	43-50	serpin family D member 1	Homo sapiens	54-58
8017769-2	1994	This may explain the observation that HCII binds nonspecifically to heparin oligosaccharides, but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate.	heparin oligosaccharides	68-92	serpin family D member 1	Homo sapiens	38-42
8017769-2	1994	This may explain the observation that HCII binds nonspecifically to heparin oligosaccharides, but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate.	hexasaccharide	130-144	serpin family D member 1	Homo sapiens	38-42
8017769-2	1994	This may explain the observation that HCII binds nonspecifically to heparin oligosaccharides, but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate.	Dermatan Sulfate	159-175	serpin family D member 1	Homo sapiens	38-42
8017769-3	1994	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	83-87
8017769-3	1994	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	114-118
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	89-93
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	196-200
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	89-93
8017769-4	1994	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	196-200
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	111-127	serpin family D member 1	Homo sapiens	0-19
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	111-127	serpin family D member 1	Homo sapiens	21-25
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	131-138	serpin family D member 1	Homo sapiens	0-19
7908224-1	1994	Heparin cofactor II (HCII) is a glycoprotein in human plasma that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	131-138	serpin family D member 1	Homo sapiens	21-25
8181003-7	1994	The HCII activities were evaluated for different relative molecular mass of dermatan sulfate.	Dermatan Sulfate	76-92	serpin family D member 1	Homo sapiens	4-8
8091403-0	1994	Relative influence of different disulphate disaccharide clusters on the HCII-mediated inhibition of thrombin by dermatan sulphates of different origins.	Dermatan Sulfate	112-130	serpin family D member 1	Homo sapiens	72-76
8091403-1	1994	Besides the major monosulphated disaccharide sequences (IdoA-GalNAc4SO3), dermatan sulphates (DS) contain the oversulphated sequences (IdoA2SO3-GalNAc4SO3) and (IdoA-GalNAc4, 6SO3), the concentration of which is correlated with the HCII-mediated inhibition of thrombin by DS.	Dermatan Sulfate	74-92	serpin family D member 1	Homo sapiens	232-236
1381850-4	1992	HCII was purified from the supernatant of barium citrate adsorbed normal human plasma by polyethylene glycol precipitation followed by affinity chromatography on heparin-Sepharose CL-6B and ion-exchange chromatography on a QAE-Sephadex A-50.	BARIUM CITRATE	42-56	serpin family D member 1	Homo sapiens	0-4
8259546-6	1993	DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	72-76
8259546-6	1993	DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation.	Heparin	51-58	serpin family D member 1	Homo sapiens	72-76
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Heparin	83-90	serpin family D member 1	Homo sapiens	59-63
8429040-9	1993	The rate constants for inhibition of wild-type thrombin by HCII in the presence of heparin or dermatan sulfate were 9.2 x 10(8) M-1 min-1 and 9.0 x 10(8) M-1 min-1, respectively.	Dermatan Sulfate	94-110	serpin family D member 1	Homo sapiens	59-63
8429040-10	1993	Compared to wild-type thrombin, the rate of inhibition by HCII with glycosaminoglycan was 5- to 15-fold slower for thrombins K52E and R70E and 50- to over 100-fold slower for thrombin R68E.	Glycosaminoglycans	68-85	serpin family D member 1	Homo sapiens	58-62
8470058-7	1993	The results from these studies on the mechanisms show that Suleparoide has anticoagulant activity primarily mediated through Heparin Cofactor-II (HC-II) and because of its novel mechanism of action, further investigations on the biochemical profile of Suleparoide are carried out.	suleparoid	59-70	serpin family D member 1	Homo sapiens	125-144
8470058-7	1993	The results from these studies on the mechanisms show that Suleparoide has anticoagulant activity primarily mediated through Heparin Cofactor-II (HC-II) and because of its novel mechanism of action, further investigations on the biochemical profile of Suleparoide are carried out.	suleparoid	59-70	serpin family D member 1	Homo sapiens	146-151
8470058-10	1993	However, in the HC-II mediated inhibitory assay for IIa, Suleparoide exhibited significant activity.	suleparoid	57-68	serpin family D member 1	Homo sapiens	16-21
8362268-1	1993	A chemically synthesized pentasaccharide, a specific ligand for AT III, and a synthetic, sulfated bis-lactobionic acid amide, a ligand for HC-II, were studied along with heparin to determine the relative contribution of AT III and HC II in the inhibition of protease activation in plasma.	bis-lactobionic acid amide	98-124	serpin family D member 1	Homo sapiens	139-144
8362268-6	1993	In the HC II-mediated inhibition of thrombin, heparin and lactobionic acid both had strong inhibitory actions.	Heparin	46-53	serpin family D member 1	Homo sapiens	7-12
8362268-6	1993	In the HC II-mediated inhibition of thrombin, heparin and lactobionic acid both had strong inhibitory actions.	lactobionic acid	58-74	serpin family D member 1	Homo sapiens	7-12
1381849-6	1992	HC II levels correlated significantly with AT III levels and with acute phase reactants including sialic acid, fibrinogen, and PAI-1.	N-Acetylneuraminic Acid	98-109	serpin family D member 1	Homo sapiens	0-5
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Heparin	102-109	serpin family D member 1	Homo sapiens	21-25
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Heparin	0-3	serpin family D member 1	Homo sapiens	21-25
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Dermatan Sulfate	120-136	serpin family D member 1	Homo sapiens	21-25
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 D member 1	Homo sapiens	154-173
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 D member 1	Homo sapiens	154-173
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 D member 1	Homo sapiens	175-179
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	serpin family D member 1	Homo sapiens	154-173
8335699-1	1993	Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors.	Heparin	62-69	serpin family D member 1	Homo sapiens	175-179
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 D member 1	Homo sapiens	61-65
1333106-3	1992	In the present study the inhibitory activity of HC II was investigated as function of various dermatan sulfate fractions and its stability was tested against oxidation reagents similar to thus secreted by activated leucocytes.	Dermatan Sulfate	94-110	serpin family D member 1	Homo sapiens	48-53
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 D member 1	Homo sapiens	86-91
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 D member 1	Homo sapiens	86-91
1333106-5	1992	Oxidation of HC II carbohydrate side chains with sodium periodate showed less inactivation effects than oxidation by chloramine T or ammonium peroxodisulfate.	metaperiodate	49-65	serpin family D member 1	Homo sapiens	13-18
1333106-5	1992	Oxidation of HC II carbohydrate side chains with sodium periodate showed less inactivation effects than oxidation by chloramine T or ammonium peroxodisulfate.	chloramine-T	117-129	serpin family D member 1	Homo sapiens	13-18
1333106-5	1992	Oxidation of HC II carbohydrate side chains with sodium periodate showed less inactivation effects than oxidation by chloramine T or ammonium peroxodisulfate.	ammonium peroxydisulfate	133-157	serpin family D member 1	Homo sapiens	13-18
1381850-1	1992	Heparin cofactor II (HCII) is a specific thrombin inhibitor; its inhibitory activity is stimulated by heparin (Hep) and dermatan sulfate (DS).	Dermatan Sulfate	138-140	serpin family D member 1	Homo sapiens	21-25
1381850-3	1992	We analyzed the effect of glycosaminoglycans (GAGs) and GAG-binding proteins on the HCII/thrombin interaction in more detail.	Glycosaminoglycans	26-44	serpin family D member 1	Homo sapiens	84-88
1381850-4	1992	HCII was purified from the supernatant of barium citrate adsorbed normal human plasma by polyethylene glycol precipitation followed by affinity chromatography on heparin-Sepharose CL-6B and ion-exchange chromatography on a QAE-Sephadex A-50.	Polyethylene Glycols	89-108	serpin family D member 1	Homo sapiens	0-4
1381850-4	1992	HCII was purified from the supernatant of barium citrate adsorbed normal human plasma by polyethylene glycol precipitation followed by affinity chromatography on heparin-Sepharose CL-6B and ion-exchange chromatography on a QAE-Sephadex A-50.	Heparin	162-169	serpin family D member 1	Homo sapiens	0-4
1381850-4	1992	HCII was purified from the supernatant of barium citrate adsorbed normal human plasma by polyethylene glycol precipitation followed by affinity chromatography on heparin-Sepharose CL-6B and ion-exchange chromatography on a QAE-Sephadex A-50.	sepharose CL 6B	170-185	serpin family D member 1	Homo sapiens	0-4
1381850-4	1992	HCII was purified from the supernatant of barium citrate adsorbed normal human plasma by polyethylene glycol precipitation followed by affinity chromatography on heparin-Sepharose CL-6B and ion-exchange chromatography on a QAE-Sephadex A-50.	qae-sephadex a	223-237	serpin family D member 1	Homo sapiens	0-4
1381850-8	1992	Using 0.03U/ml thrombin and 1nM HCII the stimulatory effect of GAGs was completely inhibited when Hep (less than or equal to 0.3 micrograms/ml) was preincubated with VN (60 micrograms/ml) and decreased to less than 50% when HS (50 micrograms/ml) was preincubated with VN (60 micrograms/ml).	Heparin	98-101	serpin family D member 1	Homo sapiens	32-36
1381850-8	1992	Using 0.03U/ml thrombin and 1nM HCII the stimulatory effect of GAGs was completely inhibited when Hep (less than or equal to 0.3 micrograms/ml) was preincubated with VN (60 micrograms/ml) and decreased to less than 50% when HS (50 micrograms/ml) was preincubated with VN (60 micrograms/ml).	Heparitin Sulfate	224-226	serpin family D member 1	Homo sapiens	32-36
1579900-0	1992	Use of purified dermatan sulfate for heparin cofactor II (HC II) assay.	Dermatan Sulfate	16-32	serpin family D member 1	Homo sapiens	37-56
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Heparin	105-112	serpin family D member 1	Homo sapiens	0-19
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Heparin	105-112	serpin family D member 1	Homo sapiens	21-25
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Dermatan Sulfate	117-133	serpin family D member 1	Homo sapiens	0-19
1521342-2	1992	Heparin cofactor II (HCII) is a thrombin inhibitor in human plasma, the activity of which is enhanced by heparin and dermatan sulfate.	Dermatan Sulfate	117-133	serpin family D member 1	Homo sapiens	21-25
1579900-0	1992	Use of purified dermatan sulfate for heparin cofactor II (HC II) assay.	Dermatan Sulfate	16-32	serpin family D member 1	Homo sapiens	58-63
1442260-1	1992	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Dermatan Sulfate	22-38	serpin family D member 1	Homo sapiens	54-58
1442260-1	1992	The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical.	Heparin	43-50	serpin family D member 1	Homo sapiens	54-58
1442260-2	1992	This may explain the observation that HCII binds non-specifically to heparin oligosaccharides but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate having the structure shown in Fig.	heparin oligosaccharides	69-93	serpin family D member 1	Homo sapiens	38-42
1442260-2	1992	This may explain the observation that HCII binds non-specifically to heparin oligosaccharides but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate having the structure shown in Fig.	hexasaccharide	130-144	serpin family D member 1	Homo sapiens	38-42
1442260-2	1992	This may explain the observation that HCII binds non-specifically to heparin oligosaccharides but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate having the structure shown in Fig.	Dermatan Sulfate	159-175	serpin family D member 1	Homo sapiens	38-42
1442260-4	1992	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	83-87
1442260-4	1992	The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo.	Dermatan Sulfate	27-43	serpin family D member 1	Homo sapiens	114-118
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	89-93
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Dermatan Sulfate	28-44	serpin family D member 1	Homo sapiens	196-200
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	89-93
1442260-5	1992	Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.	Heparin	48-55	serpin family D member 1	Homo sapiens	196-200
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Heparin	101-108	serpin family D member 1	Homo sapiens	0-19
1554154-5	1992	In fact, HRG is 10 times less effective than PF 4 in neutralizing the 50% antithrombin activity of HC II in the presence of DS.	Dermatan Sulfate	124-126	serpin family D member 1	Homo sapiens	99-104
1939083-0	1991	The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans.	Glycosaminoglycans	113-131	serpin family D member 1	Homo sapiens	32-51
1939083-4	1991	The N-terminal portion of HCII contains two acidic repeats (Glu56-Asp-Asp-Asp-Tyr-Leu-Asp and Glu69-Asp-Asp-Asp-Tyr-Ile-Asp) that may bind to anion-binding exosite I of thrombin to facilitate covalent complex formation.	asp-asp-tyr-leu-asp	70-89	serpin family D member 1	Homo sapiens	26-30
1939083-4	1991	The N-terminal portion of HCII contains two acidic repeats (Glu56-Asp-Asp-Asp-Tyr-Leu-Asp and Glu69-Asp-Asp-Asp-Tyr-Ile-Asp) that may bind to anion-binding exosite I of thrombin to facilitate covalent complex formation.	H-Asp-Asp-Asp-OH	66-77	serpin family D member 1	Homo sapiens	26-30
1939083-4	1991	The N-terminal portion of HCII contains two acidic repeats (Glu56-Asp-Asp-Asp-Tyr-Leu-Asp and Glu69-Asp-Asp-Asp-Tyr-Ile-Asp) that may bind to anion-binding exosite I of thrombin to facilitate covalent complex formation.	Tyr-Ile-Asp	112-123	serpin family D member 1	Homo sapiens	26-30
1831893-8	1991	The relationship between these severe venous thrombotic episodes and the HCII deficiency is discussed in relation to the dermatan sulphate-HCII couple physiology.	Dermatan Sulfate	121-138	serpin family D member 1	Homo sapiens	73-77
1718466-4	1991	The mean plasma HCII level was significantly higher in patients with acute deep vein thrombosis (DVT) under heparin therapy than in patients with a history of thrombosis, who were studied more than 3 months after the acute event, and were either on, or had been on, oral anticoagulant therapy.	Heparin	108-115	serpin family D member 1	Homo sapiens	16-20
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Heparin	101-108	serpin family D member 1	Homo sapiens	21-25
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Dermatan Sulfate	113-130	serpin family D member 1	Homo sapiens	0-19
2045458-1	1991	Heparin cofactor II (HCII) is an inhibitor of thrombin in human plasma whose activity is enhanced by heparin and dermatan sulphate.	Dermatan Sulfate	113-130	serpin family D member 1	Homo sapiens	21-25
2045458-7	1991	The HCII activity was evaluated as antithrombin dermatan sulphate cofactor activity.	Dermatan Sulfate	48-65	serpin family D member 1	Homo sapiens	4-8
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	109-125	serpin family D member 1	Homo sapiens	0-19
1646210-5	1991	The DS bound to the silica matrix was also tested as a chromatographic support for the purification of HCII from human plasma; the optimum conditions for HCII adsorption and desorption were determined.	Dermatan Sulfate	4-6	serpin family D member 1	Homo sapiens	103-107
1646210-5	1991	The DS bound to the silica matrix was also tested as a chromatographic support for the purification of HCII from human plasma; the optimum conditions for HCII adsorption and desorption were determined.	Dermatan Sulfate	4-6	serpin family D member 1	Homo sapiens	154-158
1646210-5	1991	The DS bound to the silica matrix was also tested as a chromatographic support for the purification of HCII from human plasma; the optimum conditions for HCII adsorption and desorption were determined.	Silicon Dioxide	20-26	serpin family D member 1	Homo sapiens	103-107
1646210-0	1991	Immobilization of dermatan sulphate on a silica matrix and its possible use as an affinity chromatography support for heparin cofactor II purification.	Dermatan Sulfate	18-35	serpin family D member 1	Homo sapiens	118-137
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	0-17	serpin family D member 1	Homo sapiens	121-140
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	0-17	serpin family D member 1	Homo sapiens	142-146
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	19-21	serpin family D member 1	Homo sapiens	121-140
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Dermatan Sulfate	19-21	serpin family D member 1	Homo sapiens	142-146
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Glycosaminoglycans	28-45	serpin family D member 1	Homo sapiens	121-140
1646210-1	1991	Dermatan sulphate (DS) is a glycosaminoglycan which catalyses specifically thrombin inhibition by a plasmatic inhibitor, Heparin cofactor II (HCII).	Glycosaminoglycans	28-45	serpin family D member 1	Homo sapiens	142-146
1646210-2	1991	DS was insolubilized on a silica matrix to study its interaction with HCII.	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	70-74
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Dermatan Sulfate	109-125	serpin family D member 1	Homo sapiens	21-25
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	129-136	serpin family D member 1	Homo sapiens	0-19
1671335-1	1991	Heparin cofactor II (HCII) is a 66-kDa plasma glycoprotein that inhibits thrombin rapidly in the presence of dermatan sulfate or heparin.	Heparin	129-136	serpin family D member 1	Homo sapiens	21-25
1994003-3	1991	Human genomic DNA was transfected into mouse L-M fibroblasts and two independently arising, clonal cell lines (L-S1 and L-S2) have been identified as expressing high-affinity serotonin (5-HT) uptake systems.	Serotonin	175-184	serpin family D member 1	Homo sapiens	120-124
1994003-4	1991	The 5-HT uptake characteristics of L-S1 and L-S2 are essentially comparable (in terms of Na+ dependence, temperature sensitivity, imipramine antagonizability, kinetic saturability and high affinities) and those of L-S1 have been reported previously.	Imipramine	130-140	serpin family D member 1	Homo sapiens	35-48
2266131-3	1990	Highly specific requirements with respect to the nature of the involved amino acids as well as to their spatial arrangements were found to be crucial for efficient activation of hLS2 by dermatan sulfate.	Dermatan Sulfate	186-202	serpin family D member 1	Homo sapiens	178-182
2028443-2	1991	Also when dermatan sulfate which does not enhance the action of AT III is used for the activation of HC II there is a considerable influence on the remaining thrombin activity which alters the test results.	Dermatan Sulfate	10-26	serpin family D member 1	Homo sapiens	101-106
2068567-8	1991	These differences, particularly the content of----4)alpha-IdoA(1----3)- beta-D-GalNAc4S6S(1----sequences (detected using SAX-HPLC as delta UA(1----3)-beta-D-GalNAc4S6S) may play an important role influencing the activity of dermatan sulfates to potentiate HC II inhibition of Factor IIa.	1----3)- beta-d-galnac4s6s	63-89	serpin family D member 1	Homo sapiens	256-261
2068567-8	1991	These differences, particularly the content of----4)alpha-IdoA(1----3)- beta-D-GalNAc4S6S(1----sequences (detected using SAX-HPLC as delta UA(1----3)-beta-D-GalNAc4S6S) may play an important role influencing the activity of dermatan sulfates to potentiate HC II inhibition of Factor IIa.	beta-d-galnac4s6s	72-89	serpin family D member 1	Homo sapiens	256-261
2266131-4	1990	In contrast, binding and activation of hLS2 by heparin seem to be determined mainly by the positive charge density of the involved inhibitor segment.	Heparin	47-54	serpin family D member 1	Homo sapiens	39-43
2266131-7	1990	Second, the acidic dimer is instrumental in glycosaminoglycan-mediated activation of hLS2.	Glycosaminoglycans	44-61	serpin family D member 1	Homo sapiens	85-89
2211700-0	1990	Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity.	dermatan sulfate hexasaccharide	15-46	serpin family D member 1	Homo sapiens	61-80
2096488-1	1990	Heparin cofactor II (HCII) is a thrombin inhibitor present in human plasma whose activity is enhanced by heparin.	Heparin	105-112	serpin family D member 1	Homo sapiens	0-19
2096488-1	1990	Heparin cofactor II (HCII) is a thrombin inhibitor present in human plasma whose activity is enhanced by heparin.	Heparin	105-112	serpin family D member 1	Homo sapiens	21-25
2211700-1	1990	Dermatan sulfate increases the rate of inhibition of thrombin by heparin cofactor II (HCII) approximately 1000-fold by providing a catalytic template to which both the inhibitor and the protease bind.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	65-84
2211700-1	1990	Dermatan sulfate increases the rate of inhibition of thrombin by heparin cofactor II (HCII) approximately 1000-fold by providing a catalytic template to which both the inhibitor and the protease bind.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	86-90
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	41-57	serpin family D member 1	Homo sapiens	20-24
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	41-57	serpin family D member 1	Homo sapiens	127-131
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	96-112	serpin family D member 1	Homo sapiens	20-24
2211700-4	1990	To characterize the HCII-binding site in dermatan sulfate, we isolated the smallest fragment of dermatan sulfate that bound to HCII with high affinity.	Dermatan Sulfate	96-112	serpin family D member 1	Homo sapiens	127-131
2211700-7	1990	The smallest HCII-binding fragments were hexasaccharides, of which approximately 6% bound.	hexasaccharides	41-56	serpin family D member 1	Homo sapiens	13-17
2211700-9	1990	Subsequently, hexasaccharides with the highest affinity for HCII were isolated by overloading the HCII-Sepharose column.	hexasaccharides	14-29	serpin family D member 1	Homo sapiens	60-64
2211700-9	1990	Subsequently, hexasaccharides with the highest affinity for HCII were isolated by overloading the HCII-Sepharose column.	hexasaccharides	14-29	serpin family D member 1	Homo sapiens	98-102
2211700-9	1990	Subsequently, hexasaccharides with the highest affinity for HCII were isolated by overloading the HCII-Sepharose column.	Sepharose	103-112	serpin family D member 1	Homo sapiens	60-64
2211700-9	1990	Subsequently, hexasaccharides with the highest affinity for HCII were isolated by overloading the HCII-Sepharose column.	Sepharose	103-112	serpin family D member 1	Homo sapiens	98-102
2211700-13	1990	Since IdoA(2-SO4)----GalNAc(4-SO4) comprises only approximately 5% of the disaccharides present in intact dermatan sulfate, clustering of these disaccharides must occur during biosynthesis to form the high-affinity binding site for HCII.	idoa(2-so4)----galnac	6-27	serpin family D member 1	Homo sapiens	232-236
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	20-27	serpin family D member 1	Homo sapiens	117-122
1962908-3	1990	The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction.	Heparin	103-110	serpin family D member 1	Homo sapiens	117-122
1962908-8	1990	Some low molecular weight heparin preparations have significant activity with HC II (approximately 10 to 20% that of standard heparin).	Heparin	26-33	serpin family D member 1	Homo sapiens	78-83
1962908-8	1990	Some low molecular weight heparin preparations have significant activity with HC II (approximately 10 to 20% that of standard heparin).	Heparin	126-133	serpin family D member 1	Homo sapiens	78-83
1962909-1	1990	The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system.	Heparin	34-41	serpin family D member 1	Homo sapiens	107-112
1962909-1	1990	The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system.	Heparin	61-69	serpin family D member 1	Homo sapiens	107-112
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 D member 1	Homo sapiens	107-112
2318889-0	1990	On the activation of human leuserpin-2, a thrombin inhibitor, by glycosaminoglycans.	Glycosaminoglycans	65-83	serpin family D member 1	Homo sapiens	27-38
2196322-2	1990	A role for HCII as an inhibitor of thrombin in the presence of dermatan sulfate and heparin has been proposed.	Dermatan Sulfate	63-79	serpin family D member 1	Homo sapiens	11-15
2196322-2	1990	A role for HCII as an inhibitor of thrombin in the presence of dermatan sulfate and heparin has been proposed.	Heparin	84-91	serpin family D member 1	Homo sapiens	11-15
2122537-0	1990	Heparin cofactor II inhibits thrombin-stimulated release of tissue plasminogen activator from cultured human endothelial cells in the presence of dermatan sulfate.	Dermatan Sulfate	146-162	serpin family D member 1	Homo sapiens	0-19
2122537-3	1990	In contrast, in the presence of dermatan sulfate, HC II inhibited thrombin stimulation of t-PA:Ag release more strongly than AT III did.	Dermatan Sulfate	32-48	serpin family D member 1	Homo sapiens	50-55
2122537-6	1990	Based on these results, it was suggested that HC II may inhibit an increase in fibrinolytic activity mediated by thrombin-stimulated endothelial cells in the liquid phase through a suppression of thrombin stimulation of t-PA:Ag release, when plasma is exposed to vascular smooth muscle cells or fibroblasts which synthesize a significant amount of dermatan sulfate.	Dermatan Sulfate	348-364	serpin family D member 1	Homo sapiens	46-51
2318889-4	1990	Deletion of another dimeric region, which spans a sequence with a high negative charge density, resulted in a strong reduction in the glycosaminoglycan-enhanced activity of hLS2.	Glycosaminoglycans	134-151	serpin family D member 1	Homo sapiens	173-177
2318889-6	1990	Based on our observations we propose a model for the activation of hLS2 by glycosaminoglycans.	Glycosaminoglycans	75-93	serpin family D member 1	Homo sapiens	67-71
2318889-7	1990	The key feature of this model is the suggestion that the glycosaminoglycan-enhanced reaction between hLS2 and thrombin is mediated by at least two regions of contact, involving both the reactive center region and the acidic domain of hLS2.	Glycosaminoglycans	57-74	serpin family D member 1	Homo sapiens	101-105
2318889-7	1990	The key feature of this model is the suggestion that the glycosaminoglycan-enhanced reaction between hLS2 and thrombin is mediated by at least two regions of contact, involving both the reactive center region and the acidic domain of hLS2.	Glycosaminoglycans	57-74	serpin family D member 1	Homo sapiens	234-238
2318889-8	1990	Binding of glycosaminoglycans to hLS2 is suggested to result first in the release of the acidic region from intramolecular interactions.	Glycosaminoglycans	11-29	serpin family D member 1	Homo sapiens	33-37
29787913-0	2018	Modulating the degree of fucosylation of fucosylated chondroitin sulfate enhances heparin cofactor II-dependent thrombin inhibition.	Chondroitin Sulfates	53-72	serpin family D member 1	Homo sapiens	82-101
2099324-3	1990	In these subjects HCII activity correlates inversely with fasting blood glucose and glycated proteins but not with Hb A1.	Glucose	72-79	serpin family D member 1	Homo sapiens	18-22
3217919-2	1988	DS accelerates thrombin inhibition by heparin cofactor II (HC II).	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	38-57
35196722-1	2022	OBJECTIVES:  The current trial aimed to compare lithium disilicate (LS2) endocrowns" clinical performance, gingival health, and parental satisfaction to those of prefabricated zirconia crowns (ZCs) over a 24-month of follow-up.	Lithium	48-55	serpin family D member 1	Homo sapiens	68-71
2760054-1	1989	Heparin cofactor II (HCII) is a highly specific serine proteinase inhibitor, which complexes covalently with thrombin in a reaction catalyzed by heparin and other polyanions.	Heparin	145-152	serpin family D member 1	Homo sapiens	0-19
2760054-1	1989	Heparin cofactor II (HCII) is a highly specific serine proteinase inhibitor, which complexes covalently with thrombin in a reaction catalyzed by heparin and other polyanions.	Heparin	145-152	serpin family D member 1	Homo sapiens	21-25
2760054-5	1989	Polyacrylamide gel electrophoresis showed that HCII(54-75) inhibited thrombin"s cleavage of both the A alpha and B beta polypeptides in fibrinogen.	polyacrylamide gels	0-18	serpin family D member 1	Homo sapiens	47-51
35057468-10	2022	The salt intakes were 7.6, 10.9, 14.7 and 22.4 g among participants in the four groups (LS1, LS2, HS1 and HS2 groups, respectively), which differed significantly in all groups (F = 252.020; all p < 0.05).	Salts	4-8	serpin family D member 1	Homo sapiens	93-96
35057468-11	2022	Compared to the LS1 and LS2 groups, the HS2 group had 310-381, 250-358 and 382-655 mL more amounts of water from the total water intake (TWI), total drinking fluids and water from food (all p < 0.05), respectively.	Water	102-107	serpin family D member 1	Homo sapiens	24-27
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Epoprostenol	66-78	serpin family D member 1	Homo sapiens	9-13
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Epoprostenol	79-91	serpin family D member 1	Homo sapiens	9-13
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Dermatan Sulfate	130-146	serpin family D member 1	Homo sapiens	9-13
2512688-4	1989	However, HCII caused a marked decrease in the thrombin-stimulated prostacyclin prostacyclin production in the presence of 2 mg/ml dermatan sulfate (DS).	Dermatan Sulfate	148-150	serpin family D member 1	Homo sapiens	9-13
2512688-5	1989	The significant inhibition by HCII occurred when the DS concentrations were 0.2 microgram/ml and higher.	Dermatan Sulfate	53-55	serpin family D member 1	Homo sapiens	30-34
2512688-6	1989	From these results we suggest that HCII may prevent a prostacyclin-induced inhibition of platelet aggregation for hemostasis when plasma is exposed to vascular smooth muscle cells or fibroblasts which synthesize a significant amount of DS.	Epoprostenol	54-66	serpin family D member 1	Homo sapiens	35-39
2512688-6	1989	From these results we suggest that HCII may prevent a prostacyclin-induced inhibition of platelet aggregation for hemostasis when plasma is exposed to vascular smooth muscle cells or fibroblasts which synthesize a significant amount of DS.	Dermatan Sulfate	236-238	serpin family D member 1	Homo sapiens	35-39
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Glycosaminoglycans	81-99	serpin family D member 1	Homo sapiens	49-53
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Dermatan Sulfate	101-117	serpin family D member 1	Homo sapiens	49-53
2713501-2	1989	An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed.	Heparin	122-129	serpin family D member 1	Homo sapiens	49-53
2922702-1	1989	Heparins from different species and tissues show similar levels of ATIII and HCII mediated anti-IIa activities.	Heparin	0-8	serpin family D member 1	Homo sapiens	77-81
2922702-3	1989	Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity.	Oligosaccharides	0-15	serpin family D member 1	Homo sapiens	246-250
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 D member 1	Homo sapiens	246-250
2922702-3	1989	Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity.	Heparin	106-113	serpin family D member 1	Homo sapiens	246-250
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 D member 1	Homo sapiens	98-102
3217919-2	1988	DS accelerates thrombin inhibition by heparin cofactor II (HC II).	Dermatan Sulfate	0-2	serpin family D member 1	Homo sapiens	59-64
3217919-11	1988	The assay is also sensitive to other HC II activators such as heparin and pentosan polysulfate.	Heparin	62-69	serpin family D member 1	Homo sapiens	37-42
3217919-11	1988	The assay is also sensitive to other HC II activators such as heparin and pentosan polysulfate.	Pentosan Sulfuric Polyester	74-94	serpin family D member 1	Homo sapiens	37-42
3169238-0	1988	Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II.	Phosphates	43-52	serpin family D member 1	Homo sapiens	90-109
3169238-2	1988	These phosphate-containing polyanions accelerate the HCII-thrombin reaction, as much as 1600-fold in the case of phosvitin.	polyanions	27-37	serpin family D member 1	Homo sapiens	53-57
3169238-0	1988	Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II.	polyanions	64-74	serpin family D member 1	Homo sapiens	90-109
3169238-3	1988	The HCII-thrombin reaction with both phosvitin and polynucleotides appears to follow the ternary complex mechanism.	Polynucleotides	51-66	serpin family D member 1	Homo sapiens	4-8
3169238-2	1988	These phosphate-containing polyanions accelerate the HCII-thrombin reaction, as much as 1600-fold in the case of phosvitin.	Phosphates	6-15	serpin family D member 1	Homo sapiens	53-57
3178923-5	1988	A synthetic imidazole derivative (1-methyl-4-nitro-5-chloro-imidazole, MNCI) develops cytostatic and cytocidal effects in two different permanent human lymphoblastoid cultures (LS2 and CH4) with threshold concentrations of 8 x 10(-5) and 6 x 10(-5) mol/l, respectively.	imidazole	12-21	serpin family D member 1	Homo sapiens	177-180
3169238-4	1988	The HCII-thrombin complex is rapidly formed in the presence of these phosphate polyanions (each at 10 micrograms/ml) when 125I-labeled thrombin is incubated with human plasma (ex vivo).	phosphate polyanions	69-89	serpin family D member 1	Homo sapiens	4-8
3169238-6	1988	Our results suggest that the antithrombotic effect of these phosphate-containing polyanions is mediated by HCII activation and not by ATIII.	Phosphates	60-69	serpin family D member 1	Homo sapiens	107-111
3169238-6	1988	Our results suggest that the antithrombotic effect of these phosphate-containing polyanions is mediated by HCII activation and not by ATIII.	polyanions	81-91	serpin family D member 1	Homo sapiens	107-111
3183355-3	1988	A statistically significant association was found between HC II and AT (r = 0.79), NT (r = 0.71) and albumin (r = 0.66) (P less than 0.001), and there was a negative association between HC II and bilirubin (r = -0.55, P less than 0.001).	Bilirubin	196-205	serpin family D member 1	Homo sapiens	186-191
3401503-0	1988	Studies on the structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II.	Heparin	42-49	serpin family D member 1	Homo sapiens	94-113
3401503-1	1988	The structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II (HC II) were investigated.	Heparin	31-38	serpin family D member 1	Homo sapiens	83-102
3401503-1	1988	The structural requirements of heparin for the catalysis of thrombin inhibition by heparin cofactor II (HC II) were investigated.	Heparin	31-38	serpin family D member 1	Homo sapiens	104-109
3401503-2	1988	A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III).	Heparin	31-38	serpin family D member 1	Homo sapiens	168-173
3178923-5	1988	A synthetic imidazole derivative (1-methyl-4-nitro-5-chloro-imidazole, MNCI) develops cytostatic and cytocidal effects in two different permanent human lymphoblastoid cultures (LS2 and CH4) with threshold concentrations of 8 x 10(-5) and 6 x 10(-5) mol/l, respectively.	1-methyl-5-chloro-4-nitroimidazole	34-69	serpin family D member 1	Homo sapiens	177-180
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Heparin	11-18	serpin family D member 1	Homo sapiens	134-153
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	120-136	serpin family D member 1	Homo sapiens	22-41
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	120-136	serpin family D member 1	Homo sapiens	43-48
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	138-140	serpin family D member 1	Homo sapiens	22-41
3348170-2	1988	Functional assays for heparin cofactor II (HC-II) are based on the inactivation of thrombin by HC-II in the presence of dermatan sulfate (DS).	Dermatan Sulfate	138-140	serpin family D member 1	Homo sapiens	43-48
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	serpin family D member 1	Homo sapiens	195-200
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Polysaccharides	127-141	serpin family D member 1	Homo sapiens	92-97
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Polysaccharides	127-141	serpin family D member 1	Homo sapiens	195-200
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Dermatan Sulfate	86-102	serpin family D member 1	Homo sapiens	0-19
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Dermatan Sulfate	86-102	serpin family D member 1	Homo sapiens	21-25
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Heparin	106-113	serpin family D member 1	Homo sapiens	0-19
2894851-1	1988	Heparin cofactor II (HCII) is an inhibitor of thrombin in plasma that is activated by dermatan sulfate or heparin.	Heparin	106-113	serpin family D member 1	Homo sapiens	21-25
2894851-11	1988	The recombinant HCII formed a complex with 125I-thrombin in a reaction that required the presence of heparin or dermatan sulfate.	Heparin	101-108	serpin family D member 1	Homo sapiens	16-20
2894851-11	1988	The recombinant HCII formed a complex with 125I-thrombin in a reaction that required the presence of heparin or dermatan sulfate.	Dermatan Sulfate	112-128	serpin family D member 1	Homo sapiens	16-20
3426230-1	1987	This study characterizes the structural and functional significance of sulfhydryl residues in human plasma heparin cofactor II (HCII).	Sulfhydryl Compounds	71-81	serpin family D member 1	Homo sapiens	107-126
3426230-1	1987	This study characterizes the structural and functional significance of sulfhydryl residues in human plasma heparin cofactor II (HCII).	Sulfhydryl Compounds	71-81	serpin family D member 1	Homo sapiens	128-132
3426230-2	1987	For quantification of sulfhydryl groups, the extinction coefficient of HCII was redetermined and found to be 0.593 ml mg-1 cm-1 using second-derivative spectroscopy and multicomponent analysis assuming 4, 10, and 2 residues of tryptophan, tyrosine, and tyrosine-O-sulfate per mole of protein, respectively.	Tryptophan	227-237	serpin family D member 1	Homo sapiens	71-75
3426230-2	1987	For quantification of sulfhydryl groups, the extinction coefficient of HCII was redetermined and found to be 0.593 ml mg-1 cm-1 using second-derivative spectroscopy and multicomponent analysis assuming 4, 10, and 2 residues of tryptophan, tyrosine, and tyrosine-O-sulfate per mole of protein, respectively.	Tyrosine	239-247	serpin family D member 1	Homo sapiens	71-75
3426230-2	1987	For quantification of sulfhydryl groups, the extinction coefficient of HCII was redetermined and found to be 0.593 ml mg-1 cm-1 using second-derivative spectroscopy and multicomponent analysis assuming 4, 10, and 2 residues of tryptophan, tyrosine, and tyrosine-O-sulfate per mole of protein, respectively.	tyrosine O-sulfate	253-271	serpin family D member 1	Homo sapiens	71-75
3426230-3	1987	The results show that tyrosine-O-sulfate residues in HCII and in cholecystokinin peptide fragments (as model compounds) do not significantly contribute to the absorbance spectrum from 280 to 300 nm.	tyrosine O-sulfate	22-40	serpin family D member 1	Homo sapiens	53-57
3426230-5	1987	Incubation of HCII with 0.1-10 mM dithioerythritol did not diminish its heparin-enhanced thrombin inhibition activity.	Dithioerythritol	34-50	serpin family D member 1	Homo sapiens	14-18
3426230-6	1987	Treatment with various sulfhydryl-specific reagents, including p-mercuribenzoate, HgCl2, and N-substituted maleimide derivatives, inactivated HCII.	Sulfhydryl Compounds	23-33	serpin family D member 1	Homo sapiens	142-146
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Dermatan Sulfate	22-38	serpin family D member 1	Homo sapiens	134-153
3426230-6	1987	Treatment with various sulfhydryl-specific reagents, including p-mercuribenzoate, HgCl2, and N-substituted maleimide derivatives, inactivated HCII.	4-mercuribenzoate	63-80	serpin family D member 1	Homo sapiens	142-146
3691797-0	1987	Binding of heparin or dermatan sulfate to thrombin is essential for the sulfated polysaccharide-accelerated inhibition of thrombin by heparin cofactor II.	Polysaccharides	81-95	serpin family D member 1	Homo sapiens	134-153
3426230-6	1987	Treatment with various sulfhydryl-specific reagents, including p-mercuribenzoate, HgCl2, and N-substituted maleimide derivatives, inactivated HCII.	Mercuric Chloride	82-87	serpin family D member 1	Homo sapiens	142-146
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Pyridoxal Phosphate	71-93	serpin family D member 1	Homo sapiens	0-19
3426230-6	1987	Treatment with various sulfhydryl-specific reagents, including p-mercuribenzoate, HgCl2, and N-substituted maleimide derivatives, inactivated HCII.	n-substituted maleimide	93-116	serpin family D member 1	Homo sapiens	142-146
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Pyridoxal Phosphate	71-93	serpin family D member 1	Homo sapiens	21-26
3426230-8	1987	However, complete methanethio derivatization of the sulfhydryl groups of HCII using methyl methanethiosulfonate did not alter heparin-catalyzed thrombin inhibition.	methanethio	18-29	serpin family D member 1	Homo sapiens	73-77
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Heparin	171-178	serpin family D member 1	Homo sapiens	0-19
3691797-1	1987	Heparin cofactor II (HC II) and thrombin were chemically modified with pyridoxal 5"-phosphate, and their effects on the inhibition of thrombin by HC II in the presence of heparin or dermatan sulfate were studied.	Dermatan Sulfate	182-198	serpin family D member 1	Homo sapiens	0-19
3426230-8	1987	However, complete methanethio derivatization of the sulfhydryl groups of HCII using methyl methanethiosulfonate did not alter heparin-catalyzed thrombin inhibition.	methyl methanethiosulfonate	84-111	serpin family D member 1	Homo sapiens	73-77
3691797-2	1987	The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate.	Heparin	84-91	serpin family D member 1	Homo sapiens	30-35
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 D member 1	Homo sapiens	0-4
3691797-2	1987	The inhibition of thrombin by HC II was enhanced about 7000-fold in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	95-111	serpin family D member 1	Homo sapiens	30-35
3691797-3	1987	However, this enhancement by heparin dwindled to 110- and 9.6-fold when the modified HC II and the modified thrombin, respectively, were substituted for native proteins.	Heparin	29-36	serpin family D member 1	Homo sapiens	85-90
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	serpin family D member 1	Homo sapiens	92-97
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Heparin	43-50	serpin family D member 1	Homo sapiens	195-200
3691797-5	1987	These results indicate that the binding of heparin or dermatan sulfate to both thrombin and HC II is required for the sulfated polysaccharide-dependent acceleration of the thrombin inhibition by HC II, and the binding to thrombin is more essential for the reaction.	Dermatan Sulfate	54-70	serpin family D member 1	Homo sapiens	92-97
3619144-11	1987	In contrast, the anticoagulant effect of dermatan sulfate is strictly dependent on HC II.	Dermatan Sulfate	41-57	serpin family D member 1	Homo sapiens	83-88
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	serpin family D member 1	Homo sapiens	87-106
3660328-1	1987	Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II).	Heparin	0-7	serpin family D member 1	Homo sapiens	108-113
3660328-9	1987	A modification of the distribution of both HC II and heparin between the vascular wall and the circulating blood is evoked to explain the relative increase in HC II activity and the need for higher heparin dosage in patients with low HC II levels.	Heparin	53-60	serpin family D member 1	Homo sapiens	159-164
3660328-9	1987	A modification of the distribution of both HC II and heparin between the vascular wall and the circulating blood is evoked to explain the relative increase in HC II activity and the need for higher heparin dosage in patients with low HC II levels.	Heparin	198-205	serpin family D member 1	Homo sapiens	43-48
3619144-4	1987	Dermatan sulfate and pentosan sulfate but not heparin sulfate increase the rate of thrombin inhibition by HC II.	Dermatan Sulfate	0-16	serpin family D member 1	Homo sapiens	106-111
3675584-0	1987	Carboxylate polyanions accelerate inhibition of thrombin by heparin cofactor II.	carboxylate polyanions	0-22	serpin family D member 1	Homo sapiens	60-79
3675584-1	1987	The heparin cofactor II (HCII)/thrombin inhibition reaction is enhanced by various carboxylate polyanions.	carboxylate polyanions	83-105	serpin family D member 1	Homo sapiens	4-23
3675584-1	1987	The heparin cofactor II (HCII)/thrombin inhibition reaction is enhanced by various carboxylate polyanions.	carboxylate polyanions	83-105	serpin family D member 1	Homo sapiens	25-29
3675584-2	1987	In the presence of polyaspartic acid, the HCII/thrombin reaction is accelerated more than 1000-fold with the second-order rate constant increasing from 3.2 x 10(4) M-1 min-1 (in the absence of polyAsp) to 3.6 x 10(7) M-1 min-1 as the polyAsp concentration is increased from 1 to 250 micrograms/ml.	polyaspartate	19-36	serpin family D member 1	Homo sapiens	42-46
3675584-3	1987	This accelerating effect was observed for HCII/thrombin, though to varying degrees, with other carboxylate polyanions.	carboxylate polyanions	95-117	serpin family D member 1	Homo sapiens	42-46
3675584-6	1987	It is possible that at physiological sites rich in carboxylate polyanions, thrombin may be preferentially inhibited by HCII.	carboxylate polyanions	51-73	serpin family D member 1	Homo sapiens	119-123
3603428-6	1987	In consumption coagulopathy, the HC II levels are as low as AT, possibly reflecting intravascular consumption accelerated by vascular glycosaminoglycans.	Glycosaminoglycans	134-152	serpin family D member 1	Homo sapiens	33-38
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	26-45
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Dermatan Sulfate	71-87	serpin family D member 1	Homo sapiens	47-51
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Heparitin Sulfate	89-104	serpin family D member 1	Homo sapiens	26-45
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Heparitin Sulfate	89-104	serpin family D member 1	Homo sapiens	47-51
3793724-1	1987	Inhibition of thrombin by heparin cofactor II (HCII) is accelerated by dermatan sulfate, heparan sulfate, and heparin.	Heparin	26-33	serpin family D member 1	Homo sapiens	47-51
3793724-6	1987	In contrast, treatment with chondroitinase ABC almost totally abolished the ability of these cells to activate HCII while chondroitinase AC had little or no effect, suggesting that dermatan sulfate was responsible for the activity observed.	Dermatan Sulfate	181-197	serpin family D member 1	Homo sapiens	111-115
3619144-4	1987	Dermatan sulfate and pentosan sulfate but not heparin sulfate increase the rate of thrombin inhibition by HC II.	pentosan sulfate	21-37	serpin family D member 1	Homo sapiens	106-111
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 D member 1	Homo sapiens	63-67
3301469-5	1987	Dermatan sulphate, a glycosaminoglycan, specifically activates HCII and increases its thrombin neutralizing activity by over a thousand fold.	Dermatan Sulfate	0-17	serpin family D member 1	Homo sapiens	63-67
3301469-10	1987	The specificity of dermatan sulphate for HCII has allowed the development of functional assays for this protein.	Dermatan Sulfate	19-36	serpin family D member 1	Homo sapiens	41-45
2436330-2	1986	As PPS has been shown to potentiate thrombin inhibition by the second heparin cofactor (HC II), the principle of this assay was to measure the formation of covalent complexes between HC II and the thrombin generated in plasma after contact activation and recalcification.	Pentosan Sulfuric Polyester	3-6	serpin family D member 1	Homo sapiens	88-93
2436330-2	1986	As PPS has been shown to potentiate thrombin inhibition by the second heparin cofactor (HC II), the principle of this assay was to measure the formation of covalent complexes between HC II and the thrombin generated in plasma after contact activation and recalcification.	Pentosan Sulfuric Polyester	3-6	serpin family D member 1	Homo sapiens	183-188
2436331-2	1986	Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively.	Heparin	0-7	serpin family D member 1	Homo sapiens	114-119
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 D member 1	Homo sapiens	114-119
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 D member 1	Homo sapiens	114-119
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 D member 1	Homo sapiens	90-95
3755134-0	1986	Molecular size of dermatan sulfate oligosaccharides required to bind and activate heparin cofactor II.	dermatan sulfate oligosaccharides	18-51	serpin family D member 1	Homo sapiens	82-101
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Heparin	88-95	serpin family D member 1	Homo sapiens	0-19
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Heparin	88-95	serpin family D member 1	Homo sapiens	21-25
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	99-115	serpin family D member 1	Homo sapiens	0-19
3755134-1	1986	Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	99-115	serpin family D member 1	Homo sapiens	21-25
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 D member 1	Homo sapiens	102-107
2432917-4	1986	The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively.	Heparin	32-39	serpin family D member 1	Homo sapiens	152-157
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 D member 1	Homo sapiens	152-157
3755134-2	1986	To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid.	Dermatan Sulfate	38-54	serpin family D member 1	Homo sapiens	76-80
3755134-2	1986	To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid.	Glycosaminoglycans	86-103	serpin family D member 1	Homo sapiens	76-80
3755134-2	1986	To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid.	metaperiodate	156-165	serpin family D member 1	Homo sapiens	76-80
3755134-2	1986	To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid.	[3h]borohydride	167-182	serpin family D member 1	Homo sapiens	76-80
3755134-2	1986	To determine the minimum structure of dermatan sulfate required to activate HCII, the glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid.	sulfuric acid	188-201	serpin family D member 1	Homo sapiens	76-80
3755134-4	1986	Purified fragments were then applied to a column of HCII bound to concanavalin A-Sepharose, and bound oligosaccharides were eluted with a gradient of sodium chloride.	Sepharose	81-90	serpin family D member 1	Homo sapiens	52-56
3755134-6	1986	Octasaccharides that bound to the HCII column had a greater negative charge than the run-through material based on anion-exchange chromatography, suggesting that they contained a greater number of sulfate groups per molecule.	octasaccharides	0-15	serpin family D member 1	Homo sapiens	34-38
3755134-6	1986	Octasaccharides that bound to the HCII column had a greater negative charge than the run-through material based on anion-exchange chromatography, suggesting that they contained a greater number of sulfate groups per molecule.	Sulfates	197-204	serpin family D member 1	Homo sapiens	34-38
3755134-7	1986	Fragments of dermatan sulfate containing a minimum of 12-14 sugar residues accelerated inhibition of thrombin by HCII.	Dermatan Sulfate	13-29	serpin family D member 1	Homo sapiens	113-117
3755134-7	1986	Fragments of dermatan sulfate containing a minimum of 12-14 sugar residues accelerated inhibition of thrombin by HCII.	Sugars	60-65	serpin family D member 1	Homo sapiens	113-117
3755134-9	1986	These studies suggest that HCII is activated by dermatan sulfate fragments greater than or equal to 12 residues in length that contain a specific octasaccharide sequence required for binding to the inhibitor.	Dermatan Sulfate	48-64	serpin family D member 1	Homo sapiens	27-31
3755134-9	1986	These studies suggest that HCII is activated by dermatan sulfate fragments greater than or equal to 12 residues in length that contain a specific octasaccharide sequence required for binding to the inhibitor.	Octasaccharide	146-160	serpin family D member 1	Homo sapiens	27-31
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 D member 1	Homo sapiens	63-67
3518132-3	1986	QAE-Sephadex A-50 chromatography provides a good separation of HCII from antithrombin III (AT) and most contaminants having a heparin affinity similar to that of HCII.	Heparin	126-133	serpin family D member 1	Homo sapiens	63-67
3518132-4	1986	HCII is eluted at 0.28 M NaCl from the heparin-Sepharose column.	Sodium Chloride	25-29	serpin family D member 1	Homo sapiens	0-4
3518132-4	1986	HCII is eluted at 0.28 M NaCl from the heparin-Sepharose column.	Heparin	39-46	serpin family D member 1	Homo sapiens	0-4
3518132-4	1986	HCII is eluted at 0.28 M NaCl from the heparin-Sepharose column.	Sepharose	47-56	serpin family D member 1	Homo sapiens	0-4
3518132-6	1986	Purified HCII shows an apparent Mr of 66,500 daltons as analyzed on SDS-polyacrylamide gel and 62,100 daltons by ultracentrifugation.	Sodium Dodecyl Sulfate	68-71	serpin family D member 1	Homo sapiens	9-13
3518132-6	1986	Purified HCII shows an apparent Mr of 66,500 daltons as analyzed on SDS-polyacrylamide gel and 62,100 daltons by ultracentrifugation.	polyacrylamide	72-86	serpin family D member 1	Homo sapiens	9-13
3518132-9	1986	Antibodies to HCII were made monospecific by immunoadsorption on HCII-free plasma linked to Sepharose 4B.	Sepharose	92-101	serpin family D member 1	Homo sapiens	14-18
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Heparin	13-20	serpin family D member 1	Homo sapiens	34-38
3003690-2	1986	The inhibitor, named human Leuserpin 2 (hLS2), comprises 480 amino acids and contains a leucine residue at its putative reactive center.	Leucine	88-95	serpin family D member 1	Homo sapiens	27-38
3003690-2	1986	The inhibitor, named human Leuserpin 2 (hLS2), comprises 480 amino acids and contains a leucine residue at its putative reactive center.	Leucine	88-95	serpin family D member 1	Homo sapiens	40-44
3841420-4	1985	The biological activity of the HC II was unchanged after labelling as was its migratory pattern by crossed immunoelectrophoresis in the presence of heparin or dermatan sulfate.	Heparin	148-155	serpin family D member 1	Homo sapiens	31-36
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	135-151	serpin family D member 1	Homo sapiens	13-32
3841420-4	1985	The biological activity of the HC II was unchanged after labelling as was its migratory pattern by crossed immunoelectrophoresis in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	159-175	serpin family D member 1	Homo sapiens	31-36
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	115-122	serpin family D member 1	Homo sapiens	0-19
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Heparin	115-122	serpin family D member 1	Homo sapiens	21-25
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	0-19
4041618-1	1985	Heparin cofactor II (HCII) is a glycoprotein in human plasma which inactivates thrombin rapidly in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	126-142	serpin family D member 1	Homo sapiens	21-25
4041618-2	1985	We have developed a functional assay for HCII in which inhibition of thrombin by plasma is determined in the presence of dermatan sulfate.	Dermatan Sulfate	121-137	serpin family D member 1	Homo sapiens	41-45
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	Sodium Dodecyl Sulfate	191-213	serpin family D member 1	Homo sapiens	26-30
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	Sodium Dodecyl Sulfate	191-213	serpin family D member 1	Homo sapiens	171-175
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	Sodium Dodecyl Sulfate	191-213	serpin family D member 1	Homo sapiens	171-175
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	polyacrylamide	214-228	serpin family D member 1	Homo sapiens	26-30
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	Sodium Dodecyl Sulfate	250-253	serpin family D member 1	Homo sapiens	26-30
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	Sodium Dodecyl Sulfate	250-253	serpin family D member 1	Homo sapiens	171-175
4041618-3	1985	The assay is specific for HCII by the following criteria: (a) under the conditions of the assay, 125I-thrombin forms complexes in plasma which comigrate with the thrombin-HCII complex during sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE); (b) activity detected by the assay is decreased in plasma absorbed with monospecific antibodies against HCII; and (c) purified antithrombin III (ATIII) is unreactive in the assay system.	Sodium Dodecyl Sulfate	250-253	serpin family D member 1	Homo sapiens	171-175
4041618-4	1985	Addition of Polybrene to the assay permits determination of HCII activity in samples containing less than or equal to 12 U/mL of heparin.	Hexadimethrine Bromide	12-21	serpin family D member 1	Homo sapiens	60-64
4041618-4	1985	Addition of Polybrene to the assay permits determination of HCII activity in samples containing less than or equal to 12 U/mL of heparin.	Heparin	129-136	serpin family D member 1	Homo sapiens	60-64
2998359-1	1985	Human plasma heparin cofactor II (HCII) inhibits thrombin by rapidly forming a stable, equimolar complex in the presence of heparin or dermatan sulfate.	Dermatan Sulfate	135-151	serpin family D member 1	Homo sapiens	34-38
3840916-2	1985	HC II was functionally determined by thrombin inhibition in the presence of heparin in AT III-free plasma prepared by immunoadsorption on anti-AT III-Sepharose 4B column.	Heparin	76-83	serpin family D member 1	Homo sapiens	0-5
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.	Sepharose	150-159	serpin family D member 1	Homo sapiens	0-5
3838315-2	1985	125I-labeled heparin cofactor II (HCII) was mixed with plasma and coagulation was initiated by addition of CaCl2, phospholipids, and kaolin or tissue factor.	Calcium Chloride	107-112	serpin family D member 1	Homo sapiens	13-32
3838315-3	1985	In the presence of 67 micrograms/ml of dermatan sulfate, radioactivity was detected in a band which corresponded to the thrombin-HCII complex (Mr = 96,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Dermatan Sulfate	39-55	serpin family D member 1	Homo sapiens	129-133
3838315-2	1985	125I-labeled heparin cofactor II (HCII) was mixed with plasma and coagulation was initiated by addition of CaCl2, phospholipids, and kaolin or tissue factor.	Phospholipids	114-127	serpin family D member 1	Homo sapiens	13-32
3838315-3	1985	In the presence of 67 micrograms/ml of dermatan sulfate, radioactivity was detected in a band which corresponded to the thrombin-HCII complex (Mr = 96,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	Sodium Dodecyl Sulfate	161-183	serpin family D member 1	Homo sapiens	129-133
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 D member 1	Homo sapiens	40-59
3838315-3	1985	In the presence of 67 micrograms/ml of dermatan sulfate, radioactivity was detected in a band which corresponded to the thrombin-HCII complex (Mr = 96,000) upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis.	polyacrylamide	184-198	serpin family D member 1	Homo sapiens	129-133
3838315-5	1985	The thrombin-HCII complex was undetectable when 5 units/ml of heparin was present or when prothrombin-deficient plasma was used.	Heparin	62-69	serpin family D member 1	Homo sapiens	13-17
3838315-7	1985	HCII inhibited leukocyte cathepsin G slowly, with a rate constant of 8 X 10(4) M-1 min-1 in the presence of dermatan sulfate.	Dermatan Sulfate	108-124	serpin family D member 1	Homo sapiens	0-4
3838315-8	1985	These results indicate that the protease specificity of HCII is more restricted than that of other plasma protease inhibitors and suggest that the anticoagulant effect of dermatan sulfate is due solely to inhibition of thrombin by HCII.	Dermatan Sulfate	171-187	serpin family D member 1	Homo sapiens	56-60
3838315-8	1985	These results indicate that the protease specificity of HCII is more restricted than that of other plasma protease inhibitors and suggest that the anticoagulant effect of dermatan sulfate is due solely to inhibition of thrombin by HCII.	Dermatan Sulfate	171-187	serpin family D member 1	Homo sapiens	231-235
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 D member 1	Homo sapiens	69-74
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 D member 1	Homo sapiens	75-94
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 D member 1	Homo sapiens	139-144
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	40-47	serpin family D member 1	Homo sapiens	69-74
6084876-0	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 D member 1	Homo sapiens	40-59
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	40-47	serpin family D member 1	Homo sapiens	139-144
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 D member 1	Homo sapiens	75-94
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	69-74
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	139-144
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 D member 1	Homo sapiens	69-74
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Sulfates	8-15	serpin family D member 1	Homo sapiens	139-144
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	69-74
6084876-7	1984	Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups.	Heparin	126-133	serpin family D member 1	Homo sapiens	139-144
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 D member 1	Homo sapiens	146-151
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.	Dextran Sulfate	41-56	serpin family D member 1	Homo sapiens	131-136
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 D member 1	Homo sapiens	131-136
6084876-6	1984	Heparin, dextran sulfate and chondroitin polysulfates 1 and 5 activated both HC II and AT III, while dermatan sulfate activated only HC II.	Heparin	0-7	serpin family D member 1	Homo sapiens	77-82
6525342-8	1984	Mild tryptic digestion of disulfide-cross-linked long S2, under conditions that resulted in partial production of short S2 from un-cross-linked LS2, produced peptides T1a and T1b (residues 1 to approximately 360), with one and two disulfide cross-links, respectively.	Disulfides	26-35	serpin family D member 1	Homo sapiens	144-147
6084876-6	1984	Heparin, dextran sulfate and chondroitin polysulfates 1 and 5 activated both HC II and AT III, while dermatan sulfate activated only HC II.	Dextran Sulfate	9-24	serpin family D member 1	Homo sapiens	77-82
6084876-6	1984	Heparin, dextran sulfate and chondroitin polysulfates 1 and 5 activated both HC II and AT III, while dermatan sulfate activated only HC II.	Chondroitin Sulfates	29-53	serpin family D member 1	Homo sapiens	77-82
6687888-0	1983	Activation of heparin cofactor II by dermatan sulfate.	Dermatan Sulfate	37-53	serpin family D member 1	Homo sapiens	14-33
6395434-3	1984	HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma.	Heparin	115-122	serpin family D member 1	Homo sapiens	0-4
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	161-177	serpin family D member 1	Homo sapiens	0-4
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 D member 1	Homo sapiens	0-4
6688430-5	1983	In contrast, with HC II inhibitor, the activities of the heparins depended only upon their charge densities and were independent of AT affinity.	Heparin	57-65	serpin family D member 1	Homo sapiens	18-23
6688430-9	1983	The behavior of the AT-inactive heparins, being fully active with HC II, demonstrates the functional domain necessary for AT binding is not needed to produce HC II activity.	Heparin	32-40	serpin family D member 1	Homo sapiens	66-71
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Dermatan Sulfate	155-171	serpin family D member 1	Homo sapiens	48-52
6687888-5	1983	The second order rate constant for the thrombin-HCII reaction reached a maximum value of 6.4 X 10(8) M-1 min-1 in the presence of 250-500 micrograms/ml of dermatan sulfate compared to 3.8 X 10(8) M-1 min-1 in the presence of 40-80 micrograms/ml of heparin.	Heparin	248-255	serpin family D member 1	Homo sapiens	48-52
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 D member 1	Homo sapiens	107-126
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 D member 1	Homo sapiens	128-132
6687888-2	1983	Heparin, dermatan sulfate, and heparan sulfate from bovine liver (in order of decreasing activity) activated HCII.	Heparin	0-7	serpin family D member 1	Homo sapiens	109-113
6687888-2	1983	Heparin, dermatan sulfate, and heparan sulfate from bovine liver (in order of decreasing activity) activated HCII.	Dermatan Sulfate	9-25	serpin family D member 1	Homo sapiens	109-113
6687888-2	1983	Heparin, dermatan sulfate, and heparan sulfate from bovine liver (in order of decreasing activity) activated HCII.	Heparitin Sulfate	31-46	serpin family D member 1	Homo sapiens	109-113
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	sulfated-dextran	87-103	serpin family D member 1	Homo sapiens	26-45
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	sulfated-dextran	87-103	serpin family D member 1	Homo sapiens	47-51
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	deae-sepharose	105-119	serpin family D member 1	Homo sapiens	26-45
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	deae-sepharose	105-119	serpin family D member 1	Homo sapiens	47-51
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	Heparin	26-33	serpin family D member 1	Homo sapiens	47-51
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	Sepharose	110-119	serpin family D member 1	Homo sapiens	26-45
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	Sepharose	110-119	serpin family D member 1	Homo sapiens	47-51
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	sephadex	143-157	serpin family D member 1	Homo sapiens	26-45
6895893-3	1982	The inhibitor, designated heparin cofactor II (HCII), was purified to homogeneity with sulfated-dextran, DEAE-Sepharose, heparin-Sepharose and Sephadex G-150.	sephadex	143-157	serpin family D member 1	Homo sapiens	47-51
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	130-137	serpin family D member 1	Homo sapiens	70-74
6895893-8	1982	The second-order rate constant for inhibition of thrombin by purified HCII increases from 5.0 X 10(5) M-1 min-1 in the absence of heparin to 4.5 x 10(8) M-1 min-1 at optimal heparin concentrations of 0.8 to 1.0 unit/ml.	Heparin	174-181	serpin family D member 1	Homo sapiens	70-74