PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
9743555-0	1998	Receptor-mediated activation of murine peritoneal macrophages by antithrombin III acts as a costimulatory signal for nitric oxide synthesis.	Nitric Oxide	117-129	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	65-81
10821379-4	2000	Heparin stimulates the activity of antithrombin, a serine-protease inhibitor.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	35-47
10213181-3	1999	An examination of the mechanism of heparin neutralization and protamine toxicity suggests that the reversal of heparin anticoagulation may only require a small arginine-rich fragment of protamine to electrostatically dissociate antithrombin III from its binding to a specific pentasaccharide sequence in heparin.	Heparin	111-118	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	228-244
10213181-3	1999	An examination of the mechanism of heparin neutralization and protamine toxicity suggests that the reversal of heparin anticoagulation may only require a small arginine-rich fragment of protamine to electrostatically dissociate antithrombin III from its binding to a specific pentasaccharide sequence in heparin.	Arginine	160-168	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	228-244
10213181-3	1999	An examination of the mechanism of heparin neutralization and protamine toxicity suggests that the reversal of heparin anticoagulation may only require a small arginine-rich fragment of protamine to electrostatically dissociate antithrombin III from its binding to a specific pentasaccharide sequence in heparin.	Heparin	111-118	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	228-244
9743555-1	1998	We evaluated the effect of antithrombin III (ATIII), a serine protease inhibitor (SERPIN), on induction of nitric oxide (NO) synthesis in murine peritoneal macrophages.	Nitric Oxide	107-119	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-43
9743555-1	1998	We evaluated the effect of antithrombin III (ATIII), a serine protease inhibitor (SERPIN), on induction of nitric oxide (NO) synthesis in murine peritoneal macrophages.	Nitric Oxide	107-119	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	45-50
9743555-2	1998	Incubation of macrophages with ATIII plus interferon-gamma (IFN-gamma) but not ATIII alone induced nitrite accumulation (a metabolite of NO) in a dose-dependent manner.	Nitrites	99-106	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	31-36
7744578-12	1995	The antimetastatic and anticoagulant activities of heparin were unrelated, as indicated by using heparin fractions with high and low affinity for antithrombin III.	Heparin	97-104	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	146-162
9129989-4	1997	Mb 28C3-1 was previously demonstrated to inhibit the heparin-accelerated formation of antithrombin III-thrombin complexes.	Heparin	53-60	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	86-102
9157603-0	1997	Antithrombin III-independent effect of depolymerized holothurian glycosaminoglycan (DHG) on acute thromboembolism in mice.	dhg	84-87	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-16
9157603-1	1997	A previous study in this laboratory showed that depolymerized holothurian glycosaminoglycan (DHG) has two different antithrombin III (ATIII)-independent inhibitory effects on the in vitro blood coagulation system: heparin cofactor II (HCII)-dependent inhibition of thrombin, and ATIII- and HCII-independent inhibition of factor X activation by factor IXa-factor VIIIa complex (Nagase et al.	holothurian glycosaminoglycan	62-91	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	116-132
9157603-1	1997	A previous study in this laboratory showed that depolymerized holothurian glycosaminoglycan (DHG) has two different antithrombin III (ATIII)-independent inhibitory effects on the in vitro blood coagulation system: heparin cofactor II (HCII)-dependent inhibition of thrombin, and ATIII- and HCII-independent inhibition of factor X activation by factor IXa-factor VIIIa complex (Nagase et al.	holothurian glycosaminoglycan	62-91	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	134-139
9157603-1	1997	A previous study in this laboratory showed that depolymerized holothurian glycosaminoglycan (DHG) has two different antithrombin III (ATIII)-independent inhibitory effects on the in vitro blood coagulation system: heparin cofactor II (HCII)-dependent inhibition of thrombin, and ATIII- and HCII-independent inhibition of factor X activation by factor IXa-factor VIIIa complex (Nagase et al.	holothurian glycosaminoglycan	62-91	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	279-285
9157603-1	1997	A previous study in this laboratory showed that depolymerized holothurian glycosaminoglycan (DHG) has two different antithrombin III (ATIII)-independent inhibitory effects on the in vitro blood coagulation system: heparin cofactor II (HCII)-dependent inhibition of thrombin, and ATIII- and HCII-independent inhibition of factor X activation by factor IXa-factor VIIIa complex (Nagase et al.	dhg	93-96	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	116-132
9157603-1	1997	A previous study in this laboratory showed that depolymerized holothurian glycosaminoglycan (DHG) has two different antithrombin III (ATIII)-independent inhibitory effects on the in vitro blood coagulation system: heparin cofactor II (HCII)-dependent inhibition of thrombin, and ATIII- and HCII-independent inhibition of factor X activation by factor IXa-factor VIIIa complex (Nagase et al.	dhg	93-96	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	134-139
9157603-1	1997	A previous study in this laboratory showed that depolymerized holothurian glycosaminoglycan (DHG) has two different antithrombin III (ATIII)-independent inhibitory effects on the in vitro blood coagulation system: heparin cofactor II (HCII)-dependent inhibition of thrombin, and ATIII- and HCII-independent inhibition of factor X activation by factor IXa-factor VIIIa complex (Nagase et al.	dhg	93-96	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	279-285
9157603-4	1997	DHG, unlike UFH and LMWH, exerted an in vivo antithrombotic effect even in mice with decreased plasma ATIII activity (about 30% of normal).	dhg	0-3	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	102-107
8808643-1	1996	Heparin and heparan sulfate are related glycosaminoglycans which demonstrate high-affinity interactions with a number of proteins, including antithrombin III.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-157
8808643-1	1996	Heparin and heparan sulfate are related glycosaminoglycans which demonstrate high-affinity interactions with a number of proteins, including antithrombin III.	Heparitin Sulfate	12-27	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-157
8808643-1	1996	Heparin and heparan sulfate are related glycosaminoglycans which demonstrate high-affinity interactions with a number of proteins, including antithrombin III.	Glycosaminoglycans	40-58	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-157
7575459-2	1995	Chromatography on antithrombin (AT)-Sepharose resulted in the separation of the 35S-labelled PGs into three fractions: PGs with no affinity for the gel (NA-PGs), PGs with low affinity (LA-PGs), and PGs with high affinity (HA-PGs) for antithrombin.	Sepharose	36-45	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	18-30
7744762-2	1995	O-Sulfation at C-3 of N-sulfated GlcN units concludes polymer modification and the formation of antithrombin binding regions in the biosynthesis of heparin/heparan sulfate.	Nitrogen	22-23	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7744762-2	1995	O-Sulfation at C-3 of N-sulfated GlcN units concludes polymer modification and the formation of antithrombin binding regions in the biosynthesis of heparin/heparan sulfate.	Glucosamine	33-37	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7744762-2	1995	O-Sulfation at C-3 of N-sulfated GlcN units concludes polymer modification and the formation of antithrombin binding regions in the biosynthesis of heparin/heparan sulfate.	Heparin	148-155	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7744762-2	1995	O-Sulfation at C-3 of N-sulfated GlcN units concludes polymer modification and the formation of antithrombin binding regions in the biosynthesis of heparin/heparan sulfate.	Heparitin Sulfate	156-171	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7744762-3	1995	The resulting GlcNSO3(3-OSO3) units are largely restricted to heparin chains with high affinity for antithrombin (HA heparin).	glcnso3	14-21	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	100-112
7744762-3	1995	The resulting GlcNSO3(3-OSO3) units are largely restricted to heparin chains with high affinity for antithrombin (HA heparin).	3-oso3	22-28	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	100-112
7744762-3	1995	The resulting GlcNSO3(3-OSO3) units are largely restricted to heparin chains with high affinity for antithrombin (HA heparin).	Heparin	62-69	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	100-112
8188336-4	1994	The purposes of this study were to determine (i) if gram-negative bacterial challenge affects circulating PA and mortality as Candida challenge does and (ii) if proteinase inhibitor treatment with aprotinin, antithrombin III, and alpha 1-proteinase inhibitor decreases circulating PA and increases the survival of burned mice infected with a bacterium.	Protactinium	281-283	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	208-224
7819073-4	1994	Fraxiparin also acted synergistically with heparin cofactor II and antithrombin III to promote megakaryocyte colony formation.	Nadroparin	0-10	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	67-83
8500274-0	1993	Monoclonal antibodies to heparan sulfate inhibit the formation of thrombin-antithrombin III complexes.	Heparitin Sulfate	25-40	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	75-91
8292610-9	1994	It is concluded that the murine myocardial microvasculature harbors at least two pools of antithrombin, the minor of which is in an activated configuration characteristic of association with heparin.	Heparin	191-198	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	90-102
8292610-4	1994	Addition of heparin educes antithrombin activity continuously into the perfusate during 6 min of recirculation.	Heparin	12-19	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
8292610-8	1994	The amount of antithrombin reacting rapidly with factor Xa is too low to detect as a burst of antithrombin activity eluted into the perfusate when the hearts are perfused with heparin.	Heparin	176-183	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	14-26
8292610-8	1994	The amount of antithrombin reacting rapidly with factor Xa is too low to detect as a burst of antithrombin activity eluted into the perfusate when the hearts are perfused with heparin.	Heparin	176-183	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	94-106
8500274-9	1993	Monoclonal antibodies to HS inhibited the binding of HS to antithrombin III and the formation of thrombin-antithrombin III complexes.	Heparitin Sulfate	25-27	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	59-75
8500274-9	1993	Monoclonal antibodies to HS inhibited the binding of HS to antithrombin III and the formation of thrombin-antithrombin III complexes.	Heparitin Sulfate	25-27	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	106-122
8500274-9	1993	Monoclonal antibodies to HS inhibited the binding of HS to antithrombin III and the formation of thrombin-antithrombin III complexes.	Heparitin Sulfate	53-55	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	59-75
8500274-13	1993	Anti-HS antibodies may promote a procoagulant state by the blockade of HS binding to antithrombin III, inhibiting the accelerated formation of thrombin-antithrombin III complexes.	Heparitin Sulfate	5-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	85-101
8500274-13	1993	Anti-HS antibodies may promote a procoagulant state by the blockade of HS binding to antithrombin III, inhibiting the accelerated formation of thrombin-antithrombin III complexes.	Heparitin Sulfate	5-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	152-168
2263629-1	1990	We have demonstrated that mouse LTA cells synthesize cell-surface heparan sulfate proteoglycans (HSPGs) with regions of defined monosaccharide sequence that specifically interact with antithrombin (HSPGact).	Monosaccharides	128-142	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	184-196
1442267-5	1992	We have demonstrated that mouse LTA cells synthesize cell surface heparan sulfate proteoglycans with regions of defined monosaccharide sequence that specifically interact with antithrombin (HSPGact).	Monosaccharides	120-134	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	176-188
1442267-7	1992	To examine this issue, we treated LTA cells with ethylmethane sulfonate and then identified mutants that exhibit decreased antithrombin binding to heparan sulfate chains but possess no gross defects in glycosaminoglycan biosynthesis.	Ethyl Methanesulfonate	49-71	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	123-135
1442267-7	1992	To examine this issue, we treated LTA cells with ethylmethane sulfonate and then identified mutants that exhibit decreased antithrombin binding to heparan sulfate chains but possess no gross defects in glycosaminoglycan biosynthesis.	Heparitin Sulfate	147-162	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	123-135
1442267-5	1992	We have demonstrated that mouse LTA cells synthesize cell surface heparan sulfate proteoglycans with regions of defined monosaccharide sequence that specifically interact with antithrombin (HSPGact).	Heparitin Sulfate	66-81	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	176-188
1902219-12	1991	The products of [35S]sulfate transfer to the pentasaccharide GlcNSO3-GlcA-GlcNSO3-IdoA-GlcNSO3 contained molecules with high affinity for antithrombin, corresponding to 0.3-0.5% of the total label.	Sulfur-35	17-20	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	138-150
1902219-12	1991	The products of [35S]sulfate transfer to the pentasaccharide GlcNSO3-GlcA-GlcNSO3-IdoA-GlcNSO3 contained molecules with high affinity for antithrombin, corresponding to 0.3-0.5% of the total label.	Sulfates	21-28	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	138-150
1902219-12	1991	The products of [35S]sulfate transfer to the pentasaccharide GlcNSO3-GlcA-GlcNSO3-IdoA-GlcNSO3 contained molecules with high affinity for antithrombin, corresponding to 0.3-0.5% of the total label.	pentasaccharide	45-60	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	138-150
1902219-15	1991	These findings point to the importance of the uronic acid sequence in the generation of the antithrombin-binding region of heparin.	Uronic Acids	46-57	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	92-104
2024889-5	1991	We have demonstrated that mouse LTA cells synthesize cell surface heparan sulfate proteoglycans with regions of defined monosaccharide sequence that specifically interact with antithrombin (HSPGact).	Heparitin Sulfate	66-81	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	176-188
2024889-5	1991	We have demonstrated that mouse LTA cells synthesize cell surface heparan sulfate proteoglycans with regions of defined monosaccharide sequence that specifically interact with antithrombin (HSPGact).	Monosaccharides	120-134	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	176-188
2024889-7	1991	To examine this issue, we treated LTA cells with ethylmethane sulfonate and then identified mutants that exhibit decreased antithrombin binding to heparan sulfate chains but possess no gross defects in glycosaminoglycan biosynthesis.	Ethyl Methanesulfonate	49-71	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	123-135
2024889-7	1991	To examine this issue, we treated LTA cells with ethylmethane sulfonate and then identified mutants that exhibit decreased antithrombin binding to heparan sulfate chains but possess no gross defects in glycosaminoglycan biosynthesis.	Heparitin Sulfate	147-162	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	123-135
35563215-2	2022	Owing to the special pentasaccharide sequence, heparin specifically binds to antithrombin (AT) and increases the inhibitory activity of AT towards coagulation enzymes.	pentasaccharide	21-36	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	77-89
34541343-3	2021	The current study examined the effect of three vitamin E analogs-alpha-tocopherol (alpha-TOC), alpha-tocotrienol (alpha-T3), and gamma-tocotrienol (gamma-T3)-on Abeta aggregation, disaggregation, and oligomerization in vitro.	tocotrienol, alpha	95-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	114-122
34541343-4	2021	Thioflavin T (ThT) assay showed alpha-T3 reduced Abeta aggregation at 10 muM concentration.	thioflavin T	0-12	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	32-40
34541343-4	2021	Thioflavin T (ThT) assay showed alpha-T3 reduced Abeta aggregation at 10 muM concentration.	thioflavin T	14-17	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	32-40
34541343-5	2021	Furthermore, both alpha-T3 and gamma-T3 demonstrated Abeta disaggregation, as shown by the reduction of ThT fluorescence.	thioflavin T	104-107	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	18-26
35563215-2	2022	Owing to the special pentasaccharide sequence, heparin specifically binds to antithrombin (AT) and increases the inhibitory activity of AT towards coagulation enzymes.	Heparin	47-54	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	77-89
3930489-3	1985	The polysaccharide produced in the presence of butyrate showed a lower charge density on anion exchange chromatography than did the control material and a 3-fold increased proportion (54 versus 17% for the control) of components with high affinity for antithrombin.	Polysaccharides	4-18	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	252-264
3258496-5	1988	The results demonstrated that the clearance of 125I-labeled heparin cofactor II-alpha-thrombin is a receptor-mediated process, and that the same hepatocyte receptor system recognizes complexes containing heparin cofactor II, antithrombin III, and alpha 1-proteinase inhibitor.	Iodine-125	47-51	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	225-241
2964821-0	1988	Isolation of heparan sulfates with antithrombin III affinity and anticoagulant potency from BALB/c 3T3, B16.F10 melanoma, and cutaneous fibrosarcoma cell lines.	Heparitin Sulfate	13-29	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	35-51
2963617-0	1987	Basement-membrane heparan sulphate with high affinity for antithrombin synthesized by normal and transformed mouse mammary epithelial cells.	Heparitin Sulfate	18-34	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	58-70
3706560-5	1986	The acceleration of thrombin-antithrombin interactions in the presence of endothelial cell-derived glycosaminoglycans was similar for W/Wv and +/+ mice, was abolished with purified bacterial heparinase, and was expressed to only a minor extent when utilizing modified antithrombin.	Glycosaminoglycans	99-117	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	29-41
3706560-5	1986	The acceleration of thrombin-antithrombin interactions in the presence of endothelial cell-derived glycosaminoglycans was similar for W/Wv and +/+ mice, was abolished with purified bacterial heparinase, and was expressed to only a minor extent when utilizing modified antithrombin.	Glycosaminoglycans	99-117	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	268-280
2757391-5	1989	The generated thrombin was inhibited by antithrombin, and this reaction was accelerated by heparin with high affinity for antithrombin but not by the corresponding oligosaccharides composed of 8-14 monosaccharide units.	Heparin	91-98	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	122-134
2757391-6	1989	Such oligosaccharides which are capable of accelerating the inactivation of Factor Xa by antithrombin, inhibited thrombin formation from prothrombin in the macrophage cultures, presumably by promoting inactivation by antithrombin of Factor Xa in a prothrombinase complex.	Oligosaccharides	5-21	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	89-101
2757391-6	1989	Such oligosaccharides which are capable of accelerating the inactivation of Factor Xa by antithrombin, inhibited thrombin formation from prothrombin in the macrophage cultures, presumably by promoting inactivation by antithrombin of Factor Xa in a prothrombinase complex.	Oligosaccharides	5-21	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	217-229
3139669-4	1988	Fractionation of the resulting 35S-labeled octasaccharide on antithrombin-Sepharose yielded a high affinity fraction that accounted for approximately 2% of the total incorporated label.	Sulfur-35	31-34	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	61-73
3139669-4	1988	Fractionation of the resulting 35S-labeled octasaccharide on antithrombin-Sepharose yielded a high affinity fraction that accounted for approximately 2% of the total incorporated label.	Octasaccharide	43-57	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	61-73
3139669-4	1988	Fractionation of the resulting 35S-labeled octasaccharide on antithrombin-Sepharose yielded a high affinity fraction that accounted for approximately 2% of the total incorporated label.	Sepharose	74-83	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	61-73
3139669-6	1988	In contrast, the fractions with low affinity for antithrombin (approximately 98% of incorporated 35S) showed no consistent O-35S sulfation pattern and essentially lacked glucosaminyl 3-O-[35S]sulfate groups.	Sulfur-35	97-100	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	49-61
3139669-6	1988	In contrast, the fractions with low affinity for antithrombin (approximately 98% of incorporated 35S) showed no consistent O-35S sulfation pattern and essentially lacked glucosaminyl 3-O-[35S]sulfate groups.	o-35s	123-128	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	49-61
3139669-6	1988	In contrast, the fractions with low affinity for antithrombin (approximately 98% of incorporated 35S) showed no consistent O-35S sulfation pattern and essentially lacked glucosaminyl 3-O-[35S]sulfate groups.	glucosaminyl 3-o	170-186	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	49-61
3139669-6	1988	In contrast, the fractions with low affinity for antithrombin (approximately 98% of incorporated 35S) showed no consistent O-35S sulfation pattern and essentially lacked glucosaminyl 3-O-[35S]sulfate groups.	Sulfates	192-199	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	49-61
3139669-10	1988	The 35S-labeled pentasaccharide recovered after incubation bound with high affinity to antithrombin-Sepharose and contained a 3-O-[35S]sulfate group at the internal glucosamine residue as the only detectable labeled component.	Sulfur-35	4-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	87-99
3139669-10	1988	The 35S-labeled pentasaccharide recovered after incubation bound with high affinity to antithrombin-Sepharose and contained a 3-O-[35S]sulfate group at the internal glucosamine residue as the only detectable labeled component.	pentasaccharide	16-31	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	87-99
3139669-10	1988	The 35S-labeled pentasaccharide recovered after incubation bound with high affinity to antithrombin-Sepharose and contained a 3-O-[35S]sulfate group at the internal glucosamine residue as the only detectable labeled component.	Sepharose	100-109	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	87-99
2951375-0	1987	Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans.	Heparitin Sulfate	43-58	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
2951375-5	1987	A high proportion of antithrombin-binding sequence was also indicated by the finding that 3-O-sulfated glucosamine residues accounted for about 10% of the total O-sulfate groups.	Glucosamine	103-114	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	21-33
2951375-5	1987	A high proportion of antithrombin-binding sequence was also indicated by the finding that 3-O-sulfated glucosamine residues accounted for about 10% of the total O-sulfate groups.	o-sulfate	92-101	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	21-33
2951375-7	1987	Only a minor proportion of this polysaccharide bound with high affinity to antithrombin, and no 3-O-sulfated glucosamine residues were detected.	Polysaccharides	32-46	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	75-87
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Heparitin Sulfate	4-20	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	55-67
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Heparitin Sulfate	4-20	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	186-198
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Glucosamine	137-148	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	186-198
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Heparin	217-224	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	55-67
3816417-8	1986	The heparan sulphate from Reichert"s membrane bound to antithrombin with high affinity and was found to contain the unique 3-O-sulphated glucosamine residue previously identified in the antithrombin-binding region of heparin.	Heparin	217-224	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	186-198
3816417-9	1986	The EHS tumour heparan sulphate showed a higher N-/O-sulphate ratio and a lower affinity for antithrombin.	Heparitin Sulfate	15-31	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	93-105
3930489-3	1985	The polysaccharide produced in the presence of butyrate showed a lower charge density on anion exchange chromatography than did the control material and a 3-fold increased proportion (54 versus 17% for the control) of components with high affinity for antithrombin.	Butyrates	47-55	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	252-264
3930489-5	1985	The presence of butyrate thus leads to an inhibition of the N-deacetylation/N-sulfation process in heparin biosynthesis, along with an augmented formation of molecules with high affinity for antithrombin.	Butyrates	16-24	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	191-203
7306974-12	1981	Dansylarginine-N-(3-ethyl-1,5-pentanediyl)amide, a highly specific, potent antithrombin antagonist, inhibits LoVo-, HCT-8-, and Hut-20-induced platelet aggregation at 4 to 15 microM, whereas its effect on SV3T3 cells is negligible.	dansylarginine N-(3-ethyl-1,5-pentanediyl)amide	0-47	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	75-87
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	69-76	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	69-76	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-153
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	110-117	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	96-108
7150243-11	1982	Factor Xa produced by the macrophages was efficiently inactivated by heparin in the presence of antithrombin, heparin with high affinity for antithrombin being more effective than the corresponding low-affinity species.	Heparin	110-117	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	141-153
6202716-4	1984	In the presence of heparin, virtually 100% of the 125I-Factor IXa was bound to ATIII by 1 min.	Heparin	19-26	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	79-84
6178438-4	1982	The clearance of 125I-labeled alpha 1-proteinase inhibitor-trypsin and 125I-labeled antithrombin III-thrombin was blocked by large molar excesses of either ligand, but not by alpha 2-macroglobulin-methylamine.	Iodine-125	71-75	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	84-100
30234153-0	2018	Antithrombin Perfluorocarbon Nanoparticles Improve Renal Allograft Function in a Murine Deceased Criteria Donor Model.	Fluorocarbons	13-28	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
33093292-3	2021	AT-III and heparinoids such as enoxaparin (ENX) demonstrate potent anti-inflammatory activity, reducing organ injury and modulating leukocyte (LEU) activation, independent of their anticoagulant effect.	Enoxaparin	31-41	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-6
6109005-4	1980	The interaction of heparin with tyrosine hydroxylase was studied in ways relating to the known interaction with antithrombin.	Heparin	19-26	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	112-124
31774537-8	2020	Systemic markers of hepatic injury, namely alanine aminotransaminase and thrombin/antithrombin levels were increased by HFD+VC co-exposures only in males.	Vinyl Chloride	124-126	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	82-94
28126521-1	2017	The HS3ST1 gene controls endothelial cell production of HSAT+ - a form of heparan sulfate containing a specific pentasaccharide motif that binds the anticoagulant protein antithrombin (AT).	Heparitin Sulfate	74-89	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	171-183
28126521-1	2017	The HS3ST1 gene controls endothelial cell production of HSAT+ - a form of heparan sulfate containing a specific pentasaccharide motif that binds the anticoagulant protein antithrombin (AT).	pentasaccharide	112-127	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	171-183
28124089-6	2017	Results showed an increase in plasma TF activity, endothelial TF expression, and thrombin-antithrombin (TAT) but lower antithrombin III (ATIII) level in mice that received celecoxib in comparison to those that received the vehicle.	Celecoxib	172-181	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	119-135
28124089-6	2017	Results showed an increase in plasma TF activity, endothelial TF expression, and thrombin-antithrombin (TAT) but lower antithrombin III (ATIII) level in mice that received celecoxib in comparison to those that received the vehicle.	Celecoxib	172-181	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	137-142
27613713-4	2016	Chronic exposure to TCDD (30 microg/kg every 4 days for 28 days) was associated with intrahepatic coagulation, indicated by increased plasma thrombin-antithrombin levels and hepatic fibrin(ogen) deposition.	Polychlorinated Dibenzodioxins	20-24	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	150-162
25929155-0	2015	Pharmacological characterization and antidiabetic activity of a long-acting glucagon-like peptide-1 analogue conjugated to an antithrombin III-binding pentasaccharide.	pentasaccharide	151-166	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	126-142
26633490-4	2015	MEA, not RA, intake dose-dependently reduced plasminogen activator inhibitor-1 activity and fibrinogen level; as well as restored antithrombin-III and protein C activities in plasma of diabetic mice.	madecassic acid	0-3	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	130-146
25929155-1	2015	AIMS: To examine the biological characteristics of a novel glucagon-like peptide-1 (GLP-1) conjugate, in which an antithrombin III (ATIII)-binding pentasaccharide is conjugated to d-Ala(8) GLP-1 using a tetraethylene glycol linker.	pentasaccharide	147-162	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	114-130
25929155-1	2015	AIMS: To examine the biological characteristics of a novel glucagon-like peptide-1 (GLP-1) conjugate, in which an antithrombin III (ATIII)-binding pentasaccharide is conjugated to d-Ala(8) GLP-1 using a tetraethylene glycol linker.	pentasaccharide	147-162	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	132-137
25929155-1	2015	AIMS: To examine the biological characteristics of a novel glucagon-like peptide-1 (GLP-1) conjugate, in which an antithrombin III (ATIII)-binding pentasaccharide is conjugated to d-Ala(8) GLP-1 using a tetraethylene glycol linker.	tetraethylene glycol	203-223	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	132-137
25153385-5	2014	CrataBL prolongs the activated partial thromboplastin time on human and mouse plasma, and it impairs the heparin-induced potentiation of antithrombin III and heparin-induced platelet activation in the presence of low-dose ADP.	Heparin	105-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	137-153
25153385-6	2014	It is likely that the dense track of positive charge on CrataBL surface competes with the heparin ability to bind to antithrombin III and to stimulate platelets.	Heparin	90-97	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	117-133
24118982-3	2013	Each FXIa subunit contains anion-binding sites (ABSs) on the apple 3 (A3) and catalytic domains that are required for normal heparin-mediated enhancement of FXIa inhibition by antithrombin.	Heparin	125-132	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	176-188
24398330-3	2014	We studied nonanticoagulant heparins produced by N-acetylation and oxidation/reduction (glycol-split) that lost antithrombin-binding affinity.	Heparin	28-36	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	112-124
22749941-5	2012	RESULTS: Administration of exogenous AT in AT(+/-) animals did not restore the values observed in WT mice, suggesting that intrahepatic AT might also offer protection against CCl(4).	Cefaclor	175-178	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	37-39
23665851-5	2013	RESULTS: Treatment with B. jararaca antithrombin (1 mg kg-1) 1 h before or after carrageenan administration significantly inhibited paw edema formation, reduced cell influx to the peritoneal cavity due to reduction in the migration of polymorphonuclear cells, and attenuated leukocyte rolling in the microcirculation of the cremaster muscle.The effects of antithrombin on vascular and cellular events of inflammation were completely abolished by treatment with the cyclo-oxygenase inhibitor indomethacin (4 mg kg-1), suggesting the involvement of prostacyclin in the mechanism of inflammation inhibition by B. jararaca antithrombin.	Indomethacin	491-503	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	36-48
23665851-5	2013	RESULTS: Treatment with B. jararaca antithrombin (1 mg kg-1) 1 h before or after carrageenan administration significantly inhibited paw edema formation, reduced cell influx to the peritoneal cavity due to reduction in the migration of polymorphonuclear cells, and attenuated leukocyte rolling in the microcirculation of the cremaster muscle.The effects of antithrombin on vascular and cellular events of inflammation were completely abolished by treatment with the cyclo-oxygenase inhibitor indomethacin (4 mg kg-1), suggesting the involvement of prostacyclin in the mechanism of inflammation inhibition by B. jararaca antithrombin.	Epoprostenol	547-559	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	36-48
23665851-7	2013	These findings suggest that antithrombin is effective in preventing paw edema formation, cell migration and leukocyte rolling induced by carrageenan in mice.	Carrageenan	137-148	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	28-40
23665851-0	2013	The anti-inflammatory action of Bothrops jararaca snake antithrombin on acute inflammation induced by carrageenan in mice.	Carrageenan	102-113	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	56-68
23665851-2	2013	The present study aimed to investigate the effects of Bothrops jararaca antithrombin on acute inflammation induced by carrageenan in mice.	Carrageenan	118-129	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	72-84
23673387-0	2013	Impact of antithrombin deficiency on efficacy of edoxaban and antithrombin-dependent anticoagulants, fondaparinux, enoxaparin, and heparin.	edoxaban	49-57	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	10-22
23673387-0	2013	Impact of antithrombin deficiency on efficacy of edoxaban and antithrombin-dependent anticoagulants, fondaparinux, enoxaparin, and heparin.	Fondaparinux	101-113	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	10-22
23673387-0	2013	Impact of antithrombin deficiency on efficacy of edoxaban and antithrombin-dependent anticoagulants, fondaparinux, enoxaparin, and heparin.	Enoxaparin	115-125	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	10-22
23673387-0	2013	Impact of antithrombin deficiency on efficacy of edoxaban and antithrombin-dependent anticoagulants, fondaparinux, enoxaparin, and heparin.	Heparin	131-138	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	10-22
23673387-10	2013	Edoxaban exerts a comparable antithrombotic effect even in mice with low plasma AT antigen and activity to that in wild-type mice.	edoxaban	0-8	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	80-82
23678987-2	2013	RESULTS: In this study, we showed a significant reduction of sialic acid content in neonatal antithrombin compared with adult antithrombin in mice.	N-Acetylneuraminic Acid	61-72	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	93-105
22749941-7	2012	An 85 kDa covalent complex involving AT was identified in immunoblottings of liver lysates from CCl(4)-treated animals.	Cefaclor	96-99	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	37-39
22446936-7	2012	Hyperglycemia of streptozotocin-induced diabetic mice receiving 200 syngeneic islets into the liver from a single donor was ameliorated with down-regulation of IFN-gamma production of natural killer T cells and neutrophils in the liver when ATIII but not vehicle was administered once at the time of islet transplantation.	Streptozocin	17-31	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	241-246
22008103-7	2012	Heparin with low affinity for antithrombin was equally as effective as standard heparin, which indicates antithrombin independent effects.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	30-42
22442348-5	2012	Early anticoagulation with 14E11 suppressed systemic thrombin- antithrombin complex formation, IL-6, and TNF-alpha levels, and reduced platelet consumption in the circulation and deposition in the blood vessels.	14e11	27-32	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	63-75
22008103-7	2012	Heparin with low affinity for antithrombin was equally as effective as standard heparin, which indicates antithrombin independent effects.	Heparin	0-7	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	105-117
22008103-7	2012	Heparin with low affinity for antithrombin was equally as effective as standard heparin, which indicates antithrombin independent effects.	Heparin	80-87	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	105-117
21048158-0	2011	Development of a recombinant antithrombin variant as a potent antidote to fondaparinux and other heparin derivatives.	Heparin	97-104	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	29-41
21048158-3	2011	To make the use of fondaparinux safer, we developed an antithrombin (AT) variant as a potent antidote to heparin derivatives.	Heparin	105-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	55-67
21048158-3	2011	To make the use of fondaparinux safer, we developed an antithrombin (AT) variant as a potent antidote to heparin derivatives.	Heparin	105-112	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	69-71
21048158-4	2011	This variant (AT-N135Q-Pro394) combines 2 mutations: substitution of Asn135 by a Gln to remove a glycosylation site and increase affinity for heparins, and the insertion of a Pro between Arg393 and Ser394 to abolish its anticoagulant activity.	Heparin	142-150	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	14-16
20888180-6	2010	In ex vivo experiments, SDS-PAGE showed that plasma of mice treated orally at dose 70 mg/kg induced the formation of covalently linked complexes between antithrombin III and thrombin.	Sodium Dodecyl Sulfate	24-27	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	153-169
19112103-1	2009	We have developed a potent antithrombin (AT)-heparin conjugate (ATH) that is retained in the lung to prevent pulmonary thrombosis associated with respiratory distress in premature newborns.	Heparin	45-52	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
19722571-4	2009	PA treatments at 2% and 4% significantly lowered plasminogen activator inhibitor-1 activity and fibrinogen level; increased plasma activity of antithrombin-III and protein C; decreased triglyceride content in plasma, heart, and liver; elevated glutathione level and the retention of glutathione peroxidase and catalase activities in heart and kidney.	protocatechuic acid	0-2	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	143-159
20807645-1	2010	Vascular endothelial cells (ECs) produce anticoagulant heparan sulfate (HSAT+)-a small subpopulation of heparan sulfate (HS) containing a specific pentasaccharide motif with high affinity for plasma antithrombin (AT).	Heparitin Sulfate	55-70	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	199-211
20807645-1	2010	Vascular endothelial cells (ECs) produce anticoagulant heparan sulfate (HSAT+)-a small subpopulation of heparan sulfate (HS) containing a specific pentasaccharide motif with high affinity for plasma antithrombin (AT).	hsat	72-76	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	199-211
20807645-1	2010	Vascular endothelial cells (ECs) produce anticoagulant heparan sulfate (HSAT+)-a small subpopulation of heparan sulfate (HS) containing a specific pentasaccharide motif with high affinity for plasma antithrombin (AT).	Heparitin Sulfate	104-119	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	199-211
20807645-1	2010	Vascular endothelial cells (ECs) produce anticoagulant heparan sulfate (HSAT+)-a small subpopulation of heparan sulfate (HS) containing a specific pentasaccharide motif with high affinity for plasma antithrombin (AT).	Heparitin Sulfate	72-74	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	199-211
19729010-0	2009	Effects of acrolein, a natural occurring aldehyde, on the anticoagulant serpin antithrombin.	Acrolein	11-19	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	79-91
19729010-0	2009	Effects of acrolein, a natural occurring aldehyde, on the anticoagulant serpin antithrombin.	Aldehydes	41-49	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	79-91
19729010-1	2009	We studied the effect of acrolein, an alpha,beta-unsaturated aldehyde that causes adduct-modification of lysine, cysteine, and histidine residues, on antithrombin, a key anticoagulant serpin.	Acrolein	25-33	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	150-162
19729010-5	2009	Acrolein, even at low dose, impaired the anticoagulant function of purified antithrombin by affecting its heparin affinity.	Acrolein	0-8	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	76-88
19729010-5	2009	Acrolein, even at low dose, impaired the anticoagulant function of purified antithrombin by affecting its heparin affinity.	Heparin	106-113	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	76-88
19729010-6	2009	However, higher concentrations of acrolein and long incubations are required to cause mild functional effects on plasma antithrombin and mice.	Acrolein	34-42	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	120-132
19573895-9	2009	Hyperglycaemia in vitro induced a transition of antithrombin to a form with low heparin affinity that explained the loss of anticoagulant activity, without generation of abnormal conformers (polymers or latent antithrombin).	Heparin	80-87	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	48-60
19112103-0	2009	Effect of covalent antithrombin-heparin complex on developmental mechanisms in the lung.	Heparin	32-39	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	19-31
18772359-4	2008	The light/dye endothelial injury model was used to elicit thrombus formation in DSS colitic mice treated with either hirudin, heparin, or antithrombin III.	dss	80-83	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	138-154
18772359-8	2008	However, all three antithrombin agents largely prevented the DSS-induced reduction in the time to flow cessation following light/dye injury, with hirudin offering complete protection.	dss	61-64	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	19-31
17139376-1	2006	Fondaparinux is a synthetic pentasaccharide that selectively inhibits factor Xa (FXa) in an antithrombin-dependent fashion.	pentasaccharide	28-43	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	92-104
17602735-8	2007	Na-MCS exhibited anticoagulation activity mainly by accelerating the inhibition of antithrombin III (AT-III) on coagulation factors FIIa and FXa in plasma.	na-mcs	0-6	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	83-99
17602735-8	2007	Na-MCS exhibited anticoagulation activity mainly by accelerating the inhibition of antithrombin III (AT-III) on coagulation factors FIIa and FXa in plasma.	na-mcs	0-6	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	101-107
17512574-9	2007	AT significantly prolonged times until thrombotic vessel occlusion in a dose-dependent manner and more effectively than heparin (p<0.05 vs. NaCl and heparin).	Sodium Chloride	143-147	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-2
17512574-9	2007	AT significantly prolonged times until thrombotic vessel occlusion in a dose-dependent manner and more effectively than heparin (p<0.05 vs. NaCl and heparin).	Heparin	152-159	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-2
16181716-5	2006	Acetaminophen treatment also significantly increased plasminogen activator inhibitor-1 (PAI-1) activity and plasma fibrinogen level, and decreased antithrombin III (AT-III) and protein C activities (P < 0.05).	Acetaminophen	0-13	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	147-163
16816478-5	2006	The gene expression of antithrombin in the liver and that of thrombomodulin in the aorta, liver and kidney were down-regulated in hypo- and normocalcemic VDRKO mice, whereas tissue factor gene expression in the liver and kidney was up-regulated in VDRKO mice regardless of plasma calcium level.	Calcium	280-287	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	23-35
16181716-5	2006	Acetaminophen treatment also significantly increased plasminogen activator inhibitor-1 (PAI-1) activity and plasma fibrinogen level, and decreased antithrombin III (AT-III) and protein C activities (P < 0.05).	Acetaminophen	0-13	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	165-171
15570020-9	2004	These cysteine-containing agents elevated the activity of 2 fibrinolytic factors, protein C and antithrombin III (P < 0.05).	Cysteine	6-14	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	90-112
12356477-3	2002	In the present work, a method is presented which induces the conversion of native AT to L-AT, using incubation at 60 degrees C, for 16 h, with 0.9 M ammonium sulfate, in 5mM Hepes buffer, pH 7.4, giving a recovery of more than 70%.	Ammonium Sulfate	149-165	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	82-84
14718579-1	2004	SanOrg123781A is a synthetic hexadecasaccharide that displays antithrombin-dependent inhibition of factor Xa and thrombin and potent antithrombotic effects.	hexadecasaccharide	29-47	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	62-74
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	pentasaccharide	134-149	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparin	170-177	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparitin Sulfate	178-193	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
14592998-1	2003	Antithrombin (AT) inhibits thrombin and some other coagulation factors in a reaction that is dramatically accelerated by binding of a pentasaccharide sequence present in heparin/heparan-sulfate to a heparin-binding site on AT.	Heparin	199-206	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-12
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparin	71-78	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparin	133-140	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparitin Sulfate	141-156	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
14592998-8	2003	This severe thrombotic phenotype underlines a critical function of the heparin-binding site of antithrombin and its interaction with heparin/heparan-sulfate moieties in health, reproduction, and survival, and represents an in vivo model for comparative analysis of heparin-derived and other antithrombotic molecules.	Heparin	133-140	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	95-107
12356477-3	2002	In the present work, a method is presented which induces the conversion of native AT to L-AT, using incubation at 60 degrees C, for 16 h, with 0.9 M ammonium sulfate, in 5mM Hepes buffer, pH 7.4, giving a recovery of more than 70%.	HEPES	174-179	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	82-84
12356477-4	2002	L-AT was determined by integration of the low heparin affinity peak when analyzed by the affinity chromatography method.	Heparin	46-53	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	2-4
11668419-5	2001	The chromogenic assays for antithrombin (AT), thrombin inhibition, and factor Xa inhibition demonstrated that this effect is related to heparin concentrations below 0.5 IU/ml.	Heparin	136-143	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	27-39
12127234-1	2002	A chromogenic bioassay was utilized to determine the antithrombin activity of the methylene chloride and methanol extracts prepared from forty-five plants of Russia.	Methylene Chloride	82-100	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	53-65
12127234-1	2002	A chromogenic bioassay was utilized to determine the antithrombin activity of the methylene chloride and methanol extracts prepared from forty-five plants of Russia.	Methanol	105-113	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	53-65
12044526-0	2002	Antithrombin III prevents concanavalin A-induced liver injury through inhibition of macrophage inflammatory protein-2 release and production of prostacyclin in mice.	Epoprostenol	144-156	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	0-16
12044526-7	2002	The inhibitory effect of AT-III on plasma ALT and MIP-2 in Con A-induced liver injury was attenuated by indomethacin (5 mg/kg, ip).	Indomethacin	104-116	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	25-31
12044526-9	2002	CONCLUSIONS: These findings suggest that AT-III prevents Con A-induced liver injury through an inhibition of MIP-2 release and a production of prostacyclin.	Epoprostenol	143-155	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	41-47
12975616-1	2002	Heparan sulfate that contains antithrombin binding sites is designated as anticoagulant heparan sulfate (HS(act)) since, in vitro, it dramatically enhances the neutralization of coagulation proteases by antithrombin.	Heparitin Sulfate	0-15	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	30-42
12975616-1	2002	Heparan sulfate that contains antithrombin binding sites is designated as anticoagulant heparan sulfate (HS(act)) since, in vitro, it dramatically enhances the neutralization of coagulation proteases by antithrombin.	Heparitin Sulfate	0-15	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	203-215
12975616-1	2002	Heparan sulfate that contains antithrombin binding sites is designated as anticoagulant heparan sulfate (HS(act)) since, in vitro, it dramatically enhances the neutralization of coagulation proteases by antithrombin.	Heparitin Sulfate	88-103	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	30-42
12975616-1	2002	Heparan sulfate that contains antithrombin binding sites is designated as anticoagulant heparan sulfate (HS(act)) since, in vitro, it dramatically enhances the neutralization of coagulation proteases by antithrombin.	Heparitin Sulfate	88-103	serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1	Mus musculus	203-215