PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 31048599-2 2019 Acquired antithrombin deficiency was suspected due to a refractory response to therapeutic anticoagulation with enoxaparin, unfractionated heparin, and fondaparinux, and a reduced antithrombin antigen level. Heparin 139-146 serpin family C member 1 Homo sapiens 9-21 30939369-6 2019 Increasing the magnesite dosage from 0.83 to 3.33 g L-1 promoted the phosphorus recovery efficiency from 2.2% to 78.3% at 3 d, which was attributed to sufficient Mg2+ supply. magnesium carbonate 15-24 serpin family C member 1 Homo sapiens 119-125 30939369-6 2019 Increasing the magnesite dosage from 0.83 to 3.33 g L-1 promoted the phosphorus recovery efficiency from 2.2% to 78.3% at 3 d, which was attributed to sufficient Mg2+ supply. Phosphorus 69-79 serpin family C member 1 Homo sapiens 119-125 30986390-18 2019 BEST PRACTICE ADVICE 10: Systemic heparin infusion is recommended for symptomatic deep vein thrombosis and portal and mesenteric vein thrombosis, but there are unresolved issues regarding monitoring with both the anti-Xa assay and the partial thromboplastin time due to cirrhosis-related antithrombin deficiency (heparin cofactor). Heparin 34-41 serpin family C member 1 Homo sapiens 288-300 31147454-0 2019 Trehalose: is it a potential inhibitor of antithrombin polymerization? Trehalose 0-9 serpin family C member 1 Homo sapiens 42-54 31147454-7 2019 Rep (2019) 5, 39] studies the role of trehalose in the prevention of the polymerization of antithrombin, which belongs to the serpin superfamily. Trehalose 38-47 serpin family C member 1 Homo sapiens 91-103 31147454-9 2019 The authors demonstrate that trehalose is able to prevent the in vitro polymerization of antithrombin, under conditions in which it usually tends to polymerize, and demonstrate it by using different techniques. Trehalose 29-38 serpin family C member 1 Homo sapiens 89-101 31147454-10 2019 However, the binding site of trehalose in antithrombin should be defined by site-directed mutagenesis. Trehalose 29-38 serpin family C member 1 Homo sapiens 42-54 31186035-1 2019 BACKGROUND: Normal levels of plasma antithrombin (AT) activity might decrease heparin requirements to achieve an adequate level of anticoagulation during treatment with extracorporeal membrane oxygenation (ECMO). Heparin 78-85 serpin family C member 1 Homo sapiens 36-48 30860622-11 2019 CONCLUSIONS: Apixaban concentrations were well correlated with PT (%), antithrombin, and dRVVT confirm test. apixaban 13-21 serpin family C member 1 Homo sapiens 71-83 30873657-12 2019 Acetazolamide improved prothrombin time, factor X, and antithrombin. Acetazolamide 0-13 serpin family C member 1 Homo sapiens 55-67 30886063-0 2019 Deciphering the role of trehalose in hindering antithrombin polymerization. Trehalose 24-33 serpin family C member 1 Homo sapiens 47-59 30322332-2 2019 PEG-Asp also lowers antithrombin (AT) levels. pegaspargase 0-7 serpin family C member 1 Homo sapiens 20-32 30714261-6 2019 Maintenance of patient-specific heparin concentrations during bypass is another key goal, since neonates have lower baseline antithrombin concentrations and, therefore, a higher risk for inadequate thrombin inhibition and postoperative bleeding. Heparin 32-39 serpin family C member 1 Homo sapiens 125-137 30886063-4 2019 Here, we screened small molecules to find potential leads that can reduce AT polymer formation. Polymers 77-84 serpin family C member 1 Homo sapiens 74-76 30886063-5 2019 We identified simple sugar molecules that successfully blocked polymer formation without a significant loss of normal activity of AT under specific buffer and temperature conditions. Sugars 21-26 serpin family C member 1 Homo sapiens 130-132 30886063-6 2019 Of these, trehalose proved to be most promising as it showed a marked decrease in the bead like polymeric structures of AT shown by electron microscopic analysis. Trehalose 10-19 serpin family C member 1 Homo sapiens 120-122 30886063-7 2019 A circular dichroism (CD) analysis indicated alteration in the secondary structure profile and an increased thermal stability of AT in the presence of trehalose. Trehalose 151-160 serpin family C member 1 Homo sapiens 129-131 30886063-8 2019 Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose. Guanidine 0-23 serpin family C member 1 Homo sapiens 60-62 30886063-8 2019 Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose. Guanidine 25-31 serpin family C member 1 Homo sapiens 60-62 30886063-8 2019 Guanidine hydrochloride (GdnHCl)-based unfolding studies of AT show the formation of a different intermediate in the presence of trehalose. Trehalose 129-138 serpin family C member 1 Homo sapiens 60-62 30886063-9 2019 A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid 42-92 serpin family C member 1 Homo sapiens 269-271 30886063-9 2019 A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid 42-92 serpin family C member 1 Homo sapiens 284-286 30886063-9 2019 A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate) 94-101 serpin family C member 1 Homo sapiens 269-271 30886063-9 2019 A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate) 94-101 serpin family C member 1 Homo sapiens 284-286 30886063-9 2019 A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. Trehalose 114-123 serpin family C member 1 Homo sapiens 269-271 30886063-9 2019 A time-dependent fluorescence study using 1,1"-bi(4-anilino)naphthalene-5,5"-disulfonic acid (Bis-ANS) shows that trehalose affects the initial conformational change step in transition from native to polymer state through its binding to exposed hydrophobic residues on AT thus making AT less polymerogenic. Trehalose 114-123 serpin family C member 1 Homo sapiens 284-286 30794399-2 2019 Thus, complexes between antithrombin and anti-VEGF RNA aptamers with single dithiophosphate moieties and thrombin and VEGF, respectively, display equilibrium dissociation constants KD of ca. dithiophosphate 76-91 serpin family C member 1 Homo sapiens 24-36 31090040-8 2019 Both baseline and nadir AT levels were significantly lower in severe than in mild and moderate AHB. nadir 18-23 serpin family C member 1 Homo sapiens 24-26 31090040-9 2019 Moreover, the concentration of AT negatively correlated with INR, aspartate aminotransferase, and total and conjugated bilirubin levels. Bilirubin 119-128 serpin family C member 1 Homo sapiens 31-33 31090040-10 2019 Interestingly, nadir AT levels positively correlated with the duration of hospitalization. nadir 15-20 serpin family C member 1 Homo sapiens 21-23 30262570-10 2019 The 5-year event-free survival was 80.9+-2.2% among patients assigned to antithrombin compared to 85.9+-2.0% in the unfractionated heparin group (P=0.06), and 86.2+-2.0% in the enoxaparin group (P=0.10). Enoxaparin 177-187 serpin family C member 1 Homo sapiens 73-85 30891093-2 2019 Therapeutic low molecular weight heparin is recommended, but it can be difficult to attain sufficient anticoagulation since low molecular weight heparin requires antithrombin to exert its anticoagulant effect. Heparin 145-152 serpin family C member 1 Homo sapiens 162-174 30845788-4 2019 Possible inter-species differences in the GAG-binding sites on antithrombin III, heparanase, and chemokines of the CCL and CXCL families were examined by sequence alignments, molecular modelling and assessment of surface electrostatic potentials to determine if one species of laboratory animal is likely to result in more clinically relevant data than another. Glycosaminoglycans 42-45 serpin family C member 1 Homo sapiens 63-79 30891093-3 2019 We carried out a multicentre case-series assessing the dose of low molecular weight heparin required to achieve therapeutic anti-activated factor X levels in pregnant women with antithrombin deficiency. Heparin 84-91 serpin family C member 1 Homo sapiens 178-190 30791534-4 2019 The most negatively charged surface and the maximum binding ability towards antithrombin III were found for the heparinized PU with the lowest amount of aryl azide/anchor sites. Polyurethanes 124-126 serpin family C member 1 Homo sapiens 76-92 30660948-0 2019 Monitoring of heparins in antithrombin-deficient patients. Heparin 14-22 serpin family C member 1 Homo sapiens 26-38 30660948-1 2019 INTRODUCTION: Heparins exert their anticoagulant effect through activation of antithrombin. Heparin 14-22 serpin family C member 1 Homo sapiens 78-90 30660948-2 2019 Whether antithrombin deficiency leads to clinically relevantly reduced anti-Xa activity of heparins is unknown. Heparin 91-99 serpin family C member 1 Homo sapiens 8-20 30660948-6 2019 RESULTS: Mean anti-Xa activity with LWMH was 0.55 IU/mL (0.30-0.74) (recovery 69%, 38-93%) in antithrombin-deficient subjects and 0.82 (0.71-0.89) IU/mL in controls (recovery 103%, 89-111%). lwmh 36-40 serpin family C member 1 Homo sapiens 94-106 30660948-9 2019 Antithrombin activity correlated with anti-Xa activity of UFH (R = 0.77) and LMWH (R = 0.66). Heparin 58-61 serpin family C member 1 Homo sapiens 0-12 30660948-9 2019 Antithrombin activity correlated with anti-Xa activity of UFH (R = 0.77) and LMWH (R = 0.66). Heparin, Low-Molecular-Weight 77-81 serpin family C member 1 Homo sapiens 0-12 30660948-12 2019 Standard LWMH- or UFH-doses are likely to lead to under treatment in antithrombin-deficient individuals. lwmh 9-13 serpin family C member 1 Homo sapiens 69-81 30660948-12 2019 Standard LWMH- or UFH-doses are likely to lead to under treatment in antithrombin-deficient individuals. Heparin 18-21 serpin family C member 1 Homo sapiens 69-81 30791534-4 2019 The most negatively charged surface and the maximum binding ability towards antithrombin III were found for the heparinized PU with the lowest amount of aryl azide/anchor sites. aryl azide 153-163 serpin family C member 1 Homo sapiens 76-92 30545931-0 2019 MPI-CDG with transient hypoglycosylation and antithrombin deficiency. mpi-cdg 0-7 serpin family C member 1 Homo sapiens 45-57 30072263-1 2019 OBJECTIVES: To determine whether precardiopulmonary bypass (CPB) normalization of antithrombin levels in infants to 100% improves heparin sensitivity and anticoagulation during CPB and has beneficial effects into the postoperative period. Heparin 130-137 serpin family C member 1 Homo sapiens 82-94 30072263-7 2019 Higher first post-heparin activated clotting times (sec) were observed in the antithrombin group despite similar initial heparin dosing. Heparin 18-25 serpin family C member 1 Homo sapiens 78-90 30072263-8 2019 There was an increase in heparin sensitivity in the antithrombin group. Heparin 25-32 serpin family C member 1 Homo sapiens 52-64 30618231-5 2019 At 3 d after I/R injury, NPcurcumin inhibited the increase in MMP-9, attenuated the decrease in occludin and zona occluden-1, and maintained BBB integrity. npcurcumin 25-35 serpin family C member 1 Homo sapiens 0-6 30808215-0 2019 The Antithrombin Effect of Ankaferd Hemostat (ABS) Is Related to the High Iron Content of the Medicine. Iron 74-78 serpin family C member 1 Homo sapiens 4-16 31069723-8 2019 Positive correlations between total cholesterol and APTT and between triglyceride and APTT and ATIII were found in the poorly controlled PGDM group. Triglycerides 69-81 serpin family C member 1 Homo sapiens 95-100 31069723-8 2019 Positive correlations between total cholesterol and APTT and between triglyceride and APTT and ATIII were found in the poorly controlled PGDM group. 9-hydroxy-11,15-dioxo-2,3,18,19-tetranorprost-5-ene-1,20-dioic acid 137-141 serpin family C member 1 Homo sapiens 95-100 30431449-2 2019 We encountered a case of inherited type I AT deficiency and identified the causative mutation; a novel c.7430A>G missense mutation in the SERPINC1 gene in which tyrosine was substituted for cysteine at the 292nd amino acid. Tyrosine 164-172 serpin family C member 1 Homo sapiens 141-149 30431449-2 2019 We encountered a case of inherited type I AT deficiency and identified the causative mutation; a novel c.7430A>G missense mutation in the SERPINC1 gene in which tyrosine was substituted for cysteine at the 292nd amino acid. Cysteine 193-201 serpin family C member 1 Homo sapiens 141-149 30774881-4 2019 Through an experimental and computational approach using fluorescence polarization, ITC, docking and molecular dynamics simulations we investigate the binding of these functionalized GAG derivatives to ten representative regulatory proteins including IL-8, IL-10, BMP-2, sclerostin, TIMP-3, CXCL-12, TGF-beta, FGF-1, FGF-2, and AT-III, and we establish structure-activity relationships for GAG recognition. Glycosaminoglycans 183-186 serpin family C member 1 Homo sapiens 328-334 32821443-7 2019 Conclusion: Both ATIII and pentoxifylline treatments had positive effects on fibrinogen, FDP, D-Dimer, AT III activity and DIC scores in patients with Gram-negative sepsis who developed DIC. Pentoxifylline 27-41 serpin family C member 1 Homo sapiens 103-109 31030756-5 2019 Low antithrombin III levels in blood circulation also affects the efficacy of Fondaparinux. Fondaparinux 78-90 serpin family C member 1 Homo sapiens 4-20 30574006-4 2018 It remains controversial as to which anticoagulation therapy, defined as antithrombin or antiplatelet therapy, is better for patients with CS and a PFO. Cesium 139-141 serpin family C member 1 Homo sapiens 73-85 30118980-5 2018 As proof of principle, we generated alkyne-modified heparin, immobilized it onto azide-incorporated acellular lungs, and demonstrated its bioactivity by Antithrombin III immobilization and Factor Xa inhibition. Alkynes 36-42 serpin family C member 1 Homo sapiens 153-169 30118980-5 2018 As proof of principle, we generated alkyne-modified heparin, immobilized it onto azide-incorporated acellular lungs, and demonstrated its bioactivity by Antithrombin III immobilization and Factor Xa inhibition. Heparin 52-59 serpin family C member 1 Homo sapiens 153-169 30319401-0 2018 Dexamethasone Preconditioning in Cardiac Procedures Reduces Decreased Antithrombin Activity and Is Associated to Beneficial Outcomes: Role of Endothelium. Dexamethasone 0-13 serpin family C member 1 Homo sapiens 70-82 29173042-0 2018 Antithrombin conformational modulation by D-myo-inositol 3,4,5,6-tetrakisphosphate (TMI), a novel scaffold for the development of antithrombotic agents. D-myo-inositol 3,4,5,6-tetrakisphosphate 42-82 serpin family C member 1 Homo sapiens 0-12 29173042-0 2018 Antithrombin conformational modulation by D-myo-inositol 3,4,5,6-tetrakisphosphate (TMI), a novel scaffold for the development of antithrombotic agents. 4-tolyl isocyanate 84-87 serpin family C member 1 Homo sapiens 0-12 29173042-1 2018 Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate. Glycosaminoglycans 104-122 serpin family C member 1 Homo sapiens 0-12 29173042-1 2018 Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate. Heparin 126-133 serpin family C member 1 Homo sapiens 0-12 29173042-1 2018 Antithrombin (AT) is a serpin that inhibits mainly thrombin and fXa after being activated by binding to glycosaminoglycans as heparin and heparan sulfate. Heparitin Sulfate 138-153 serpin family C member 1 Homo sapiens 0-12 29173042-3 2018 Recently, a new compound, named TMI, was discovered in our group with nanomolar affinity to antithrombin, and shown to be able to induce a partial activation of antithrombin. 4-tolyl isocyanate 32-35 serpin family C member 1 Homo sapiens 92-104 29173042-3 2018 Recently, a new compound, named TMI, was discovered in our group with nanomolar affinity to antithrombin, and shown to be able to induce a partial activation of antithrombin. 4-tolyl isocyanate 32-35 serpin family C member 1 Homo sapiens 161-173 29999301-1 2018 Factor Xa (fXa) inhibition by antithrombin (AT) enabled by heparin or heparan sulfate is critical for controlling blood coagulation. Heparitin Sulfate 70-85 serpin family C member 1 Homo sapiens 30-42 30077924-0 2018 Isolation of recombinant human antithrombin isoforms by Cellufine Sulfate affinity chromatography. cellufine sulfate 56-73 serpin family C member 1 Homo sapiens 31-43 30174468-1 2018 Fitusiran is an RNA interference therapeutic that targets antithrombin (AT) in the liver and interferes with AT translation by binding and degrading messenger RNA-AT, thereby silencing AT gene expression and preventing AT synthesis. Givosiran 0-9 serpin family C member 1 Homo sapiens 58-70 32254968-5 2018 With the introduction of heparin, the antithrombin III (AT-III) binding ability was significantly enhanced with prolonged APTT time. Heparin 25-32 serpin family C member 1 Homo sapiens 38-54 32254968-5 2018 With the introduction of heparin, the antithrombin III (AT-III) binding ability was significantly enhanced with prolonged APTT time. Heparin 25-32 serpin family C member 1 Homo sapiens 56-62 29999301-1 2018 Factor Xa (fXa) inhibition by antithrombin (AT) enabled by heparin or heparan sulfate is critical for controlling blood coagulation. Heparin 59-66 serpin family C member 1 Homo sapiens 30-42 29907123-0 2018 Overcoming heparin resistance in pregnant women with antithrombin deficiency: a case report and review of the literature. Heparin 11-18 serpin family C member 1 Homo sapiens 53-65 29733637-7 2018 The anticoagulant action of copolymers is probably mediated by antithrombin, but it differs from that of unfractionated heparin. copolymers 28-38 serpin family C member 1 Homo sapiens 63-75 29526957-6 2018 Rivaroxaban (15 mg) was continued for 6 months with no recurrence, indicating the efficacy of this factor Xa inhibitor for the treatment and prevention of VTE in patients with antithrombin deficiency. Rivaroxaban 0-11 serpin family C member 1 Homo sapiens 176-188 30181723-0 2018 Effect of Exogenous Antithrombin Administration on Anti-Xa Levels in Infants Treated With Enoxaparin. Enoxaparin 90-100 serpin family C member 1 Homo sapiens 20-32 30181723-1 2018 OBJECTIVES: Determine the effect of exogenous antithrombin III administration on low molecular weight heparin anti-Xa levels in the context of enoxaparin dosing in infants. Heparin 102-109 serpin family C member 1 Homo sapiens 46-62 30181723-1 2018 OBJECTIVES: Determine the effect of exogenous antithrombin III administration on low molecular weight heparin anti-Xa levels in the context of enoxaparin dosing in infants. Enoxaparin 143-153 serpin family C member 1 Homo sapiens 46-62 30181723-8 2018 The median dose of antithrombin III was 50 units/kg and was administered when patients were receiving a median enoxaparin dose of 1.71 mg/kg. Enoxaparin 111-121 serpin family C member 1 Homo sapiens 19-35 30181723-10 2018 CONCLUSIONS: These results demonstrated that administration of exogenous antithrombin III to infants who were being treated with enoxaparin results in a significant increase in anti-Xa levels. Enoxaparin 129-139 serpin family C member 1 Homo sapiens 73-89 30181723-12 2018 However, antithrombin III supplementation could be considered a potential option for patients who are unable to adequately achieve therapeutic anti-Xa levels with enoxaparin alone. Enoxaparin 163-173 serpin family C member 1 Homo sapiens 9-25 29561141-0 2018 Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin. Heparin 42-49 serpin family C member 1 Homo sapiens 109-121 29353463-0 2018 Protective effect of a newly developed fucose-deficient recombinant antithrombin against histone-induced endothelial damage. Fucose 39-45 serpin family C member 1 Homo sapiens 68-80 29353463-2 2018 In the present study, we sought to evaluate the protective effects of a newly developed fucose-deficient recombinant antithrombin. Fucose 88-94 serpin family C member 1 Homo sapiens 117-129 29561141-0 2018 Cooperative Interactions of Three Hotspot Heparin Binding Residues Are Critical for Allosteric Activation of Antithrombin by Heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 109-121 29561141-1 2018 Heparin allosterically activates the anticoagulant serpin, antithrombin, by binding through a sequence-specific pentasaccharide and inducing activating conformational changes in the protein. Heparin 0-7 serpin family C member 1 Homo sapiens 59-71 29561141-1 2018 Heparin allosterically activates the anticoagulant serpin, antithrombin, by binding through a sequence-specific pentasaccharide and inducing activating conformational changes in the protein. pentasaccharide 112-127 serpin family C member 1 Homo sapiens 59-71 29561141-2 2018 Three basic residues of antithrombin, Lys114, Lys125, and Arg129, have been shown to be hotspots for binding the pentasaccharide, but the molecular basis for such hotspot binding has been unclear. pentasaccharide 113-128 serpin family C member 1 Homo sapiens 24-36 29561141-5 2018 Rapid kinetic studies showed that the hotspot residue mutations progressively abrogated the ability of the pentasaccharide to bind productively to native antithrombin and to conformationally activate the serpin by engaging the hotspot residues in an induced-fit interaction. pentasaccharide 107-122 serpin family C member 1 Homo sapiens 154-166 29561141-6 2018 Examination of the antithrombin-pentasaccharide complex structure revealed that the hotspot residues form two adjoining binding pockets for critical sulfates of the pentasaccharide that structurally link these residues. pentasaccharide 32-47 serpin family C member 1 Homo sapiens 19-31 29561141-6 2018 Examination of the antithrombin-pentasaccharide complex structure revealed that the hotspot residues form two adjoining binding pockets for critical sulfates of the pentasaccharide that structurally link these residues. pentasaccharide 165-180 serpin family C member 1 Homo sapiens 19-31 29561141-7 2018 Together, these findings demonstrate that cooperative interactions of Lys114, Lys125, and Arg129 are critical for the productive induced-fit binding of the heparin pentasaccharide to antithrombin that allosterically activates the anticoagulant function of the serpin. IC 831423 156-179 serpin family C member 1 Homo sapiens 183-195 29784539-8 2018 These assays are not equivalent in terms of diagnosing protein abnormalities, associated with increased thrombotic incidence, and they have variable performance for reflecting impaired antithrombin binding capacity for heparin, reduced progressive inhibition of serine proteases, or accelerated switch rates to the latent and less active forms. Heparin 219-226 serpin family C member 1 Homo sapiens 185-197 29215785-0 2018 Expression and functional characterization of two natural heparin-binding site variants of antithrombin. Heparin 58-65 serpin family C member 1 Homo sapiens 91-103 29573524-2 2018 These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA). pentasaccharide 102-117 serpin family C member 1 Homo sapiens 72-84 29573524-2 2018 These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA). 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 127-133 serpin family C member 1 Homo sapiens 72-84 29573524-2 2018 These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA). 6s-glca 137-144 serpin family C member 1 Homo sapiens 72-84 29573524-2 2018 These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA). N-sulfo-D-glucosamine 145-150 serpin family C member 1 Homo sapiens 72-84 29573524-2 2018 These properties are principally based on the binding and activation of antithrombin (AT) through the pentasaccharide sequence GlcNAc/NS,6S-GlcA-GlcNS,3,6S-IdoA2S-GlcNS,6S (AGA*IA). 3,6s-idoa2s-glcns 151-168 serpin family C member 1 Homo sapiens 72-84 29215785-1 2018 Essentials Heparin-binding site (HBS) variants of antithrombin (AT) are associated with thrombosis risk. Heparin 11-18 serpin family C member 1 Homo sapiens 50-62 29215785-5 2018 SUMMARY: Background Several heparin-binding site (HBS) variants of antithrombin (AT) have been identified that predispose carriers to a higher incidence of thrombosis. Heparin 28-35 serpin family C member 1 Homo sapiens 67-79 30271699-4 2018 The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. Heparin 44-51 serpin family C member 1 Homo sapiens 102-118 30271699-4 2018 The impact of temperature on the binding of heparin to three representative heparin-binding proteins, antithrombin III (AT III), fibroblast growth factor-1 (FGF1) and fibroblast growth factor-2 (FGF2) are evaluated. Heparin 44-51 serpin family C member 1 Homo sapiens 120-126 30271699-6 2018 In the two state binding process between AT III and heparin, temperature played a negligible role on ATIII binding to heparin (1st state reaction), but demonstrated a role in the conformational change process (2nd state reaction). Heparin 118-125 serpin family C member 1 Homo sapiens 41-47 28301908-1 2018 Thrombate III is a human plasma-derived antithrombin III (AT-III) often utilized in patients on extracorporeal membrane oxygenation (ECMO) with suspected AT-III-mediated heparin resistance. Heparin 170-177 serpin family C member 1 Homo sapiens 58-64 28888219-10 2018 CONCLUSIONS: Residual plasma rivaroxaban at the trough steady state may explain the antithrombin effect of rivaroxaban in patients with nonvalvular atrial fibrillation. Rivaroxaban 29-40 serpin family C member 1 Homo sapiens 84-96 28888219-10 2018 CONCLUSIONS: Residual plasma rivaroxaban at the trough steady state may explain the antithrombin effect of rivaroxaban in patients with nonvalvular atrial fibrillation. Rivaroxaban 107-118 serpin family C member 1 Homo sapiens 84-96 29466798-13 2018 After multivariable analysis, ATIII activity <75% remained a significant independent predictor of CIN (OR 2.207,95%CI [1.29-3.777]; P=0.004) as well as baseline serum creatinine (OR 1.009,95%CI [1.001-1.016]; P=0.026). Creatinine 170-180 serpin family C member 1 Homo sapiens 30-35 28301908-1 2018 Thrombate III is a human plasma-derived antithrombin III (AT-III) often utilized in patients on extracorporeal membrane oxygenation (ECMO) with suspected AT-III-mediated heparin resistance. Heparin 170-177 serpin family C member 1 Homo sapiens 154-160 29399079-1 2018 The anticoagulation effect of heparin requires adequate serum antithrombin (AT)-III levels. Heparin 30-37 serpin family C member 1 Homo sapiens 62-83 27624738-0 2018 Antithrombin Administration During Intravenous Heparin Anticoagulation in the Intensive Care Unit: A Single-Center Matched Retrospective Cohort Study. Heparin 47-54 serpin family C member 1 Homo sapiens 0-12 27624738-1 2018 Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition. Heparin 15-22 serpin family C member 1 Homo sapiens 122-134 27624738-1 2018 Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition. Heparin 15-22 serpin family C member 1 Homo sapiens 136-138 27624738-1 2018 Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition. Heparin 24-27 serpin family C member 1 Homo sapiens 122-134 27624738-1 2018 Unfractionated heparin (UFH) is a frequently utilized indirect anticoagulant that induces therapeutic effect by enhancing antithrombin (AT)-mediated procoagulant enzyme inhibition. Heparin 24-27 serpin family C member 1 Homo sapiens 136-138 27624738-2 2018 In suspected heparin resistance (HR) during cardiopulmonary bypass, AT activity may be decreased and AT supplementation helps restore UFH responsiveness. Heparin 13-20 serpin family C member 1 Homo sapiens 68-70 27624738-2 2018 In suspected heparin resistance (HR) during cardiopulmonary bypass, AT activity may be decreased and AT supplementation helps restore UFH responsiveness. Heparin 13-20 serpin family C member 1 Homo sapiens 101-103 28301908-1 2018 Thrombate III is a human plasma-derived antithrombin III (AT-III) often utilized in patients on extracorporeal membrane oxygenation (ECMO) with suspected AT-III-mediated heparin resistance. Heparin 170-177 serpin family C member 1 Homo sapiens 40-56 29031112-0 2017 Quantitative analysis of antithrombin III binding site in low molecular weight heparins by exhausetive heparinases digestion and capillary electrophoresis. Heparin 79-87 serpin family C member 1 Homo sapiens 25-41 28602126-7 2017 Normalized LAC ratio was positively correlated with D-dimer, fibrinogen, and procoagulant activity of coagulating factor VIII, and negatively correlated with antithrombin activity, respectively ( P < .01). Lactose 11-14 serpin family C member 1 Homo sapiens 158-170 28664670-12 2017 CONCLUSIONS: Antithrombin pharmacokinetics are significantly influenced by the concurrent use of unfractionated heparin and baseline antithrombin activity. Heparin 112-119 serpin family C member 1 Homo sapiens 13-25 29031112-1 2017 The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin. 3-o 68-71 serpin family C member 1 Homo sapiens 4-20 29031112-1 2017 The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin. 3-o 68-71 serpin family C member 1 Homo sapiens 22-27 29031112-1 2017 The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin. Glucosamine 93-104 serpin family C member 1 Homo sapiens 4-20 29031112-1 2017 The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin. Glucosamine 93-104 serpin family C member 1 Homo sapiens 22-27 29031112-1 2017 The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin. Heparin 200-207 serpin family C member 1 Homo sapiens 4-20 29031112-1 2017 The antithrombin III (ATIII)-binding site, which contains a special 3-O-sulfated, N-sulfated glucosamine residue with or without 6-O-sulfation, is mainly responsible for the anticoagulant activity of heparin. Heparin 200-207 serpin family C member 1 Homo sapiens 22-27 29031112-2 2017 Undergoing the chemical depolymerization process, the preservation of the ATIII-binding site in low molecular weight heparins (LMWHs) are varied leading to the fluctuation of the anticoagulant activity. Heparin 117-125 serpin family C member 1 Homo sapiens 74-79 29031112-4 2017 After exhaustively digesting LMWHs with the mixture of heparinase I, II and III, almost all the resulting oligosaccharide building blocks, including the three 3-O-sulfated tetrasaccharides derived from the ATIII-binding site, were resolved by CE separation. tetrasaccharides 172-188 serpin family C member 1 Homo sapiens 206-211 29031112-7 2017 The peak assignment was further confirmed by analysis of the high ATIII affinity fractions, which contains much high 3-O-sulfated tetrasaccharides. 3-o-sulfated tetrasaccharides 117-146 serpin family C member 1 Homo sapiens 66-71 29031112-8 2017 With the method, the molar percentage of the ATIII-binding site of enoxaparin from different batches and different manufactures were measured and compared. Enoxaparin 67-77 serpin family C member 1 Homo sapiens 45-50 28617415-9 2017 Antithrombin-III levels and transferrin-glycosylation showed significant improvement, and increase in galactosylation and whole glycan content. Polysaccharides 128-134 serpin family C member 1 Homo sapiens 0-16 28760491-0 2017 Effects of tibolone on fibrinogen and antithrombin III: A systematic review and meta-analysis of controlled trials. tibolone 11-19 serpin family C member 1 Homo sapiens 38-54 28880550-12 2017 Finally, fluorescence and ELISA experiments show that UHRA disrupts antithrombin-UFH complexes to neutralize heparin"s activity. Heparin 109-116 serpin family C member 1 Homo sapiens 68-80 28693359-11 2017 Incorporating individual variation, age and antithrombin activity in a model with heparin dose explained less than 50% of the variation in test results. Heparin 82-89 serpin family C member 1 Homo sapiens 44-56 28961453-1 2017 INTRODUCTION: Antithrombin resistance (ATR) prothrombinemia is an inherited thrombophilic disorder caused by missense mutations in prothrombin gene (F2) at Arg596 of the sodium-binding region. Sodium 170-176 serpin family C member 1 Homo sapiens 14-26 28760491-1 2017 Tibolone is a synthetic steroid with estrogenic, androgenic and progestogenic activity, but the evidence regarding its effects on fibrinogen and antithrombin III (ATIII) has not been conclusive. tibolone 0-8 serpin family C member 1 Homo sapiens 145-161 28760491-1 2017 Tibolone is a synthetic steroid with estrogenic, androgenic and progestogenic activity, but the evidence regarding its effects on fibrinogen and antithrombin III (ATIII) has not been conclusive. tibolone 0-8 serpin family C member 1 Homo sapiens 163-168 28760491-2 2017 We assessed the impact of tibolone on fibrinogen and ATIII through a systematic review and meta-analysis of available randomized controlled trials (RCTs). tibolone 26-34 serpin family C member 1 Homo sapiens 53-58 28760491-3 2017 The search included PUBMED, Web of Science, Scopus, and Google Scholar (up to January 31st, 2016) to identify controlled clinical studies investigating the effects of oral tibolone treatment on fibrinogen and ATIII. tibolone 172-180 serpin family C member 1 Homo sapiens 209-214 28691885-2 2017 Fitusiran, an investigational RNA interference (RNAi) therapy that targets antithrombin (encoded by SERPINC1), is in development to address these and other limitations. Givosiran 0-9 serpin family C member 1 Homo sapiens 75-87 27898513-1 2017 : The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH. Heparin 45-52 serpin family C member 1 Homo sapiens 128-140 27898513-1 2017 : The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH. Heparin 54-57 serpin family C member 1 Homo sapiens 128-140 27898513-1 2017 : The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH. Heparin 84-91 serpin family C member 1 Homo sapiens 128-140 27898513-1 2017 : The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH. Heparin, Low-Molecular-Weight 93-97 serpin family C member 1 Homo sapiens 128-140 27898513-1 2017 : The clinical limitations of unfractionated heparin (UFH) and low molecular weight heparin (LMWH) led to the development of an antithrombin-heparin covalent complex (ATH), which displays superior anticoagulant abilities compared with UFH. Heparin 235-238 serpin family C member 1 Homo sapiens 128-140 27898513-10 2017 Plasmin generation may be mildly inhibited by heparin-based anticoagulants; however, heparin-catalyzed antithrombin activity is not a major inhibitor of plasmin, as compared to its natural inhibitors alpha2-AP and alpha2-M. Heparin 85-92 serpin family C member 1 Homo sapiens 103-115 28485404-10 2017 Finally, we also obtained confirmatory results extending previous findings implicating AUTS2, SGOL1 and SERPINC1 genes in alcohol consumption traits in non-Hispanic whites. Alcohols 122-129 serpin family C member 1 Homo sapiens 104-112 28820035-10 2017 CONCLUSION: It can be hypothesized that the wide discrepancy in HDR slope versus heparin sensitivity may be explained by an inaccurate prediction of the plasma heparin level and/or the change in HDR of individual patients, depending on in vivo factors such as extravascular sequestration of heparin, decreased intrinsic antithrombin activity level and platelet count and/or activity. Heparin 160-167 serpin family C member 1 Homo sapiens 320-332 28820035-10 2017 CONCLUSION: It can be hypothesized that the wide discrepancy in HDR slope versus heparin sensitivity may be explained by an inaccurate prediction of the plasma heparin level and/or the change in HDR of individual patients, depending on in vivo factors such as extravascular sequestration of heparin, decreased intrinsic antithrombin activity level and platelet count and/or activity. Heparin 160-167 serpin family C member 1 Homo sapiens 320-332 28667866-1 2017 Using an illustrative case of a patient with antithrombin (AT) deficiency who developed a recurrent venous thromboembolism (VTE) in pregnancy despite therapeutic low-molecular-weight heparin (LMWH), we highlight what is known in the literature and address areas of controversy through a series of questions around the case. Heparin 183-190 serpin family C member 1 Homo sapiens 45-57 28667866-1 2017 Using an illustrative case of a patient with antithrombin (AT) deficiency who developed a recurrent venous thromboembolism (VTE) in pregnancy despite therapeutic low-molecular-weight heparin (LMWH), we highlight what is known in the literature and address areas of controversy through a series of questions around the case. Heparin, Low-Molecular-Weight 192-196 serpin family C member 1 Homo sapiens 45-57 28892658-1 2017 We report four children from different families with homozygous antithrombin (AT) deficiency type II affecting the heparin binding site (p.Leu131Phe mutation). Heparin 115-122 serpin family C member 1 Homo sapiens 64-76 28794370-5 2017 The present case illustrates the effectiveness of rivaroxaban in preventing thromboembolisms due to surgery, even in very elderly patients with antithrombin deficiency. Rivaroxaban 50-61 serpin family C member 1 Homo sapiens 144-156 29042831-1 2017 OBJECTIVES: To determine the percentage of patients with >10% reduction in heparin infusion rate within 48 hours of antithrombin III (ATIII) administration. Heparin 78-85 serpin family C member 1 Homo sapiens 119-135 29042831-1 2017 OBJECTIVES: To determine the percentage of patients with >10% reduction in heparin infusion rate within 48 hours of antithrombin III (ATIII) administration. Heparin 78-85 serpin family C member 1 Homo sapiens 137-142 29042831-6 2017 58.3% of the patients (n = 7) had a >=10% reduction from the baseline heparin infusion rate within 48 hours of ATIII administration. Heparin 73-80 serpin family C member 1 Homo sapiens 114-119 29042831-9 2017 CONCLUSIONS: Administration of ATIII is associated with >10% decrease in heparin requirements in more than half of the patients identified. Heparin 76-83 serpin family C member 1 Homo sapiens 31-36 30787791-5 2017 Anticoagulants such as anti-Xa and antithrombin have been found to be effective and safe as compared with the standard of care using low-molecular-weight heparin and warfarin. Heparin 154-161 serpin family C member 1 Homo sapiens 35-47 28691885-2 2017 Fitusiran, an investigational RNA interference (RNAi) therapy that targets antithrombin (encoded by SERPINC1), is in development to address these and other limitations. Givosiran 0-9 serpin family C member 1 Homo sapiens 100-108 28691885-12 2017 CONCLUSIONS: Once-monthly subcutaneous administration of fitusiran resulted in dose-dependent lowering of the antithrombin level and increased thrombin generation in participants with hemophilia A or B who did not have inhibitory alloantibodies. Givosiran 57-66 serpin family C member 1 Homo sapiens 110-122 29701427-4 2017 Heparin resistance was considered and treated with 1000 UI of antithrombin III concentrate. Heparin 0-7 serpin family C member 1 Homo sapiens 62-78 28304137-8 2017 At 225 ng/mL apixaban, the median percentage increase in antithrombin level was 31% when measured with the Liquid Antithrombin reagent and 44% with the Innovance Antithrombin reagent. apixaban 13-21 serpin family C member 1 Homo sapiens 57-69 30046692-10 2017 A deeper intronic mutation (c.1154-14G>A), identified in three unrelated patients with traces of disulphide dimers of antithrombin in plasma, created a cryptic splicing site that might generate a variant with 4 additional in frame residues according to in silico predictions. disulphide 100-110 serpin family C member 1 Homo sapiens 121-133 28943821-9 2017 Compared with nonprotocolized intermittent dosing, the use of a continuous infusion ATIII protocol demonstrated increased time within goal ACT range at a lower heparin dose, no increase in hemostatic complications, and trends toward fewer heparin changes and lower blood product usage. Heparin 160-167 serpin family C member 1 Homo sapiens 84-89 28943821-9 2017 Compared with nonprotocolized intermittent dosing, the use of a continuous infusion ATIII protocol demonstrated increased time within goal ACT range at a lower heparin dose, no increase in hemostatic complications, and trends toward fewer heparin changes and lower blood product usage. Heparin 239-246 serpin family C member 1 Homo sapiens 84-89 30279820-4 2017 Patients with low antithrombin III activity may have resistance to heparin therapy, leading to insufficient anticoagulation during the acute phase of thromboembolism. Heparin 67-74 serpin family C member 1 Homo sapiens 18-34 30279820-8 2017 The present case suggests that rivaroxaban is a direct Factor Xa inhibitor and does not require cofactors such as antithrombin-III, thus it is suitable for anticoagulation therapy in patients with low antithrombin-III activity.>. Rivaroxaban 31-42 serpin family C member 1 Homo sapiens 201-217 28317410-0 2017 Sex hormone-binding globulin and antithrombin III activity in women with oral ultra-low-dose estradiol. Estradiol 93-102 serpin family C member 1 Homo sapiens 33-49 28242144-0 2017 Supplemental Antithrombin Is Effective in Achieving Adequate Anticoagulation in Infants and Children With an Inadequate Response to Heparin. Heparin 132-139 serpin family C member 1 Homo sapiens 13-25 28322799-2 2017 The anticoagulant activity of target heparin was evaluated by measuring the competitive antithrombin III binding of analyte heparin in the solution phase and USP heparin immobilized on chip surface. Heparin 37-44 serpin family C member 1 Homo sapiens 88-104 28322799-2 2017 The anticoagulant activity of target heparin was evaluated by measuring the competitive antithrombin III binding of analyte heparin in the solution phase and USP heparin immobilized on chip surface. Heparin 124-131 serpin family C member 1 Homo sapiens 88-104 28322799-2 2017 The anticoagulant activity of target heparin was evaluated by measuring the competitive antithrombin III binding of analyte heparin in the solution phase and USP heparin immobilized on chip surface. Heparin 124-131 serpin family C member 1 Homo sapiens 88-104 28242144-1 2017 OBJECTIVE: To demonstrate that supplemental antithrombin (AT) is effective in establishing adequate anticoagulation in infants and children with initially inadequate responses to heparin. Heparin 179-186 serpin family C member 1 Homo sapiens 44-56 28242144-1 2017 OBJECTIVE: To demonstrate that supplemental antithrombin (AT) is effective in establishing adequate anticoagulation in infants and children with initially inadequate responses to heparin. Heparin 179-186 serpin family C member 1 Homo sapiens 58-60 28242144-13 2017 CONCLUSION: AT was effective in achieving adequate anticoagulation in a small cohort of infants and children undergoing cardiac surgery who initially were poorly responsive to heparin. Heparin 176-183 serpin family C member 1 Homo sapiens 12-14 28445754-8 2017 Antithrombin (2.6 muM) plus heparin (4 U/mL) inhibits 72% of the active clot-bound thrombin after ~10 min at 92 s-1, while no inhibition is observed in the absence of heparin. Heparin 167-174 serpin family C member 1 Homo sapiens 0-12 28481865-12 2017 4) HES significantly decreased antithrombin activity (AT: A) of the anticoagulant system with increasing HR vs. baseline and RL. Hydroxyethyl Starch Derivatives 3-6 serpin family C member 1 Homo sapiens 31-43 28229161-8 2017 Antithrombin deficiency in these cases should be classified as pleiotropic based on the impaired reactivity and low heparin affinity of the variant. Heparin 116-123 serpin family C member 1 Homo sapiens 0-12 28229167-7 2017 The corresponding mutations in SERPINC1 (anti-thrombin III) at position 456 (Gly456Arg) and SERPINI1 (neuroserpin) at position 392 (Gly392Glu) caused an anti-thrombin deficiency and severe dementia due to intracellular retention of the polymers. Polymers 236-244 serpin family C member 1 Homo sapiens 31-39 28282887-1 2017 Low Molecular Weight Heparins (LMWH) are complex anticoagulant drugs that mainly inhibit the blood coagulation cascade through indirect interaction with antithrombin. Heparin 21-29 serpin family C member 1 Homo sapiens 153-165 28007564-0 2017 Structural Analysis of Heparin-Derived 3-O-Sulfated Tetrasaccharides: Antithrombin Binding Site Variants. 3-o-sulfated tetrasaccharides 39-68 serpin family C member 1 Homo sapiens 70-82 28007564-2 2017 The mechanism for heparin"s anticoagulant activity is primarily through its interaction with a serine protease inhibitor, antithrombin III (AT), that enhances its ability to inactivate blood coagulation serine proteases, including thrombin (factor IIa) and factor Xa. Heparin 18-25 serpin family C member 1 Homo sapiens 122-138 28303970-9 2017 The decrease in the strong electronegative charge of terminal glycans may modulate hemostatic protein-protein interactions, which in combination with a strong prothrombotic situation, such as antithrombin deficiency, could increase the risk of thrombosis. Polysaccharides 62-69 serpin family C member 1 Homo sapiens 192-204 28340300-7 2017 We identified a novel octasaccharide that interacts with antithrombin and displays anti factor Xa activity. Octasaccharide 22-36 serpin family C member 1 Homo sapiens 57-69 28772696-0 2017 Effect of Immobilized Antithrombin III on the Thromboresistance of Polycarbonate Urethane. polycarbonate urethane 67-89 serpin family C member 1 Homo sapiens 22-38 28282887-3 2017 In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin). Heparin, Low-Molecular-Weight 165-169 serpin family C member 1 Homo sapiens 70-82 28282887-3 2017 In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin). Enoxaparin 215-225 serpin family C member 1 Homo sapiens 70-82 28282887-1 2017 Low Molecular Weight Heparins (LMWH) are complex anticoagulant drugs that mainly inhibit the blood coagulation cascade through indirect interaction with antithrombin. Heparin, Low-Molecular-Weight 31-35 serpin family C member 1 Homo sapiens 153-165 28282887-3 2017 In fact, a minimal chain length of 18 saccharides units, including an antithrombin (AT) binding pentasaccharide, is mandatory to form the active ternary complex for LMWH obtained by alkaline beta-elimination (e.g., enoxaparin). pentasaccharide 96-111 serpin family C member 1 Homo sapiens 70-82 27783482-0 2017 An Asymmetric Runaway Domain Swap Antithrombin Dimer as a Key Intermediate for Polymerization Revealed by Hydrogen/Deuterium-Exchange Mass Spectrometry. Hydrogen 106-114 serpin family C member 1 Homo sapiens 34-46 28243911-2 2017 Antithrombin activity of dextran sulfate with a molecular weight of 20 kDa reached 12.6-15.3 U/mg. Dextran Sulfate 25-40 serpin family C member 1 Homo sapiens 0-12 28722442-4 2017 When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles. Heparin 100-107 serpin family C member 1 Homo sapiens 58-75 28722442-4 2017 When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles. Heparin 100-107 serpin family C member 1 Homo sapiens 77-83 28722442-4 2017 When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles. Heparin 100-107 serpin family C member 1 Homo sapiens 129-135 28219627-5 2017 Our data demonstrated ATIII significantly attenuated the elevation of serum creatinine, blood urea nitrogen, and renal histological injury. Creatinine 76-86 serpin family C member 1 Homo sapiens 22-27 28219627-5 2017 Our data demonstrated ATIII significantly attenuated the elevation of serum creatinine, blood urea nitrogen, and renal histological injury. Urea 94-98 serpin family C member 1 Homo sapiens 22-27 28219627-5 2017 Our data demonstrated ATIII significantly attenuated the elevation of serum creatinine, blood urea nitrogen, and renal histological injury. Nitrogen 99-107 serpin family C member 1 Homo sapiens 22-27 28722442-4 2017 When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles. Heparin 170-177 serpin family C member 1 Homo sapiens 58-75 28722442-4 2017 When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles. Heparin 170-177 serpin family C member 1 Homo sapiens 77-83 28722442-4 2017 When cationic micelles and fluorescence QDs modified with anti-thrombin III (AT III) are added into heparin sample solution, the AT III-QDs, which specifically bind with heparin, aggregate around the micelles. Heparin 170-177 serpin family C member 1 Homo sapiens 129-135 27783482-0 2017 An Asymmetric Runaway Domain Swap Antithrombin Dimer as a Key Intermediate for Polymerization Revealed by Hydrogen/Deuterium-Exchange Mass Spectrometry. Deuterium 115-124 serpin family C member 1 Homo sapiens 34-46 27783482-6 2017 Here, we show how hydrogen/deuterium-exchange mass spectrometry (HDX-MS) provides detailed insight into the structural dynamics of each subunit in a polymerization-competent antithrombin dimer. Hydrogen 18-26 serpin family C member 1 Homo sapiens 174-186 27783482-6 2017 Here, we show how hydrogen/deuterium-exchange mass spectrometry (HDX-MS) provides detailed insight into the structural dynamics of each subunit in a polymerization-competent antithrombin dimer. Deuterium 27-36 serpin family C member 1 Homo sapiens 174-186 27783482-9 2017 The local subunit-specific deuterium uptake of this polymerization-competent dimer strongly supports a beta4A-beta5A beta-hairpin runaway domain swap mechanism for antithrombin polymerization. Deuterium 27-36 serpin family C member 1 Homo sapiens 164-176 27862941-4 2016 In 1976, three teams independently found that a specific structure in heparin binds tightly to antithrombin. Heparin 70-77 serpin family C member 1 Homo sapiens 95-107 28168066-3 2017 We present a case of a woman with antithrombin (AT) deficiency who presented with a VTE despite therapeutic low molecular weight heparin (LMWH). Heparin 129-136 serpin family C member 1 Homo sapiens 34-46 28168066-3 2017 We present a case of a woman with antithrombin (AT) deficiency who presented with a VTE despite therapeutic low molecular weight heparin (LMWH). Heparin, Low-Molecular-Weight 138-142 serpin family C member 1 Homo sapiens 34-46 27862941-6 2016 It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin). Heparin 275-282 serpin family C member 1 Homo sapiens 81-93 28036320-1 2017 Acquired antithrombin (AT) deficiency is not uncommon in cardiothoracic surgery because of heparin exposure and dilutional or consumptive losses. Heparin 91-98 serpin family C member 1 Homo sapiens 9-21 28804827-3 2017 Acting alone, AT inhibits coagulation factors, but does this very slowly; however, when coupled with heparin as a cofactor, the speed of inhibition is increased many fold. Heparin 101-108 serpin family C member 1 Homo sapiens 14-16 28804827-4 2017 The AT/Heparin complex is the most powerful naturally occurring anticoagulant in blood. Heparin 7-14 serpin family C member 1 Homo sapiens 4-6 27810279-0 2016 Synthesis and characterisation of magnetised Dacron-heparin composite employed for antithrombin affinity purification. Polyethylene Terephthalates 45-51 serpin family C member 1 Homo sapiens 83-95 27810279-0 2016 Synthesis and characterisation of magnetised Dacron-heparin composite employed for antithrombin affinity purification. Heparin 52-59 serpin family C member 1 Homo sapiens 83-95 27810279-9 2016 Human plasma antithrombin activity was reduced by approximately 20% in the presence of the 1.0M NaCl fraction, and this eluate was able to prolong coagulation time (aPTT) using both preparations. Sodium Chloride 96-100 serpin family C member 1 Homo sapiens 13-25 27862941-7 2016 Antithrombin action therefore requires a minimum length of seven sugar units next to the pentasaccharide whereas anti-factor Xa action does not. Sugars 65-70 serpin family C member 1 Homo sapiens 0-12 27862941-7 2016 Antithrombin action therefore requires a minimum length of seven sugar units next to the pentasaccharide whereas anti-factor Xa action does not. pentasaccharide 89-104 serpin family C member 1 Homo sapiens 0-12 27862941-6 2016 It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin). Heparin 37-44 serpin family C member 1 Homo sapiens 81-93 27862941-6 2016 It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin). Heparin 37-44 serpin family C member 1 Homo sapiens 145-157 27862941-6 2016 It was found (Olson and others) that heparin facilitates the interaction between antithrombin and a clotting enzyme by allosteric changes in the antithrombin (important for factor Xa) and by facilitating the approach of the enzyme to antithrombin via its "sliding" along the heparin molecule (important for thrombin). Heparin 37-44 serpin family C member 1 Homo sapiens 145-157 27611497-3 2016 In this study, we report the effects of dFG-3 (Mw ~14kDa) on the catalysis rates of factor IIa (FIIa), factor Xa (FXa) and factor IXa (FIXa) inhibition by antithrombin (AT), and the kinetic of the interactions between coagulation proteases or inhibitors and dFG-3 were also studied using biolayer interferometry (BLI) technology. 1,3-Diphenylguanidine 40-43 serpin family C member 1 Homo sapiens 155-167 27655335-2 2016 The current monitoring practice for heparin in plasma, such as the chromogenic anti-factor Xa assay, relies on heparin-triggered activation of antithrombin, an inhibitor of coagulation proteases. Heparin 36-43 serpin family C member 1 Homo sapiens 143-155 27655335-2 2016 The current monitoring practice for heparin in plasma, such as the chromogenic anti-factor Xa assay, relies on heparin-triggered activation of antithrombin, an inhibitor of coagulation proteases. Heparin 111-118 serpin family C member 1 Homo sapiens 143-155 27322714-1 2016 BACKGROUND: Heparin fulfills its anticoagulant action through activation of antithrombin (AT), and thus thrombosis secondary to AT deficiency can be associated with heparin resistance. Heparin 12-19 serpin family C member 1 Homo sapiens 76-88 27322714-1 2016 BACKGROUND: Heparin fulfills its anticoagulant action through activation of antithrombin (AT), and thus thrombosis secondary to AT deficiency can be associated with heparin resistance. Heparin 165-172 serpin family C member 1 Homo sapiens 76-88 27301751-1 2016 Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma. Heparin 15-22 serpin family C member 1 Homo sapiens 58-70 27301751-1 2016 Unfractionated heparin (UFH) has procoagulant activity in antithrombin/heparin cofactor II (HCII)-depleted plasma. Heparin 24-27 serpin family C member 1 Homo sapiens 58-70 27479819-0 2016 Identification of a new potential mechanism responsible for severe bleeding in myeloma: immunoglobulins bind the heparin binding domain of antithrombin activating this endogenous anticoagulant. Heparin 113-120 serpin family C member 1 Homo sapiens 139-151 27611497-3 2016 In this study, we report the effects of dFG-3 (Mw ~14kDa) on the catalysis rates of factor IIa (FIIa), factor Xa (FXa) and factor IXa (FIXa) inhibition by antithrombin (AT), and the kinetic of the interactions between coagulation proteases or inhibitors and dFG-3 were also studied using biolayer interferometry (BLI) technology. 1,3-Diphenylguanidine 258-261 serpin family C member 1 Homo sapiens 155-167 27412396-1 2016 In the absence of specific antidote to fondaparinux, two modified forms of antithrombin (AT), one recombinant inactive (ri-AT) and the other chemically inactivated (chi-AT), were designed to antagonise AT-mediated anticoagulants, e. g. heparins or fondaparinux. Heparin 236-244 serpin family C member 1 Homo sapiens 75-87 27497655-2 2016 The antithrombotic activity of heparin is mediated mainly through its activation of antithrombin (AT) and subsequent inhibition of coagulation factors. Heparin 31-38 serpin family C member 1 Homo sapiens 84-96 27322195-0 2016 Heparanase Activates Antithrombin through the Binding to Its Heparin Binding Site. Heparin 61-68 serpin family C member 1 Homo sapiens 21-33 27324768-8 2016 Independent covariates related to significant decreases of linezolid concentrations included higher weight, creatinine clearance rates, and fibrinogen and antithrombin concentrations, lower concentrations of lactate, and the presence of acute respiratory distress syndrome (ARDS). Linezolid 59-68 serpin family C member 1 Homo sapiens 155-167 27441845-0 2016 Correction: Identification of Regulatory Mutations in SERPINC1 Affecting Vitamin D Response Elements Associated with Antithrombin Deficiency. Vitamin D 73-82 serpin family C member 1 Homo sapiens 54-62 27098529-9 2016 In conclusion, p.Val30Glu by affecting the cleavage of antithrombin"s signal peptide, results in a mature protein lacking the N-terminal dipeptide with no functional consequences in normal conditions, but that increases the sensitivity to be folded intracellularly into polymers, facilitating transient antithrombin deficiency and the subsequent risk of thrombosis. Dipeptides 137-146 serpin family C member 1 Homo sapiens 55-67 27098529-9 2016 In conclusion, p.Val30Glu by affecting the cleavage of antithrombin"s signal peptide, results in a mature protein lacking the N-terminal dipeptide with no functional consequences in normal conditions, but that increases the sensitivity to be folded intracellularly into polymers, facilitating transient antithrombin deficiency and the subsequent risk of thrombosis. Dipeptides 137-146 serpin family C member 1 Homo sapiens 303-315 27701728-9 2016 Warfarin-induced skin necrosis is a rare but serious complication that can be prevented by routine screening for protein C, protein S or antithrombin deficiencies or for the presence of antiphospholipid antibodies before beginning warfarin therapy. Warfarin 0-8 serpin family C member 1 Homo sapiens 137-149 27214821-11 2016 Moreover, intermittent antithrombin deficiency and hypoglycosylation was recorded in five out of these eight patients, all associated with moderate alcohol intake. Alcohols 148-155 serpin family C member 1 Homo sapiens 23-35 27214821-14 2016 An aberrant N-glycosylation causing a recessive or transient antithrombin deficiency is a new form of thrombophilia. Nitrogen 12-13 serpin family C member 1 Homo sapiens 61-73 26989842-4 2016 We developed a capillary zone electrophoresis method, based on a neutral polyethylene oxide-coated capillary and a buffer close to physiological conditions, enabling the separation of more than eight forms of AT. Polyethylene Glycols 73-91 serpin family C member 1 Homo sapiens 209-211 27366296-1 2016 We report a challenging case of cerebral venous sinus thrombosis (multiple etiologic factors) that was complicated by heparin resistance secondary to suspected antithrombin III (ATIII) deficiency. Heparin 118-125 serpin family C member 1 Homo sapiens 160-176 27366296-1 2016 We report a challenging case of cerebral venous sinus thrombosis (multiple etiologic factors) that was complicated by heparin resistance secondary to suspected antithrombin III (ATIII) deficiency. Heparin 118-125 serpin family C member 1 Homo sapiens 178-183 27366296-7 2016 Deficiency of ATIII was suspected as a possible etiology of her heparin resistance. Heparin 64-71 serpin family C member 1 Homo sapiens 14-19 27322195-4 2016 Trying to check the effect of heparanase on heparin, a highly sulphated glycosaminoglycan, when it activates antithrombin, our results demonstrated that heparanase, but not proheparanase, interacted directly with antithrombin in a non-covalent manner. Heparin 44-51 serpin family C member 1 Homo sapiens 109-121 27322195-7 2016 Heparanase bound to the heparin binding site of antithrombin as the activation of Pro41Leu, Arg47Cys, Lys114Ala and Lys125Alaantithrombin mutants was impaired when it was compared to wild type antithrombin. Heparin 24-31 serpin family C member 1 Homo sapiens 48-60 27322195-7 2016 Heparanase bound to the heparin binding site of antithrombin as the activation of Pro41Leu, Arg47Cys, Lys114Ala and Lys125Alaantithrombin mutants was impaired when it was compared to wild type antithrombin. Heparin 24-31 serpin family C member 1 Homo sapiens 125-137 27322195-7 2016 Heparanase bound to the heparin binding site of antithrombin as the activation of Pro41Leu, Arg47Cys, Lys114Ala and Lys125Alaantithrombin mutants was impaired when it was compared to wild type antithrombin. lys125alaantithrombin 116-137 serpin family C member 1 Homo sapiens 48-60 27322195-8 2016 Intrinsic fluorescence analysis showed that heparanase induced an activating conformational change in antithrombin similar to that induced by heparin and with a KD of 18.81 pM. Heparin 142-149 serpin family C member 1 Homo sapiens 102-114 27270881-4 2016 The inhibitory process required the activation of antithrombin by heparin, and the reactive center loop and the heparin binding domain were essential. Heparin 66-73 serpin family C member 1 Homo sapiens 50-62 27270881-4 2016 The inhibitory process required the activation of antithrombin by heparin, and the reactive center loop and the heparin binding domain were essential. Heparin 112-119 serpin family C member 1 Homo sapiens 50-62 27148674-3 2016 Heparin activates antithrombin and promotes the inactivation of thrombin and other target proteinases. Heparin 0-7 serpin family C member 1 Homo sapiens 18-30 27222580-6 2016 ATIII has three disulfide bonds, two near the N terminus and one near the C terminus. Disulfides 16-25 serpin family C member 1 Homo sapiens 0-5 27222580-7 2016 Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state. Disulfides 74-83 serpin family C member 1 Homo sapiens 15-20 27222580-7 2016 Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state. Disulfides 139-148 serpin family C member 1 Homo sapiens 15-20 27222580-7 2016 Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state. Disulfides 185-195 serpin family C member 1 Homo sapiens 15-20 27222580-9 2016 N-linked glycans and carbohydrate-binding molecular chaperones contribute to the efficient folding and secretion of functional ATIII. n-linked glycans 0-16 serpin family C member 1 Homo sapiens 127-132 27222580-9 2016 N-linked glycans and carbohydrate-binding molecular chaperones contribute to the efficient folding and secretion of functional ATIII. Carbohydrates 21-33 serpin family C member 1 Homo sapiens 127-132 27010094-7 2016 Genetic analysis revealed a single-base substitution (C>T) at the codon 359 (Arg to STOP) in the 5th exon portion of the antithrombin gene, heterozygote. Arginine 80-83 serpin family C member 1 Homo sapiens 124-136 26747427-1 2016 The structure of the N-linked oligosaccharides attached to antithrombin (AT) has been shown to affect its anticoagulant activity and pharmacokinetics. n-linked oligosaccharides 21-46 serpin family C member 1 Homo sapiens 59-71 27088203-7 2016 The patient had a steroid-dependent submicroscopic glomerulonephritis with a severe episode of nephrotic syndrome associated with centralization of circulation, proteinuria 40.9 g/day, deep hypoproteinemia (albumin=1.2 g/dl), hyperlipidemia, hypercoagulable state (antithrombin activity 29%), polycythemia (Hb=21.1 g/dl, HTC=60%). Steroids 18-25 serpin family C member 1 Homo sapiens 265-277 26998583-7 2016 OBJECTIVES: To assess whether the prophylactic administration of antithrombin (started within the first 24 hours after birth) reduces the incidence of germinal matrix-intraventricular hemorrhage in very preterm neonates when compared to placebo, no treatment, or heparin. Heparin 263-270 serpin family C member 1 Homo sapiens 65-77 27102510-4 2016 In Phase III trials, rivaroxaban, apixaban, edoxaban (antifactor Xa agents), and dabigatran (an antithrombin agent) were noninferior and probably safer than conventional anticoagulation therapy (low-molecular-weight heparin followed by vitamin K antagonists). Dabigatran 81-91 serpin family C member 1 Homo sapiens 96-108 27053426-7 2016 Antithrombin inactivation of thrombin was impaired in the presence of the sulfated coumarins suggesting that allosteric partial inhibition arises from catalytic dysfunction of the active site. Coumarins 83-92 serpin family C member 1 Homo sapiens 0-12 27003919-0 2016 Identification of Regulatory Mutations in SERPINC1 Affecting Vitamin D Response Elements Associated with Antithrombin Deficiency. Vitamin D 61-70 serpin family C member 1 Homo sapiens 42-50 27003919-7 2016 The relevance of the vitamin D pathway on the regulation of SERPINC1 was confirmed in a cell model. Vitamin D 21-30 serpin family C member 1 Homo sapiens 60-68 27003919-8 2016 Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium. paricalcitol 25-37 serpin family C member 1 Homo sapiens 100-108 27003919-8 2016 Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium. paricalcitol 25-37 serpin family C member 1 Homo sapiens 124-136 27003919-8 2016 Incubation of HepG2 with paricalcitol, a vitamin D analog, increased dose-dependently the levels of SERPINC1transcripts and antithrombin released to the conditioned medium. Vitamin D 41-50 serpin family C member 1 Homo sapiens 100-108 27003919-9 2016 This study shows further evidence of the transcriptional regulation of SERPINC1 by vitamin D and first describes the functional and pathological relevance of mutations affecting VDRE of this gene. Vitamin D 83-92 serpin family C member 1 Homo sapiens 71-79 27088203-20 2016 We supposed that the heparin was ineffective due to an antithrombin deficiency. Heparin 21-28 serpin family C member 1 Homo sapiens 55-67 26553458-6 2016 Lower baseline antithrombin activity was associated with lower postheparin anti-Xa activity (EST [SE]: +0.47 (0.19) U/mL per 100 U/kg heparin; P = .01) and higher heparin doses during surgery (EST [SE]: +51 (17) U/kg per hour; P = .003). Heparin 67-74 serpin family C member 1 Homo sapiens 15-27 26797521-2 2016 Although another plasma serpin with an Arg-Ser reactive centre, antithrombin (AT), has been shown to inhibit factor VIIa (FVIIa), no published data are available with respect to FVIIa inhibition by API M358R. Arginine 39-42 serpin family C member 1 Homo sapiens 64-76 26797521-2 2016 Although another plasma serpin with an Arg-Ser reactive centre, antithrombin (AT), has been shown to inhibit factor VIIa (FVIIa), no published data are available with respect to FVIIa inhibition by API M358R. Serine 43-46 serpin family C member 1 Homo sapiens 64-76 26758598-8 2016 The utility of this approach is demonstrated for tetrasaccharide SEC fractions of the low molecular weight heparin drug enoxaparin facilitating the isolation and characterization of an unsaturated 3-O-sulfated tetrasaccharide containing a portion of the antithrombin-III binding sequence. tetrasaccharide 49-64 serpin family C member 1 Homo sapiens 254-270 26758598-8 2016 The utility of this approach is demonstrated for tetrasaccharide SEC fractions of the low molecular weight heparin drug enoxaparin facilitating the isolation and characterization of an unsaturated 3-O-sulfated tetrasaccharide containing a portion of the antithrombin-III binding sequence. Heparin 107-114 serpin family C member 1 Homo sapiens 254-270 26758598-8 2016 The utility of this approach is demonstrated for tetrasaccharide SEC fractions of the low molecular weight heparin drug enoxaparin facilitating the isolation and characterization of an unsaturated 3-O-sulfated tetrasaccharide containing a portion of the antithrombin-III binding sequence. Enoxaparin 120-130 serpin family C member 1 Homo sapiens 254-270 26758598-8 2016 The utility of this approach is demonstrated for tetrasaccharide SEC fractions of the low molecular weight heparin drug enoxaparin facilitating the isolation and characterization of an unsaturated 3-O-sulfated tetrasaccharide containing a portion of the antithrombin-III binding sequence. 3-o-sulfated tetrasaccharide 197-225 serpin family C member 1 Homo sapiens 254-270 26578266-1 2016 The antithrombin activity of unfractionated heparin (UFH) is offset by extracellular histones, which, along with DNA, represent a novel mediator of thrombosis and a structural component of thrombi. Heparin 44-51 serpin family C member 1 Homo sapiens 4-16 26578266-1 2016 The antithrombin activity of unfractionated heparin (UFH) is offset by extracellular histones, which, along with DNA, represent a novel mediator of thrombosis and a structural component of thrombi. Heparin 53-56 serpin family C member 1 Homo sapiens 4-16 26553458-6 2016 Lower baseline antithrombin activity was associated with lower postheparin anti-Xa activity (EST [SE]: +0.47 (0.19) U/mL per 100 U/kg heparin; P = .01) and higher heparin doses during surgery (EST [SE]: +51 (17) U/kg per hour; P = .003). Heparin 134-141 serpin family C member 1 Homo sapiens 15-27 26553458-9 2016 CONCLUSIONS: Low circulating antithrombin activity is associated with lower heparin efficacy, which ultimately leads to a lower ability to suppress thrombin generation during CPB. Heparin 76-83 serpin family C member 1 Homo sapiens 29-41 26581031-1 2016 UNLABELLED: ESSENTIALS: Antithrombin III (AT)beta binds heparin with higher affinity than ATalpha. Heparin 56-63 serpin family C member 1 Homo sapiens 24-40 26581031-5 2016 BACKGROUND: Antithrombin III (AT)beta is an isoform of AT that lacks the post-translational carbohydrate modification at Asn135. Carbohydrates 92-104 serpin family C member 1 Homo sapiens 12-28 26584351-2 2016 METHODS: Polymer particles were incubated in (1) EDTA-plasma (10 mM) to monitor the adsorption of 20 selected proteins; (2) lepirudin-anticoagulated plasma to evaluate contact system activation, monitored by the formation of complexes between the generated proteases factor[F]XIIa, FXIa and kallikrein and the serpins C1-inhibitor [C1INH] and antithrombin [AT]; (3) lepirudin-anticoagulated whole blood to determine cytokine release. Polymers 9-16 serpin family C member 1 Homo sapiens 343-355 26431853-5 2016 Multivariable linear regression analyses were used to explore the relationship between AT activity and heparin response measured by HSI. Heparin 103-110 serpin family C member 1 Homo sapiens 87-89 26431853-7 2016 After adjusting for low-molecular-weight heparin, unfractionated heparin, and platelet count, there was a significant relationship between AT activity and HSI (r = 0.44; P = 0.009). Heparin 41-48 serpin family C member 1 Homo sapiens 139-141 26431853-2 2016 The primary aim of this study was to evaluate the relationship between preoperative antithrombin (AT) activity and heparin responsiveness in neonates and infants undergoing congenital cardiac surgery. Heparin 115-122 serpin family C member 1 Homo sapiens 84-96 26431853-2 2016 The primary aim of this study was to evaluate the relationship between preoperative antithrombin (AT) activity and heparin responsiveness in neonates and infants undergoing congenital cardiac surgery. Heparin 115-122 serpin family C member 1 Homo sapiens 98-100 26431853-7 2016 After adjusting for low-molecular-weight heparin, unfractionated heparin, and platelet count, there was a significant relationship between AT activity and HSI (r = 0.44; P = 0.009). Heparin 65-72 serpin family C member 1 Homo sapiens 139-141 26431853-9 2016 CONCLUSIONS: There was a moderate relationship between AT activity and heparin response measured by HSI. Heparin 71-78 serpin family C member 1 Homo sapiens 55-57 26411319-7 2016 In this minireview paper, we are to summarize the structural features of antithrombin, as well as its heparin binding modes and anti-coagulation mechanisms, in hopes that the discussion and analysis presented in this paper can stimulate new strategies to find more effective approaches or compounds to modulate the antithrombin. Heparin 102-109 serpin family C member 1 Homo sapiens 73-85 26554332-0 2016 Oxidized antithrombin is a dual inhibitor of coagulation and angiogenesis: Importance of low heparin affinity. Heparin 93-100 serpin family C member 1 Homo sapiens 9-21 26686866-2 2016 The molecule is a recombinant protein analog of factor Xa that binds to Factor Xa inhibitors and antithrombin:LMWH complex but does not trigger prothrombotic activity. Heparin, Low-Molecular-Weight 110-114 serpin family C member 1 Homo sapiens 97-109 26554332-5 2016 Chorioallantoic membrane assay (CAM) shows that antiangiogenic activity of latent and oxidized AT are better than thalidomide, a potent antiangiogenic drug. Thalidomide 114-125 serpin family C member 1 Homo sapiens 95-97 26554332-7 2016 Latent and cleaved conformations of AT shows an increase in alpha-helical content in the presence of unfractionated heparin, but not the oxidized AT. Heparin 116-123 serpin family C member 1 Homo sapiens 36-38 26554332-9 2016 The results of our study establish that active conformation of AT can become antiangiogenic while maintaining its anticoagulant activity possibly through chelation of low affinity heparin in the vicinity of endothelial cell. Heparin 180-187 serpin family C member 1 Homo sapiens 63-65 25361738-0 2015 Prothrombotic SERPINC1 gene polymorphism may affect heparin sensitivity among different ethnicities of Chinese patients receiving heart surgery. Heparin 52-59 serpin family C member 1 Homo sapiens 14-22 26674994-7 2016 Compared to the PMMA group, the BCC group exhibited significantly lower levels of arterial pressure, pulmonary artery pressure, blood oxygen pressure, blood carbon dioxide pressure, blood bicarbonate, base excess, antithrombin III and D-dimer. bcc 32-35 serpin family C member 1 Homo sapiens 214-230 26359493-0 2015 Saturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated States. Heparin 111-118 serpin family C member 1 Homo sapiens 30-42 26359493-1 2015 Past studies have suggested that a key feature of the mechanism of heparin allosteric activation of the anticoagulant serpin, antithrombin, is the release of the reactive center loop P14 residue from a native state stabilizing interaction with the hydrophobic core. Heparin 67-74 serpin family C member 1 Homo sapiens 126-138 26280926-10 2015 These results were further confirmed by orthogonal analytical techniques, including NMR, which revealed compositional differences of oligosaccharides both in low- and high-affinity antithrombin fractions of enoxaparin. Oligosaccharides 133-149 serpin family C member 1 Homo sapiens 181-193 26280926-10 2015 These results were further confirmed by orthogonal analytical techniques, including NMR, which revealed compositional differences of oligosaccharides both in low- and high-affinity antithrombin fractions of enoxaparin. Enoxaparin 207-217 serpin family C member 1 Homo sapiens 181-193 26672027-2 2016 The anticoagulant activity of heparin is mainly attributable to the action of a specific pentasaccharide sequence that acts in concert with antithrombin, a plasma coagulation factor inhibitor. Heparin 30-37 serpin family C member 1 Homo sapiens 140-152 26672027-2 2016 The anticoagulant activity of heparin is mainly attributable to the action of a specific pentasaccharide sequence that acts in concert with antithrombin, a plasma coagulation factor inhibitor. pentasaccharide 89-104 serpin family C member 1 Homo sapiens 140-152 26510969-11 2016 Edoxaban impairs the assessment of lupus anticoagulant, protein S (clotting method), APC-R, antithrombin (FXa-based assay) and measurement of clotting factor activity. edoxaban 0-8 serpin family C member 1 Homo sapiens 92-104 25361738-1 2015 The purpose of this study was to investigate a possible correlation between single-nucleotide polymorphisms (SNPs) of the antithrombin (gene, SERPINC1, and perioperative sensitivity to heparin in patients receiving heart surgery. Heparin 185-192 serpin family C member 1 Homo sapiens 122-134 25361738-1 2015 The purpose of this study was to investigate a possible correlation between single-nucleotide polymorphisms (SNPs) of the antithrombin (gene, SERPINC1, and perioperative sensitivity to heparin in patients receiving heart surgery. Heparin 185-192 serpin family C member 1 Homo sapiens 142-150 25361738-6 2015 The increased SERPINC1 SNP frequency among Han patients receiving heart surgery might contribute to the differences in their perioperative sensitivity to heparin. Heparin 154-161 serpin family C member 1 Homo sapiens 14-22 25483839-1 2015 While antithrombin (AT) has small basal inhibitory activity, it reaches its full inhibitory potential against activated blood coagulation factors, FXa, FIXa, and FIIa (thrombin), via an allosteric and/or template (bridging) mechanism by the action of heparin, heparan sulfate, or heparin-mimetic pentasaccharides (PS). Heparin 251-258 serpin family C member 1 Homo sapiens 6-18 26115461-0 2015 Investigating changes in the gas-phase conformation of Antithrombin III upon binding of Arixtra using traveling wave ion mobility spectrometry (TWIMS). Fondaparinux 88-95 serpin family C member 1 Homo sapiens 55-71 26115461-2 2015 Heparin has been used as a therapeutic anticoagulant drug for several decades through its interaction with ATIII, a serine protease inhibitor that plays a central role in the blood coagulation cascade. Heparin 0-7 serpin family C member 1 Homo sapiens 107-112 26115461-4 2015 Arixtra is the smallest synthetic Hp containing the specific pentasaccharide sequence required to bind with ATIII. Fondaparinux 0-7 serpin family C member 1 Homo sapiens 108-113 26115461-4 2015 Arixtra is the smallest synthetic Hp containing the specific pentasaccharide sequence required to bind with ATIII. Heparin 34-36 serpin family C member 1 Homo sapiens 108-113 26115461-4 2015 Arixtra is the smallest synthetic Hp containing the specific pentasaccharide sequence required to bind with ATIII. pentasaccharide 61-76 serpin family C member 1 Homo sapiens 108-113 26115461-5 2015 Here we report the first travelling wave ion mobility mass spectrometry (TWIMS) investigation of the conformational changes in ATIII induced by its interaction with Arixtra. Fondaparinux 165-172 serpin family C member 1 Homo sapiens 127-132 26115461-6 2015 Native electrospray ionization mass spectrometry allowed the gentle transfer of the native topology of ATIII and ATIII-Arixtra complex. Fondaparinux 119-126 serpin family C member 1 Homo sapiens 113-118 26115461-7 2015 IM measurements of ATIII and ATIII-Arixtra complex showed a single structure, with well-defined collisional cross section (CCS) values. Fondaparinux 35-42 serpin family C member 1 Homo sapiens 29-34 26115461-8 2015 An average 3.6% increase in CCS of ATIII occurred as a result of its interaction with Arixtra, which agrees closely with the theoretical estimation of the change in CCS based on protein crystal structures. Fondaparinux 86-93 serpin family C member 1 Homo sapiens 35-40 26115461-10 2015 A Hp oligosaccharide whose structure is similar to Arixtra but missing the 3-O sulfo group on the central glucosamine residue showed a dramatic decrease in binding affinity towards ATIII, but no change in the mobility behavior of the complex, consistent with prior studies that suggested that 3-O sulfation affects the equilibrium constant for binding to ATIII, but not the mode of interaction. hp oligosaccharide 2-20 serpin family C member 1 Homo sapiens 181-186 26115461-10 2015 A Hp oligosaccharide whose structure is similar to Arixtra but missing the 3-O sulfo group on the central glucosamine residue showed a dramatic decrease in binding affinity towards ATIII, but no change in the mobility behavior of the complex, consistent with prior studies that suggested that 3-O sulfation affects the equilibrium constant for binding to ATIII, but not the mode of interaction. hp oligosaccharide 2-20 serpin family C member 1 Homo sapiens 355-360 26115461-11 2015 In contrast, nonspecific binding by a Hp tetrasaccharide showed more complex mobility behavior, suggesting more promiscuous interactions with ATIII. hp tetrasaccharide 38-56 serpin family C member 1 Homo sapiens 142-147 26115461-12 2015 The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding. Fondaparinux 56-63 serpin family C member 1 Homo sapiens 50-55 26115461-12 2015 The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding. Fondaparinux 56-63 serpin family C member 1 Homo sapiens 50-55 26115461-12 2015 The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding. Fondaparinux 122-129 serpin family C member 1 Homo sapiens 40-45 26115461-12 2015 The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding. Fondaparinux 122-129 serpin family C member 1 Homo sapiens 50-55 26115461-12 2015 The effect of collisional activation of ATIII and ATIII-Arixtra complex were also assessed, revealing that the binding of Arixtra provided ATIII with additional stability against unfolding. Fondaparinux 122-129 serpin family C member 1 Homo sapiens 50-55 26340667-8 2015 The comparison of the glycosidic linkage torsion angle values in solution with the antithrombin-pentasaccharide complex also indicates that the pentasaccharide conformation changes upon binding to antithrombin III. pentasaccharide 96-111 serpin family C member 1 Homo sapiens 197-213 26340667-8 2015 The comparison of the glycosidic linkage torsion angle values in solution with the antithrombin-pentasaccharide complex also indicates that the pentasaccharide conformation changes upon binding to antithrombin III. pentasaccharide 144-159 serpin family C member 1 Homo sapiens 197-213 26340667-9 2015 The data supports the assumption that the protein selects the more populated (2)S0 conformer of heparin pentasaccharide and, consequently, the binding process of heparin pentasaccharide with antithrombin III is energetically more favorable than formerly expected. IC 831423 96-119 serpin family C member 1 Homo sapiens 191-207 26340667-9 2015 The data supports the assumption that the protein selects the more populated (2)S0 conformer of heparin pentasaccharide and, consequently, the binding process of heparin pentasaccharide with antithrombin III is energetically more favorable than formerly expected. IC 831423 162-185 serpin family C member 1 Homo sapiens 191-207 26250112-7 2015 The comparative structural analyses indicated that neither the stability, nor the topology of the G4s, but the different localization of the two benzene rings of the linker was responsible for the loss of the antithrombin activity for TBA-bs13. thrombin aptamer 235-238 serpin family C member 1 Homo sapiens 209-221 25483839-1 2015 While antithrombin (AT) has small basal inhibitory activity, it reaches its full inhibitory potential against activated blood coagulation factors, FXa, FIXa, and FIIa (thrombin), via an allosteric and/or template (bridging) mechanism by the action of heparin, heparan sulfate, or heparin-mimetic pentasaccharides (PS). Heparitin Sulfate 260-275 serpin family C member 1 Homo sapiens 6-18 25483839-1 2015 While antithrombin (AT) has small basal inhibitory activity, it reaches its full inhibitory potential against activated blood coagulation factors, FXa, FIXa, and FIIa (thrombin), via an allosteric and/or template (bridging) mechanism by the action of heparin, heparan sulfate, or heparin-mimetic pentasaccharides (PS). pentasaccharides 296-312 serpin family C member 1 Homo sapiens 6-18 25483839-1 2015 While antithrombin (AT) has small basal inhibitory activity, it reaches its full inhibitory potential against activated blood coagulation factors, FXa, FIXa, and FIIa (thrombin), via an allosteric and/or template (bridging) mechanism by the action of heparin, heparan sulfate, or heparin-mimetic pentasaccharides (PS). ps 314-316 serpin family C member 1 Homo sapiens 6-18 32262660-0 2015 Surface modification of poly(dimethylsiloxane) with a covalent antithrombin-heparin complex for the prevention of thrombosis: use of polydopamine as bonding agent. baysilon 24-46 serpin family C member 1 Homo sapiens 63-75 26148660-0 2015 Antithrombin Concentrate Use in Children Receiving Unfractionated Heparin for Acute Thrombosis. Heparin 66-73 serpin family C member 1 Homo sapiens 0-12 26148660-1 2015 OBJECTIVE: To characterize features of antithrombin concentrate (ATC) use in children receiving unfractionated heparin (UFH) therapy for acute thrombosis. Heparin 111-118 serpin family C member 1 Homo sapiens 39-51 26148660-1 2015 OBJECTIVE: To characterize features of antithrombin concentrate (ATC) use in children receiving unfractionated heparin (UFH) therapy for acute thrombosis. Heparin 120-123 serpin family C member 1 Homo sapiens 39-51 26188924-8 2015 A direct FXa inhibitor, edoxaban, and an antithrombin-dependent anticoagulant, unfractionated heparin (UFH), did not increase, but simply decreased TG under each condition in a concentration dependent manner. Heparin 103-106 serpin family C member 1 Homo sapiens 41-53 26232351-0 2015 Extracellular histone H3 levels are inversely correlated with antithrombin levels and platelet counts and are associated with mortality in sepsis patients. HS 3 22-24 serpin family C member 1 Homo sapiens 62-74 26232351-6 2015 H3 levels are positively correlated with lactate dehydrogenase (LDH) activity (Spearman"s rho=0.49, P<0.001), and negatively correlated with antithrombin levels (rho=-0.34, P=0.027) and platelet counts (rho=-0.33, P=0.031). HS 3 0-2 serpin family C member 1 Homo sapiens 144-156 26232351-7 2015 CONCLUSIONS: We conclude that circulating H3 levels correlate with mortality in sepsis patients and inversely correlate with antithrombin levels and platelet counts. HS 3 42-44 serpin family C member 1 Homo sapiens 125-137 26186963-1 2015 INTRODUCTION: beta-antithrombin, the minor antithrombin glycoform in plasma, is probably the major thrombin inhibitor in vivo because of its high heparin affinity. Heparin 146-153 serpin family C member 1 Homo sapiens 19-31 26186963-7 2015 RESULTS: High salt concentrations specifically restricted the pentassacharide-induced activation of antithrombin to the beta glycoform. Salts 14-18 serpin family C member 1 Homo sapiens 100-112 26186963-7 2015 RESULTS: High salt concentrations specifically restricted the pentassacharide-induced activation of antithrombin to the beta glycoform. pentassacharide 62-77 serpin family C member 1 Homo sapiens 100-112 26188924-8 2015 A direct FXa inhibitor, edoxaban, and an antithrombin-dependent anticoagulant, unfractionated heparin (UFH), did not increase, but simply decreased TG under each condition in a concentration dependent manner. Heparin 94-101 serpin family C member 1 Homo sapiens 41-53 32262660-0 2015 Surface modification of poly(dimethylsiloxane) with a covalent antithrombin-heparin complex for the prevention of thrombosis: use of polydopamine as bonding agent. Heparin 76-83 serpin family C member 1 Homo sapiens 63-75 32262660-0 2015 Surface modification of poly(dimethylsiloxane) with a covalent antithrombin-heparin complex for the prevention of thrombosis: use of polydopamine as bonding agent. polydopamine 133-145 serpin family C member 1 Homo sapiens 63-75 32262660-2 2015 To prevent thrombosis triggered by blood-material contact, an antithrombin-heparin (ATH) covalent complex was coated on PDMS surface using polydopamine (PDA) as a "bioglue". Heparin 75-82 serpin family C member 1 Homo sapiens 62-74 32262660-2 2015 To prevent thrombosis triggered by blood-material contact, an antithrombin-heparin (ATH) covalent complex was coated on PDMS surface using polydopamine (PDA) as a "bioglue". polydopamine 139-151 serpin family C member 1 Homo sapiens 62-74 32262660-2 2015 To prevent thrombosis triggered by blood-material contact, an antithrombin-heparin (ATH) covalent complex was coated on PDMS surface using polydopamine (PDA) as a "bioglue". polydopamine 153-156 serpin family C member 1 Homo sapiens 62-74 26059252-1 2015 The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers. pentasaccharide 199-214 serpin family C member 1 Homo sapiens 158-174 26059252-1 2015 The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers. pentasaccharide 199-214 serpin family C member 1 Homo sapiens 176-181 26059252-1 2015 The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers. tetraethylene glycol 223-243 serpin family C member 1 Homo sapiens 158-174 26059252-1 2015 The present study details the development of a family of novel D-Ala(8) glucagon-like peptide-1 (GLP-1) peptide conjugates by site specific conjugation to an antithrombin III (ATIII) binding carrier pentasaccharide through tetraethylene glycol linkers. tetraethylene glycol 223-243 serpin family C member 1 Homo sapiens 176-181 26059252-10 2015 In conclusion, GLP-1 peptides conjugated to an ATIII binding carrier pentasaccharide have a substantially prolonged bioactive profile compatible for possible once-weekly treatment of type 2 diabetes in humans. pentasaccharide 69-84 serpin family C member 1 Homo sapiens 47-52 29123765-13 2016 The thrombin-antithrombin complex may be useful for monitoring the plasma dabigatran level. Dabigatran 74-84 serpin family C member 1 Homo sapiens 13-25 25869030-0 2015 Successful treatment with rivaroxaban of an extended superficial vein thrombosis in a patient with acquired antithrombin deficiency due to Peg-asparaginase treatment. Rivaroxaban 26-37 serpin family C member 1 Homo sapiens 108-120 25811451-8 2015 However, activation of FV with rhFIIa was approximately 25% more effective than with pdhFIIa and heparin-enhanced inhibition of rhFIIa by antithrombin was significantly more efficient compared with pdhFIIa with 10% higher inhibition both at steady state and at initial rate conditions. Heparin 97-104 serpin family C member 1 Homo sapiens 138-150 26082359-10 2015 Multiple regression analyses indicated that HCY level was negatively correlated with AT-III (beta = -0.199, P = 0.011) and positively correlated with age (beta = 0.217, P = 0.04), female gender (beta = 5.667, P = 0.001) and TM (beta = 2.341, P = 0.003). Homocysteine 44-47 serpin family C member 1 Homo sapiens 85-91 25851619-2 2015 Hemophilia B prophylaxis targets plasma FIX levels > 1% but neglects extravascular FIX, which colocalizes with antithrombin-heparan sulfate. Heparitin Sulfate 127-142 serpin family C member 1 Homo sapiens 114-126 25851619-9 2015 Dual mutations in the heparin exosite or combined mutations in both exosites synergistically reduced the inhibition rate for antithrombin-heparin. heparin exosite 22-37 serpin family C member 1 Homo sapiens 125-137 25851619-9 2015 Dual mutations in the heparin exosite or combined mutations in both exosites synergistically reduced the inhibition rate for antithrombin-heparin. Heparin 22-29 serpin family C member 1 Homo sapiens 125-137 25585615-5 2015 The results revealed that the antithrombin activity of the boronophenylalanine-modified hirudin to human thrombin was more enhanced than that of rHirudin. 4-boronophenylalanine 59-78 serpin family C member 1 Homo sapiens 30-42 25585615-5 2015 The results revealed that the antithrombin activity of the boronophenylalanine-modified hirudin to human thrombin was more enhanced than that of rHirudin. rhirudin 145-153 serpin family C member 1 Homo sapiens 30-42 26023895-6 2015 Further studies revealed that the reactivity of FIXa-G317R and FIXa-G317E with antithrombin has been impaired 10- and 13-fold, respectively, in the absence and 166- and 500-fold, respectively, in the presence of pentasaccharide. pentasaccharide 212-227 serpin family C member 1 Homo sapiens 79-91 25765603-6 2015 The ability of heparin-based NCs to bind to antithrombin (AT III) was investigated using isothermal titration calorimetry and dynamic light scattering experiments. Heparin 15-22 serpin family C member 1 Homo sapiens 44-64 25921251-0 2015 High-resolution probing heparan sulfate-antithrombin interaction on a single endothelial cell surface: single-molecule AFM studies. Heparitin Sulfate 24-39 serpin family C member 1 Homo sapiens 40-52 25921251-1 2015 Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT). Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 179-191 25921251-1 2015 Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT). Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 193-195 25921251-1 2015 Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT). Heparitin Sulfate 17-19 serpin family C member 1 Homo sapiens 179-191 25921251-1 2015 Heparan sulfate (HS) plays diverse functions in multiple biological processes by interacting with a wide range of important protein ligands, such as the key anticoagulant factor, antithrombin (AT). Heparitin Sulfate 17-19 serpin family C member 1 Homo sapiens 193-195 25817684-4 2015 Liquid chromatography-mass spectrometry and nuclear magnetic resonance spectroscopy analysis confirms an abundance of heparin"s characteristic trisulfated disaccharide, as well as 3-O-sulfo containing residues critical for heparin binding to antithrombin III and its anticoagulant activity. Heparin 118-125 serpin family C member 1 Homo sapiens 242-258 25817684-4 2015 Liquid chromatography-mass spectrometry and nuclear magnetic resonance spectroscopy analysis confirms an abundance of heparin"s characteristic trisulfated disaccharide, as well as 3-O-sulfo containing residues critical for heparin binding to antithrombin III and its anticoagulant activity. Heparin 223-230 serpin family C member 1 Homo sapiens 242-258 26390679-8 2015 Data were collected on 15 patients undergoing CPB who received antithrombin III (AT) replacement therapy for diminished heparin response. Heparin 120-127 serpin family C member 1 Homo sapiens 63-79 25811371-9 2015 AT purified from patient"s plasma on hi-trap heparin column showed a marked decrease in heparin affinity and thrombin inhibition rates. Heparin 45-52 serpin family C member 1 Homo sapiens 0-2 25811371-9 2015 AT purified from patient"s plasma on hi-trap heparin column showed a marked decrease in heparin affinity and thrombin inhibition rates. Heparin 88-95 serpin family C member 1 Homo sapiens 0-2 25581634-11 2015 For those who received antithrombin concentrate, heparin infusion rates decreased by an average of 10.2 U/kg/hr for at least 12 hours following administration. Heparin 49-56 serpin family C member 1 Homo sapiens 23-35 25581634-14 2015 Patients who received antithrombin concentrate also had decreased heparin requirements for at least 12 hours after dosing. Heparin 66-73 serpin family C member 1 Homo sapiens 22-34 25594496-2 2015 The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation. Heparin 88-95 serpin family C member 1 Homo sapiens 126-142 25600805-6 2015 Other serpins, including antithrombin III and pigment epithelium-derived factor, were also degraded by heparan sulfate. Heparitin Sulfate 103-118 serpin family C member 1 Homo sapiens 25-41 25594496-2 2015 The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation. Heparin 88-95 serpin family C member 1 Homo sapiens 144-146 25594496-2 2015 The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation. argatroban 193-203 serpin family C member 1 Homo sapiens 126-142 25594496-2 2015 The aim of this study was to investigate whether critically ill patients suffering from heparin resistance generally have low antithrombin III (AT) levels, and if the direct thrombin inhibitor argatroban in that case can be an effective option to achieve prophylactic anticoagulation. argatroban 193-203 serpin family C member 1 Homo sapiens 144-146 25486437-1 2015 Heparan sulfate (HS) 3-O-sulfation determines the binding specificity of HS/heparin for antithrombin III and plays a key role in herpes simplex virus (HSV) infection. heparan sulfate (hs) 3- 0-23 serpin family C member 1 Homo sapiens 88-104 25486437-1 2015 Heparan sulfate (HS) 3-O-sulfation determines the binding specificity of HS/heparin for antithrombin III and plays a key role in herpes simplex virus (HSV) infection. Heparin 76-83 serpin family C member 1 Homo sapiens 88-104 25687119-5 2015 Biacore experiments revealed that the binding affinity of Bothrops jararaca snake antithrombin to heparin was ~30 times higher than that of human antithrombin. Heparin 98-105 serpin family C member 1 Homo sapiens 82-94 25325940-2 2015 One example, the extensively studied heparin pentasaccharide sequence-which binds antithrombin-III, inducing a conformational change that increases its serpin protease activity by 1,000-fold-is unique in that no other specific GAG-protein structure-function relations have been described to the same degree. IC 831423 37-60 serpin family C member 1 Homo sapiens 82-98 25325940-2 2015 One example, the extensively studied heparin pentasaccharide sequence-which binds antithrombin-III, inducing a conformational change that increases its serpin protease activity by 1,000-fold-is unique in that no other specific GAG-protein structure-function relations have been described to the same degree. Glycosaminoglycans 227-230 serpin family C member 1 Homo sapiens 82-98 25325941-3 2015 However, only 3-O sulfonated heparin pentasaccharide units have been proven to bind to antithrombin and elicit an anticoagulant response. IC 831423 29-52 serpin family C member 1 Homo sapiens 87-99 25553275-5 2015 RESULTS: The procoagulant factors II, VII, IX, X, and XI and anticoagulant factors protein C and protein S showed significant correlations with triglyceride, and the procoagulant factors II, V, VII, IX, X, XI, and XII and anticoagulant factors antithrombin and protein C correlated with total cholesterol. Triglycerides 144-156 serpin family C member 1 Homo sapiens 244-256 25863018-0 2015 A fast capillary electrophoresis method to assess the binding affinity of recombinant antithrombin toward heparin directly from cell culture supernatants. Heparin 106-113 serpin family C member 1 Homo sapiens 86-98 25863018-1 2015 With the aim to determine the binding affinity of a new generation of recombinant antithrombin (AT) toward heparin, we developed a dynamic equilibrium-affinity capillary electrophoresis (DE-ACE) method. Heparin 107-114 serpin family C member 1 Homo sapiens 82-94 25687119-6 2015 Furthermore, Bothrops jararaca antithrombin is more effective in preventing acute inflammation induced by carrageenan when compared to human antithrombin. Carrageenan 106-117 serpin family C member 1 Homo sapiens 31-43 25231101-10 2015 The presence of dabigatran caused an overestimation of the antithrombin level when measured with a thrombin-based activity assay and the presence of rivaroxaban an overestimation of the antithrombin level when measured with a FXa-based assay. Dabigatran 16-26 serpin family C member 1 Homo sapiens 59-71 24711209-2 2014 This study evaluates how the mode of covalent heparin bonding affects the hemocompatibility and uptake of antithrombin on surfaces in whole blood. Heparin 46-53 serpin family C member 1 Homo sapiens 106-118 25466846-0 2015 Development of a novel, rapid assay for detection of heparin-binding defect antithrombin deficiencies: the heparin-antithrombin binding (HAB) ratio. Heparin 53-60 serpin family C member 1 Homo sapiens 76-88 25466846-3 2015 PATIENTS/METHODS: Extended heparin incubation in antithrombin activity assays can overestimate levels in patients with HBDs. Heparin 27-34 serpin family C member 1 Homo sapiens 49-61 25466848-7 2015 Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression. Retinoids 0-9 serpin family C member 1 Homo sapiens 112-114 25466848-7 2015 Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression. Dexamethasone 36-49 serpin family C member 1 Homo sapiens 112-114 25466848-7 2015 Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression. Cortisone 51-60 serpin family C member 1 Homo sapiens 112-114 25466848-7 2015 Retinoids, activating RXR, and GCs (Dexamethasone, cortisone and methylprednisolone) also resulted in increased AT expression. Methylprednisolone 65-83 serpin family C member 1 Homo sapiens 112-114 25331949-0 2014 Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease. Heparin 45-52 serpin family C member 1 Homo sapiens 29-41 25331949-1 2014 Heparin allosterically activates antithrombin as an inhibitor of factors Xa and IXa by enhancing the initial Michaelis complex interaction of inhibitor with protease through exosites. Heparin 0-7 serpin family C member 1 Homo sapiens 33-45 25331949-3 2014 Mutations of antithrombin Tyr(253) and His(319) exosite residues produced massive 10-200-fold losses in reactivity with factors Xa and IXa in both unactivated and heparin-activated states, indicating that these residues made critical attractive interactions with protease independent of heparin activation. Tyrosine 26-29 serpin family C member 1 Homo sapiens 13-25 25331949-3 2014 Mutations of antithrombin Tyr(253) and His(319) exosite residues produced massive 10-200-fold losses in reactivity with factors Xa and IXa in both unactivated and heparin-activated states, indicating that these residues made critical attractive interactions with protease independent of heparin activation. exosite 48-55 serpin family C member 1 Homo sapiens 13-25 25331949-6 2014 These results demonstrate that the exosite is a key determinant of antithrombin reactivity with factors Xa and IXa in the native as well as the heparin-activated state and support a new model of allosteric activation we recently proposed in which a balance between attractive and repulsive exosite interactions in the native state is shifted to favor the attractive interactions in the activated state through core conformational changes induced by heparin binding. exosite 35-42 serpin family C member 1 Homo sapiens 67-79 25331949-6 2014 These results demonstrate that the exosite is a key determinant of antithrombin reactivity with factors Xa and IXa in the native as well as the heparin-activated state and support a new model of allosteric activation we recently proposed in which a balance between attractive and repulsive exosite interactions in the native state is shifted to favor the attractive interactions in the activated state through core conformational changes induced by heparin binding. Heparin 144-151 serpin family C member 1 Homo sapiens 67-79 25331949-6 2014 These results demonstrate that the exosite is a key determinant of antithrombin reactivity with factors Xa and IXa in the native as well as the heparin-activated state and support a new model of allosteric activation we recently proposed in which a balance between attractive and repulsive exosite interactions in the native state is shifted to favor the attractive interactions in the activated state through core conformational changes induced by heparin binding. Heparin 449-456 serpin family C member 1 Homo sapiens 67-79 25396040-5 2014 Soc., 2013, 135, 167 - 173) to a piperidinone-piperidine chemotype 1 indicated specific derivatives were candidates to perturb a protein-protein interface in the alpha-antithrombin dimer; those particular derivatives of 1 were prepared and tested. 2-piperidone 33-45 serpin family C member 1 Homo sapiens 168-180 25396040-5 2014 Soc., 2013, 135, 167 - 173) to a piperidinone-piperidine chemotype 1 indicated specific derivatives were candidates to perturb a protein-protein interface in the alpha-antithrombin dimer; those particular derivatives of 1 were prepared and tested. piperidine 46-56 serpin family C member 1 Homo sapiens 168-180 25307422-3 2014 MGO has been shown to inhibit ATIII activity in vitro, however the mechanism of inhibition is incompletely understood. Pyruvaldehyde 0-3 serpin family C member 1 Homo sapiens 30-35 25307422-4 2014 As such, we designed this study to investigate the kinetics and mechanism of MGO-mediated ATIII inhibition. Pyruvaldehyde 77-80 serpin family C member 1 Homo sapiens 90-95 25307422-5 2014 METHODS: MGO-mediated ATIII inhibition was confirmed using inverse experiments detecting activity of the ATIII targets thrombin and factor Xa. Pyruvaldehyde 9-12 serpin family C member 1 Homo sapiens 22-27 25307422-5 2014 METHODS: MGO-mediated ATIII inhibition was confirmed using inverse experiments detecting activity of the ATIII targets thrombin and factor Xa. Pyruvaldehyde 9-12 serpin family C member 1 Homo sapiens 105-110 25307422-6 2014 Fluorogenic assays were performed in both PBS and plasma after incubation of ATIII with MGO, at molar ratios comparable to those observed in the plasma of diabetic patients. Pyruvaldehyde 88-91 serpin family C member 1 Homo sapiens 77-82 25307422-7 2014 LC-coupled tandem mass spectrometry was utilized to investigate the exact mechanism of MGO-mediated ATIII inhibition. Pyruvaldehyde 87-90 serpin family C member 1 Homo sapiens 100-105 25307422-8 2014 RESULTS AND CONCLUSIONS: MGO concentration-dependently attenuated inhibition of thrombin and factor Xa by ATIII in PBS-based assays, both in the presence and absence of heparin. Pyruvaldehyde 25-28 serpin family C member 1 Homo sapiens 106-111 25307422-9 2014 In addition, MGO concentration-dependently inhibited ATIII activity in a plasma-based system, to the level of plasma completely deficient in ATIII, again both in the presence and absence of heparin. Pyruvaldehyde 13-16 serpin family C member 1 Homo sapiens 53-58 25307422-9 2014 In addition, MGO concentration-dependently inhibited ATIII activity in a plasma-based system, to the level of plasma completely deficient in ATIII, again both in the presence and absence of heparin. Pyruvaldehyde 13-16 serpin family C member 1 Homo sapiens 141-146 25307422-10 2014 Results from LC-MS/MS experiments revealed that MGO covalently adducts the active site Arg 393 of ATIII through two distinct glyoxalation mechanisms. Pyruvaldehyde 48-51 serpin family C member 1 Homo sapiens 98-103 25307422-10 2014 Results from LC-MS/MS experiments revealed that MGO covalently adducts the active site Arg 393 of ATIII through two distinct glyoxalation mechanisms. Arginine 87-90 serpin family C member 1 Homo sapiens 98-103 25307422-11 2014 We posit that active site adduction is the mechanism of MGO-mediated inhibition of ATIII, and thus contributes to the underlying pathophysiology of the diabetic hypercoagulable state and complications thereof. Pyruvaldehyde 56-59 serpin family C member 1 Homo sapiens 83-88 25312341-0 2014 Identification of a new SERPINC1 mutation in a Kazak family that alters the heparin binding capacity of antithrombin. Heparin 76-83 serpin family C member 1 Homo sapiens 24-32 25312341-0 2014 Identification of a new SERPINC1 mutation in a Kazak family that alters the heparin binding capacity of antithrombin. Heparin 76-83 serpin family C member 1 Homo sapiens 104-116 25312341-1 2014 INTRODUCTION: Given its central role in mediating heparin-induced anti-coagulation, antithrombin (AT) gene mutations may result in heparin resistance. Heparin 50-57 serpin family C member 1 Homo sapiens 84-96 25312341-1 2014 INTRODUCTION: Given its central role in mediating heparin-induced anti-coagulation, antithrombin (AT) gene mutations may result in heparin resistance. Heparin 131-138 serpin family C member 1 Homo sapiens 84-96 25485983-1 2014 The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: alpha and beta, with four and three N-glycans, respectively. N-[3-(Trimethoxysilyl)propyl]aniline 55-59 serpin family C member 1 Homo sapiens 63-75 25485983-1 2014 The inefficient glycosylation of consensus sequence on N135 in antithrombin explains the two glycoforms of this key anticoagulant serpin found in plasma: alpha and beta, with four and three N-glycans, respectively. n-glycans 190-199 serpin family C member 1 Homo sapiens 63-75 23698186-1 2014 Valsartan is known to inhibit platelet activity in both in vitro and ex vivo clinical setting, whereas aliskiren in vitro modulates antithrombin-III in plasma. aliskiren 103-112 serpin family C member 1 Homo sapiens 132-148 24711209-8 2014 In addition, antithrombin constituted ~40% of the total adsorbed plasma protein concentration on the EPA-heparin surfaces. Eicosapentaenoic Acid 101-104 serpin family C member 1 Homo sapiens 13-25 24711209-8 2014 In addition, antithrombin constituted ~40% of the total adsorbed plasma protein concentration on the EPA-heparin surfaces. Heparin 105-112 serpin family C member 1 Homo sapiens 13-25 25202017-2 2014 Previous investigations have shown that ATIII is degraded by Staphylococcus aureus V8 protease, leading to release of heparin binding fragments derived from its D helix. Heparin 118-125 serpin family C member 1 Homo sapiens 40-45 25202017-5 2014 Correspondingly, the heparin-binding, helix D-derived, peptide FFFAKLNCRLYRKANKSSKLV (FFF21) of human ATIII, was found to be antimicrobial against particularly the Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa. Heparin 21-28 serpin family C member 1 Homo sapiens 102-107 25361933-6 2014 The uHcy/Cr ratio correlated more closely with protein C, antithrombin III, TNF-alpha, and NOx levels than did sHcy concentrations. Chromium 9-11 serpin family C member 1 Homo sapiens 58-74 24901804-0 2014 Antithrombin concentrate in pediatric patients requiring unfractionated heparin anticoagulation: a retrospective cohort study. Heparin 72-79 serpin family C member 1 Homo sapiens 0-12 25145542-0 2014 Antithrombin-binding oligosaccharides: structural diversities in a unique function? Oligosaccharides 21-37 serpin family C member 1 Homo sapiens 0-12 25145542-3 2014 Moreover, the position of the pentasaccharide along the chain as well as the structure of the neighbor units affects the affinity to antithrombin. pentasaccharide 30-45 serpin family C member 1 Homo sapiens 133-145 25145542-4 2014 The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin. Oligosaccharides 197-213 serpin family C member 1 Homo sapiens 176-188 25145542-4 2014 The development of separation and purification techniques, in conjunction with physico-chemical approaches (mostly NMR), allowed to characterize several structural variants of antithrombin-binding oligosaccharides, both in the free state and in complex with antithrombin. Oligosaccharides 197-213 serpin family C member 1 Homo sapiens 258-270 24901804-15 2014 In cohort 2, unfractionated heparin doses to achieve a target anti-factor Xa activity pre-post antithrombin concentrate were 28 and 19 U/kg/hr, respectively, for children 12 months old or younger and 25 and 19 U/kg/hr, respectively, for children older than 12 months. Heparin 28-35 serpin family C member 1 Homo sapiens 95-107 25130453-10 2014 At 3-D imaging and dissection, the DAEM was found to be an extension of the metacarpophalangeal joint capsule. daem 35-39 serpin family C member 1 Homo sapiens 0-6 24979180-1 2014 CONTEXT: The results of studies among patients with antithrombin deficiency have suggested that the use of warfarin will increase the level of antithrombin. Warfarin 107-115 serpin family C member 1 Homo sapiens 52-64 24705477-3 2014 One key target of heparin, among others, is antithrombin, a serine protease inhibitor that, upon activation, mainly targets anticoagulation factors IIa and Xa. Heparin 18-25 serpin family C member 1 Homo sapiens 44-56 24994735-4 2014 Heparin resistance is very rare in these patients, especially when antithrombin levels are near normal. Heparin 0-7 serpin family C member 1 Homo sapiens 67-79 24770491-7 2014 The antithrombin (AT) binding affinities of a GlcA2S- and an IdoA2S-hexasaccharide were determined by affinity co-electrophoresis. 2-O-sulfo-beta-D-glucuronic acid 46-52 serpin family C member 1 Homo sapiens 4-16 24770491-7 2014 The antithrombin (AT) binding affinities of a GlcA2S- and an IdoA2S-hexasaccharide were determined by affinity co-electrophoresis. idoa2s-hexasaccharide 61-82 serpin family C member 1 Homo sapiens 4-16 24920241-0 2014 Outstanding effects on antithrombin activity of modified TBA diastereomers containing an optically pure acyclic nucleotide analogue. tba 57-60 serpin family C member 1 Homo sapiens 23-35 24522239-1 2014 Antithrombin (AT) is a heparin-binding serpin in plasma which regulates the proteolytic activity of procoagulant proteases of the clotting cascade. Heparin 23-30 serpin family C member 1 Homo sapiens 0-12 24979180-4 2014 RESULTS: Patients receiving warfarin had a mean antithrombin level of 100.40% (range, 81%-153%). Warfarin 28-36 serpin family C member 1 Homo sapiens 48-60 24979180-1 2014 CONTEXT: The results of studies among patients with antithrombin deficiency have suggested that the use of warfarin will increase the level of antithrombin. Warfarin 107-115 serpin family C member 1 Homo sapiens 143-155 24979180-2 2014 OBJECTIVE: To reevaluate the effect of warfarin on antithrombin levels using an automated amidolytic method in current use. Warfarin 39-47 serpin family C member 1 Homo sapiens 51-63 24979180-3 2014 DESIGN: Antithrombin levels were measured in patients who were receiving warfarin for atrial fibrillation and were compared with antithrombin levels in preoperative patients who had not received warfarin. Warfarin 73-81 serpin family C member 1 Homo sapiens 8-20 24824609-0 2014 Role of the C-sheet in the maturation of N-glycans on antithrombin: functional relevance of pleiotropic mutations. n-glycans 41-50 serpin family C member 1 Homo sapiens 54-66 24801362-2 2014 The capacity of antithrombin to inhibit thrombin is known to increase a 1000-fold whilst in the presence of unfractionated heparin. Heparin 123-130 serpin family C member 1 Homo sapiens 16-28 24801362-3 2014 beta-antithrombin is an isoform of antithrombin with a high affinity for unfractionated heparin. Heparin 88-95 serpin family C member 1 Homo sapiens 5-17 24801362-3 2014 beta-antithrombin is an isoform of antithrombin with a high affinity for unfractionated heparin. Heparin 88-95 serpin family C member 1 Homo sapiens 35-47 24824609-11 2014 In contrast, variant 2, with similar electrophoretic mobility and heparin affinity to wild-type antithrombin, had impaired inhibitory activity that was partially compensated for by activation with heparin. Heparin 197-204 serpin family C member 1 Homo sapiens 96-108 24801362-7 2014 The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms. Salts 199-203 serpin family C member 1 Homo sapiens 86-98 24801362-7 2014 The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms. Salts 199-203 serpin family C member 1 Homo sapiens 151-163 24824609-12 2014 Our results suggest the C-sheet of antithrombin as a new region that is relevant for proper maturation of the N-glycans. n-glycans 110-119 serpin family C member 1 Homo sapiens 35-47 24801362-7 2014 The modified version of this assay allows for the specific quantification of the beta-antithrombin glycoform anticoagulant activity alone, as the beta-antithrombin molecule is activated under a high salt concentration, which in turn does not allow activation of other antithrombin isoforms. Salts 199-203 serpin family C member 1 Homo sapiens 151-163 24616065-1 2014 The anticoagulant properties of heparin stem in part from high-affinity binding to antithrombin-III (AT-III) inducing a 300-fold increase in its inhibitory activity against the coagulation protease factor Xa. Heparin 32-39 serpin family C member 1 Homo sapiens 83-99 24561026-3 2014 Activated AT also inhibits thrombin by forming a stable ternary complex of AT, thrombin, and a polysaccharide (requires at least an 18-mer/octadeca-mer polysaccharide). Polysaccharides 152-166 serpin family C member 1 Homo sapiens 10-12 24561026-3 2014 Activated AT also inhibits thrombin by forming a stable ternary complex of AT, thrombin, and a polysaccharide (requires at least an 18-mer/octadeca-mer polysaccharide). Polysaccharides 152-166 serpin family C member 1 Homo sapiens 75-77 24375987-0 2014 Retrospective evaluation of antithrombin III supplementation in neonates and infants receiving enoxaparin for treatment of thrombosis. Enoxaparin 95-105 serpin family C member 1 Homo sapiens 28-44 24375987-5 2014 PROCEDURE: This retrospective study compared time to therapeutic anti-Xa levels in patients <1 year of age receiving enoxaparin with AT3 (Group 1) and without AT3 (Group 2) for treatment of thrombosis. Enoxaparin 120-130 serpin family C member 1 Homo sapiens 136-139 24561026-0 2014 Isolation of a pure octadecasaccharide with antithrombin activity from an ultra-low-molecular-weight heparin. octadecasaccharide 20-38 serpin family C member 1 Homo sapiens 44-56 24561026-2 2014 Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine. pentasaccharide 87-102 serpin family C member 1 Homo sapiens 27-39 24561026-2 2014 Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine. pentasaccharide 87-102 serpin family C member 1 Homo sapiens 41-43 24561026-2 2014 Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine. pentasaccharide 87-102 serpin family C member 1 Homo sapiens 72-74 24561026-2 2014 Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine. glucosamine 3-O-sulfate 124-148 serpin family C member 1 Homo sapiens 27-39 24561026-2 2014 Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine. glucosamine 3-O-sulfate 124-148 serpin family C member 1 Homo sapiens 41-43 24561026-2 2014 Inhibition of factor Xa by antithrombin (AT) requires the activation of AT by specific pentasaccharide sequences containing 3-O-sulfated glucosamine. glucosamine 3-O-sulfate 124-148 serpin family C member 1 Homo sapiens 72-74 24561026-3 2014 Activated AT also inhibits thrombin by forming a stable ternary complex of AT, thrombin, and a polysaccharide (requires at least an 18-mer/octadeca-mer polysaccharide). Polysaccharides 95-109 serpin family C member 1 Homo sapiens 10-12 24616065-3 2014 ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). Tinzaparin 148-158 serpin family C member 1 Homo sapiens 49-55 24616065-3 2014 ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). pentasaccharide 177-192 serpin family C member 1 Homo sapiens 49-55 24616065-3 2014 ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). Fondaparinux 198-210 serpin family C member 1 Homo sapiens 49-55 24616065-3 2014 ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). Fondaparinux 212-219 serpin family C member 1 Homo sapiens 49-55 24616065-1 2014 The anticoagulant properties of heparin stem in part from high-affinity binding to antithrombin-III (AT-III) inducing a 300-fold increase in its inhibitory activity against the coagulation protease factor Xa. Heparin 32-39 serpin family C member 1 Homo sapiens 101-107 24616065-2 2014 The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue. IC 831423 81-104 serpin family C member 1 Homo sapiens 40-46 24616065-2 2014 The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue. 3,6-o 127-132 serpin family C member 1 Homo sapiens 40-46 24616065-2 2014 The minimal structural requirements for AT-III binding are contained in the rare heparin pentasaccharide sequence containing a 3,6-O-sulfated N-sulfoglucosamine residue. glucosamine 2-sulfate 142-160 serpin family C member 1 Homo sapiens 40-46 24616065-3 2014 ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). Heparin 103-111 serpin family C member 1 Homo sapiens 49-55 24616065-3 2014 ACE is used in this work to measure the relative AT-III binding affinities of the low molecular weight heparins (LWMHs) dalteparin, enoxaparin, and tinzaparin and the synthetic pentasaccharide drug fondaparinux (Arixtra). Enoxaparin 132-142 serpin family C member 1 Homo sapiens 49-55 24361527-3 2014 Sulfation at the C3 position of glucosamine is a relatively rare, yet biologically significant modification, initially described as a key determinant for binding and activation of antithrombin and later for infection by type I herpes simplex virus. Glucosamine 32-43 serpin family C member 1 Homo sapiens 180-192 24632519-7 2014 P-beads bound LPS dissolved in antithrombin III (AT III) solution which is a strong inhibitor of activated factors C and B as well as the clotting enzyme in the LAL assay; the inhibitory effect of AT III was completely reversed upon washing the P-beads with 25% acetonitrile. acetonitrile 262-274 serpin family C member 1 Homo sapiens 31-47 24632519-7 2014 P-beads bound LPS dissolved in antithrombin III (AT III) solution which is a strong inhibitor of activated factors C and B as well as the clotting enzyme in the LAL assay; the inhibitory effect of AT III was completely reversed upon washing the P-beads with 25% acetonitrile. acetonitrile 262-274 serpin family C member 1 Homo sapiens 49-55 24632519-7 2014 P-beads bound LPS dissolved in antithrombin III (AT III) solution which is a strong inhibitor of activated factors C and B as well as the clotting enzyme in the LAL assay; the inhibitory effect of AT III was completely reversed upon washing the P-beads with 25% acetonitrile. acetonitrile 262-274 serpin family C member 1 Homo sapiens 197-203 23460104-9 2014 The novel oral anticoagulants (NOAC) dabigatran etexilat (Pradaxa ), rivaroxaban (Xarelto ) and apixaban (Eliquis ), also known as "direct" anticoagulants, act independently from antithrombin by inhibiting thrombin, as in the case of dabigatran, or by inhibiting factor Xa, as in the case of rivaroxaban and apixaban. apixaban 96-104 serpin family C member 1 Homo sapiens 179-191 24196373-1 2014 Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE). Heparin 78-85 serpin family C member 1 Homo sapiens 17-29 24196373-1 2014 Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE). Heparin 78-85 serpin family C member 1 Homo sapiens 31-33 24196373-1 2014 Mutations in the antithrombin (AT) gene can impair the capacity of AT to bind heparin (AT deficiency type IIHBS), its target proteases such as thrombin (type IIRS), or both (type IIPE). Heparin 78-85 serpin family C member 1 Homo sapiens 67-69 24779124-1 2014 Acquired antithrombin (AT) deficiency has been associated with patients on extracorporeal membrane oxygenation (ECMO) as a result of hemodilution, blood coagulation activation, and the use of heparin. Heparin 192-199 serpin family C member 1 Homo sapiens 9-21 24438318-4 2014 Our study aimed to monitor AT-III levels in the early post-LT period to assess the need for the administration of AT-III concentrate to ensure the effectiveness of heparin. Heparin 164-171 serpin family C member 1 Homo sapiens 27-33 24438318-4 2014 Our study aimed to monitor AT-III levels in the early post-LT period to assess the need for the administration of AT-III concentrate to ensure the effectiveness of heparin. Heparin 164-171 serpin family C member 1 Homo sapiens 114-120 24438318-14 2014 AT-III levels were low in 70% of pediatric patients following LT, thereby risking heparin ineffectiveness. Heparin 82-89 serpin family C member 1 Homo sapiens 0-6 24647152-4 2014 Fondaparinux, a chemically synthesized ULMWH of pentasaccharide, has the same antithrombin III (AT-III)-binding sequence as found in UFH and LMWH. Fondaparinux 0-12 serpin family C member 1 Homo sapiens 78-94 24647152-4 2014 Fondaparinux, a chemically synthesized ULMWH of pentasaccharide, has the same antithrombin III (AT-III)-binding sequence as found in UFH and LMWH. Fondaparinux 0-12 serpin family C member 1 Homo sapiens 96-102 24647152-4 2014 Fondaparinux, a chemically synthesized ULMWH of pentasaccharide, has the same antithrombin III (AT-III)-binding sequence as found in UFH and LMWH. pentasaccharide 48-63 serpin family C member 1 Homo sapiens 78-94 24647152-4 2014 Fondaparinux, a chemically synthesized ULMWH of pentasaccharide, has the same antithrombin III (AT-III)-binding sequence as found in UFH and LMWH. pentasaccharide 48-63 serpin family C member 1 Homo sapiens 96-102 24647152-4 2014 Fondaparinux, a chemically synthesized ULMWH of pentasaccharide, has the same antithrombin III (AT-III)-binding sequence as found in UFH and LMWH. Heparin 133-136 serpin family C member 1 Homo sapiens 96-102 23460104-9 2014 The novel oral anticoagulants (NOAC) dabigatran etexilat (Pradaxa ), rivaroxaban (Xarelto ) and apixaban (Eliquis ), also known as "direct" anticoagulants, act independently from antithrombin by inhibiting thrombin, as in the case of dabigatran, or by inhibiting factor Xa, as in the case of rivaroxaban and apixaban. Dabigatran 37-47 serpin family C member 1 Homo sapiens 179-191 24339381-3 2014 We have discovered that exosite-targeting antithrombin aptamers enhance the activity of thrombin toward a small peptide substrate, Sar(N-methylglycine)-Pro-Arg-paranitroanilide, and that the activation of the enzyme by these aptamers is strongly inhibited by their complementary DNAs. exosite 24-31 serpin family C member 1 Homo sapiens 42-54 24627861-2 2014 Heparin resistance was defined as at least one activated clothing time <400 seconds after heparinization and/or the need for purified antithrombin III (AT-III) administration. Heparin 0-7 serpin family C member 1 Homo sapiens 137-153 24627861-2 2014 Heparin resistance was defined as at least one activated clothing time <400 seconds after heparinization and/or the need for purified antithrombin III (AT-III) administration. Heparin 0-7 serpin family C member 1 Homo sapiens 155-161 24339381-3 2014 We have discovered that exosite-targeting antithrombin aptamers enhance the activity of thrombin toward a small peptide substrate, Sar(N-methylglycine)-Pro-Arg-paranitroanilide, and that the activation of the enzyme by these aptamers is strongly inhibited by their complementary DNAs. (n-methylglycine)-pro-arg-paranitroanilide 134-176 serpin family C member 1 Homo sapiens 42-54 24201825-6 2014 Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes. Heparin 14-21 serpin family C member 1 Homo sapiens 126-138 24354321-1 2014 Heparin is best known for its anticoagulant activity, which is mediated by the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin-III (AT-III). Heparin 0-7 serpin family C member 1 Homo sapiens 152-168 24354321-1 2014 Heparin is best known for its anticoagulant activity, which is mediated by the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin-III (AT-III). Heparin 0-7 serpin family C member 1 Homo sapiens 170-176 24354321-1 2014 Heparin is best known for its anticoagulant activity, which is mediated by the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin-III (AT-III). pentasaccharide 101-116 serpin family C member 1 Homo sapiens 152-168 24354321-1 2014 Heparin is best known for its anticoagulant activity, which is mediated by the binding of a specific pentasaccharide sequence to the protease inhibitor antithrombin-III (AT-III). pentasaccharide 101-116 serpin family C member 1 Homo sapiens 170-176 24296776-0 2014 Antithrombin III supplementation on extracorporeal membrane oxygenation: impact on heparin dose and circuit life. Heparin 83-90 serpin family C member 1 Homo sapiens 0-16 24296776-3 2014 We hypothesized that ATIII supplementation would reduce heparin infusion rates, increase unfractionated heparin anti-Xa levels, and prolong ECMO circuit life. Heparin 56-63 serpin family C member 1 Homo sapiens 21-26 24296776-3 2014 We hypothesized that ATIII supplementation would reduce heparin infusion rates, increase unfractionated heparin anti-Xa levels, and prolong ECMO circuit life. Heparin 104-111 serpin family C member 1 Homo sapiens 21-26 24296776-6 2014 The primary outcome was whether the heparin infusion rate was reduced by 10% or more as a result of ATIII administration. Heparin 36-43 serpin family C member 1 Homo sapiens 100-105 24201825-6 2014 Additionally, heparin orientation observed on the surface of fIIa, but not fXa, allows a linear long-chain heparin binding to antithrombin in ternary complexes. Heparin 107-114 serpin family C member 1 Homo sapiens 126-138 24266905-8 2014 The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p < 0.0001 for F1+2 ). Heparin 4-11 serpin family C member 1 Homo sapiens 57-69 24014620-5 2014 Antithrombin (AT) binds to heparin and increases the rate at which it binds to thrombin. Heparin 27-34 serpin family C member 1 Homo sapiens 0-12 24014620-6 2014 The levels of antithrombin in the blood are an important aspect of the heparin dose-response curve. Heparin 71-78 serpin family C member 1 Homo sapiens 14-26 24014620-8 2014 Heparin resistance is usually treated with a combination of supplementary heparin, fresh frozen plasma (FFP) or antithrombin III concentrate. Heparin 0-7 serpin family C member 1 Homo sapiens 112-128 24014620-11 2014 Antithrombin (AT) concentrate is a safe and efficient treatment for heparin resistance to elevate the activated clotting time (ACT). Heparin 68-75 serpin family C member 1 Homo sapiens 0-12 24014620-13 2014 Antithrombin concentrates are more expensive than fresh frozen plasma and may put patients at risk of heparin rebound in the early postoperative period. Heparin 102-109 serpin family C member 1 Homo sapiens 0-12 24735089-0 2014 Surface modification of polydimethylsiloxane with a covalent antithrombin-heparin complex to prevent thrombosis. baysilon 24-44 serpin family C member 1 Homo sapiens 61-73 24735089-1 2014 To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer. baysilon 46-66 serpin family C member 1 Homo sapiens 95-107 24735089-1 2014 To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer. baysilon 68-72 serpin family C member 1 Homo sapiens 95-107 24735089-1 2014 To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer. Heparin 108-115 serpin family C member 1 Homo sapiens 95-107 24735089-1 2014 To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer. Polyethylene Glycols 145-164 serpin family C member 1 Homo sapiens 95-107 24735089-1 2014 To prevent coagulation in contact with blood, polydimethylsiloxane (PDMS) was modified with an antithrombin-heparin (ATH) covalent complex using polyethylene glycol (PEG) as a linker/spacer. Polyethylene Glycols 166-169 serpin family C member 1 Homo sapiens 95-107 24735089-6 2014 It was shown that surfaces modified with ATH bound antithrombin selectively from plasma through the pentasaccharide sequence on the heparin moiety of ATH, indicating the ability of the ATH-modified surfaces to inhibit coagulation. pentasaccharide 100-115 serpin family C member 1 Homo sapiens 51-63 24735089-6 2014 It was shown that surfaces modified with ATH bound antithrombin selectively from plasma through the pentasaccharide sequence on the heparin moiety of ATH, indicating the ability of the ATH-modified surfaces to inhibit coagulation. Heparin 132-139 serpin family C member 1 Homo sapiens 51-63 24735089-6 2014 It was shown that surfaces modified with ATH bound antithrombin selectively from plasma through the pentasaccharide sequence on the heparin moiety of ATH, indicating the ability of the ATH-modified surfaces to inhibit coagulation. 4-Hydroxy-trans-aconitic acid 41-44 serpin family C member 1 Homo sapiens 51-63 24266905-8 2014 The heparin-induced TFPI elevation reduced both thrombin-antithrombin complex and F1+2 to control levels in rTF + TFPI boost group (p = 0.0158 for thrombin-antithrombin complex, p < 0.0001 for F1+2 ). Heparin 4-11 serpin family C member 1 Homo sapiens 156-168 24678194-0 2014 Elucidating the specificity of non-heparin-based conformational activators of antithrombin for factor Xa inhibition. Heparin 35-42 serpin family C member 1 Homo sapiens 78-90 24678194-1 2014 INTRODUCTION: Antithrombin, the principal inhibitor of coagulation proteases, requires allosteric activation by its physiological cofactor, heparin or heparin sulfate to achieve physiologically permissible rates. Heparin 140-147 serpin family C member 1 Homo sapiens 14-26 24678194-1 2014 INTRODUCTION: Antithrombin, the principal inhibitor of coagulation proteases, requires allosteric activation by its physiological cofactor, heparin or heparin sulfate to achieve physiologically permissible rates. Heparitin Sulfate 151-166 serpin family C member 1 Homo sapiens 14-26 23990470-1 2013 The nonspecific binding of heparin to plasma proteins compromises its anticoagulant activity by reducing the amount of heparin available to bind antithrombin. Heparin 27-34 serpin family C member 1 Homo sapiens 145-157 24048327-3 2013 We have developed a covalent conjugate of antithrombin (AT) and heparin (ATH) with superior anticoagulant properties compared with UFH. Heparin 131-134 serpin family C member 1 Homo sapiens 42-54 24068708-0 2013 The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin. Heparin 100-107 serpin family C member 1 Homo sapiens 42-54 24068708-0 2013 The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin. Heparin 100-107 serpin family C member 1 Homo sapiens 212-224 24068708-0 2013 The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin. IC 831423 255-278 serpin family C member 1 Homo sapiens 42-54 24068708-0 2013 The allosteric mechanism of activation of antithrombin as an inhibitor of factor IXa and factor Xa: heparin-independent full activation through mutations adjacent to helix D. Allosteric conformational changes in antithrombin induced by binding a specific heparin pentasaccharide result in very large increases in the rates of inhibition of factors IXa and Xa but not of thrombin. IC 831423 255-278 serpin family C member 1 Homo sapiens 212-224 24068708-7 2013 These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role. Tyrosine 189-192 serpin family C member 1 Homo sapiens 34-46 24068708-7 2013 These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role. Tyrosine 189-192 serpin family C member 1 Homo sapiens 121-133 24068708-7 2013 These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role. Alanine 201-204 serpin family C member 1 Homo sapiens 34-46 24068708-7 2013 These findings suggest that in WT antithrombin there are two major complementary sources of conformational activation of antithrombin, probably involving altered contacts of side chains of Tyr-131 and Ala-134 with core hydrophobic residues, whereas the reactive center loop hinge expulsion plays only a minor additional role. Alanine 201-204 serpin family C member 1 Homo sapiens 121-133 24124146-0 2013 The superiority of anti-FXa assay over anti-FIIa assay in detecting heparin-binding site antithrombin deficiency. Heparin 68-75 serpin family C member 1 Homo sapiens 89-101 24124146-9 2013 CONCLUSIONS: Anti-FXa antithrombin assay is recommended as a first-line test to detect type II heparin-binding site antithrombin deficiency. Heparin 95-102 serpin family C member 1 Homo sapiens 22-34 24124146-9 2013 CONCLUSIONS: Anti-FXa antithrombin assay is recommended as a first-line test to detect type II heparin-binding site antithrombin deficiency. Heparin 95-102 serpin family C member 1 Homo sapiens 116-128 23855665-10 2014 c) An isozyme specific antithrombin study showed the structural basis of improved heparin binding to beta antithrombin as compared to alpha-antithrombin. Heparin 82-89 serpin family C member 1 Homo sapiens 23-35 23855665-10 2014 c) An isozyme specific antithrombin study showed the structural basis of improved heparin binding to beta antithrombin as compared to alpha-antithrombin. Heparin 82-89 serpin family C member 1 Homo sapiens 106-118 23855665-10 2014 c) An isozyme specific antithrombin study showed the structural basis of improved heparin binding to beta antithrombin as compared to alpha-antithrombin. Heparin 82-89 serpin family C member 1 Homo sapiens 106-118 23820940-8 2013 ETP ratios were higher in patients than in controls and were directly correlated with platelet counts and inversely with the plasma levels of free protein S, protein C and antithrombin. etp 0-3 serpin family C member 1 Homo sapiens 172-184 24121110-1 2013 Antithrombin III (ATIII) performs a critical anticoagulant function by precluding the activation of blood clotting proteinases, aided by its two cofactors, heparin and heparan sulfate. Heparin 156-163 serpin family C member 1 Homo sapiens 18-23 24121110-1 2013 Antithrombin III (ATIII) performs a critical anticoagulant function by precluding the activation of blood clotting proteinases, aided by its two cofactors, heparin and heparan sulfate. Heparitin Sulfate 168-183 serpin family C member 1 Homo sapiens 18-23 24121110-6 2013 We found that heparin binding basic residues, hD helix, three pairs of Cys-Cys salt bridges, N-glycosylation sites, serpin motifs and inhibitory reactive center loop (RCL) of ATIII protein are highly conserved. Heparin 14-21 serpin family C member 1 Homo sapiens 175-180 24121110-6 2013 We found that heparin binding basic residues, hD helix, three pairs of Cys-Cys salt bridges, N-glycosylation sites, serpin motifs and inhibitory reactive center loop (RCL) of ATIII protein are highly conserved. Nitrogen 93-94 serpin family C member 1 Homo sapiens 175-180 24095600-2 2013 The anticoagulation process is mainly caused by the interaction of heparin with antithrombin followed by inhibition of anticoagulant factor IIa and factor Xa. Heparin 67-74 serpin family C member 1 Homo sapiens 80-92 23990470-1 2013 The nonspecific binding of heparin to plasma proteins compromises its anticoagulant activity by reducing the amount of heparin available to bind antithrombin. Heparin 119-126 serpin family C member 1 Homo sapiens 145-157 23990470-2 2013 In addition, interaction of heparin with fibrin promotes formation of a ternary heparin-thrombin-fibrin complex that protects fibrin-bound thrombin from inhibition by the heparin-antithrombin complex. Heparin 28-35 serpin family C member 1 Homo sapiens 179-191 23990470-9 2013 As a consequence, heparin-catalyzed inhibition of factor Xa by antithrombin is compromised by fibrinogen to a greater extent when Zn(2+) is present. Heparin 18-25 serpin family C member 1 Homo sapiens 63-75 23990470-9 2013 As a consequence, heparin-catalyzed inhibition of factor Xa by antithrombin is compromised by fibrinogen to a greater extent when Zn(2+) is present. Zinc 130-132 serpin family C member 1 Homo sapiens 63-75 23911501-8 2013 This contributes to the better preservation of the ATIII pentasaccharide binding sequence, which results in a high Anti-Xa/Anti-IIa ratio (1.86). pentasaccharide 57-72 serpin family C member 1 Homo sapiens 51-56 24142738-0 2013 Pharmacokinetic and pharmacodynamic properties of batifiban coadministered with antithrombin agents in Chinese healthy volunteers. batifiban 50-59 serpin family C member 1 Homo sapiens 80-92 24142738-2 2013 To observe whether antithrombin agents affect the pharmacokinetic and pharmacodynamic properties of batifiban in combination therapy and optimize clinical administration dosage of batifiban, an open-label and parallel study was conducted. batifiban 100-109 serpin family C member 1 Homo sapiens 19-31 24142738-3 2013 Thirty healthy subjects were randomly divided into three groups, which were sequentially treated with batifiban alone, or oral coadministration of clopidogrel, aspirin and UFH, or batifiban coadministered with these antithrombin agents. batifiban 180-189 serpin family C member 1 Homo sapiens 216-228 24074654-7 2013 CONCLUSIONS: Introduction of routine ATIII administration was associated with decreases in FFP, platelet, and PRBC exposure in neonates with CDH and decreases in PRBC transfusions in neonates without CDH during the first three days of ECMO support. prbc 110-114 serpin family C member 1 Homo sapiens 37-42 23843463-0 2013 Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties. heparin dodecasaccharide 0-24 serpin family C member 1 Homo sapiens 40-52 23843463-0 2013 Heparin dodecasaccharide containing two antithrombin-binding pentasaccharides: structural features and biological properties. pentasaccharides 61-77 serpin family C member 1 Homo sapiens 40-52 23843463-1 2013 The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)). Heparin 44-51 serpin family C member 1 Homo sapiens 4-16 23843463-1 2013 The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)). Heparin 77-85 serpin family C member 1 Homo sapiens 4-16 23843463-1 2013 The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)). pentasaccharide 133-148 serpin family C member 1 Homo sapiens 4-16 23843463-1 2013 The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)). nac 168-171 serpin family C member 1 Homo sapiens 4-16 23843463-1 2013 The antithrombin (AT) binding properties of heparin and low molecular weight heparins are strongly associated to the presence of the pentasaccharide sequence AGA*IA (A(NAc,6S)-GlcUA-A(NS,3,6S)-I(2S)-A(NS,6S)). glcua 176-181 serpin family C member 1 Homo sapiens 4-16 23752481-0 2013 Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots. mn-doped 97-105 serpin family C member 1 Homo sapiens 50-62 23903049-14 2013 In conclusion, in antithrombin deficiency the use of low-molecular-weight heparin in pregnancy and puerperium with antithrombin concentrate pre-delivery was associated with successful pregnancy outcome; rates of VTE appear to be lower than previously reported, but remain elevated. Heparin 74-81 serpin family C member 1 Homo sapiens 18-30 23903049-14 2013 In conclusion, in antithrombin deficiency the use of low-molecular-weight heparin in pregnancy and puerperium with antithrombin concentrate pre-delivery was associated with successful pregnancy outcome; rates of VTE appear to be lower than previously reported, but remain elevated. Heparin 74-81 serpin family C member 1 Homo sapiens 115-127 23752481-0 2013 Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots. Heparin 0-7 serpin family C member 1 Homo sapiens 50-62 23752481-0 2013 Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots. Zinc 106-109 serpin family C member 1 Homo sapiens 50-62 23752481-0 2013 Heparin-mediated fluorescence anisotropy assay of antithrombin based on polyethyleneimine capped Mn-doped ZnS quantum dots. aziridine 72-89 serpin family C member 1 Homo sapiens 50-62 23752481-1 2013 We presented a homogeneous heparin-mediated fluorescence anisotropy (FA) assay of antithrombin (AT) based on long-lived luminescent polyethyleneimine capped Mn-doped ZnS (PEI-Mn-ZnS) QDs. Heparin 27-34 serpin family C member 1 Homo sapiens 82-94 23752481-1 2013 We presented a homogeneous heparin-mediated fluorescence anisotropy (FA) assay of antithrombin (AT) based on long-lived luminescent polyethyleneimine capped Mn-doped ZnS (PEI-Mn-ZnS) QDs. aziridine 132-149 serpin family C member 1 Homo sapiens 82-94 23752481-1 2013 We presented a homogeneous heparin-mediated fluorescence anisotropy (FA) assay of antithrombin (AT) based on long-lived luminescent polyethyleneimine capped Mn-doped ZnS (PEI-Mn-ZnS) QDs. mn-doped 157-165 serpin family C member 1 Homo sapiens 82-94 23752481-1 2013 We presented a homogeneous heparin-mediated fluorescence anisotropy (FA) assay of antithrombin (AT) based on long-lived luminescent polyethyleneimine capped Mn-doped ZnS (PEI-Mn-ZnS) QDs. Zinc 166-169 serpin family C member 1 Homo sapiens 82-94 23752481-1 2013 We presented a homogeneous heparin-mediated fluorescence anisotropy (FA) assay of antithrombin (AT) based on long-lived luminescent polyethyleneimine capped Mn-doped ZnS (PEI-Mn-ZnS) QDs. pei-mn-zns 171-181 serpin family C member 1 Homo sapiens 82-94 24164039-2 2013 The methodology of an anti-factor Xa assay is that LMWH is added to a known amount of excess factor Xa and excess antithrombin. Heparin, Low-Molecular-Weight 51-55 serpin family C member 1 Homo sapiens 114-126 23917140-2 2013 As perioperative anticoagulation, AT III was administered to have its activity>=70% in addition to heparin. Heparin 102-109 serpin family C member 1 Homo sapiens 34-40 23974171-6 2013 A cell cultivation system using heparin-functionalized thermoresponsive cell culture surface is versatile for immobilizing other heparin-binding proteins such as vascular endothelial growth factor, fibronectin, antithrombin III, and hepatocyte growth factor, etc. Heparin 32-39 serpin family C member 1 Homo sapiens 211-227 23840401-8 2013 HOCl-altered isolated proteins antithrombin III and human serum albumin, taken as representative examples of the whole pool of plasma proteins, were both able to exert the same activity of binding to gp120 and inhibition of viral proliferation. Hypochlorous Acid 0-4 serpin family C member 1 Homo sapiens 31-47 23494009-0 2013 Covalently linking heparin to antithrombin enhances prothrombinase inhibition on activated platelets. Heparin 19-26 serpin family C member 1 Homo sapiens 30-42 23408671-3 2013 Although antithrombin deficiency has generally been thought to be the primary mechanism of heparin resistance, the reasons for heparin resistance are both complex and multifactorial. Heparin 91-98 serpin family C member 1 Homo sapiens 9-21 23408671-7 2013 Treatments for heparin resistance/alterations in heparin responsiveness include additional heparin or antithrombin supplementation. Heparin 15-22 serpin family C member 1 Homo sapiens 102-114 23408671-7 2013 Treatments for heparin resistance/alterations in heparin responsiveness include additional heparin or antithrombin supplementation. Heparin 49-56 serpin family C member 1 Homo sapiens 102-114 23408671-7 2013 Treatments for heparin resistance/alterations in heparin responsiveness include additional heparin or antithrombin supplementation. Heparin 49-56 serpin family C member 1 Homo sapiens 102-114 23408673-0 2013 The influence of antithrombin substitution on heparin sensitivity and activation of hemostasis during coronary artery bypass graft surgery: a dose-finding study. Heparin 46-53 serpin family C member 1 Homo sapiens 17-29 23408673-2 2013 Supplementation of antithrombin (AT) may attenuate this activation and increase a patient"s susceptibility to heparin. Heparin 110-117 serpin family C member 1 Homo sapiens 19-31 23408673-2 2013 Supplementation of antithrombin (AT) may attenuate this activation and increase a patient"s susceptibility to heparin. Heparin 110-117 serpin family C member 1 Homo sapiens 33-35 23408673-14 2013 DISCUSSION: High dosages of AT were required to preserve physiologic AT activity during coronary artery bypass graft surgery and to significantly enhance heparin sensitivity, respectively. Heparin 154-161 serpin family C member 1 Homo sapiens 28-30 23581397-1 2013 BACKGROUND: Heparin and its analogs, mediating their anticoagulant activity through antithrombin (AT) activation, remain largely used for the preventive and curative treatment of thrombosis. Heparin 12-19 serpin family C member 1 Homo sapiens 84-96 23581397-1 2013 BACKGROUND: Heparin and its analogs, mediating their anticoagulant activity through antithrombin (AT) activation, remain largely used for the preventive and curative treatment of thrombosis. Heparin 12-19 serpin family C member 1 Homo sapiens 98-100 23581397-4 2013 To secure administration of AT-mediated anticoagulants and counteract bleeding disorders, we previously designed a recombinant inactive AT as an antidote to heparin derivatives. Heparin 157-164 serpin family C member 1 Homo sapiens 28-30 23581397-4 2013 To secure administration of AT-mediated anticoagulants and counteract bleeding disorders, we previously designed a recombinant inactive AT as an antidote to heparin derivatives. Heparin 157-164 serpin family C member 1 Homo sapiens 136-138 23581397-5 2013 OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs. Heparin 190-197 serpin family C member 1 Homo sapiens 70-72 23581397-5 2013 OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs. Heparin 190-197 serpin family C member 1 Homo sapiens 165-167 23581397-5 2013 OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs. Heparin 228-235 serpin family C member 1 Homo sapiens 70-72 23581397-5 2013 OBJECTIVES: To get around the limited production level of recombinant AT, we propose in this study an alternative strategy to produce a chemically modified inactive AT, exhibiting increased heparin affinity, as an antagonist of heparin analogs. Heparin 228-235 serpin family C member 1 Homo sapiens 165-167 23581397-6 2013 METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain. Diacetyl 56-71 serpin family C member 1 Homo sapiens 24-26 23581397-6 2013 METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain. 1,4-diselenophene-1,4-diketone 75-83 serpin family C member 1 Homo sapiens 24-26 23581397-6 2013 METHODS: Plasma-derived AT was chemically modified with 2,3 butanedione, a diketone known to specifically react with the arginine side chain. Arginine 121-129 serpin family C member 1 Homo sapiens 24-26 23581397-8 2013 RESULTS: AT treated by butanedione and selected for its high heparin affinity (AT-BD) was indeed modified on reactive Arg393 and thus exhibited decreased anticoagulant activity and increased heparin affinity. Diacetyl 23-34 serpin family C member 1 Homo sapiens 9-11 23581397-8 2013 RESULTS: AT treated by butanedione and selected for its high heparin affinity (AT-BD) was indeed modified on reactive Arg393 and thus exhibited decreased anticoagulant activity and increased heparin affinity. Diacetyl 23-34 serpin family C member 1 Homo sapiens 79-81 23581397-8 2013 RESULTS: AT treated by butanedione and selected for its high heparin affinity (AT-BD) was indeed modified on reactive Arg393 and thus exhibited decreased anticoagulant activity and increased heparin affinity. Heparin 61-68 serpin family C member 1 Homo sapiens 9-11 23581397-8 2013 RESULTS: AT treated by butanedione and selected for its high heparin affinity (AT-BD) was indeed modified on reactive Arg393 and thus exhibited decreased anticoagulant activity and increased heparin affinity. Heparin 61-68 serpin family C member 1 Homo sapiens 79-81 23581397-9 2013 AT-BD was able to neutralize anticoagulant activity of heparin derivatives in vitro and in vivo and was devoid of intrinsic anticoagulant activity, as assessed by activated partial thromboplastin time assay. Heparin 55-62 serpin family C member 1 Homo sapiens 0-2 23581397-10 2013 CONCLUSIONS: AT-BD appears to be as efficient as protamine to neutralize UFH in vivo but could be more largely used because it also reverses fondaparinux and LMWH. UFH 73-76 serpin family C member 1 Homo sapiens 13-15 23219177-12 2013 In conclusion, prasugrel, when given after bivalirudin as the intraprocedural antithrombin agent for patients with acute coronary syndrome undergoing PCI, is as safe and effective as clopidogrel. Prasugrel Hydrochloride 15-24 serpin family C member 1 Homo sapiens 78-90 23102903-1 2013 OBJECTIVES: Purified antithrombin supplementation in cardiac surgery has been suggested for the treatment of heparin resistance and the prevention of thromboembolic complications. Heparin 109-116 serpin family C member 1 Homo sapiens 21-33 23102903-7 2013 Heparin resistance rate was significantly (P = .001) higher in the control group (38.2%) versus the antithrombin group (17%). Heparin 0-7 serpin family C member 1 Homo sapiens 100-112 23102903-10 2013 CONCLUSIONS: Preoperative antithrombin supplementation prevents heparin resistance and avoids excessive postoperative decrease of antithrombin activity. Heparin 64-71 serpin family C member 1 Homo sapiens 26-38 23705025-5 2013 This validation study suggested LARGE, a gene encoding a protein with xylosyltransferase and glucuronyltransferase activities that forms heparin-like linear polysaccharides, as a potential modulator of antithrombin based on the significant association of one SNPs, rs762057, with anti-FXa activity, particularly after adjustment for age, sex and SERPINC1 rs2227589 genotype, all factors influencing antithrombin levels (p = 0.02). Polysaccharides 157-172 serpin family C member 1 Homo sapiens 202-214 23705025-5 2013 This validation study suggested LARGE, a gene encoding a protein with xylosyltransferase and glucuronyltransferase activities that forms heparin-like linear polysaccharides, as a potential modulator of antithrombin based on the significant association of one SNPs, rs762057, with anti-FXa activity, particularly after adjustment for age, sex and SERPINC1 rs2227589 genotype, all factors influencing antithrombin levels (p = 0.02). Polysaccharides 157-172 serpin family C member 1 Homo sapiens 346-354 23705025-5 2013 This validation study suggested LARGE, a gene encoding a protein with xylosyltransferase and glucuronyltransferase activities that forms heparin-like linear polysaccharides, as a potential modulator of antithrombin based on the significant association of one SNPs, rs762057, with anti-FXa activity, particularly after adjustment for age, sex and SERPINC1 rs2227589 genotype, all factors influencing antithrombin levels (p = 0.02). Polysaccharides 157-172 serpin family C member 1 Homo sapiens 399-411 22978318-0 2013 Half-life prolongation of therapeutic proteins by conjugation to ATIII-binding pentasaccharides: a first-in-human study of CarboCarrier insulin. pentasaccharides 79-95 serpin family C member 1 Homo sapiens 65-70 22978318-1 2013 AIM: Conjugation to antithrombin III ATIII-binding pentasaccharides has been proposed as a novel method to extend the half-life of therapeutic proteins. pentasaccharides 51-67 serpin family C member 1 Homo sapiens 37-42 22978318-12 2013 The elimination half-life of the molecule was clearly extended compared with endogenous insulin, indicating that conjugation to ATIII-binding pentasaccharides is a viable approach to extend the half-life of therapeutic proteins in humans. pentasaccharides 142-158 serpin family C member 1 Homo sapiens 128-133 23016581-6 2013 The native form of antithrombin binds with high affinity to vascular heparan sulfate proteoglycans containing a specific pentasaccharide sequence and it is this cofactor interaction that activates antithrombin to maximal rate of thrombin inhibition. pentasaccharide 121-136 serpin family C member 1 Homo sapiens 19-31 23016581-6 2013 The native form of antithrombin binds with high affinity to vascular heparan sulfate proteoglycans containing a specific pentasaccharide sequence and it is this cofactor interaction that activates antithrombin to maximal rate of thrombin inhibition. pentasaccharide 121-136 serpin family C member 1 Homo sapiens 197-209 23016581-7 2013 Upon inhibitory complex formation with target proteinases the antithrombin undergoes stressed to relaxed transformation and lose their high affinity for pentasacchride. pentasacchride 153-167 serpin family C member 1 Homo sapiens 62-74 23016581-8 2013 Low affinity relaxed conformation with reduced heparin binding like cleaved and latent are antiangiogenic but native high affinity heparin binding stressed conformation is not, indicating the critical importance of heparin affinity in antithrombin antiangiogenic function. Heparin 47-54 serpin family C member 1 Homo sapiens 235-247 23016581-9 2013 Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation. Heparin 167-174 serpin family C member 1 Homo sapiens 234-246 23016581-9 2013 Based on evidence of interactions of the endothelial cell growth factors bFGF (basic fibroblast growth factor) and VEGF (vascular endothelial cell growth factor) with heparin like molecule in matrix, the possibility of antiangiogenic antithrombin to interfere with endothelial cell growth and angiogenesis through heparin mediated mechanism deserves serious consideration and investigation. Heparin 314-321 serpin family C member 1 Homo sapiens 234-246 23016581-10 2013 It is also possible that cleaved and latent conformations with reduced affinity for heparins can also induce conformational change in the antithrombin which can open an epitope on the antithrombin surface for appropriate interactions on the endothelial surface for better antiangiogenic activity. Heparin 84-92 serpin family C member 1 Homo sapiens 138-150 23016581-10 2013 It is also possible that cleaved and latent conformations with reduced affinity for heparins can also induce conformational change in the antithrombin which can open an epitope on the antithrombin surface for appropriate interactions on the endothelial surface for better antiangiogenic activity. Heparin 84-92 serpin family C member 1 Homo sapiens 184-196 23388336-4 2013 The cells were induced by IPTG to express AT-III. Isopropyl Thiogalactoside 26-30 serpin family C member 1 Homo sapiens 42-48 23329795-0 2013 Emerging applications of argatroban in the management of systemic malignancies: potential benefits besides its primary role as an antithrombin agent. argatroban 25-35 serpin family C member 1 Homo sapiens 130-142 23083208-0 2013 An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence. heparin octasaccharide 32-54 serpin family C member 1 Homo sapiens 11-23 23083208-0 2013 An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence. glucosamine 3-O-sulfate 74-98 serpin family C member 1 Homo sapiens 11-23 23083208-0 2013 An unusual antithrombin-binding heparin octasaccharide with an additional 3-O-sulfated glucosamine in the active pentasaccharide sequence. pentasaccharide 113-128 serpin family C member 1 Homo sapiens 11-23 23083208-1 2013 The 3-O-sulfation of N-sulfated glucosamine is the last event in the biosynthesis of heparin/heparan sulfate, giving rise to the antithrombin-binding pentasaccharide sequence AGA*IA, which is largely associated with the antithrombotic activity of these molecules. n-sulfated glucosamine 21-43 serpin family C member 1 Homo sapiens 129-141 23083208-1 2013 The 3-O-sulfation of N-sulfated glucosamine is the last event in the biosynthesis of heparin/heparan sulfate, giving rise to the antithrombin-binding pentasaccharide sequence AGA*IA, which is largely associated with the antithrombotic activity of these molecules. Heparin 85-92 serpin family C member 1 Homo sapiens 129-141 23083208-1 2013 The 3-O-sulfation of N-sulfated glucosamine is the last event in the biosynthesis of heparin/heparan sulfate, giving rise to the antithrombin-binding pentasaccharide sequence AGA*IA, which is largely associated with the antithrombotic activity of these molecules. Heparitin Sulfate 93-108 serpin family C member 1 Homo sapiens 129-141 23083208-1 2013 The 3-O-sulfation of N-sulfated glucosamine is the last event in the biosynthesis of heparin/heparan sulfate, giving rise to the antithrombin-binding pentasaccharide sequence AGA*IA, which is largely associated with the antithrombotic activity of these molecules. pentasaccharide 150-165 serpin family C member 1 Homo sapiens 129-141 23083208-4 2013 The molecular conformation of the octasaccharide-antithrombin complex has been determined by NMR experiments and docking/energy minimization. Octasaccharide 34-48 serpin family C member 1 Homo sapiens 49-61 23083208-5 2013 The presence of the second 3-O-sulfated glucosamine in the octasaccharide induced more than one order of magnitude increase in affinity to antithrombin compared to the pentasaccharide AGA*IA. glucosamine 3-O-sulfate 27-51 serpin family C member 1 Homo sapiens 139-151 23083208-5 2013 The presence of the second 3-O-sulfated glucosamine in the octasaccharide induced more than one order of magnitude increase in affinity to antithrombin compared to the pentasaccharide AGA*IA. Octasaccharide 59-73 serpin family C member 1 Homo sapiens 139-151 23010574-0 2012 Potentiation of anti-angiogenic activity of heparin by blocking the ATIII-interacting pentasaccharide unit and increasing net anionic charge. Heparin 44-51 serpin family C member 1 Homo sapiens 68-73 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 41-43 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 274-277 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 41-43 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Arginine 303-306 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Serine 350-353 serpin family C member 1 Homo sapiens 41-43 23010574-7 2012 Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding. Taurocholic Acid 73-92 serpin family C member 1 Homo sapiens 178-183 23010574-7 2012 Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding. Prednisolone 151-158 serpin family C member 1 Homo sapiens 178-183 23010574-7 2012 Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding. pentasaccharide 192-207 serpin family C member 1 Homo sapiens 178-183 23010574-7 2012 Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding. Heparin, Low-Molecular-Weight 216-220 serpin family C member 1 Homo sapiens 178-183 23010574-7 2012 Following up on this finding, we showed that the bidirectional effect of sodium taurocholate conjugation was due to its unique structure, that is, the sterane core hindering the ATIII-binding pentasaccharide unit of LMWH with its bulky and rigid structural characteristics while the terminal sulfate group interacts with VEGF to produce stronger binding. Sulfates 292-299 serpin family C member 1 Homo sapiens 178-183 23263338-9 2013 AT was inversely correlated with ACT (r = -0.33), even after adjusting for heparin dose, and positively correlated with antifactor Xa (r = 0.57). Heparin 75-82 serpin family C member 1 Homo sapiens 0-2 23263338-11 2013 ACT is poorly correlated with antifactor Xa and AT modifies the relationship between ACT and the heparin dose, indicating that results should be interpreted with caution when managing anticoagulation on ECMO. Heparin 97-104 serpin family C member 1 Homo sapiens 48-50 23100269-0 2013 Inhibition of the prothrombinase complex on red blood cells by heparin and covalent antithrombin-heparin complex. Heparin 97-104 serpin family C member 1 Homo sapiens 84-96 23100269-4 2013 Therefore, this study examines the ability of heparin and a covalent antithrombin-heparin complex (ATH) to inhibit the RBC-prothrombinase system. Heparin 82-89 serpin family C member 1 Homo sapiens 69-81 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Serine 350-353 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Serine 350-353 serpin family C member 1 Homo sapiens 120-122 23578459-6 2013 RESULTS: Compared to the wild-types, the AT expression of HEK293T cells sharply increased when they were transfected by AT-c.342T > G or AT-c.134G > A and c.342T > G. Homology modeling showed that the mutation (AT-c.342T > G) caused a decreased distance between Arg and surrounding bases as Arg"s side chain was significantly longer than Ser"s. Serine 350-353 serpin family C member 1 Homo sapiens 120-122 23578459-7 2013 The mutation of 13th base pair decreases the distance between AT and heparin. Heparin 69-76 serpin family C member 1 Homo sapiens 62-64 23010574-0 2012 Potentiation of anti-angiogenic activity of heparin by blocking the ATIII-interacting pentasaccharide unit and increasing net anionic charge. pentasaccharide 86-101 serpin family C member 1 Homo sapiens 68-73 23010574-5 2012 This study showed that the conjugation of sodium taurocholates selectively blocked interaction with antithrombin III (ATIII) while enhancing the binding with VEGF. Sodium 42-48 serpin family C member 1 Homo sapiens 100-116 23010574-5 2012 This study showed that the conjugation of sodium taurocholates selectively blocked interaction with antithrombin III (ATIII) while enhancing the binding with VEGF. Sodium 42-48 serpin family C member 1 Homo sapiens 118-123 22923734-0 2012 Stable complex formation between serine protease inhibitor and zymogen: coagulation factor X cleaves the Arg393-Ser394 bond in a reactive centre loop of antithrombin in the presence of heparin. Heparin 185-192 serpin family C member 1 Homo sapiens 153-165 22672269-5 2012 HARP was shown to compete with both antithrombin and thrombin for binding to heparin and to OTR4120, respectively. Heparin 77-84 serpin family C member 1 Homo sapiens 36-48 22978548-0 2012 By increasing the affinity of heparin for fibrin, Zn(2+) promotes the formation of a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin. Heparin 30-37 serpin family C member 1 Homo sapiens 167-179 22978548-0 2012 By increasing the affinity of heparin for fibrin, Zn(2+) promotes the formation of a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin. Zinc 50-56 serpin family C member 1 Homo sapiens 167-179 22978548-8 2012 Therefore, by enhancing the binding of heparin to fibrin, physiological concentrations of Zn(2+) render fibrin-bound thrombin more protected from inhibition by antithrombin. Heparin 39-46 serpin family C member 1 Homo sapiens 160-172 22978548-8 2012 Therefore, by enhancing the binding of heparin to fibrin, physiological concentrations of Zn(2+) render fibrin-bound thrombin more protected from inhibition by antithrombin. Zinc 90-96 serpin family C member 1 Homo sapiens 160-172 22534410-2 2012 Therefore, the authors determined the relationship between AT and other coagulation-related factors that affect the ACT measurement and heparin sensitivity index before the establishment of cardiopulmonary bypass. Heparin 136-143 serpin family C member 1 Homo sapiens 59-61 22542983-9 2012 DISCUSSION: Tranexamic acid associated to direct anti-Xa (antithrombin-independent) oral anticoagulants was effective in reducing postoperative blood loss, improving hemoglobinemia at 5 days and reducing transfusion rates. Tranexamic Acid 12-27 serpin family C member 1 Homo sapiens 58-70 22641607-0 2012 Polyurethane modified with an antithrombin-heparin complex via polyethylene oxide linker/spacers: influence of PEO molecular weight and PEO-ATH bond on catalytic and direct anticoagulant functions. Polyurethanes 0-12 serpin family C member 1 Homo sapiens 30-42 22641607-0 2012 Polyurethane modified with an antithrombin-heparin complex via polyethylene oxide linker/spacers: influence of PEO molecular weight and PEO-ATH bond on catalytic and direct anticoagulant functions. Heparin 43-50 serpin family C member 1 Homo sapiens 30-42 22641607-0 2012 Polyurethane modified with an antithrombin-heparin complex via polyethylene oxide linker/spacers: influence of PEO molecular weight and PEO-ATH bond on catalytic and direct anticoagulant functions. Polyethylene Glycols 63-81 serpin family C member 1 Homo sapiens 30-42 22641607-9 2012 On PEO-ATH surfaces fibrinogen adsorption was minimal while AT adsorption was high showing the selectivity of the heparin moiety of ATH for AT. Heparin 114-121 serpin family C member 1 Homo sapiens 7-9 22641607-9 2012 On PEO-ATH surfaces fibrinogen adsorption was minimal while AT adsorption was high showing the selectivity of the heparin moiety of ATH for AT. Heparin 114-121 serpin family C member 1 Homo sapiens 60-62 22905983-8 2012 UFH (62-fold) and fondaparinux (42-fold) demonstrated markedly increased EC(50) values in antithrombin-depleted plasma, whereas LMWH (9.4-fold) and ssLMWH (two-fold) were less affected, with an EC(50) within the therapeutic range for LMWH. Heparin 0-3 serpin family C member 1 Homo sapiens 90-102 22905983-9 2012 The molecular target for LMWH/ssLMWH was confirmed by supplementing FIX/antithrombin-depleted plasma with 90 nm recombinant FIX possessing mutations in the heparin-binding exosite. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 72-84 22905983-9 2012 The molecular target for LMWH/ssLMWH was confirmed by supplementing FIX/antithrombin-depleted plasma with 90 nm recombinant FIX possessing mutations in the heparin-binding exosite. sslmwh 30-36 serpin family C member 1 Homo sapiens 72-84 22905983-11 2012 CONCLUSIONS: Therapeutic LMWH concentrations inhibit plasma thrombin generation via antithrombin-independent interaction with the FIXa heparin-binding exosite. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 84-96 22204993-7 2012 Antithrombin increased to the normal level on day 1 in the antithrombin group but on day 7 in the gabexate mesilate group. Gabexate 98-115 serpin family C member 1 Homo sapiens 0-12 22641771-7 2012 Functional studies observed that HSCF inhibited antithrombin binding to heparin and neutralized the antifactor IIa and Xa activities of heparin and the antifactor IIa activity of low-molecular-weight heparin (LMWH). Heparin 72-79 serpin family C member 1 Homo sapiens 48-60 22758787-11 2012 Surprisingly, the insertion resulted in a type II antithrombin deficiency with heparin binding defect. Heparin 79-86 serpin family C member 1 Homo sapiens 50-62 22758787-12 2012 The mutant antithrombin, with a molecular weight of 59 kDa, had a proteolytic cleavage at W49 but maintained the N-terminal disulphide bonds, and was conformationally sensitive. disulphide 124-134 serpin family C member 1 Homo sapiens 11-23 22453684-0 2012 Limitations of conventional anticoagulant therapy and the promises of non-heparin based conformational activators of antithrombin. Heparin 74-81 serpin family C member 1 Homo sapiens 117-129 22535529-4 2012 Sequencing analysis of SERPINC1 gene of three families revealed that Family I had double novel missense mutations (c.134G > A&c.342T > G), Family II had a nonsense mutation (c.770G > A) while Family III had a frameshift mutation (c.800-803del). Adenosine Monophosphate 129-132 serpin family C member 1 Homo sapiens 23-31 22453684-4 2012 The conformational activation of antithrombin by heparin is a critical step in the inhibition of factor Xa by antithrombin. Heparin 49-56 serpin family C member 1 Homo sapiens 33-45 22453684-4 2012 The conformational activation of antithrombin by heparin is a critical step in the inhibition of factor Xa by antithrombin. Heparin 49-56 serpin family C member 1 Homo sapiens 110-122 22453684-5 2012 Despite heparin being the most potent physiological activator which enhances the otherwise very lethargic antithrombin inhibition of factor Xa by approximately 1,000-fold, the conventional heparin therapy poses serious complications because of heparin"s polyanionic nature and its cross-reactivity. Heparin 8-15 serpin family C member 1 Homo sapiens 106-118 22453684-6 2012 A number of attempts have been carried out in designing alternative non-heparin based conformational activators of antithrombin for factor Xa inhibition. Heparin 72-79 serpin family C member 1 Homo sapiens 115-127 22453684-8 2012 It is assumed that these activators of antithrombin perform their function by binding to heparin binding site. Heparin 89-96 serpin family C member 1 Homo sapiens 39-51 22453684-9 2012 A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin. Heparin 45-52 serpin family C member 1 Homo sapiens 87-99 22453684-9 2012 A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin. Heparin 45-52 serpin family C member 1 Homo sapiens 178-190 22453684-9 2012 A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin. Heparin 154-161 serpin family C member 1 Homo sapiens 87-99 22453684-9 2012 A recently identified cavity which links the heparin binding site to the strand 2A for antithrombin activation also seems to be an ideal target apart the heparin binding site of antithrombin. Heparin 154-161 serpin family C member 1 Homo sapiens 178-190 22453684-11 2012 This review summarizes the current literature on the mainstay anticoagulants and non-heparin based antithrombin conformation modulators. Heparin 85-92 serpin family C member 1 Homo sapiens 99-111 22819492-0 2012 Effect of antithrombin III on glycoprotein Ib/IX/V activation in human platelets: suppression of thromboxane A2 generation. Thromboxane A2 97-111 serpin family C member 1 Homo sapiens 10-26 22819492-2 2012 In the present study, we investigated the effect of antithrombin-III (AT-III), an anticoagulant, on the ristocetin-induced glycoprotein Ib/IX/V activation in human platelets. Ristocetin 104-114 serpin family C member 1 Homo sapiens 52-68 22819492-2 2012 In the present study, we investigated the effect of antithrombin-III (AT-III), an anticoagulant, on the ristocetin-induced glycoprotein Ib/IX/V activation in human platelets. Ristocetin 104-114 serpin family C member 1 Homo sapiens 70-76 22819492-3 2012 AT-III inhibited ristocetin-stimulated platelet aggregation. Ristocetin 17-27 serpin family C member 1 Homo sapiens 0-6 22819492-4 2012 The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III. Ristocetin 4-14 serpin family C member 1 Homo sapiens 138-144 22819492-4 2012 The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III. 11-dehydro-txb 37-51 serpin family C member 1 Homo sapiens 138-144 22819492-4 2012 The ristocetin-induced production of 11-dehydro-TXB(2), a stable metabolite of TXA(2), and the release of sCD40 ligand were suppressed by AT-III. txa 79-82 serpin family C member 1 Homo sapiens 138-144 22819492-5 2012 AT-III also reduced the ristocetin-stimulated secretion of platelet-derived growth factor (PDGF)-AB. Ristocetin 24-34 serpin family C member 1 Homo sapiens 0-6 22819492-7 2012 AT-III reduced the binding of SZ2, a monoclonal antibody to the sulfated sequence in the alpha-chain of glycoprotein Ib, to the ristocetin-stimulated platelets. Ristocetin 128-138 serpin family C member 1 Homo sapiens 0-6 22819492-8 2012 These results strongly suggest that AT-III reduced ristocetin-stimulated release of sCD40 ligand due to inhibiting TXA(2) production in human platelets. Ristocetin 51-61 serpin family C member 1 Homo sapiens 36-42 22819492-8 2012 These results strongly suggest that AT-III reduced ristocetin-stimulated release of sCD40 ligand due to inhibiting TXA(2) production in human platelets. Thromboxane A2 115-121 serpin family C member 1 Homo sapiens 36-42 22742452-0 2012 In silico discovery of a compound with nanomolar affinity to antithrombin causing partial activation and increased heparin affinity. Heparin 115-122 serpin family C member 1 Homo sapiens 61-73 22742452-2 2012 Heparin is widely used as activator of antithrombin but incurs side effects. Heparin 0-7 serpin family C member 1 Homo sapiens 39-51 22498748-0 2012 Amelioration of the severity of heparin-binding antithrombin mutations by posttranslational mosaicism. Heparin 32-39 serpin family C member 1 Homo sapiens 48-60 22742452-3 2012 We screened a large database in silico to find alternative molecules and predicted d-myo-inositol 3,4,5,6-tetrakisphosphate (TMI) to strongly interact with antithrombin. D-myo-inositol 3,4,5,6-tetrakisphosphate 83-123 serpin family C member 1 Homo sapiens 156-168 22498748-4 2012 These mutations do not modify the folding or secretion of the protein, but abolish the glycosaminoglycan-induced activation of antithrombin by affecting the heparin-binding domain. Glycosaminoglycans 87-104 serpin family C member 1 Homo sapiens 127-139 22742452-3 2012 We screened a large database in silico to find alternative molecules and predicted d-myo-inositol 3,4,5,6-tetrakisphosphate (TMI) to strongly interact with antithrombin. 4-tolyl isocyanate 125-128 serpin family C member 1 Homo sapiens 156-168 22498748-4 2012 These mutations do not modify the folding or secretion of the protein, but abolish the glycosaminoglycan-induced activation of antithrombin by affecting the heparin-binding domain. Heparin 157-164 serpin family C member 1 Homo sapiens 127-139 22742452-5 2012 Functional studies, fluorescence analysis, and citrullination experiments revealed that TMI induced a partial activation of antithrombin that facilitated the interaction with heparin and low affinity heparins. 4-tolyl isocyanate 88-91 serpin family C member 1 Homo sapiens 124-136 22498748-5 2012 We speculated that the natural beta-glycoform of antithrombin might compensate for the effect of heparin-binding mutations. Heparin 97-104 serpin family C member 1 Homo sapiens 49-61 22742452-5 2012 Functional studies, fluorescence analysis, and citrullination experiments revealed that TMI induced a partial activation of antithrombin that facilitated the interaction with heparin and low affinity heparins. Heparin 175-182 serpin family C member 1 Homo sapiens 124-136 22742452-5 2012 Functional studies, fluorescence analysis, and citrullination experiments revealed that TMI induced a partial activation of antithrombin that facilitated the interaction with heparin and low affinity heparins. Heparin 200-208 serpin family C member 1 Homo sapiens 124-136 22498748-10 2012 In conclusion, we identified a new type of mosaicism associated with mutations causing heparin-binding defects in antithrombin. Heparin 87-94 serpin family C member 1 Homo sapiens 114-126 22498748-11 2012 The presence of a fully functional beta-glycoform together with the activity retained by these variants helps to explain the viability of homozygous and the milder thrombotic risk of heterozygous patients with these specific antithrombin mutations. glycoform 40-49 serpin family C member 1 Homo sapiens 225-237 22742452-6 2012 TMI improved antithrombin inhibitory function of plasma from homozygous patients with antithrombin deficiency with a heparin binding defect and also in a model with endothelial cells. 4-tolyl isocyanate 0-3 serpin family C member 1 Homo sapiens 13-25 22742452-6 2012 TMI improved antithrombin inhibitory function of plasma from homozygous patients with antithrombin deficiency with a heparin binding defect and also in a model with endothelial cells. 4-tolyl isocyanate 0-3 serpin family C member 1 Homo sapiens 86-98 22742452-6 2012 TMI improved antithrombin inhibitory function of plasma from homozygous patients with antithrombin deficiency with a heparin binding defect and also in a model with endothelial cells. Heparin 117-124 serpin family C member 1 Homo sapiens 86-98 22742452-7 2012 Our in silico screen identified a new, non-polysaccharide scaffold able to interact with the heparin binding domain of antithrombin. Polysaccharides 43-57 serpin family C member 1 Homo sapiens 119-131 22742452-7 2012 Our in silico screen identified a new, non-polysaccharide scaffold able to interact with the heparin binding domain of antithrombin. Heparin 93-100 serpin family C member 1 Homo sapiens 119-131 22454106-7 2012 The antithrombin binding capacity of the immobilized heparin was determined to be 60-80 pmol/cm(2) in an antithrombin uptake assay. Heparin 53-60 serpin family C member 1 Homo sapiens 4-16 22481271-8 2012 Under moderate stress, coexpression of WT and conformational variants in HEK-EBNA cells increased the intracellular retention of antithrombin and the formation of disulfide-linked polymers, which correlated with impaired secretion and reduction of anticoagulant activity in the medium. N-tert-Butyl-N-ethylnitrosamine 77-81 serpin family C member 1 Homo sapiens 129-141 22481271-8 2012 Under moderate stress, coexpression of WT and conformational variants in HEK-EBNA cells increased the intracellular retention of antithrombin and the formation of disulfide-linked polymers, which correlated with impaired secretion and reduction of anticoagulant activity in the medium. Disulfides 163-172 serpin family C member 1 Homo sapiens 129-141 22454106-7 2012 The antithrombin binding capacity of the immobilized heparin was determined to be 60-80 pmol/cm(2) in an antithrombin uptake assay. Heparin 53-60 serpin family C member 1 Homo sapiens 105-117 22534775-7 2012 However, the assay with the addition of exogenous antithrombin detected falsely high concentrations of rivaroxaban even in plasma samples from controls who had not taken rivaroxaban (intercept values using the high calibrator set and the low calibrator set: +26.49 ng/ml and +13.71 ng/ml, respectively). Rivaroxaban 103-114 serpin family C member 1 Homo sapiens 50-62 22864323-1 2012 Warfarin sodium is an antithrombin agent used in patients with prosthetic valve and atrial fibrillation. Warfarin 0-15 serpin family C member 1 Homo sapiens 22-34 22134617-5 2012 His antithrombin (AT) activity was decreased and DNA sequence analysis revealed heterozygosity for AT Basel (p.Pro41Leu), a variant with impaired heparin binding. Heparin 146-153 serpin family C member 1 Homo sapiens 4-16 22134617-5 2012 His antithrombin (AT) activity was decreased and DNA sequence analysis revealed heterozygosity for AT Basel (p.Pro41Leu), a variant with impaired heparin binding. Heparin 146-153 serpin family C member 1 Homo sapiens 99-101 22353523-9 2012 ATIII is correlated with 13 of 14 other clinical tests, including albumin, bilirubin, prothrombin time, rapid turnover proteins, HGF, ICGR15 and others. Bilirubin 75-84 serpin family C member 1 Homo sapiens 0-5 22382418-2 2012 Low-molecular-weight (LMW) heparin mimetics that potentiate antithrombin III (AT) action are also valuable as anti-thrombotics. Heparin 27-34 serpin family C member 1 Homo sapiens 60-76 22161774-0 2012 Heparin-coated colloidal mesoporous silica nanoparticles efficiently bind to antithrombin as an anticoagulant drug-delivery system. Heparin 0-7 serpin family C member 1 Homo sapiens 77-89 22161774-0 2012 Heparin-coated colloidal mesoporous silica nanoparticles efficiently bind to antithrombin as an anticoagulant drug-delivery system. mesoporous 25-35 serpin family C member 1 Homo sapiens 77-89 22161774-0 2012 Heparin-coated colloidal mesoporous silica nanoparticles efficiently bind to antithrombin as an anticoagulant drug-delivery system. Silicon Dioxide 36-42 serpin family C member 1 Homo sapiens 77-89 22315264-3 2012 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes. Heparin 0-3 serpin family C member 1 Homo sapiens 66-78 22315264-3 2012 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 66-78 22315264-3 2012 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin, factor Xa, and other clotting enzymes. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 66-78 22315264-9 2012 Fondaparinux, a synthetic pentasaccharide, catalyzes the inhibition of factor Xa, but not thrombin, in an antithrombin-dependent fashion. pentasaccharide 26-41 serpin family C member 1 Homo sapiens 106-118 22149666-0 2012 Modification of polyurethane surface with an antithrombin-heparin complex for blood contact: influence of molecular weight of polyethylene oxide used as a linker/spacer. Polyurethanes 16-28 serpin family C member 1 Homo sapiens 45-57 22149666-2 2012 An antithrombin-heparin (ATH) covalent complex was subsequently attached to the free PEO chain ends, which had been functionalized with N-hydroxysuccinimide (NHS) groups. Heparin 16-23 serpin family C member 1 Homo sapiens 3-15 22149666-2 2012 An antithrombin-heparin (ATH) covalent complex was subsequently attached to the free PEO chain ends, which had been functionalized with N-hydroxysuccinimide (NHS) groups. N-hydroxysuccinimide 136-156 serpin family C member 1 Homo sapiens 3-15 22149666-2 2012 An antithrombin-heparin (ATH) covalent complex was subsequently attached to the free PEO chain ends, which had been functionalized with N-hydroxysuccinimide (NHS) groups. N-hydroxysuccinimide 158-161 serpin family C member 1 Homo sapiens 3-15 21819239-7 2012 In this review, the pharmacology of warfarin and the pharmacology of the newly developed oral anti-Xa and antithrombin agents are discussed. Warfarin 36-44 serpin family C member 1 Homo sapiens 106-118 22566218-4 2012 In 1976, it was found that only one third of heparin chains bound with high affinity to antithrombin, and subsequent studies identified a unique pentasaccharide sequence, which was essential for antithrombin binding and anticoagulant activity - this pentasaccharide was synthesised in 1983. Heparin 45-52 serpin family C member 1 Homo sapiens 88-100 22149018-1 2012 OBJECTIVE: Recent findings suggest that cerebral edema is a characteristic finding on magnetic resonance imaging in women with eclampsia and that pregnancy-induced antithrombin deficiency (PIATD) may reflect enhanced vascular permeability and may allow the retention of excess water in the interstitial space. Water 277-282 serpin family C member 1 Homo sapiens 164-176 21835782-9 2012 We also designed a synthetic path to prepare a nonasaccharide with an antithrombin-binding affinity of 3 nM. Nonasaccharide Glc4Xyl3Gal2 47-61 serpin family C member 1 Homo sapiens 70-82 22566218-4 2012 In 1976, it was found that only one third of heparin chains bound with high affinity to antithrombin, and subsequent studies identified a unique pentasaccharide sequence, which was essential for antithrombin binding and anticoagulant activity - this pentasaccharide was synthesised in 1983. pentasaccharide 145-160 serpin family C member 1 Homo sapiens 195-207 22566218-4 2012 In 1976, it was found that only one third of heparin chains bound with high affinity to antithrombin, and subsequent studies identified a unique pentasaccharide sequence, which was essential for antithrombin binding and anticoagulant activity - this pentasaccharide was synthesised in 1983. pentasaccharide 250-265 serpin family C member 1 Homo sapiens 88-100 22566218-4 2012 In 1976, it was found that only one third of heparin chains bound with high affinity to antithrombin, and subsequent studies identified a unique pentasaccharide sequence, which was essential for antithrombin binding and anticoagulant activity - this pentasaccharide was synthesised in 1983. pentasaccharide 250-265 serpin family C member 1 Homo sapiens 195-207 22566220-1 2012 The molecular basis for the anticoagulant action of heparin lies in its ability to bind to and enhance the inhibitory activity of the plasma protein antithrombin against several serine proteases of the coagulation system, most importantly factors IIa (thrombin), Xa and IXa. Heparin 52-59 serpin family C member 1 Homo sapiens 149-161 22566220-2 2012 Two major mechanisms underlie heparin"s potentiation of antithrombin. Heparin 30-37 serpin family C member 1 Homo sapiens 56-68 22566220-3 2012 The conformational changes induced by heparin binding cause both expulsion of the reactive loop and exposure of exosites of the surface of antithrombin, which bind directly to the enzyme target; and a template mechanism exists in which both inhibitor and enzyme bind to the same heparin molecule. Heparin 38-45 serpin family C member 1 Homo sapiens 139-151 22566220-3 2012 The conformational changes induced by heparin binding cause both expulsion of the reactive loop and exposure of exosites of the surface of antithrombin, which bind directly to the enzyme target; and a template mechanism exists in which both inhibitor and enzyme bind to the same heparin molecule. Heparin 279-286 serpin family C member 1 Homo sapiens 139-151 22566226-2 2012 Heparin exerts its antithrombotic effects by facilitating the ability of antithrombin (AT), a plasma serum protease inhibitor, to inhibit thrombin (factor IIa) and factor Xa. Heparin 0-7 serpin family C member 1 Homo sapiens 73-85 22566226-2 2012 Heparin exerts its antithrombotic effects by facilitating the ability of antithrombin (AT), a plasma serum protease inhibitor, to inhibit thrombin (factor IIa) and factor Xa. Heparin 0-7 serpin family C member 1 Homo sapiens 87-89 22566227-3 2012 Nonbleeding complications of heparins are caused by binding of heparin molecules to proteins other than antithrombin and to cells, which is generally more pronounced with unfractionated heparin than with low-molecular-weight heparins. Heparin 29-37 serpin family C member 1 Homo sapiens 104-116 23152789-2 2012 BACKGROUND: The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively. Heparitin Sulfate 37-52 serpin family C member 1 Homo sapiens 16-28 23152789-4 2012 The availability of multiple co-crystal structures facilitates a structural analysis that challenges the long-held belief that the GAG binding sites in antithrombin and thrombin are essentially similar with high solvent exposure and shallow surface characteristics. Glycosaminoglycans 131-134 serpin family C member 1 Homo sapiens 152-164 23152789-2 2012 BACKGROUND: The antithrombin-heparin/heparan sulfate (H/HS) and thrombin-H/HS interactions are recognized as prototypic specific and non-specific glycosaminoglycan (GAG)-protein interactions, respectively. Heparin 29-36 serpin family C member 1 Homo sapiens 16-28 23152789-9 2012 Cavity analyses suggest the presence of a reasonably sized bifurcated cavity in antithrombin that facilitates a firm "hand-shake" with H/HS, but with thrombin, a weaker "high-five". Hydrogen 137-139 serpin family C member 1 Homo sapiens 80-92 23152789-10 2012 Tightly bound water molecules were predicted to be localized in the pentasaccharide binding pocket of antithrombin, but absent in thrombin. Water 14-19 serpin family C member 1 Homo sapiens 102-114 23152789-10 2012 Tightly bound water molecules were predicted to be localized in the pentasaccharide binding pocket of antithrombin, but absent in thrombin. pentasaccharide 68-83 serpin family C member 1 Homo sapiens 102-114 22012070-5 2011 In this assay, direct factor Xa (FXa) inhibitors such as edoxaban and antithrombin (AT)-dependent anticoagulants such as heparin did not increase, but simply suppressed TG. Heparin 121-128 serpin family C member 1 Homo sapiens 70-82 22900053-6 2012 However, concomitant administration of an antithrombin activator or direct factor Xa inhibitor and direct thrombin inhibitor proved to be a particularly effective combination for controlling the procoagulant effects of hALPCs both in vitro and in vivo. halpcs 219-225 serpin family C member 1 Homo sapiens 42-54 21569219-1 2011 Antithrombin inhibits VIIa when bound to cellular tissue factor in the presence of heparin. Heparin 83-90 serpin family C member 1 Homo sapiens 0-12 21569219-6 2011 There is an approximate twofold increase in measurable VIIa-antithrombin complexes in patients undergoing cardiac surgery, which is apparent after heparin administration. Heparin 147-154 serpin family C member 1 Homo sapiens 60-72 22097980-2 2011 Heparin acts by potentiating the anticoagulant effect of antithrombin (ATIII). Heparin 0-7 serpin family C member 1 Homo sapiens 57-69 21795523-6 2011 Using purified active matriptase, we further characterize the formation of matriptase-antithrombin complex and show that heparin can significantly potentiate the inhibitory potency of antithrombin against matriptase. Heparin 121-128 serpin family C member 1 Homo sapiens 86-98 21795523-6 2011 Using purified active matriptase, we further characterize the formation of matriptase-antithrombin complex and show that heparin can significantly potentiate the inhibitory potency of antithrombin against matriptase. Heparin 121-128 serpin family C member 1 Homo sapiens 184-196 21795523-7 2011 Second-order rate constants for the inhibition were determined to be 3.9 x 10(3) M(-1)s(-1) in the absence of heparin and 1.2 x 10(5) M(-1)s(-1) in the presence of heparin, a 30-fold increase, consistent with the established role of heparin in activating antithrombin function. Heparin 110-117 serpin family C member 1 Homo sapiens 255-267 21931955-8 2011 The binding affinities of these heparins to antithrombin III and thrombin were evaluated by using a surface plasmon resonance competitive binding assay. Heparin 32-40 serpin family C member 1 Homo sapiens 44-60 22097980-2 2011 Heparin acts by potentiating the anticoagulant effect of antithrombin (ATIII). Heparin 0-7 serpin family C member 1 Homo sapiens 71-76 22097980-3 2011 Acquired ATIII deficiency, common in pediatric patients requiring ECMO, may result in ineffective anticoagulation with heparin. Heparin 119-126 serpin family C member 1 Homo sapiens 9-14 21799398-0 2011 Peroperative effects of fresh frozen plasma and antithrombin III on heparin sensitivity and coagulation during nitroglycerine infusion in coronary artery bypass surgery. Heparin 68-75 serpin family C member 1 Homo sapiens 48-64 21325262-0 2011 A heparin binding site Arg79Cys missense mutation in the SERPINC1 gene in a Korean patient with hereditary antithrombin deficiency. Heparin 2-9 serpin family C member 1 Homo sapiens 57-65 21325262-1 2011 We describe a case of heparin binding site Arg79Cys mutation in the gene encoding antithrombin, SERPINC1, in a Korean patient with hereditary antithrombin (AT) deficiency. Heparin 22-29 serpin family C member 1 Homo sapiens 82-94 21325262-1 2011 We describe a case of heparin binding site Arg79Cys mutation in the gene encoding antithrombin, SERPINC1, in a Korean patient with hereditary antithrombin (AT) deficiency. Heparin 22-29 serpin family C member 1 Homo sapiens 96-104 21325262-1 2011 We describe a case of heparin binding site Arg79Cys mutation in the gene encoding antithrombin, SERPINC1, in a Korean patient with hereditary antithrombin (AT) deficiency. Heparin 22-29 serpin family C member 1 Homo sapiens 142-154 21325262-5 2011 Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys). Cytosine 115-123 serpin family C member 1 Homo sapiens 25-33 21325262-5 2011 Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys). Cytosine 115-123 serpin family C member 1 Homo sapiens 192-200 21325262-5 2011 Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys). Thymine 127-134 serpin family C member 1 Homo sapiens 25-33 21325262-5 2011 Direct sequencing of the SERPINC1 gene in the patient and his father revealed a heterozygotic missense mutation, a cytosine to thymine substitution at nucleotide position 235 in exon 2 of the SERPINC1 gene (p.Arg79Cys). Thymine 127-134 serpin family C member 1 Homo sapiens 192-200 21799398-9 2011 ATIII administration increases heparin sensitivity and decreases heparin requirements compared with FFP in patients undergoing CABGS with peroperative NTG infusion. Heparin 31-38 serpin family C member 1 Homo sapiens 0-5 21799398-9 2011 ATIII administration increases heparin sensitivity and decreases heparin requirements compared with FFP in patients undergoing CABGS with peroperative NTG infusion. Heparin 65-72 serpin family C member 1 Homo sapiens 0-5 21799398-9 2011 ATIII administration increases heparin sensitivity and decreases heparin requirements compared with FFP in patients undergoing CABGS with peroperative NTG infusion. Nitroglycerin 151-154 serpin family C member 1 Homo sapiens 0-5 21799398-10 2011 ATIII may be preferred to FFP in patients with heparin resistance due to NTG infusion undergoing CABGS. Heparin 47-54 serpin family C member 1 Homo sapiens 0-5 21799398-10 2011 ATIII may be preferred to FFP in patients with heparin resistance due to NTG infusion undergoing CABGS. Nitroglycerin 73-76 serpin family C member 1 Homo sapiens 0-5 21665912-8 2011 CONCLUSIONS: Patient"s age could be a moderate indicator of AT activity drop and low preoperative AT activity could be a sign of reduced anticoagulant efficacy of heparin during CPB. Heparin 163-170 serpin family C member 1 Homo sapiens 98-100 21799398-0 2011 Peroperative effects of fresh frozen plasma and antithrombin III on heparin sensitivity and coagulation during nitroglycerine infusion in coronary artery bypass surgery. Nitroglycerin 111-125 serpin family C member 1 Homo sapiens 48-64 21799398-2 2011 Fresh frozen plasma (FFP) and antithrombin III (ATIII) may be used for the treatment of heparin resistance. Heparin 88-95 serpin family C member 1 Homo sapiens 30-46 21799398-2 2011 Fresh frozen plasma (FFP) and antithrombin III (ATIII) may be used for the treatment of heparin resistance. Heparin 88-95 serpin family C member 1 Homo sapiens 48-53 21866963-3 2011 The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2). Adenosine Triphosphate 139-142 serpin family C member 1 Homo sapiens 23-35 21875153-0 2011 Energetics of hydrogen bond switch, residue burial and cavity analysis reveals molecular basis of improved heparin binding to antithrombin. Hydrogen 14-22 serpin family C member 1 Homo sapiens 126-138 21875153-0 2011 Energetics of hydrogen bond switch, residue burial and cavity analysis reveals molecular basis of improved heparin binding to antithrombin. Heparin 107-114 serpin family C member 1 Homo sapiens 126-138 21875153-2 2011 Anticoagulant activity of ATIII is increased by several thousand folds when activated by vascular wall heparan sulfate proteoglycans (HSPGs) and pharmaceutical heparins. Heparin 160-168 serpin family C member 1 Homo sapiens 26-31 21875153-3 2011 ATIII isoforms in human plasma, alpha-ATIII and beta-ATIII differ in the amount of glycosylation which is the basis of differences in their heparin binding affinity and function. Heparin 140-147 serpin family C member 1 Homo sapiens 0-5 21875153-4 2011 Crystal structures and site directed mutagenesis studies have mapped the heparin binding site in ATIII, however the hydrogen bond switch and energetics of interaction during the course of heparin dependent conformational change remains largely unclear. Heparin 73-80 serpin family C member 1 Homo sapiens 97-102 21875153-4 2011 Crystal structures and site directed mutagenesis studies have mapped the heparin binding site in ATIII, however the hydrogen bond switch and energetics of interaction during the course of heparin dependent conformational change remains largely unclear. Hydrogen 116-124 serpin family C member 1 Homo sapiens 97-102 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Heparin 15-22 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Heparin 97-104 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Arginine 131-134 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Arginine 142-145 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Hydrogen 163-171 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Heparin 97-104 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Lysine 225-228 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Lysine 236-239 serpin family C member 1 Homo sapiens 54-59 21875153-5 2011 An analysis of heparin bound conformational states of ATIII using PEARLS software showed that in heparin bound intermediate state, Arg 47 and Arg 13 residues make hydrogen bonds with heparin but in the activated conformation Lys 11 and Lys 114 have more hydrogen bond interactions. Hydrogen 254-262 serpin family C member 1 Homo sapiens 54-59 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. pentasaccharide 35-50 serpin family C member 1 Homo sapiens 22-34 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Lysine 59-62 serpin family C member 1 Homo sapiens 22-34 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Proline 68-71 serpin family C member 1 Homo sapiens 22-34 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Lysine 79-82 serpin family C member 1 Homo sapiens 22-34 21875153-6 2011 In the protease bound-antithrombin-pentasaccharide complex Lys 114, Pro 12 and Lys 125 form important hydrogen bonding interactions. Hydrogen 102-110 serpin family C member 1 Homo sapiens 22-34 21875153-11 2011 We hypothesize that during the process of conformational change after heparin binding beta form of antithrombin has low energy barrier to form D-helix extension toward N and C-terminal end as compared to alpha isoform. Heparin 70-77 serpin family C member 1 Homo sapiens 99-111 21866963-3 2011 The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2). cdse 60-64 serpin family C member 1 Homo sapiens 23-35 21866963-3 2011 The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2). Zinc 65-68 serpin family C member 1 Homo sapiens 23-35 21866963-3 2011 The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2). Adenosine Triphosphate 139-142 serpin family C member 1 Homo sapiens 23-35 22097175-12 2011 Urinary excretion of Hcy significantly increases, in comparison to control, and correlates with serum AT III level. Homocysteine 21-24 serpin family C member 1 Homo sapiens 102-108 21866963-3 2011 The conjugation of the antithrombin or anti-ATP aptamers to CdSe/ZnS semiconductor quantum dots (QDs) allowed the detection of thrombin or ATP through the luminescence of the QDs that is powered by a chemiluminescence resonance energy-transfer (CRET) process stimulated by the hemin/G-quadruplex/thrombin complex or the hemin/G-quadruplex/ATP nanostructure, in the presence of luminol/H(2)O(2). Luminol 377-384 serpin family C member 1 Homo sapiens 23-35 21751805-1 2011 The observed salt dependence of charged ligand binding to polyelectrolytes, such as proteins to DNA or antithrombin to heparin, is often interpreted by means of the "oligolysine model." Salts 13-17 serpin family C member 1 Homo sapiens 103-115 21769943-0 2011 Effects of glycosylation on heparin binding and antithrombin activation by heparin. Heparin 75-82 serpin family C member 1 Homo sapiens 48-60 21769943-1 2011 Antithrombin (AT), a serine protease inhibitor, circulates in blood in two major isoforms, alpha and beta, which differ in their amount of glycosylation and affinity for heparin. Heparin 170-177 serpin family C member 1 Homo sapiens 0-12 21769943-1 2011 Antithrombin (AT), a serine protease inhibitor, circulates in blood in two major isoforms, alpha and beta, which differ in their amount of glycosylation and affinity for heparin. Heparin 170-177 serpin family C member 1 Homo sapiens 14-16 21769943-3 2011 In this process, beta-AT presents the higher affinity for heparin, being suggested as the major AT glycoform inhibitor in vivo. Heparin 58-65 serpin family C member 1 Homo sapiens 22-24 21769943-3 2011 In this process, beta-AT presents the higher affinity for heparin, being suggested as the major AT glycoform inhibitor in vivo. Heparin 58-65 serpin family C member 1 Homo sapiens 96-98 21769943-4 2011 However, either the molecular basis demonstrating the differences in heparin binding to both AT isoforms or the mechanism of its conformational activation are not fully understood. Heparin 69-76 serpin family C member 1 Homo sapiens 93-95 21769943-5 2011 Thus, the present work evaluated the effects of glycosylation and heparin binding on AT structure, function, and dynamics. Heparin 66-73 serpin family C member 1 Homo sapiens 85-87 21769943-7 2011 Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT. asn135-linked oligosaccharide 14-43 serpin family C member 1 Homo sapiens 64-66 21769943-7 2011 Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT. asn135-linked oligosaccharide 14-43 serpin family C member 1 Homo sapiens 176-178 21769943-7 2011 Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT. Heparin 75-82 serpin family C member 1 Homo sapiens 64-66 21769943-7 2011 Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT. Heparin 75-82 serpin family C member 1 Homo sapiens 176-178 21769943-7 2011 Additionally, Asn135-linked oligosaccharide caused a bending in AT-bounded heparin, moving such polysaccharide away from helix D, which supports its reduced affinity for alpha-AT. Polysaccharides 96-110 serpin family C member 1 Homo sapiens 64-66 21769943-9 2011 Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation. Heparin 50-57 serpin family C member 1 Homo sapiens 72-74 21769943-9 2011 Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation. Heparin 50-57 serpin family C member 1 Homo sapiens 188-190 21769943-9 2011 Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation. Polysaccharides 146-152 serpin family C member 1 Homo sapiens 72-74 21769943-9 2011 Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation. Polysaccharides 146-152 serpin family C member 1 Homo sapiens 188-190 21769943-9 2011 Such intramolecular rearrangements, together with heparin dynamics over AT surface, may support an atomic-level explanation for the Asn135-linked glycan influence over heparin binding and AT activation. Heparin 168-175 serpin family C member 1 Homo sapiens 72-74 21866614-20 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide. Heparin 0-3 serpin family C member 1 Homo sapiens 87-103 21866614-20 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 87-103 21866614-20 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to the enzyme inhibitor antithrombin III via the pentasaccharide. pentasaccharide 112-127 serpin family C member 1 Homo sapiens 87-103 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Sodium Dodecyl Sulfate 31-53 serpin family C member 1 Homo sapiens 0-12 21726720-0 2011 Electrochemical impedance spectroscopy as a highly sensitive tool for a dynamic interaction study between heparin and antithrombin: a novel antithrombin sensor. Heparin 106-113 serpin family C member 1 Homo sapiens 140-152 21416466-2 2011 A new method to follow loss in heparin binding to the serine protease inhibitor, antithrombin III, and the serine protease, thrombin, was developed using a surface plasmon resonance competitive binding assay. Heparin 31-38 serpin family C member 1 Homo sapiens 81-97 21416466-6 2011 It is this sulfo group loss that probably accounts for a decrease in the binding of autoclaved heparin to antithrombin III and thrombin as well as the observed decrease in its amidolytic activity. Parathion 11-16 serpin family C member 1 Homo sapiens 106-122 21416466-6 2011 It is this sulfo group loss that probably accounts for a decrease in the binding of autoclaved heparin to antithrombin III and thrombin as well as the observed decrease in its amidolytic activity. Heparin 95-102 serpin family C member 1 Homo sapiens 106-122 21655682-0 2011 Massive muscle haematoma three months after starting vitamin K antagonist therapy for deep-vein thrombosis in an antithrombin deficient patient: another case of factor IX propeptide mutation. Vitamin K 53-62 serpin family C member 1 Homo sapiens 113-125 21655672-8 2011 The AT assay dependent on thrombin activity was not influenced by rivaroxaban, whereas the AT levels dependent on factor Xa activity were significantly increased by rivaroxaban. Rivaroxaban 165-176 serpin family C member 1 Homo sapiens 91-93 21297450-1 2011 The effect of protamine sulfate on factor Xa (FXa) and the factor Xa-antithrombin complex was studied via SDS-PAGE and Western blot analysis. Sodium Dodecyl Sulfate 106-109 serpin family C member 1 Homo sapiens 69-81 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Sodium Dodecyl Sulfate 55-58 serpin family C member 1 Homo sapiens 0-12 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Heparin 218-225 serpin family C member 1 Homo sapiens 0-12 20211924-6 2011 Antithrombin"s ability to form sodium dodecyl sulfate (SDS)-stable complex with thrombin, stoichiometry of thrombin inhibition, second-order rate constant for thrombin and factor Xa (fXa) inhibition (M(-1) s(-1)), and heparin dissociation constant (K(D); tryptophan fluorescence emission spectra) were determined. Tryptophan 255-265 serpin family C member 1 Homo sapiens 0-12 21297455-5 2011 For 0.2-1.5 mug/ml fondaparinux (plasma concentrations achieved with dosages for prophylaxis and treatment of venous thromboembolism) and AT levels of 0.5 U/ml there was 20% loss of activity and with 0.25 U/ml AT there was a 45% loss of activity compared to 1 U/ml AT. Fondaparinux 19-31 serpin family C member 1 Homo sapiens 210-212 21277398-4 2011 Antithrombin (AT) uptake was measured before and after selectively destroying the active pentasaccharide sequence of the heparin moiety, and was found to be predominantly through the active sequence on all of the surfaces. pentasaccharide 89-104 serpin family C member 1 Homo sapiens 0-12 21277398-4 2011 Antithrombin (AT) uptake was measured before and after selectively destroying the active pentasaccharide sequence of the heparin moiety, and was found to be predominantly through the active sequence on all of the surfaces. Heparin 121-128 serpin family C member 1 Homo sapiens 0-12 21297455-5 2011 For 0.2-1.5 mug/ml fondaparinux (plasma concentrations achieved with dosages for prophylaxis and treatment of venous thromboembolism) and AT levels of 0.5 U/ml there was 20% loss of activity and with 0.25 U/ml AT there was a 45% loss of activity compared to 1 U/ml AT. Fondaparinux 19-31 serpin family C member 1 Homo sapiens 210-212 21297455-0 2011 Functionality of fondaparinux (pentasaccharide) depends on clinical antithrombin levels. pentasaccharide 31-46 serpin family C member 1 Homo sapiens 68-80 21297455-10 2011 With AT levels below 30% of normal induced by anti-AT antibodies, there was a 60% in-vivo reduction in the antithrombotic activity of fondaparinux (ED50 75 vs. 240 mug/kg). Fondaparinux 134-146 serpin family C member 1 Homo sapiens 5-7 21297455-10 2011 With AT levels below 30% of normal induced by anti-AT antibodies, there was a 60% in-vivo reduction in the antithrombotic activity of fondaparinux (ED50 75 vs. 240 mug/kg). Fondaparinux 134-146 serpin family C member 1 Homo sapiens 51-53 21297455-1 2011 Fondaparinux (Arixtra) is an antithrombin (AT)-dependent synthetic inhibitor of factor Xa (FXa). Fondaparinux 0-12 serpin family C member 1 Homo sapiens 29-41 21220417-5 2011 Maximal accelerations of ZPI-factor Xa reactions required calcium, which augmented the heparin acceleration by relieving Gla domain inhibition as previously shown for heparin bridging of the antithrombin-factor Xa reaction. Calcium 58-65 serpin family C member 1 Homo sapiens 191-203 21297455-1 2011 Fondaparinux (Arixtra) is an antithrombin (AT)-dependent synthetic inhibitor of factor Xa (FXa). Fondaparinux 14-21 serpin family C member 1 Homo sapiens 29-41 21220417-5 2011 Maximal accelerations of ZPI-factor Xa reactions required calcium, which augmented the heparin acceleration by relieving Gla domain inhibition as previously shown for heparin bridging of the antithrombin-factor Xa reaction. Heparin 87-94 serpin family C member 1 Homo sapiens 191-203 20946166-4 2011 MATERIALS AND METHODS: Rivaroxaban was added to plasma from healthy subjects in the concentration range 0-1000 mug L(-1) and analyzed using different reagents for activated partial thromboplastin time (APTT), prothrombin time (PT), antithrombin, fibrinogen and activated protein C (APC) resistance assays. Rivaroxaban 23-34 serpin family C member 1 Homo sapiens 232-244 20557984-0 2011 [Antithrombin homozygous type II HBS deficiency (99Leu-Phe) associated with recurrent arterial thrombosis]. 99leu-phe 49-58 serpin family C member 1 Homo sapiens 1-13 21103660-3 2011 Dabigatran was added to plasma from healthy subjects in the concentration range 0-1,000 mug/l and analysed using several reagents for activated thromboplastin time (APTT), prothrombin time (PT), fibrinogen, antithrombin, and activated protein C resistance. Dabigatran 0-10 serpin family C member 1 Homo sapiens 207-219 21345279-2 2011 There is, however, increasing evidence questioning its safety, particularly in the critically ill. Heparin mainly confers its anticoagulant effect by binding to antithrombin. Heparin 99-106 serpin family C member 1 Homo sapiens 161-173 21345279-4 2011 Owing to antithrombin consumption and degradation, and to the binding of heparin to acute phase proteins, and to apoptotic and necrotic cells, critical illness confers heparin resistance. Heparin 168-175 serpin family C member 1 Homo sapiens 9-21 21327876-5 2011 Since heparin is a conditio sine qua non for cardiopulmonary bypass, rapid consumption of AT-III promoted by heparin may lead to systemic thrombosis. Heparin 6-13 serpin family C member 1 Homo sapiens 90-96 21327876-5 2011 Since heparin is a conditio sine qua non for cardiopulmonary bypass, rapid consumption of AT-III promoted by heparin may lead to systemic thrombosis. Heparin 109-116 serpin family C member 1 Homo sapiens 90-96 21138266-6 2011 The following structure-activity relationships were found: 3-O-rutinosides (10, 13) were direct inhibitors of FXa, while 7-O-rutinosides (7, 8) showed inhibition of FXa by ATIII activation. 7-o-rutinosides 121-136 serpin family C member 1 Homo sapiens 172-177 21568083-7 2011 RESULTS: Short-term use (3 months) of both tibolone and CCHT had a detrimental effect on antithrombin, protein C and protein S levels (decreased), and even more so in the group treated with CCHT. tibolone 43-51 serpin family C member 1 Homo sapiens 89-101 21568083-7 2011 RESULTS: Short-term use (3 months) of both tibolone and CCHT had a detrimental effect on antithrombin, protein C and protein S levels (decreased), and even more so in the group treated with CCHT. ccht 56-60 serpin family C member 1 Homo sapiens 89-101 20850172-1 2011 INTRODUCTION: Low-molecular-weight heparins (LMWHs) and fondaparinux are antithrombin dependent anticoagulant drugs considered to need no laboratory monitoring because of their reputedly predictable anticoagulant effect. Heparin 35-43 serpin family C member 1 Homo sapiens 73-85 21134627-2 2011 We present a case of a female with heterozygous type I antithrombin deficiency who presented with a central nervous system transverse sinus thrombosis in the third trimester of pregnancy despite the use of therapeutic doses of low molecular weight heparin, as venous thromboembolic prophylaxis, since conception. Heparin 248-255 serpin family C member 1 Homo sapiens 55-67 20816747-0 2010 Kinetic evidence that allosteric activation of antithrombin by heparin is mediated by two sequential conformational changes. Heparin 63-70 serpin family C member 1 Homo sapiens 47-59 20816747-1 2010 The serpin, antithrombin, requires allosteric activation by a sequence-specific pentasaccharide unit of heparin or heparan sulfate glycosaminoglycans to function as an anticoagulant regulator of blood clotting proteases. pentasaccharide 80-95 serpin family C member 1 Homo sapiens 12-24 20816747-1 2010 The serpin, antithrombin, requires allosteric activation by a sequence-specific pentasaccharide unit of heparin or heparan sulfate glycosaminoglycans to function as an anticoagulant regulator of blood clotting proteases. Heparin 104-111 serpin family C member 1 Homo sapiens 12-24 20816747-1 2010 The serpin, antithrombin, requires allosteric activation by a sequence-specific pentasaccharide unit of heparin or heparan sulfate glycosaminoglycans to function as an anticoagulant regulator of blood clotting proteases. heparan sulfate glycosaminoglycans 115-149 serpin family C member 1 Homo sapiens 12-24 20816747-2 2010 Surprisingly, X-ray structures have shown that the pentasaccharide produces similar induced-fit changes in the heparin binding site of native and latent antithrombin despite large differences in the heparin affinity and global conformation of these two forms. pentasaccharide 51-66 serpin family C member 1 Homo sapiens 153-165 20816747-2 2010 Surprisingly, X-ray structures have shown that the pentasaccharide produces similar induced-fit changes in the heparin binding site of native and latent antithrombin despite large differences in the heparin affinity and global conformation of these two forms. Heparin 111-118 serpin family C member 1 Homo sapiens 153-165 20816747-3 2010 Here we present kinetic evidence for similar induced-fit mechanisms of pentasaccharide binding to native and latent antithrombins and kinetic simulations which together support a three-step mechanism of allosteric activation of native antithrombin involving two successive conformational changes. pentasaccharide 71-86 serpin family C member 1 Homo sapiens 116-128 20816747-5 2010 The observation that variant antithrombins that cannot undergo the second conformational change bind the pentasaccharide like latent antithrombin and are partially activated suggests that both conformational changes contribute to allosteric activation, in agreement with a recently proposed model of allosteric activation. pentasaccharide 105-120 serpin family C member 1 Homo sapiens 29-41 19825921-4 2010 Fondaparinux is a synthetic pentasaccharide that binds to antithrombin and potentiates inhibition of factor Xa. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 58-70 21028827-0 2010 Effects on molecular conformation and anticoagulant activities of 1,6-anhydrosugars at the reducing terminal of antithrombin-binding octasaccharides isolated from low-molecular-weight heparin enoxaparin. 1,6-anhydrosugars 66-83 serpin family C member 1 Homo sapiens 112-124 21028827-0 2010 Effects on molecular conformation and anticoagulant activities of 1,6-anhydrosugars at the reducing terminal of antithrombin-binding octasaccharides isolated from low-molecular-weight heparin enoxaparin. octasaccharides 133-148 serpin family C member 1 Homo sapiens 112-124 20660032-10 2010 Mean serum Ca and P significantly increased compared to baseline, whereas serum Mg decreased at 3 d. Magnesium 80-82 serpin family C member 1 Homo sapiens 93-99 20685328-3 2010 The serpin, antithrombin, together with its cofactors, heparin and heparan sulfate, perform a critical anticoagulant function by preventing the activation of blood clotting proteinases except when needed at the site of a vascular injury. Heparin 55-62 serpin family C member 1 Homo sapiens 12-24 20685328-3 2010 The serpin, antithrombin, together with its cofactors, heparin and heparan sulfate, perform a critical anticoagulant function by preventing the activation of blood clotting proteinases except when needed at the site of a vascular injury. Heparitin Sulfate 67-82 serpin family C member 1 Homo sapiens 12-24 20685328-7 2010 Binding of a specific heparin or heparan sulfate pentasaccharide to antithrombin induces allosteric activating changes that mitigate the unfavorable interactions and promote template bridging of the serpin and proteinase. Heparin 22-29 serpin family C member 1 Homo sapiens 68-80 20685328-7 2010 Binding of a specific heparin or heparan sulfate pentasaccharide to antithrombin induces allosteric activating changes that mitigate the unfavorable interactions and promote template bridging of the serpin and proteinase. heparan sulfate pentasaccharide 33-64 serpin family C member 1 Homo sapiens 68-80 21204288-3 2010 The anticoagulative effect of heparin is a result of the binding of heparin to the plasma protein antithrombin III and the subsequent inactivation of blood clotting factors (e.g. factor IIa, IXa, Xa, XIa, XIIa). Heparin 30-37 serpin family C member 1 Homo sapiens 98-114 21204288-3 2010 The anticoagulative effect of heparin is a result of the binding of heparin to the plasma protein antithrombin III and the subsequent inactivation of blood clotting factors (e.g. factor IIa, IXa, Xa, XIa, XIIa). Heparin 68-75 serpin family C member 1 Homo sapiens 98-114 21572750-9 2010 Idrabiotaparinux is an indirect inhibitor of Xa as it accelerates the activity of antithrombin. idrabiotaparinux 0-16 serpin family C member 1 Homo sapiens 82-94 20945941-1 2010 Supersulfated low molecular weight heparin (ssLMWH) inhibits the intrinsic tenase (factor IXa-factor VIIIa) complex in an antithrombin-independent manner. Heparin 35-42 serpin family C member 1 Homo sapiens 122-134 20142342-1 2010 BACKGROUND: Unfractionated heparin"s primary mechanism of action is to enhance the enzymatic activity of antithrombin (AT). Heparin 27-34 serpin family C member 1 Homo sapiens 105-117 20660032-11 2010 1,25-Dihydroxyvitamin D significantly increased from 46.8 +- 18.9 to 97.8 +- 38.3 pg/ml at 3 d (P < 0.001) and to 59.5 +- 27.3 pg/ml at 60 d (P < 0.05). 1,25-dihydroxyvitamin D 0-23 serpin family C member 1 Homo sapiens 88-94 20659659-5 2010 This review proposes that alternative anticoagulants (danaparoid, fondaparinux) that share certain properties of heparin-namely its irreversible antithrombin-mediated inhibition of factor Xa-and that have relatively long half-lives, have several advantages in the therapy for HIT over short-acting agents that inhibit thrombin directly (recombinant hirudin, argatroban, and bivalirudin). danaparoid 54-64 serpin family C member 1 Homo sapiens 145-157 20627942-1 2010 BACKGROUND: Antithrombin concentrate (AT) is used to treat heparin resistance (HR) in cardiac surgery. Heparin 59-66 serpin family C member 1 Homo sapiens 12-24 20628058-1 2010 The activation of antithrombin (AT) by heparin facilitates the exosite-dependent interaction of the serpin with factors IXa (FIXa) and Xa (FXa), thereby improving the rate of reactions by 300- to 500-fold. Heparin 39-46 serpin family C member 1 Homo sapiens 18-30 20628058-1 2010 The activation of antithrombin (AT) by heparin facilitates the exosite-dependent interaction of the serpin with factors IXa (FIXa) and Xa (FXa), thereby improving the rate of reactions by 300- to 500-fold. Heparin 39-46 serpin family C member 1 Homo sapiens 32-34 20628058-7 2010 The chimeric mutant cleaved a FIXa-specific chromogenic substrate with normal catalytic efficiency, however, the mutant exhibited approximately 5-fold enhanced reactivity with AT specifically in the absence of the cofactor, heparin. Heparin 224-231 serpin family C member 1 Homo sapiens 176-178 20197127-0 2010 Surface modification with an antithrombin-heparin complex for anticoagulation: studies on a model surface with gold as substrate. Heparin 42-49 serpin family C member 1 Homo sapiens 29-41 20659659-5 2010 This review proposes that alternative anticoagulants (danaparoid, fondaparinux) that share certain properties of heparin-namely its irreversible antithrombin-mediated inhibition of factor Xa-and that have relatively long half-lives, have several advantages in the therapy for HIT over short-acting agents that inhibit thrombin directly (recombinant hirudin, argatroban, and bivalirudin). Fondaparinux 66-78 serpin family C member 1 Homo sapiens 145-157 20659659-5 2010 This review proposes that alternative anticoagulants (danaparoid, fondaparinux) that share certain properties of heparin-namely its irreversible antithrombin-mediated inhibition of factor Xa-and that have relatively long half-lives, have several advantages in the therapy for HIT over short-acting agents that inhibit thrombin directly (recombinant hirudin, argatroban, and bivalirudin). Heparin 113-120 serpin family C member 1 Homo sapiens 145-157 20443661-1 2010 OBJECTIVE: This retrospective study was performed to characterize the laboratory features and water metabolism of women with pregnancy-induced antithrombin deficiency (PIATD). Water 94-99 serpin family C member 1 Homo sapiens 143-155 21507819-1 2010 UNLABELLED: Fondaparinux, a pentasaccharide which selectively binds to antithrombin III, has negligible to no cross-reactivity with heparin-induced thrombocytopenia (HIT) antibodies in in vitro studies. Fondaparinux 12-24 serpin family C member 1 Homo sapiens 71-87 21507819-1 2010 UNLABELLED: Fondaparinux, a pentasaccharide which selectively binds to antithrombin III, has negligible to no cross-reactivity with heparin-induced thrombocytopenia (HIT) antibodies in in vitro studies. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 71-87 20216984-4 2010 Heparin (H) increases the rate of IIa-TM inhibition by antithrombin (AT) and enhances FV cleavage by APC. Heparin 0-7 serpin family C member 1 Homo sapiens 55-67 20531960-6 2010 The anti-Xa agent rivaroxaban and the antithrombin agent dabigatran are already available for the prophylaxis of venous thromboembolism in some countries. Dabigatran 57-67 serpin family C member 1 Homo sapiens 38-50 20378948-1 2010 Heparin is a potent anticoagulant agent that interacts strongly with antithrombin III to prevent the formation of fibrin clots. Heparin 0-7 serpin family C member 1 Homo sapiens 69-85 20514621-0 2010 Conventional chromogenic heparin assays are influenced by patient"s endogenous plasma Antithrombin levels. Heparin 25-32 serpin family C member 1 Homo sapiens 86-98 20215909-2 2010 Heparin exerts its major effect via antithrombin, converting antithrombin to a more efficient inhibitor of circulating thrombin (factor IIa), factor Xa, factor IXa, factor XIIa, and kallikrein. Heparin 0-7 serpin family C member 1 Homo sapiens 36-48 20184328-0 2010 Inhibitory properties of the P1 Tyr variant of antithrombin. Tyrosine 32-35 serpin family C member 1 Homo sapiens 47-59 20215909-2 2010 Heparin exerts its major effect via antithrombin, converting antithrombin to a more efficient inhibitor of circulating thrombin (factor IIa), factor Xa, factor IXa, factor XIIa, and kallikrein. Heparin 0-7 serpin family C member 1 Homo sapiens 61-73 20437787-9 2010 In addition, recent studies suggest that children need larger doses of heparin than adults, because they have lower antithrombin levels, and they metabolize heparin more rapidly. Heparin 71-78 serpin family C member 1 Homo sapiens 116-128 20135058-3 2010 The main depolymerisation mechanism involves Hep radical intermediates that cleave the glycosidic linkage at unsulphated uronic acids followed by a 6-O-nonsulphated glucosamine, thus largely preserving the pentasaccharide sequence responsible for the binding to antithrombin III (AT). Heparin 45-48 serpin family C member 1 Homo sapiens 262-278 19805567-5 2010 We report on the development of long-lasting enfuvirtide conjugates by the use of the site-specific conjugation of enfuvirtide to an antithrombin-binding carrier pentasaccharide (CP) through polyethylene glycol (PEG) linkers of various lengths. Polyethylene Glycols 191-210 serpin family C member 1 Homo sapiens 133-145 20024502-0 2010 Contribution of exosite occupancy by heparin to the regulation of coagulation proteases by antithrombin. Heparin 37-44 serpin family C member 1 Homo sapiens 91-103 20024502-1 2010 Heparin promotes the antithrombin (AT) inactivation of factors IXa (fIXa) and Xa (fXa) through a conformational activation of the serpin and also by a template mechanism in the presence of physiological levels of Ca2+. Heparin 0-7 serpin family C member 1 Homo sapiens 21-33 20014840-6 2010 The three oxidation states present in the range of water stability are At(-I), At(+I), and At(+III) and exist as At(-), At(+), and AtO(+), respectively, in the 1-2 pH range. Water 51-56 serpin family C member 1 Homo sapiens 91-98 19805567-5 2010 We report on the development of long-lasting enfuvirtide conjugates by the use of the site-specific conjugation of enfuvirtide to an antithrombin-binding carrier pentasaccharide (CP) through polyethylene glycol (PEG) linkers of various lengths. pentasaccharide 162-177 serpin family C member 1 Homo sapiens 133-145 19805567-5 2010 We report on the development of long-lasting enfuvirtide conjugates by the use of the site-specific conjugation of enfuvirtide to an antithrombin-binding carrier pentasaccharide (CP) through polyethylene glycol (PEG) linkers of various lengths. Polyethylene Glycols 212-215 serpin family C member 1 Homo sapiens 133-145 22111528-1 2010 Idraparinux is a polymethylated synthetic pentasaccharide that binds to antithrombin with high affinity. idraparinux 0-11 serpin family C member 1 Homo sapiens 72-84 22111528-1 2010 Idraparinux is a polymethylated synthetic pentasaccharide that binds to antithrombin with high affinity. synthetic pentasaccharide 32-57 serpin family C member 1 Homo sapiens 72-84 20229677-11 2010 One case (0.62%) of DVT propagation into the vena cava occurred in a woman with antithrombin deficiency treated with LMWH. Heparin, Low-Molecular-Weight 117-121 serpin family C member 1 Homo sapiens 80-92 22282689-2 2010 This antithrombotic and antithrombin activity is of great pharmacologic interest and makes sulodexide a suitable drug for the prophylaxis and treatment of arterial and venous peripheral diseases. glucuronyl glucosamine glycan sulfate 91-101 serpin family C member 1 Homo sapiens 24-36 19899825-5 2010 Additionally, we characterized alterations in the glycan structures of vitronectin (Asn-169, 242) and antithrombin III (Asn-225) that were identified in HCC patient plasma. Asparagine 120-123 serpin family C member 1 Homo sapiens 102-118 20196517-9 2010 In cases of resistance to heparin, additional doses of the drug were injected, in combination with plasma or antithrombin in 29% and 12% of the hospitals, respectively. Heparin 26-33 serpin family C member 1 Homo sapiens 109-121 22282689-1 2010 Sulodexide is a highly purified glycosaminoglycan containing a combination of heparan sulfate with affinity for antithrombin III and dermatan sulfate with affinity for heparin cofactor II. glucuronyl glucosamine glycan sulfate 0-10 serpin family C member 1 Homo sapiens 112-128 19837548-1 2009 We present the case of a 73-year-old man, operated on for paralyzing sciatica, who displayed acute postoperative respiratory distress and intra-alveolar haemorrhage following the administration of dabigatran etexilate, a new oral antithrombin used in the prevention of venous thromboembolism. Dabigatran 197-217 serpin family C member 1 Homo sapiens 230-242 19748283-8 2009 Further in vitro experiments indicate that heparin prevents the activation of latent TGF-beta into its bioactive form probably by virtue of accelerating the complex-formation between AT-III and thrombin. Heparin 43-50 serpin family C member 1 Homo sapiens 183-189 19967150-9 2009 Similar to heparin, the ability of sulfated galactan to potentiate FXa inhibition by antithrombin is calcium-dependent. Calcium 101-108 serpin family C member 1 Homo sapiens 85-97 19888512-2 2009 De novo chemical synthesis of the corresponding pentasaccharide as well as simplified analogues has provided very specific, antithrombin-mediated inhibitors of factor Xa with various pharmacokinetic profiles. pentasaccharide 48-63 serpin family C member 1 Homo sapiens 124-136 19888512-4 2009 Because of the very specific binding to antithrombin the pharmacokinetics of pentasaccharides can be predicted and transferred to other molecules covalently bound to them. pentasaccharides 77-93 serpin family C member 1 Homo sapiens 40-52 19888516-7 2009 The fucosylated chondroitin sulfate inhibits thrombin by heparin cofactor II, whereas sulfated fucan inhibits thrombin by both antithrombin and heparin cofactor II. fucan 95-100 serpin family C member 1 Homo sapiens 127-139 19888521-0 2009 Structural features of low-molecular-weight heparins affecting their affinity to antithrombin. Heparin 44-52 serpin family C member 1 Homo sapiens 81-93 19715676-0 2009 Role of P2 glycine in determining the specificity of antithrombin reaction with coagulation proteases. Glycine 11-18 serpin family C member 1 Homo sapiens 53-65 19818773-1 2009 Allosteric activation of antithrombin as a rapid inhibitor of factors IXa and Xa requires binding of a high-affinity heparin pentasaccharide. IC 831423 117-140 serpin family C member 1 Homo sapiens 25-37 19818773-2 2009 The currently-accepted mechanism involves removal of a constraint on the antithrombin reactive center loop (RCL) so that the proteinase can simultaneously engage both the P1 arginine and an exosite at Y253. Arginine 174-182 serpin family C member 1 Homo sapiens 73-85 19818773-4 2009 We propose a quite different mechanism in which heparin activates antithrombin by mitigating an unfavorable surface interaction, by altering its nature, and by moving the attached proteinase away from the site of the unfavorable interaction through RCL expulsion. Heparin 48-55 serpin family C member 1 Homo sapiens 66-78 19931793-4 2009 Heparin can then act as an anticoagulant by binding to antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 55-67 19843180-3 2009 We have evaluated the functional and conformational effects on antithrombin of citrullination, a post-translational modification catalyzed by peptidylarginine deiminase (PAD), which changes arginine to citrulline. Arginine 150-158 serpin family C member 1 Homo sapiens 63-75 19843180-3 2009 We have evaluated the functional and conformational effects on antithrombin of citrullination, a post-translational modification catalyzed by peptidylarginine deiminase (PAD), which changes arginine to citrulline. Citrulline 202-212 serpin family C member 1 Homo sapiens 63-75 19843180-8 2009 We confirmed that citrullination of antithrombin abolished its activity; this abolition of activity was accelerated by heparin, which facilitated the early citrullination of Arg393 (P1 residue). Heparin 119-126 serpin family C member 1 Homo sapiens 36-48 19888512-1 2009 The elucidation of the structure of the antithrombin binding sequence in heparin has given a large impulse to the rational design of heparin related drugs. Heparin 73-80 serpin family C member 1 Homo sapiens 40-52 19661062-0 2009 The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation. Heparin 51-58 serpin family C member 1 Homo sapiens 103-115 19661062-1 2009 Heparin and heparan sulfate glycosaminoglycans allosterically activate the serpin, antithrombin, by binding through a specific pentasaccharide sequence containing a critical 3-O-sulfo group. Heparin 0-7 serpin family C member 1 Homo sapiens 83-95 19661062-1 2009 Heparin and heparan sulfate glycosaminoglycans allosterically activate the serpin, antithrombin, by binding through a specific pentasaccharide sequence containing a critical 3-O-sulfo group. heparan sulfate glycosaminoglycans 12-46 serpin family C member 1 Homo sapiens 83-95 19661062-1 2009 Heparin and heparan sulfate glycosaminoglycans allosterically activate the serpin, antithrombin, by binding through a specific pentasaccharide sequence containing a critical 3-O-sulfo group. pentasaccharide 127-142 serpin family C member 1 Homo sapiens 83-95 19661062-2 2009 To elucidate the role of the 3-O-sulfo group in the activation mechanism, we compared the effects of deleting the 3-O-sulfo group or mutating the Lys(114) binding partner of this group on antithrombin-pentasaccharide interactions by equilibrium binding and rapid kinetic analyses. pentasaccharide 201-216 serpin family C member 1 Homo sapiens 188-200 19661062-3 2009 Binding studies over a wide range of ionic strength and pH showed that loss of the 3-O-sulfo group caused a massive approximately 60% loss in binding energy for the antithrombin-pentasaccharide interaction due to the disruption of a cooperative network of ionic and nonionic interactions. 3-o-sulfo 83-92 serpin family C member 1 Homo sapiens 165-177 19661062-3 2009 Binding studies over a wide range of ionic strength and pH showed that loss of the 3-O-sulfo group caused a massive approximately 60% loss in binding energy for the antithrombin-pentasaccharide interaction due to the disruption of a cooperative network of ionic and nonionic interactions. pentasaccharide 178-193 serpin family C member 1 Homo sapiens 165-177 19661062-4 2009 Despite this affinity loss, the 3-O-desulfonated pentasaccharide retained the ability to induce tryptophan fluorescence changes and to enhance factor Xa reactivity in antithrombin, indicative of normal conformational activation. 3-o-desulfonated pentasaccharide 32-64 serpin family C member 1 Homo sapiens 167-179 19661062-5 2009 Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin. Parathion 50-55 serpin family C member 1 Homo sapiens 131-143 19661062-5 2009 Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin. Parathion 50-55 serpin family C member 1 Homo sapiens 207-219 19661062-5 2009 Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin. pentasaccharide 95-110 serpin family C member 1 Homo sapiens 131-143 19661062-5 2009 Rapid kinetic studies showed that loss of the 3-O-sulfo group affected both the ability of the pentasaccharide to recognize native antithrombin and its ability to preferentially bind and stabilize activated antithrombin. pentasaccharide 95-110 serpin family C member 1 Homo sapiens 207-219 19661062-6 2009 By contrast, mutation of Lys(114) solely affected the preferential interaction of the pentasaccharide with activated antithrombin. Lysine 25-28 serpin family C member 1 Homo sapiens 117-129 19661062-6 2009 By contrast, mutation of Lys(114) solely affected the preferential interaction of the pentasaccharide with activated antithrombin. pentasaccharide 86-101 serpin family C member 1 Homo sapiens 117-129 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. 3-o-sulfo 36-45 serpin family C member 1 Homo sapiens 124-136 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. 3-o-sulfo 36-45 serpin family C member 1 Homo sapiens 208-220 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. 3-o-sulfo 36-45 serpin family C member 1 Homo sapiens 208-220 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. IC 831423 86-109 serpin family C member 1 Homo sapiens 124-136 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. IC 831423 86-109 serpin family C member 1 Homo sapiens 208-220 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. IC 831423 86-109 serpin family C member 1 Homo sapiens 208-220 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. Lysine 165-168 serpin family C member 1 Homo sapiens 124-136 19661062-7 2009 These findings demonstrate that the 3-O-sulfo group functions as a key determinant of heparin pentasaccharide activation of antithrombin both by contributing to the Lys(114)-independent recognition of native antithrombin and by triggering a Lys(114)-dependent induced fit interaction with activated antithrombin that locks the serpin in the activated state. Lysine 241-244 serpin family C member 1 Homo sapiens 124-136 19573895-5 2009 We incubated in vitro plasma and purified antithrombin and human hepatoma cells (HepG2) with methyl-glyoxal and glucose. Pyruvaldehyde 93-107 serpin family C member 1 Homo sapiens 42-54 19414859-1 2009 Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chondroitin sulfate with antithrombin-independent antithrombotic properties. holothurian glycosaminoglycan 14-43 serpin family C member 1 Homo sapiens 92-104 19414859-1 2009 Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chondroitin sulfate with antithrombin-independent antithrombotic properties. dhg 45-48 serpin family C member 1 Homo sapiens 92-104 19414859-1 2009 Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chondroitin sulfate with antithrombin-independent antithrombotic properties. Chondroitin Sulfates 67-86 serpin family C member 1 Homo sapiens 92-104 19861246-10 2009 CONCLUSION: DHPLC allows automated and rapid high-throughput detection of AT- III gene mutation and polymorphisms in the clinical setting and prenatal diagnosis. dhplc 12-17 serpin family C member 1 Homo sapiens 74-81 19664058-8 2009 Heparin was also an effective co-factor for inhibition of FSAP by plasminogen activator inhibitor 1 (PAI-1) and antithrombin, whereas polyphosphate served as co-factor for the inhibition of FSAP by PAI-1 only. Heparin 0-7 serpin family C member 1 Homo sapiens 112-124 19597879-9 2009 CONCLUSIONS: Heparin responsiveness during CPB was significantly reduced in the IE group, and it seems to be associated with preoperative hypercoagulability and reduced antithrombin III activity. Heparin 13-20 serpin family C member 1 Homo sapiens 169-185 19690236-1 2009 BACKGROUND: Low antithrombin levels may compromise the anticoagulant effect of heparin and heparin-related compounds, such as fondaparinux. Heparin 79-86 serpin family C member 1 Homo sapiens 16-28 19690236-1 2009 BACKGROUND: Low antithrombin levels may compromise the anticoagulant effect of heparin and heparin-related compounds, such as fondaparinux. Heparin 91-98 serpin family C member 1 Homo sapiens 16-28 19690236-3 2009 RESULTS: Heptest clotting time was shorter at any given fondaparinux concentration in the antithrombin-deficient samples, indicating less anticoagulant effect than in the group with normal antithrombin levels. Fondaparinux 56-68 serpin family C member 1 Homo sapiens 90-102 19690236-9 2009 Higher levels of antithrombin lead to an exaggerated effect of fondaparinux on Heptest. Fondaparinux 63-75 serpin family C member 1 Homo sapiens 17-29 19631608-0 2009 Antithrombin III suppresses ADP-induced platelet granule secretion: inhibition of HSP27 phosphorylation. Adenosine Diphosphate 28-31 serpin family C member 1 Homo sapiens 0-16 19631608-4 2009 In the present study, we investigated the relationship between AT-III and the ADP-induced platelet granule secretion. Adenosine Diphosphate 78-81 serpin family C member 1 Homo sapiens 63-69 19631608-5 2009 The ADP-induced secretion of platelet-derived growth factor (PDGF)-AB and serotonin (5-HT) were significantly suppressed by AT-III. Adenosine Diphosphate 4-7 serpin family C member 1 Homo sapiens 124-130 19631608-5 2009 The ADP-induced secretion of platelet-derived growth factor (PDGF)-AB and serotonin (5-HT) were significantly suppressed by AT-III. Serotonin 74-83 serpin family C member 1 Homo sapiens 124-130 19631608-8 2009 AT-III markedly attenuated the ADP-induced phosphorylation levels of p44/p42 MAPK and p38 MAPK. Adenosine Diphosphate 31-34 serpin family C member 1 Homo sapiens 0-6 19631608-9 2009 Furthermore, the ADP-induced HSP27 phosphorylation was suppressed by AT-III. Adenosine Diphosphate 17-20 serpin family C member 1 Homo sapiens 69-75 19631608-10 2009 These results strongly suggest that AT-III directly acts on platelets and suppresses ADP-induced platelet granule secretion due to inhibiting HSP27 phosphorylation via p44/p42 MAPK and p38 MAPK. Adenosine Diphosphate 85-88 serpin family C member 1 Homo sapiens 36-42 19573895-5 2009 We incubated in vitro plasma and purified antithrombin and human hepatoma cells (HepG2) with methyl-glyoxal and glucose. Glucose 112-119 serpin family C member 1 Homo sapiens 42-54 19389385-5 2009 While oversulfated chondroitin sulfate binds tightly to antithrombin III, unlike heparin, OSCS does not induce antithrombin III to undergo the conformational change required for its inactivation of thrombin and factor Xa. Chondroitin Sulfates 19-38 serpin family C member 1 Homo sapiens 56-72 19543696-1 2009 Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa). Heparin 15-22 serpin family C member 1 Homo sapiens 38-50 19172319-5 2009 However, detailed comparison of our modeled structure of ZPI/FXa with that of AT3/FXa points to differences in interaction specificity at the reactive center and in the stability of the inhibitory complex, due to the presence of a tyrosine residue at the P1 position in ZPI, instead of the P1 arginine residue in AT3. Tyrosine 231-239 serpin family C member 1 Homo sapiens 78-81 19172319-5 2009 However, detailed comparison of our modeled structure of ZPI/FXa with that of AT3/FXa points to differences in interaction specificity at the reactive center and in the stability of the inhibitory complex, due to the presence of a tyrosine residue at the P1 position in ZPI, instead of the P1 arginine residue in AT3. Arginine 293-301 serpin family C member 1 Homo sapiens 78-81 19172319-6 2009 The modeled structure also shows specific structural differences between AT3 and ZPI in the heparin-binding and flexible N-terminal tail regions. Heparin 92-99 serpin family C member 1 Homo sapiens 73-76 19543696-1 2009 Unfractionated heparin (UFH) enhances antithrombin (AT) inhibition of thrombin (IIa) and factor Xa (FXa). Heparin 24-27 serpin family C member 1 Homo sapiens 38-50 19386495-1 2009 An efficient [DEF+GH] route was developed to the synthesis of Idraparinux, which is a fully O-sulfated, O-methylated mimic of the unique Antithrombin III binding domain of heparin. idraparinux 62-73 serpin family C member 1 Homo sapiens 137-153 19497853-0 2009 Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function. Lignin 64-71 serpin family C member 1 Homo sapiens 15-27 19497853-0 2009 Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function. Lignin 64-71 serpin family C member 1 Homo sapiens 123-135 19497853-1 2009 Antithrombin, a major regulator of coagulation and angiogenesis, is known to interact with several natural sulfated polysaccharides. Polysaccharides 116-131 serpin family C member 1 Homo sapiens 0-12 19497853-6 2009 Fluorescence binding studies indicate that sulfated DHPs bind to antithrombin with micromolar affinity under physiological conditions. dhps 52-56 serpin family C member 1 Homo sapiens 65-77 19497853-7 2009 Salt dependence of binding affinity indicates that the antithrombin-sulfated DHP interaction involves a massive 80-87% non-ionic component to the free energy of binding. Salts 0-4 serpin family C member 1 Homo sapiens 55-67 19497853-8 2009 Competitive binding studies with heparin pentasaccharide, epicatechin sulfate, and full-length heparin indicate that sulfated DHPs bind to both the pentasaccharide-binding site and extended heparin-binding site of antithrombin. IC 831423 33-56 serpin family C member 1 Homo sapiens 214-226 19497853-8 2009 Competitive binding studies with heparin pentasaccharide, epicatechin sulfate, and full-length heparin indicate that sulfated DHPs bind to both the pentasaccharide-binding site and extended heparin-binding site of antithrombin. dhps 126-130 serpin family C member 1 Homo sapiens 214-226 19497853-11 2009 Enzyme inhibition studies indicate that only one of the three sulfated DHPs studied is a potent inhibitor of free factor VIIa in the presence of antithrombin. dhps 71-75 serpin family C member 1 Homo sapiens 145-157 19497853-12 2009 Overall, the chemo-enzymatic origin and antithrombin binding properties of sulfated DHPs present novel opportunities for potent and selective modulation of the serpin function, especially for inhibiting the initiation phase of hemostasis. dhps 84-88 serpin family C member 1 Homo sapiens 40-52 19422445-0 2009 Dexamethasone induces a heat-stress response that ameliorates the conformational consequences on antithrombin of L-asparaginase treatment. Dexamethasone 0-13 serpin family C member 1 Homo sapiens 97-109 19371327-4 2009 Given the complex nature of cell-surface and extracellular matrix glycan structures, this therapeutic site has been neglected for a long time, the only exception being the antithrombin III-glycan interaction which has been successfully targeted by unfractionated and low-molecular weight heparins for many decades. Polysaccharides 66-72 serpin family C member 1 Homo sapiens 172-188 19371327-4 2009 Given the complex nature of cell-surface and extracellular matrix glycan structures, this therapeutic site has been neglected for a long time, the only exception being the antithrombin III-glycan interaction which has been successfully targeted by unfractionated and low-molecular weight heparins for many decades. Polysaccharides 189-195 serpin family C member 1 Homo sapiens 172-188 19371327-4 2009 Given the complex nature of cell-surface and extracellular matrix glycan structures, this therapeutic site has been neglected for a long time, the only exception being the antithrombin III-glycan interaction which has been successfully targeted by unfractionated and low-molecular weight heparins for many decades. Heparin 288-296 serpin family C member 1 Homo sapiens 172-188 19564340-10 2009 Also, MASP-1"s multifunctional behavior as both a complement and a coagulation enzyme is in accordance with our observation that antithrombin in the presence of heparin is a more potent inhibitor of MASP-1 than C1 inhibitor. Heparin 161-168 serpin family C member 1 Homo sapiens 129-141 19422445-3 2009 OBJECTIVES: We have investigated the effect of two corticoids, dexamethasone and prednisone, on the conformational consequences of L-ASP treatment on antithrombin. Dexamethasone 63-76 serpin family C member 1 Homo sapiens 150-162 19422445-6 2009 RESULTS: In all models, L-ASP alone or in combination with prednisone caused the intracellular retention of antithrombin associated with a severe deficiency. Prednisone 59-69 serpin family C member 1 Homo sapiens 108-120 19422445-8 2009 CONCLUSIONS: These results suggest a protective effect of dexamethasone on the conformational consequences of L-ASP on antithrombin as a result of exacerbated HSR and UPR that help to explain the reduced risk of thrombosis reported in patients that follow this scheme of treatment. Dexamethasone 58-71 serpin family C member 1 Homo sapiens 119-131 19533051-5 2009 The main clinically relevant situations in which AT-dependent HR occurs, with possible indication of AT substitution, are congenital AT deficiency, asparaginase therapy, disseminated intravascular coagulation (DIC) and administration of high doses of heparin during extracorporeal circulation, where it is significant, due to the need to maintain a very high ACT (> 400 s), that use of heart-lung machines is associated with an HR incidence of approximately 20%. Heparin 251-258 serpin family C member 1 Homo sapiens 49-51 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. Glucuronic Acid 0-13 serpin family C member 1 Homo sapiens 70-82 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. Iduronic Acid 18-29 serpin family C member 1 Homo sapiens 70-82 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. Disaccharides 41-54 serpin family C member 1 Homo sapiens 70-82 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. pentasaccharide 91-106 serpin family C member 1 Homo sapiens 70-82 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. Heparin 110-117 serpin family C member 1 Homo sapiens 70-82 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. sulfate esters 139-153 serpin family C member 1 Homo sapiens 70-82 19473011-1 2009 D-glucuronate and l-iduronate containing disaccharides related to the antithrombin-binding pentasaccharide of heparin, in which one of the sulfate esters is systematically replaced by a sodium sulfonatomethyl moiety, were synthesized. sodium sulfonatomethyl 186-208 serpin family C member 1 Homo sapiens 70-82 19533051-8 2009 Under normalized and stable AT activity, the UFH dose should be adjusted such that aPTT is within a range of 60-100 s. If anticoagulation over a longer term is indicated, then overlapping anticoagulation with a vitamin K antagonist should be started as quickly as possible. Heparin 45-48 serpin family C member 1 Homo sapiens 28-30 19425011-0 2009 Capillary electrophoretic study of small, highly sulfated, non-sugar molecules interacting with antithrombin. Sugars 63-68 serpin family C member 1 Homo sapiens 96-108 18996625-1 2009 Antithrombin, a plasma glycoprotein serpin, requires conformational activation by heparin to induce an anticoagulant effect, which is mediated through accelerated factor Xa inhibition. Heparin 82-89 serpin family C member 1 Homo sapiens 0-12 18996625-5 2009 Activator IAS(5) containing 5,6-disulfated tetrahydroisoquinoline and 3,4,5-trisulfated phenyl rings was found to bind antithrombin at pH 7.4 with an affinity comparable to the reference trisaccharide DEF. 5,6-disulfated tetrahydroisoquinoline 28-65 serpin family C member 1 Homo sapiens 119-131 18996625-5 2009 Activator IAS(5) containing 5,6-disulfated tetrahydroisoquinoline and 3,4,5-trisulfated phenyl rings was found to bind antithrombin at pH 7.4 with an affinity comparable to the reference trisaccharide DEF. 3,4,5-trisulfated 70-87 serpin family C member 1 Homo sapiens 119-131 19425011-3 2009 Scatchard analysis of the interaction of three tetrahydroisoquinoline-based polysulfated molecules with AT results in monophasic profiles with affinities in the range of 40-60 microM in 20 mM sodium phosphate buffer, pH 7.4. 1,2,3,4-tetrahydroisoquinoline 47-69 serpin family C member 1 Homo sapiens 104-106 19425011-3 2009 Scatchard analysis of the interaction of three tetrahydroisoquinoline-based polysulfated molecules with AT results in monophasic profiles with affinities in the range of 40-60 microM in 20 mM sodium phosphate buffer, pH 7.4. sodium phosphate 192-208 serpin family C member 1 Homo sapiens 104-106 19035835-6 2008 Affinities of latent and cleaved antithrombin for longer heparin chains, containing the pentasaccharide sequence, were 2-fold lower than for the pentasaccharide itself. pentasaccharide 88-103 serpin family C member 1 Homo sapiens 33-45 19185514-1 2009 The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. 3-o 16-19 serpin family C member 1 Homo sapiens 107-123 19185514-1 2009 The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. sulfated 20-28 serpin family C member 1 Homo sapiens 107-123 19185514-1 2009 The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. Glucosamine 29-40 serpin family C member 1 Homo sapiens 107-123 19185514-1 2009 The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. Heparin 53-60 serpin family C member 1 Homo sapiens 107-123 19185514-1 2009 The presence of 3-O-sulfated glucosamine residues in heparin or heparan sulfate plays a role in binding to antithrombin III and HSV infection. Heparitin Sulfate 64-79 serpin family C member 1 Homo sapiens 107-123 19327165-5 2009 RESULTS: Upon normalization of serum testosterone there was an improvement of hyperglycemia, a decrease of leukocytes and of fibrinogen levels, an increase of antithrombin III activity and of tissue oxygen pressure. Testosterone 37-49 serpin family C member 1 Homo sapiens 159-175 19178150-0 2009 Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor. Heparin 22-29 serpin family C member 1 Homo sapiens 156-168 19178150-0 2009 Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor. Heparin 95-102 serpin family C member 1 Homo sapiens 156-168 19178150-1 2009 Heparin accelerates inhibition of factor XIa (fXIa) by the serpins antithrombin (AT) and C1-inhibitor (C1-INH) by more than 2 orders of magnitude. Heparin 0-7 serpin family C member 1 Homo sapiens 67-79 19049827-1 2009 Antithrombin was purified from Bothrops jararaca plasma by affinity chromatography using HiTrap Heparin HP column, and its molecular weight, amino-terminal sequence, carbohydrate content, isoelectric point, inhibition of bovine thrombin, and immunological properties were studied and compared with previously described antithrombins. Carbohydrates 166-178 serpin family C member 1 Homo sapiens 0-12 19049827-2 2009 B. jararaca antithrombin is a single-chain glycoprotein with a total carbohydrate content of 18%. Carbohydrates 69-81 serpin family C member 1 Homo sapiens 12-24 19170587-4 2009 Rivaroxaban is a small molecule directed at active sites, and the agent mechanistically differs from traditional anticoagulants, such as heparins and fondaparinux, in that its activity is independent of antithrombin and its ability to inhibit prothrombinase bound factor Xa. Rivaroxaban 0-11 serpin family C member 1 Homo sapiens 203-215 19010776-1 2009 We have previously shown that residues Tyr-253 and Glu-255 in the serpin antithrombin function as exosites to promote the inhibition of factor Xa and factor IXa when the serpin is conformationally activated by heparin. Tyrosine 39-42 serpin family C member 1 Homo sapiens 73-85 19010776-1 2009 We have previously shown that residues Tyr-253 and Glu-255 in the serpin antithrombin function as exosites to promote the inhibition of factor Xa and factor IXa when the serpin is conformationally activated by heparin. Glutamic Acid 51-54 serpin family C member 1 Homo sapiens 73-85 19010776-1 2009 We have previously shown that residues Tyr-253 and Glu-255 in the serpin antithrombin function as exosites to promote the inhibition of factor Xa and factor IXa when the serpin is conformationally activated by heparin. Heparin 210-217 serpin family C member 1 Homo sapiens 73-85 19010776-5 2009 Mutation of Arg-150 in factor Xa, which interacts with the exosite residues in heparin-activated antithrombin, abrogated the ability of the engineered exosites in alpha1PI to promote factor Xa inhibition. Arginine 12-15 serpin family C member 1 Homo sapiens 97-109 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Arginine 113-121 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Serine 193-199 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Serine 193-199 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Serine 193-199 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 255-262 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 255-262 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 255-262 serpin family C member 1 Homo sapiens 107-112 19689280-4 2009 On the other side, low molecular weight heparins (LMWHs) are too short to be able to form this ternary complex, and mainly exert their anticoagulant effect by binding the factor Xa, always via ATIII. Heparin 40-48 serpin family C member 1 Homo sapiens 193-198 19689280-5 2009 Lastly, the short unique pentasaccharidic sequence which is crucial for heparin"s activity and has been recently synthesized as Fondaparinux, only acts via the formation of the high affinity ternary complex with ATIII-factor Xa. Fondaparinux 128-140 serpin family C member 1 Homo sapiens 212-217 19514602-11 2009 Prophylactic treatment with heparin should be recommended from the very beginning of the following pregnancy in women with antithrombin, protein C or protein S deficiency. Heparin 28-35 serpin family C member 1 Homo sapiens 123-135 19035835-1 2008 A specific pentasaccharide sequence of heparin binds with high affinity to native antithrombin and induces a conformational change in the inhibitor by a previously described two-step interaction mechanism. pentasaccharide 11-26 serpin family C member 1 Homo sapiens 82-94 19035835-1 2008 A specific pentasaccharide sequence of heparin binds with high affinity to native antithrombin and induces a conformational change in the inhibitor by a previously described two-step interaction mechanism. Heparin 39-46 serpin family C member 1 Homo sapiens 82-94 19035835-2 2008 In this work, the interactions of heparin with the antiangiogenic latent and cleaved antithrombin forms were studied. Heparin 34-41 serpin family C member 1 Homo sapiens 85-97 19035835-3 2008 Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin. Heparin 11-18 serpin family C member 1 Homo sapiens 28-40 19035835-3 2008 Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin. Heparin 11-18 serpin family C member 1 Homo sapiens 108-120 19035835-3 2008 Binding of heparin to these antithrombin forms was specific for the same pentasaccharide sequence as native antithrombin. pentasaccharide 73-88 serpin family C member 1 Homo sapiens 28-40 19035835-4 2008 Rapid kinetic studies demonstrated that this pentasaccharide induced a conformational change also in latent and cleaved antithrombin. pentasaccharide 45-60 serpin family C member 1 Homo sapiens 120-132 19035835-5 2008 The binding affinities of these antithrombin forms for the pentasaccharide, as compared to native antithrombin, were approximately 30-fold lower due to two to three fewer ionic interactions, resulting in less stable conformationally altered states. pentasaccharide 59-74 serpin family C member 1 Homo sapiens 32-44 19035835-5 2008 The binding affinities of these antithrombin forms for the pentasaccharide, as compared to native antithrombin, were approximately 30-fold lower due to two to three fewer ionic interactions, resulting in less stable conformationally altered states. pentasaccharide 59-74 serpin family C member 1 Homo sapiens 98-110 19320820-2 2009 OBJECTIVES: The purpose of this study was to investigate the mechanism of the intracellular signaling activities of AT using wild-type and mutant serpins that have reduced anticoagulant activities due to mutations in either the reactive center loop (RCL) or the heparin-binding site. Heparin 262-269 serpin family C member 1 Homo sapiens 116-118 19320820-7 2009 The heparin-binding site mutants, AT-K114E and AT-K125E, did not exhibit any protective activity in either one of these assays, but a potent pro-apoptotic activity was observed for the AT-K114E in endothelial cells. Heparin 4-11 serpin family C member 1 Homo sapiens 34-36 19320820-9 2009 CONCLUSIONS: The interaction of AT with syndecan-4 is required for its prostacyclin-dependent protective effect through a PTX-sensitive and non-S1P(1)-related G(i)-protein coupled receptor. Epoprostenol 71-83 serpin family C member 1 Homo sapiens 32-34 19275167-1 2009 The recently arising antithrombin drug, angiomax, was successfully conjugated with a 5"-amino oligonucleotide through click chemistry. 5"-amino oligonucleotide 85-109 serpin family C member 1 Homo sapiens 21-33 19452598-0 2009 The critical role of hinge-region expulsion in the induced-fit heparin binding mechanism of antithrombin. Heparin 63-70 serpin family C member 1 Homo sapiens 92-104 18306296-3 2009 Such an inhibitor is antithrombin, the effect of which may be enhanced with heparin. Heparin 76-83 serpin family C member 1 Homo sapiens 21-33 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 24-31 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 24-31 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 24-31 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 33-36 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 33-36 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Heparin 33-36 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Lysine 53-59 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Lysine 53-59 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Lysine 53-59 serpin family C member 1 Homo sapiens 107-112 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Arginine 113-121 serpin family C member 1 Homo sapiens 47-52 19689280-3 2009 In fact, unfractionated heparin (UFH) binds to ATIII lysine site leading to a conformational change of the ATIII arginine reactive centre able to create a covalent binding to the active centre serine of thrombin in a ternary complex formation composed by heparin, ATIII and thrombin. Arginine 113-121 serpin family C member 1 Homo sapiens 107-112 19035835-6 2008 Affinities of latent and cleaved antithrombin for longer heparin chains, containing the pentasaccharide sequence, were 2-fold lower than for the pentasaccharide itself. pentasaccharide 145-160 serpin family C member 1 Homo sapiens 33-45 19035835-7 2008 This contrasts the interaction with native antithrombin and demonstrates that residues flanking the pentasaccharide sequence of heparin are repelled by the latent and cleaved forms. pentasaccharide 100-115 serpin family C member 1 Homo sapiens 43-55 19035835-7 2008 This contrasts the interaction with native antithrombin and demonstrates that residues flanking the pentasaccharide sequence of heparin are repelled by the latent and cleaved forms. Heparin 128-135 serpin family C member 1 Homo sapiens 43-55 19035835-8 2008 These findings contribute to delineating the mechanism by which heparin or heparan sulfate mediates antiangiogenic activity of antithrombin. Heparin 64-71 serpin family C member 1 Homo sapiens 127-139 19035835-8 2008 These findings contribute to delineating the mechanism by which heparin or heparan sulfate mediates antiangiogenic activity of antithrombin. Heparitin Sulfate 75-90 serpin family C member 1 Homo sapiens 127-139 18761723-0 2008 Heparan sulfates from arteries and veins differ in their antithrombin-mediated anticoagulant activity. Heparitin Sulfate 0-16 serpin family C member 1 Homo sapiens 57-69 18722996-4 2008 This on-chip signal amplification platform was successfully demonstrated by probing the heparin microarray with the highly specific heparin-binding protein antithrombin III (AT III). Heparin 88-95 serpin family C member 1 Homo sapiens 156-172 18722996-4 2008 This on-chip signal amplification platform was successfully demonstrated by probing the heparin microarray with the highly specific heparin-binding protein antithrombin III (AT III). Heparin 88-95 serpin family C member 1 Homo sapiens 174-180 18832918-2 2008 Specifically, activated coagulation time values are obtained with devices that utilize contact protein activators to generate thrombin and assess the efficacy of heparin-mediated antithrombin activation, with an activated coagulation time value of 480 s considered "safe". Heparin 162-169 serpin family C member 1 Homo sapiens 179-191 18669628-1 2008 Anticoagulant heparan sulfate proteoglycans bind and activate antithrombin by virtue of a specific 3-O-sulfated pentasaccharide. 3-o-sulfated pentasaccharide 99-127 serpin family C member 1 Homo sapiens 62-74 18669628-8 2008 Heparan sulfate chains were fractionated according to their affinity for antithrombin, and their structure was analyzed by 1H NMR and MS/MS. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 73-85 18669628-10 2008 These antithrombin-binding chains contain more than 6% 3-O-sulfated glucosamine residues, convey an anticoagulant activity of 2.5 IU/ml to human follicular fluid, and have an anti-Factor Xa specific activity of 167 IU/mg. Glucosamine 68-79 serpin family C member 1 Homo sapiens 6-18 18806070-0 2008 Does preoperative level of antithrombin III predict heparin resistance during extracorporeal circulation? Heparin 52-59 serpin family C member 1 Homo sapiens 27-43 18558097-4 2008 Our results indicate the following: 1) both the sulfated galactan and heparin potentiate protease inactivation by antithrombin at similar molar concentrations, however they differ markedly in the molecular size required for their activities; 2) this galactan interacts predominantly with exosite II on alpha-thrombin and, similar to heparin, catalyzes the formation of a covalent complex between antithrombin and the protease; 3) the sulfated galactan has a higher affinity for alpha-thrombin than for antithrombin. Galactans 57-65 serpin family C member 1 Homo sapiens 114-126 18691229-9 2008 Beriplex P/N showed the greatest capacity for thrombin inhibition, a reflection of the observed high levels of the coagulation inhibitors protein C, protein S, protein Z, and small amounts of antithrombin III and heparin in this product. beriplex p 0-10 serpin family C member 1 Homo sapiens 192-208 18691229-9 2008 Beriplex P/N showed the greatest capacity for thrombin inhibition, a reflection of the observed high levels of the coagulation inhibitors protein C, protein S, protein Z, and small amounts of antithrombin III and heparin in this product. Nitrogen 11-12 serpin family C member 1 Homo sapiens 192-208 18698082-7 2008 A reduced dexamethasone related increase of antithrombin and protein S, and subsequent decline below normal levels after introduction of asparaginase, may result in a hypercoagulable state, contributing to development of symptomatic osteonecrosis. Dexamethasone 10-23 serpin family C member 1 Homo sapiens 44-56 18640975-0 2008 Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction. octasaccharides 21-36 serpin family C member 1 Homo sapiens 0-12 18640975-0 2008 Antithrombin-binding octasaccharides and role of extensions of the active pentasaccharide sequence in the specificity and strength of interaction. pentasaccharide 74-89 serpin family C member 1 Homo sapiens 0-12 18640975-2 2008 The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)). Heparin 52-60 serpin family C member 1 Homo sapiens 100-112 18640975-2 2008 The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)). pentasaccharide 126-141 serpin family C member 1 Homo sapiens 100-112 18640975-2 2008 The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)). Glucosamine 161-165 serpin family C member 1 Homo sapiens 100-112 18640975-2 2008 The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)). Glucuronic Acid 177-181 serpin family C member 1 Homo sapiens 100-112 18640975-2 2008 The antithrombotic activity of low molecular weight heparins (LMWHs) is largely associated with the antithrombin (AT)-binding pentasaccharide sequence AGA(*)IA (GlcN(NAc/NS,6S)-GlcA-GlcN(NS,3,6S)-IdoUA(2S)-GlcN(NS,6S)). idoua 196-201 serpin family C member 1 Homo sapiens 100-112 18558097-7 2008 Finally, the antithrombin-alpha-thrombin covalent complex dissociates from the polysaccharide chain. Polysaccharides 79-93 serpin family C member 1 Homo sapiens 13-25 18558097-8 2008 This mechanism resembles the action of heparin with low affinity for antithrombin, as opposed to heparin with high affinity for serpin. Heparin 39-46 serpin family C member 1 Homo sapiens 69-81 18558097-4 2008 Our results indicate the following: 1) both the sulfated galactan and heparin potentiate protease inactivation by antithrombin at similar molar concentrations, however they differ markedly in the molecular size required for their activities; 2) this galactan interacts predominantly with exosite II on alpha-thrombin and, similar to heparin, catalyzes the formation of a covalent complex between antithrombin and the protease; 3) the sulfated galactan has a higher affinity for alpha-thrombin than for antithrombin. Galactans 57-65 serpin family C member 1 Homo sapiens 396-408 18558097-4 2008 Our results indicate the following: 1) both the sulfated galactan and heparin potentiate protease inactivation by antithrombin at similar molar concentrations, however they differ markedly in the molecular size required for their activities; 2) this galactan interacts predominantly with exosite II on alpha-thrombin and, similar to heparin, catalyzes the formation of a covalent complex between antithrombin and the protease; 3) the sulfated galactan has a higher affinity for alpha-thrombin than for antithrombin. Galactans 57-65 serpin family C member 1 Homo sapiens 396-408 18558097-5 2008 We propose that the preferred pathway of sulfated galactan-induced inactivation of alpha-thrombin by antithrombin starts with the polysaccharide binding to the protease through a high-affinity interaction. Galactans 50-58 serpin family C member 1 Homo sapiens 101-113 18558097-5 2008 We propose that the preferred pathway of sulfated galactan-induced inactivation of alpha-thrombin by antithrombin starts with the polysaccharide binding to the protease through a high-affinity interaction. Polysaccharides 130-144 serpin family C member 1 Homo sapiens 101-113 18433074-0 2008 Conjugation of ATIII-binding pentasaccharides to extend the half-life of proteins: long-acting insulin. pentasaccharides 29-45 serpin family C member 1 Homo sapiens 15-20 18695376-4 2008 RECENT FINDINGS: Fondaparinux is a synthetic pentasaccharide, which binds to antithrombin, thereby indirectly inhibiting factor Xa. pentasaccharide 45-60 serpin family C member 1 Homo sapiens 77-89 18022801-9 2008 After the heparin was immobilized on the BA-PEG-grafted 316L SS surface by SP, the surface showed an improvement in antithrombrin III (AT III) binding ability, its anticoagulant property, and hemocompatibility in comparison with heparin grafted by 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide. Heparin 10-17 serpin family C member 1 Homo sapiens 116-133 18022801-9 2008 After the heparin was immobilized on the BA-PEG-grafted 316L SS surface by SP, the surface showed an improvement in antithrombrin III (AT III) binding ability, its anticoagulant property, and hemocompatibility in comparison with heparin grafted by 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide. Heparin 10-17 serpin family C member 1 Homo sapiens 135-141 18022801-9 2008 After the heparin was immobilized on the BA-PEG-grafted 316L SS surface by SP, the surface showed an improvement in antithrombrin III (AT III) binding ability, its anticoagulant property, and hemocompatibility in comparison with heparin grafted by 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide. ba-peg 41-47 serpin family C member 1 Homo sapiens 116-133 18022801-9 2008 After the heparin was immobilized on the BA-PEG-grafted 316L SS surface by SP, the surface showed an improvement in antithrombrin III (AT III) binding ability, its anticoagulant property, and hemocompatibility in comparison with heparin grafted by 1-ethyl-3-(3-dimethyl-aminopropyl) carbodiimide. ba-peg 41-47 serpin family C member 1 Homo sapiens 135-141 18041724-3 2008 The coatings containing heparin were tested for their ability to potentiate thrombin inhibition by antithrombin and its dependence on the layer arrangement. Heparin 24-31 serpin family C member 1 Homo sapiens 99-111 18447601-1 2008 BACKGROUND: Idraparinux is a synthetic pentasaccharide that binds to antithrombin with high affinity. pentasaccharide 39-54 serpin family C member 1 Homo sapiens 69-81 18541230-0 2008 Protective effects of antithrombin on puromycin aminonucleoside nephrosis in rats. Puromycin 38-47 serpin family C member 1 Homo sapiens 22-34 18541230-1 2008 We investigated the effects of antithrombin, a plasma inhibitor of coagulation factors, in rats with puromycin aminonucleoside-induced nephrosis, which is an experimental model of human nephrotic syndrome. Puromycin Aminonucleoside 101-126 serpin family C member 1 Homo sapiens 31-43 18541230-4 2008 Treatment with antithrombin attenuated the puromycin aminonucleoside-induced hematological abnormalities. Puromycin Aminonucleoside 43-68 serpin family C member 1 Homo sapiens 15-27 18541230-7 2008 In addition, antithrombin treatment markedly suppressed puromycin aminonucleoside-induced apoptosis of renal tubular epithelial cells. Puromycin Aminonucleoside 56-81 serpin family C member 1 Homo sapiens 13-25 18498854-1 2008 Heparin resistance occurs in up to 22% of patients undergoing cardiac surgery requiring cardiopulmonary bypass and it is associated with decreased levels of antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 157-169 18498854-2 2008 Treatment options for heparin resistance include administration of antithrombin or fresh frozen plasma. Heparin 22-29 serpin family C member 1 Homo sapiens 67-79 18498854-4 2008 Thus, the aim of this review is to discuss the limited number of published reports assessing antithrombin or fresh frozen plasma in managing heparin resistance and to present emerging data regarding fresh frozen plasma safety issues and practical considerations for antithrombin treatment in patients with heparin resistance undergoing cardiopulmonary bypass. Heparin 141-148 serpin family C member 1 Homo sapiens 93-105 18574264-2 2008 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors. Heparin 0-3 serpin family C member 1 Homo sapiens 66-78 18574264-2 2008 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 66-78 18574264-2 2008 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a unique pentasaccharide sequence and catalyze the inactivation of thrombin factor Xa and other clotting factors. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 66-78 18574264-8 2008 Fondaparinux, a synthetic pentasaccharide, catalyzes the inhibition of factor Xa, but not thrombin, in an antithrombin-dependent fashion. pentasaccharide 26-41 serpin family C member 1 Homo sapiens 106-118 18273869-7 2008 Antithrombin deficiency correlated with underlying malignancy, donor HLA-mismatch, and TBI, whereas decreased PC activity demonstrated a trend of association with lack of T-cell depletion and TBI. Thioacetazone 87-90 serpin family C member 1 Homo sapiens 0-12 18452898-1 2008 2-O-Sulfo-alpha-l-iduronic acid (IdoA2S) is one of the main components of heparin, an anticoagulant and antithrombotic polysaccharide able to potentiate the inhibitory effect of antithrombin over plasma serine proteases. iminodisuccinic acid 0-31 serpin family C member 1 Homo sapiens 178-190 18452898-1 2008 2-O-Sulfo-alpha-l-iduronic acid (IdoA2S) is one of the main components of heparin, an anticoagulant and antithrombotic polysaccharide able to potentiate the inhibitory effect of antithrombin over plasma serine proteases. idoa2s 33-39 serpin family C member 1 Homo sapiens 178-190 18452898-1 2008 2-O-Sulfo-alpha-l-iduronic acid (IdoA2S) is one of the main components of heparin, an anticoagulant and antithrombotic polysaccharide able to potentiate the inhibitory effect of antithrombin over plasma serine proteases. Heparin 74-81 serpin family C member 1 Homo sapiens 178-190 18452898-1 2008 2-O-Sulfo-alpha-l-iduronic acid (IdoA2S) is one of the main components of heparin, an anticoagulant and antithrombotic polysaccharide able to potentiate the inhibitory effect of antithrombin over plasma serine proteases. Polysaccharides 119-133 serpin family C member 1 Homo sapiens 178-190 18570058-8 2008 We found an increase in AT-III in men receiving E(2) which may be related to gonadal steroid withdrawal, but no significant differences in other inflammatory or clotting factor parameters. Steroids 85-92 serpin family C member 1 Homo sapiens 24-30 18574277-8 2008 In addition to aspirin and other antiplatelet therapies, we recommend the use of antithrombin therapy (eg, unfractionated heparin (UFH), enoxaparin, or fondaparinux) over no antithrombin therapy (Grade 1A), including for those patients receiving fibrinolysis (and regardless of which lytic agent is administered), primary PCI, or patients not receiving reperfusion therapy. Heparin 122-129 serpin family C member 1 Homo sapiens 81-93 18574277-8 2008 In addition to aspirin and other antiplatelet therapies, we recommend the use of antithrombin therapy (eg, unfractionated heparin (UFH), enoxaparin, or fondaparinux) over no antithrombin therapy (Grade 1A), including for those patients receiving fibrinolysis (and regardless of which lytic agent is administered), primary PCI, or patients not receiving reperfusion therapy. Heparin 131-134 serpin family C member 1 Homo sapiens 81-93 18375953-5 2008 Here, we show that the previously characterized prelatent antithrombin is a mixture of native antithrombin and a modified, true prelatent antithrombin that are resolvable by heparin-agarose chromatography. Heparin 174-181 serpin family C member 1 Homo sapiens 58-70 18375953-5 2008 Here, we show that the previously characterized prelatent antithrombin is a mixture of native antithrombin and a modified, true prelatent antithrombin that are resolvable by heparin-agarose chromatography. Sepharose 182-189 serpin family C member 1 Homo sapiens 58-70 18375953-7 2008 Purified prelatent antithrombin had reduced anticoagulant function compared with native antithrombin, due to a reduced heparin affinity and consequent impaired ability of heparin to either bridge prelatent antithrombin and coagulation proteases in a ternary complex or to induce full conformational activation of the serpin. Heparin 119-126 serpin family C member 1 Homo sapiens 19-31 18375953-7 2008 Purified prelatent antithrombin had reduced anticoagulant function compared with native antithrombin, due to a reduced heparin affinity and consequent impaired ability of heparin to either bridge prelatent antithrombin and coagulation proteases in a ternary complex or to induce full conformational activation of the serpin. Heparin 171-178 serpin family C member 1 Homo sapiens 19-31 18375953-9 2008 The prelatent form was conformationally altered from native antithrombin as judged from an attenuation of tryptophan fluorescence changes following heparin activation and a reduced thermal stability. Tryptophan 106-116 serpin family C member 1 Homo sapiens 60-72 18375953-9 2008 The prelatent form was conformationally altered from native antithrombin as judged from an attenuation of tryptophan fluorescence changes following heparin activation and a reduced thermal stability. Heparin 148-155 serpin family C member 1 Homo sapiens 60-72 18720820-7 2008 The result showed that the resonance scattering intensity at 491 nm (I(RS)) is linear to the AT-III concentration in the range of 62.5 to 850 ng x mL(-1), under the optimum conditions of 0.30 mL goat-anti-human AT-III antibody, 30 mg x mL(-1) polyethelene glycol-6000, being incubated at 37 degrees C for 15 min, the voltage at 400 V, and the excitation and emission slit width both at 5.0 nm. polyethelene glycol-6000 243-267 serpin family C member 1 Homo sapiens 93-99 18393915-3 2008 Fondaparinux is a relative new pharmacological agent that selectively binds to antithrombin, and represents a new class of synthetic selective inhibitors of activated factor X. Eleven percent of the fondaparinux-related English language literature, between 2001 and 2007, refers to orthopaedic trauma, and was the sample assessed for this critical analysis review. Fondaparinux 0-12 serpin family C member 1 Homo sapiens 79-91 18345636-8 2008 Binding characteristics of the neutral resins for the natural anticoagulants protein C and antithrombin showed remarkable differences, with weak binding of antithrombin but strong removal of protein C, not only for the anion exchanger, but also for neutral polymers of the large pore size range. Polymers 257-265 serpin family C member 1 Homo sapiens 91-103 18082175-8 2008 Compared with the directly immobilized large nanogold particles, the in situ grown particles with the same size occupy more sensor surface, resulting in higher frequency shifts to AT III in the interaction study between heparin and AT III. Heparin 220-227 serpin family C member 1 Homo sapiens 232-238 18260648-0 2008 Characterization of heparin oligosaccharides binding specifically to antithrombin III using mass spectrometry. heparin oligosaccharides 20-44 serpin family C member 1 Homo sapiens 69-85 18260648-4 2008 Here we describe a hydrophobic trapping assay for screening a library of heparin hexasaccharides for binders to antithrombin III (ATIII). heparin hexasaccharides 73-96 serpin family C member 1 Homo sapiens 112-128 18260648-4 2008 Here we describe a hydrophobic trapping assay for screening a library of heparin hexasaccharides for binders to antithrombin III (ATIII). heparin hexasaccharides 73-96 serpin family C member 1 Homo sapiens 130-135 18260648-8 2008 The specificity of the hexasaccharides binding ATIII was confirmed by assaying their ability to enhance ATIII-mediated inhibition of Factor Xa in vitro. hexasaccharides 23-38 serpin family C member 1 Homo sapiens 47-52 18260648-8 2008 The specificity of the hexasaccharides binding ATIII was confirmed by assaying their ability to enhance ATIII-mediated inhibition of Factor Xa in vitro. hexasaccharides 23-38 serpin family C member 1 Homo sapiens 104-109 18160297-2 2008 In this study, we investigated their interactions with synthetic heparin-binding peptides, derived from human antithrombin III (hAT III) and heparin-interacting protein (HIP), using surface noncovalent affinity mass spectrometry. Heparin 65-72 serpin family C member 1 Homo sapiens 110-126 18160297-2 2008 In this study, we investigated their interactions with synthetic heparin-binding peptides, derived from human antithrombin III (hAT III) and heparin-interacting protein (HIP), using surface noncovalent affinity mass spectrometry. Heparin 65-72 serpin family C member 1 Homo sapiens 128-135 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. Heparin 40-47 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. oligo 73-78 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. tyrosine O-sulfate 79-95 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. oligo 150-155 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. tyrosine O-sulfate 156-172 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. Heparin 222-229 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. hexasaccharide 238-252 serpin family C member 1 Homo sapiens 183-190 18160297-3 2008 We compared binding affinities to those heparin-binding peptides between oligo(tyrosine sulfate)s and several known sulfated compounds and found that oligo(tyrosine sulfate)s bind to hAT III (123-139) more strongly than a heparin-derived hexasaccharide dp6. 5-diphosphomevalonic acid 253-256 serpin family C member 1 Homo sapiens 183-190 18160297-4 2008 Moreover, we found longer oligo(tyrosine sulfate) has higher binding affinity to hAT III (123-139). tyrosine O-sulfate 32-48 serpin family C member 1 Homo sapiens 81-88 18082175-0 2008 In situ growth of nanogold on quartz crystal microbalance and its application in the interaction between heparin and antithrombin III. Heparin 105-112 serpin family C member 1 Homo sapiens 117-133 18082175-7 2008 After that, both the immobilized amount of heparin and the sensor response to AT III decreased gradually. Heparin 43-50 serpin family C member 1 Homo sapiens 78-84 18082175-8 2008 Compared with the directly immobilized large nanogold particles, the in situ grown particles with the same size occupy more sensor surface, resulting in higher frequency shifts to AT III in the interaction study between heparin and AT III. Heparin 220-227 serpin family C member 1 Homo sapiens 180-186 18082175-9 2008 The obtained constants of AT III binding to immobilized heparin are k(ass)=(1.65+/-0.12)x10(3) L/mols, k diss=(2.63+/-0.18)x10(-2) 1/s and K(A)=(6.27+/-0.42)x10(4) L/mol. Heparin 56-63 serpin family C member 1 Homo sapiens 26-32 18195690-0 2008 Inhibition of proteasome by bortezomib causes intracellular aggregation of hepatic serpins and increases the latent circulating form of antithrombin. Bortezomib 28-38 serpin family C member 1 Homo sapiens 136-148 18195690-13 2008 Finally, bortezomib had only minor effects on the mature circulating antithrombin, with increased amounts of latent antithrombin in plasma. Bortezomib 9-19 serpin family C member 1 Homo sapiens 116-128 18055456-6 2008 Previous studies demonstrated that heparin heightens the affinity of thrombin for fibrin by simultaneously binding to fibrin and exosite 2 on thrombin to generate a ternary heparin-thrombin-fibrin complex that protects thrombin from inhibition by antithrombin and heparin cofactor II. Heparin 35-42 serpin family C member 1 Homo sapiens 247-259 18206177-0 2008 Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine. Acrolein 38-46 serpin family C member 1 Homo sapiens 0-12 18206177-0 2008 Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine. Homocysteine 51-63 serpin family C member 1 Homo sapiens 0-12 18206177-0 2008 Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine. Thiolactone 64-75 serpin family C member 1 Homo sapiens 0-12 18206177-0 2008 Antithrombin activity is inhibited by acrolein and homocysteine thiolactone: Protection by cysteine. Cysteine 55-63 serpin family C member 1 Homo sapiens 0-12 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. Heparin 98-105 serpin family C member 1 Homo sapiens 0-12 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. Heparin 98-105 serpin family C member 1 Homo sapiens 236-248 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. Lysine 157-160 serpin family C member 1 Homo sapiens 0-12 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. Acrolein 192-200 serpin family C member 1 Homo sapiens 0-12 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. Acrolein 192-200 serpin family C member 1 Homo sapiens 236-248 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. homocysteine thiolactone 204-228 serpin family C member 1 Homo sapiens 0-12 18206177-3 2008 Antithrombin is one of the most important inhibitors of blood coagulation Since its activation by heparin binding requires critical interactions involving 3 Lys residues; we hypothesized that acrolein or homocysteine thiolactone impair antithrombin activity. homocysteine thiolactone 204-228 serpin family C member 1 Homo sapiens 236-248 18206177-4 2008 When we incubated human antithrombin with increasing concentrations of acrolein (0-2 mmol/L) over a short period of time (0-4 h), a time and concentration dependent loss of activity was apparent (IC(50)=0.25 mmol/L). Acrolein 71-79 serpin family C member 1 Homo sapiens 24-36 18206177-7 2008 When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost. Acrolein 40-48 serpin family C member 1 Homo sapiens 5-17 18206177-7 2008 When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost. Acrolein 40-48 serpin family C member 1 Homo sapiens 85-97 18206177-7 2008 When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost. Cysteine 53-61 serpin family C member 1 Homo sapiens 5-17 18206177-7 2008 When antithrombin was co-incubated with acrolein and cysteine, only less than 10% of antithrombin activity was lost. Cysteine 53-61 serpin family C member 1 Homo sapiens 85-97 18278163-6 2008 They share a common mechanism of action together with the endogenous antithrombotic heparan sulfate, i.e. the catalysis of the antithrombin-mediated inhibition of factor Xa. Heparitin Sulfate 84-99 serpin family C member 1 Homo sapiens 127-139 18327412-2 2008 In these patients, exogenous AT may be used in association with heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 29-31 17909966-2 2008 A specific pentasaccharide in heparinoids activates antithrombin III, resulting in inactivation of factor Xa and-when additional saccharides are present-inactivation of factor IIa. pentasaccharide 11-26 serpin family C member 1 Homo sapiens 52-68 17909966-2 2008 A specific pentasaccharide in heparinoids activates antithrombin III, resulting in inactivation of factor Xa and-when additional saccharides are present-inactivation of factor IIa. Heparinoids 30-41 serpin family C member 1 Homo sapiens 52-68 18065202-7 2008 RESULTS: The levels of hemostatic variables did not change significantly throughout the study in the isoflavone group; however, the isoflavone group showed a statistically significant reduction in plasma concentration of prothrombin fragments 1 plus 2; both groups showed a statistically significant reduction in antithrombin, protein C, and free protein S levels. Isoflavones 132-142 serpin family C member 1 Homo sapiens 313-325 18226138-1 2008 We present a case of a pregnant woman with hereditary antithrombin III deficiency and deep vein thrombosis of the left lower extremity managed by perinatal unfractionated heparin injection with antithrombin III replacement as well as by intrapartum placement of a temporary inferior vena cava filter. Heparin 171-178 serpin family C member 1 Homo sapiens 54-70 18303934-4 2008 Although unfractionated heparin (UFH) has been the mainstay of antithrombin therapy in the past, it has numerous clinical and biochemical limitations, including substantial protein binding (leading to inconsistent bioavailability), a need for frequent monitoring and adjustment, unreliable and variable degrees of anticoagulation, significant platelet activation, risk of heparin-induced thrombocytopenia, and the inability to block clot bound thrombin. Heparin 24-31 serpin family C member 1 Homo sapiens 63-75 18303934-4 2008 Although unfractionated heparin (UFH) has been the mainstay of antithrombin therapy in the past, it has numerous clinical and biochemical limitations, including substantial protein binding (leading to inconsistent bioavailability), a need for frequent monitoring and adjustment, unreliable and variable degrees of anticoagulation, significant platelet activation, risk of heparin-induced thrombocytopenia, and the inability to block clot bound thrombin. Heparin 33-36 serpin family C member 1 Homo sapiens 63-75 17996279-5 2008 Pentasaccharides are synthetic drugs that accelerate the interaction between factor Xa and antithrombin but selectively inhibit factor Xa activity. pentasaccharides 0-16 serpin family C member 1 Homo sapiens 91-103 18184032-1 2008 Fondaparinux is a synthetic pentasaccharide that inhibits thrombin formation and thrombus development via selective antithrombin mediated inhibition of factor Xa. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 116-128 22275964-9 2008 Antithrombin-III showed a 4% borderline significant reduction in the fenretinide arm relative to placebo, irrespective of the HRT administration route (p = 0.055). Fenretinide 69-80 serpin family C member 1 Homo sapiens 0-16 18560242-1 2008 BACKGROUND/AIMS: Argatroban, a hepatically metabolized direct thrombin inhibitor, is approved for use in heparin-induced thrombocytopenia (HIT; several countries) and in antithrombin-deficient patients undergoing hemodialysis (Japan). argatroban 17-27 serpin family C member 1 Homo sapiens 170-182 18560242-3 2008 METHODS: A literature search identified 34 publications (12 prospective studies, 4 retrospective studies, 18 anecdotal reports) that together described 644 argatroban-treated patients (446 with HIT, 82 with antithrombin deficiency) with varying degrees of renal function. argatroban 156-166 serpin family C member 1 Homo sapiens 207-219 18560242-9 2008 CONCLUSION: Current literature suggests that argatroban is well tolerated and provides adequate anticoagulation in patients with renal dysfunction or failure, including individuals with HIT or antithrombin deficiency where anticoagulant options are limited. argatroban 45-55 serpin family C member 1 Homo sapiens 193-205 17875649-1 2007 Heparin activates the serpin, antithrombin, to inhibit its target blood-clotting proteases by generating new protease interaction exosites. Heparin 0-7 serpin family C member 1 Homo sapiens 30-42 17875649-4 2007 Equilibrium binding of NBD-labeled antithrombins to S195A proteases showed that exosites generated by conformationally activating antithrombin with a heparin pentasaccharide enhanced the affinity of the serpin for S195A factor Xa minimally 100-fold. IC 831423 150-173 serpin family C member 1 Homo sapiens 35-47 17875649-8 2007 Together these results show that exosites generated by heparin activation of antithrombin function both to promote the formation of an initial antithrombin-protease Michaelis complex and to favor the subsequent acylation of this complex. Heparin 55-62 serpin family C member 1 Homo sapiens 77-89 17875649-8 2007 Together these results show that exosites generated by heparin activation of antithrombin function both to promote the formation of an initial antithrombin-protease Michaelis complex and to favor the subsequent acylation of this complex. Heparin 55-62 serpin family C member 1 Homo sapiens 143-155 18284938-0 2008 Heparin and low molecular weight heparins as scaffolds for assembling antithrombin and serine proteases. Heparin 0-7 serpin family C member 1 Homo sapiens 70-82 18284938-0 2008 Heparin and low molecular weight heparins as scaffolds for assembling antithrombin and serine proteases. Heparin 33-41 serpin family C member 1 Homo sapiens 70-82 17584894-6 2007 SDS-PAGE showed that OTR4120 induced the formation of covalently linked complexes between antithrombin III or heparin cofactor II and thrombin. Sodium Dodecyl Sulfate 0-3 serpin family C member 1 Homo sapiens 90-106 18085394-10 2007 There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis. Heparin 74-81 serpin family C member 1 Homo sapiens 33-49 18085394-10 2007 There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis. Heparin 74-81 serpin family C member 1 Homo sapiens 51-56 18085394-10 2007 There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis. Heparin 133-140 serpin family C member 1 Homo sapiens 33-49 18085394-10 2007 There may have been a deficit of antithrombin III (ATIII) - a cofactor of heparin - because of the proteinuria; thus, the continuous heparin treatment might not have been effective for the prevention of thrombosis. Heparin 133-140 serpin family C member 1 Homo sapiens 51-56 18220975-7 2007 Chemical modification of the natural or synthetic heparin increased factor activation of AT III Xa affinity. Heparin 50-57 serpin family C member 1 Homo sapiens 89-95 17621651-0 2007 Macroscopic thrombus formation on angioplasty equipment following antithrombin therapy with enoxaparin. Enoxaparin 92-102 serpin family C member 1 Homo sapiens 66-78 17621651-2 2007 We evaluated the incidence and consequences of periprocedural macroscopic thrombus formation on PCI equipment following antithrombin therapy with enoxaparin. Enoxaparin 146-156 serpin family C member 1 Homo sapiens 120-132 17621651-3 2007 Between April 2003 and December 2004, all patients undergoing cardiac catheterization following antithrombin therapy with enoxaparin were evaluated. Enoxaparin 122-132 serpin family C member 1 Homo sapiens 96-108 17621651-11 2007 Percutaneous coronary intervention following antithrombin therapy with enoxaparin is associated with a 5% incidence of macroscopic thrombus formation on PCI equipment. Enoxaparin 71-81 serpin family C member 1 Homo sapiens 45-57 17621651-13 2007 Our findings suggest that the safety of antithrombin therapy with low molecular weight heparin during PCI requires further evaluation. Heparin 87-94 serpin family C member 1 Homo sapiens 40-52 17907113-5 2007 Pioglitazone significantly (p < or = 0.001) decreased circulating levels of von Willebrand factor (-9.7%, -9.4%) and plasminogen activator inhibitor-1 (-16.8 ng/ml, -12.3 ng/ml), and increased levels of antithrombin-III (+1.3 mg/dL, +1.5 mg/dL) after six and 12 months, respectively. Pioglitazone 0-12 serpin family C member 1 Homo sapiens 206-222 17879089-0 2007 Comparison of planar SDS-PAGE, CGE-on-a-chip, and MALDI-TOF mass spectrometry for analysis of the enzymatic de-N-glycosylation of antithrombin III and coagulation factor IX with PNGase F. Three different analytical techniques (planar SDS-PAGE, CGE-on-a-chip and MALDI-TOF-MS) applied for determination of the molecular weight of intact and partly and completely de-N-glycosylated human serum glycoproteins (antithrombin III and coagulation factor IX) have been compared. Sodium Dodecyl Sulfate 234-237 serpin family C member 1 Homo sapiens 130-146 18663937-1 2007 For the first time it is proved, that patients with an acute virus myocarditis have statistically confirmed authentic reduction in quantity of thrombocytes, extention of parameters of a activated partial thrombin time, reduction in concentration of a heparin-antithrombin III (AT-III) complex against suppressed enzyme of antiradical protection - superoxide dismutase and it has led to activization of a malonic dialdehyde in erythrocytes, thrombocytes and blood serum. Malondialdehyde 404-422 serpin family C member 1 Homo sapiens 251-275 17577134-8 2007 Decreases in antithrombin III, platelet count and fibrinogen levels, prolongation of prothrombin time, and increases in the plasma fibrin degradation products were significantly suppressed by the administration of methylprednisolone. Methylprednisolone 214-232 serpin family C member 1 Homo sapiens 13-29 17884631-7 2007 We discovered that polysaccharides without the iduronic acid residue displayed strong binding affinity to antithrombin and high anti-Xa and anti-IIa activities. Polysaccharides 19-34 serpin family C member 1 Homo sapiens 106-118 17884631-7 2007 We discovered that polysaccharides without the iduronic acid residue displayed strong binding affinity to antithrombin and high anti-Xa and anti-IIa activities. Iduronic Acid 47-60 serpin family C member 1 Homo sapiens 106-118 17890948-1 2007 Fondaparinux is a new anticoagulant that interacts with antithrombin III and activated coagulation factor X resulting in an inhibition of the coagulation system. Fondaparinux 0-12 serpin family C member 1 Homo sapiens 56-72 17912162-8 2007 The antithrombin agents, unfractionated heparin, low molecular weight (LMW) heparin, Xa inhibitors, and direct thrombin antagonists, act specifically to target thrombin generation, thrombin activity, or both. Heparin 76-83 serpin family C member 1 Homo sapiens 4-16 17709798-7 2007 Tamoxifen increased IGFBP-3 and lowered antithrombin-III, C reactive protein, and mammographic density, with greater effects of 5 mg/day. Tamoxifen 0-9 serpin family C member 1 Homo sapiens 40-56 17492649-6 2007 We further studied the heparin cofactor activity and the binding to heparin of each recombinant AT molecule. Heparin 23-30 serpin family C member 1 Homo sapiens 96-98 17600038-8 2007 CONCLUSIONS: When compared with UFH, enoxaparin was associated with superior efficacy as adjunctive antithrombin therapy among >49 000 patients across the ACS spectrum. Enoxaparin 37-47 serpin family C member 1 Homo sapiens 100-112 17849067-0 2007 Report of a novel kindred with antithrombin heparin-binding site variant (47 Arg to His): demand for an automated progressive antithrombin assay to detect molecular variants with low thrombotic risk. Heparin 44-51 serpin family C member 1 Homo sapiens 31-43 17849067-0 2007 Report of a novel kindred with antithrombin heparin-binding site variant (47 Arg to His): demand for an automated progressive antithrombin assay to detect molecular variants with low thrombotic risk. Heparin 44-51 serpin family C member 1 Homo sapiens 126-138 17492649-8 2007 In contrast, we found that Ala59Val mutant AT unexpectedly showed a normal affinity to heparin, but severely impaired the heparin cofactor activity. Heparin 87-94 serpin family C member 1 Homo sapiens 43-45 17536781-0 2007 Frontal analysis capillary electrophoresis hyphenated to electrospray ionization mass spectrometry for the characterization of the antithrombin/heparin pentasaccharide complex. Heparin 144-151 serpin family C member 1 Homo sapiens 131-143 17536781-0 2007 Frontal analysis capillary electrophoresis hyphenated to electrospray ionization mass spectrometry for the characterization of the antithrombin/heparin pentasaccharide complex. pentasaccharide 152-167 serpin family C member 1 Homo sapiens 131-143 17536781-5 2007 This FACE-MS coupling was applied to the analysis of the complex between antithrombin and the sulfated pentasaccharide reproducing the antithrombin-binding sequence in heparin. pentasaccharide 103-118 serpin family C member 1 Homo sapiens 73-85 17536781-5 2007 This FACE-MS coupling was applied to the analysis of the complex between antithrombin and the sulfated pentasaccharide reproducing the antithrombin-binding sequence in heparin. pentasaccharide 103-118 serpin family C member 1 Homo sapiens 135-147 17536781-5 2007 This FACE-MS coupling was applied to the analysis of the complex between antithrombin and the sulfated pentasaccharide reproducing the antithrombin-binding sequence in heparin. Heparin 168-175 serpin family C member 1 Homo sapiens 73-85 17536781-5 2007 This FACE-MS coupling was applied to the analysis of the complex between antithrombin and the sulfated pentasaccharide reproducing the antithrombin-binding sequence in heparin. Heparin 168-175 serpin family C member 1 Homo sapiens 135-147 17536781-7 2007 The intact noncovalent complex antithrombin/heparin pentasaccharide was detected on-line by ESIMS in positive ionization mode and in nondenaturing sheath liquid conditions. Heparin 44-51 serpin family C member 1 Homo sapiens 31-43 17536781-7 2007 The intact noncovalent complex antithrombin/heparin pentasaccharide was detected on-line by ESIMS in positive ionization mode and in nondenaturing sheath liquid conditions. pentasaccharide 52-67 serpin family C member 1 Homo sapiens 31-43 17385667-1 2007 We evaluated the role of nonspecific electrostatic binding in the interaction of antithrombin (AT) with heparin (Hp), a paradigmatic protein-glycosaminoglycan (GAG) system. Heparin 104-111 serpin family C member 1 Homo sapiens 81-93 17560876-8 2007 In contrast, among patients randomized to receive unfractionated heparin and planned glycoprotein IIb/IIIa, pretreatment with antithrombin therapy was associated with increased protocol-defined composite major or minor bleeding and increased need for transfusion. Heparin 65-72 serpin family C member 1 Homo sapiens 126-138 17537059-10 2007 The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process. Heparin 35-42 serpin family C member 1 Homo sapiens 23-26 17537059-10 2007 The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process. Heparin 47-54 serpin family C member 1 Homo sapiens 23-26 17511500-3 2007 Thiol functionalization of heparin carboxylic groups was controlled from 10% to 60% of the available COOH groups, and the retained bioactivity of the modified heparin, characterized by its binding affinity to antithrombin III, decreased with increasing functionalization. Sulfhydryl Compounds 0-5 serpin family C member 1 Homo sapiens 209-225 17511500-3 2007 Thiol functionalization of heparin carboxylic groups was controlled from 10% to 60% of the available COOH groups, and the retained bioactivity of the modified heparin, characterized by its binding affinity to antithrombin III, decreased with increasing functionalization. Heparin 27-34 serpin family C member 1 Homo sapiens 209-225 17511500-3 2007 Thiol functionalization of heparin carboxylic groups was controlled from 10% to 60% of the available COOH groups, and the retained bioactivity of the modified heparin, characterized by its binding affinity to antithrombin III, decreased with increasing functionalization. Heparin 159-166 serpin family C member 1 Homo sapiens 209-225 17489664-1 2007 Enoxaparin is a low-molecular-weight heparin (LMWH) derivative that exerts its anticoagulant activity through antithrombin III, an endogenous inhibitor of factor Xa and thrombin IIa. Enoxaparin 0-10 serpin family C member 1 Homo sapiens 110-126 17478454-7 2007 Plasma selenium was positively correlated with minimum platelet count, minimum plasma antithrombin activity, and protein C activity. Selenium 7-15 serpin family C member 1 Homo sapiens 86-98 17546440-7 2007 The synthetic, selective antithrombin-binding pentasaccharide fondaparinux has been successfully used in prophylaxis for the prevention of thrombosis in highest risk patients. pentasaccharide 46-61 serpin family C member 1 Homo sapiens 25-37 17047995-3 2007 Thus, anticoagulant treatment with melagatran is of special interest in neonatal patients, whose plasma is relatively deficient in antithrombin. melagatran 35-45 serpin family C member 1 Homo sapiens 131-143 17489664-1 2007 Enoxaparin is a low-molecular-weight heparin (LMWH) derivative that exerts its anticoagulant activity through antithrombin III, an endogenous inhibitor of factor Xa and thrombin IIa. Heparin 37-44 serpin family C member 1 Homo sapiens 110-126 17489664-1 2007 Enoxaparin is a low-molecular-weight heparin (LMWH) derivative that exerts its anticoagulant activity through antithrombin III, an endogenous inhibitor of factor Xa and thrombin IIa. Heparin, Low-Molecular-Weight 46-50 serpin family C member 1 Homo sapiens 110-126 17364989-6 2007 The AT-3 level after engraftment was significantly higher in the CBT group than in the BMT group and it did not fail along with the elevation of elastase in the CBT group (p < 0.01 by the Mann-Whitney U-test vs. the BMT group). N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE 65-68 serpin family C member 1 Homo sapiens 4-8 17323934-0 2007 High affinity interaction between a synthetic, highly negatively charged pentasaccharide and alpha- or beta-antithrombin is predominantly due to nonionic interactions. pentasaccharide 73-88 serpin family C member 1 Homo sapiens 108-120 17323934-1 2007 Idraparinux is a synthetic O-sulfated, O-methylated pentasaccharide that binds tightly to antithrombin (AT) and thereby specifically and efficiently induces the inactivation of the procoagulant protease, factor Xa. idraparinux 0-11 serpin family C member 1 Homo sapiens 90-102 17323934-1 2007 Idraparinux is a synthetic O-sulfated, O-methylated pentasaccharide that binds tightly to antithrombin (AT) and thereby specifically and efficiently induces the inactivation of the procoagulant protease, factor Xa. pentasaccharide 52-67 serpin family C member 1 Homo sapiens 90-102 17376263-5 2007 Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI. Heparin 43-50 serpin family C member 1 Homo sapiens 130-142 17376263-5 2007 Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI. Heparin 75-82 serpin family C member 1 Homo sapiens 130-142 17376263-5 2007 Blame had been laid on the combined use of heparin or low molecular weight heparin (LMWH), as it might interfere with efficacy of antithrombin and TFPI. Heparin, Low-Molecular-Weight 84-88 serpin family C member 1 Homo sapiens 130-142 17229412-5 2007 The example of interactions between heparin and antithrombin III illustrates how such a complex mechanism as the regulation of blood coagulation by a specific pentasaccharide can be dissected through the combined use of dedicated carbohydrate chemistry and structural glycobiology. pentasaccharide 159-174 serpin family C member 1 Homo sapiens 48-64 17229412-5 2007 The example of interactions between heparin and antithrombin III illustrates how such a complex mechanism as the regulation of blood coagulation by a specific pentasaccharide can be dissected through the combined use of dedicated carbohydrate chemistry and structural glycobiology. Carbohydrates 230-242 serpin family C member 1 Homo sapiens 48-64 17364989-7 2007 In conclusion, the lower risk of severe acute GVHD in the CBT group may have been related to the smaller decrease of AT-3 after transplantation. N,N-BIS(4-CHLOROBENZYL)-1H-1,2,3,4-TETRAAZOL-5-AMINE 58-61 serpin family C member 1 Homo sapiens 117-121 17600786-8 2007 Although the mechanism of heparin binding involves covalent boronate ester formation, it can be completely reversed by protamine addition, similar to heparin"s complex formation with antithrombin III. Heparin 26-33 serpin family C member 1 Homo sapiens 183-199 17600786-8 2007 Although the mechanism of heparin binding involves covalent boronate ester formation, it can be completely reversed by protamine addition, similar to heparin"s complex formation with antithrombin III. Heparin 150-157 serpin family C member 1 Homo sapiens 183-199 17600391-9 2007 In the case of pregnancy, antithrombin concentrate is often used around the time of birth when LMWH may increase the risk of post-partum haemorrhage. Heparin, Low-Molecular-Weight 95-99 serpin family C member 1 Homo sapiens 26-38 17167048-0 2007 Analysis of inhibition rate enhancement by covalent linkage of antithrombin to heparin as a potential predictor of reaction mechanism. Heparin 79-86 serpin family C member 1 Homo sapiens 63-75 18333219-8 2007 The postoperative level of AT-III in the control group was significantly lower than in the steroid group (ANOVA p < 0.01). Steroids 91-98 serpin family C member 1 Homo sapiens 27-33 17167048-1 2007 Antithrombin (AT) inhibition of coagulation enzymes is catalyzed by unfractionated heparin (UFH) and other heparinoids. Heparin 83-90 serpin family C member 1 Homo sapiens 0-12 17167048-1 2007 Antithrombin (AT) inhibition of coagulation enzymes is catalyzed by unfractionated heparin (UFH) and other heparinoids. Heparin 92-95 serpin family C member 1 Homo sapiens 0-12 17167048-1 2007 Antithrombin (AT) inhibition of coagulation enzymes is catalyzed by unfractionated heparin (UFH) and other heparinoids. Heparinoids 107-118 serpin family C member 1 Homo sapiens 0-12 16515805-0 2007 Heparin chain-length dependence of factor Xa inhibition by antithrombin in plasma. Heparin 0-7 serpin family C member 1 Homo sapiens 59-71 17966105-0 2007 [The insufficiency of low molecular weight heparin (LMWH) prophylaxis in patients with hereditary antithrombin (AT) deficiency]. Heparin, Low-Molecular-Weight 52-56 serpin family C member 1 Homo sapiens 98-110 17297193-4 2007 Also not previously reported is the use of bivaluridin as the periprocedural antithrombin agent during and after high-risk aortic valvuloplasty. bivaluridin 43-54 serpin family C member 1 Homo sapiens 77-89 17477084-7 2007 RESULTS: After 2-months therapy with simvastatin in patients with hlp II it was observed significantly decrease of activity of factor X (20.94 +/- 19.04 vs. 9.44 +/- 7.31 mU/mL), thrombin generation (79.62 +/- 36.68 vs. 67.99 +/- 37.69 U/mL), clot bound thrombin (49.73 +/- 21.17 vs. 37.08 +/- 26.10 U/mL) and increase of antithrombin III activity (13.03 +/- 6.11 vs. 20.64 +/- 4.18 U/mL). Simvastatin 37-48 serpin family C member 1 Homo sapiens 322-338 17917621-8 2007 UFH is likely to be replaced by more effective and safer antithrombin agents, such as DTIs. Heparin 0-3 serpin family C member 1 Homo sapiens 57-69 17270255-1 2007 INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action. Dermatan Sulfate 14-30 serpin family C member 1 Homo sapiens 131-143 17156824-6 2007 Compared with the low-dose HT group those treated with tibolone showed more pronounced decreases in factor VII, less reduction of antithrombin and protein C and even increased levels in protein S and tissue factor pathway inhibitor. tibolone 55-63 serpin family C member 1 Homo sapiens 130-142 17200767-1 2007 Fondaparinux is a synthetic pentasaccharide consisting of the minimal sequence of heparin which interacts with antithrombin (AT). pentasaccharide 28-43 serpin family C member 1 Homo sapiens 111-123 17270255-1 2007 INTRODUCTION: Dermatan sulfate (DS) is well-known for its anticoagulant activity through binding to heparin cofactor II to enhance antithrombin action. Dermatan Sulfate 32-34 serpin family C member 1 Homo sapiens 131-143 17040907-0 2006 Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains. Heparitin Sulfate 39-54 serpin family C member 1 Homo sapiens 15-27 17482241-2 2007 INTRODUCTION: A heparin preparation with low antithrombin activity and different disaccharide composition than mammalian heparin was isolated from the body of the ascidian Styela plicata (Chordata-Tunicata). Heparin 16-23 serpin family C member 1 Homo sapiens 45-57 17482241-9 2007 CONCLUSION: The antithrombin-mediated anticoagulant activity of heparin polymers is not directly related to antithrombotic potency in the arterio-venous shunt. Heparin 64-71 serpin family C member 1 Homo sapiens 16-28 17040907-0 2006 Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains. Heparitin Sulfate 39-54 serpin family C member 1 Homo sapiens 221-233 17040907-0 2006 Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains. Heparitin Sulfate 251-266 serpin family C member 1 Homo sapiens 15-27 17156576-2 2006 This review focuses on five diseases caused by serpin dysfunction: variants of antithrombin III lose their ability to interact with heparin; the alpha1-antitrypsin Pittsburgh mutation causes a change in target proteinase; the alpha1-antitrypsin Z mutation and neuroserpin, polymerisation of which lead to cellular cytotoxicity; and a loss of maspin expression resulting in cancer. Heparin 132-139 serpin family C member 1 Homo sapiens 79-95 17040907-0 2006 Antiangiogenic antithrombin blocks the heparan sulfate-dependent binding of proangiogenic growth factors to their endothelial cell receptors: evidence for differential binding of antiangiogenic and anticoagulant forms of antithrombin to proangiogenic heparan sulfate domains. Heparitin Sulfate 251-266 serpin family C member 1 Homo sapiens 221-233 17040907-8 2006 Moreover, the inability of native antithrombin to bind this co-receptor implies that native and conformationally altered forms of antithrombin differentially bind proangiogenic heparan sulfate domains. Heparitin Sulfate 177-192 serpin family C member 1 Homo sapiens 130-142 18221095-6 2006 These drugs do not rely on blocking serine proteases nor do they require a co-factor (antithrombin III) like unfractionated heparin (UFH) or low molecular weight heparin (LMWH). Heparin 124-131 serpin family C member 1 Homo sapiens 86-102 17146553-2 2006 A heparin-like substance with an anticoagulant activity equivalent to 10% of mammalian heparin and about 5% as potent as the mammalian counterpart for the inhibition of thrombin by antithrombin was isolated from the oocyte test cells. Heparin 2-9 serpin family C member 1 Homo sapiens 181-193 18221095-6 2006 These drugs do not rely on blocking serine proteases nor do they require a co-factor (antithrombin III) like unfractionated heparin (UFH) or low molecular weight heparin (LMWH). Heparin 133-136 serpin family C member 1 Homo sapiens 86-102 17174877-6 2006 CASE REPORT: We present a case of recurrent acute in-stent thrombosis in a patient with mild antithrombin III (AT) deficiency despite the combined administration of clopidogrel and aspirin. Clopidogrel 165-176 serpin family C member 1 Homo sapiens 93-109 16940049-0 2006 Disruption of a tight cluster surrounding tyrosine 131 in the native conformation of antithrombin III activates it for factor Xa inhibition. Tyrosine 42-50 serpin family C member 1 Homo sapiens 85-101 16940049-2 2006 This study focused on tyrosine 131, which is located at the helix D-sheet A interface, adjacent to the ATIII pentasaccharide and heparin cofactor-binding sites and some 17A away from the RCL insertion. Tyrosine 22-30 serpin family C member 1 Homo sapiens 103-108 16940049-2 2006 This study focused on tyrosine 131, which is located at the helix D-sheet A interface, adjacent to the ATIII pentasaccharide and heparin cofactor-binding sites and some 17A away from the RCL insertion. pentasaccharide 109-124 serpin family C member 1 Homo sapiens 103-108 16940049-3 2006 Crystallographic structures show that the Tyr(131) ring is buried in native ATIII and then becomes exposed when pentasaccharide binds to the inhibitor and activates it. Tyrosine 42-45 serpin family C member 1 Homo sapiens 76-81 16940049-3 2006 Crystallographic structures show that the Tyr(131) ring is buried in native ATIII and then becomes exposed when pentasaccharide binds to the inhibitor and activates it. pentasaccharide 112-127 serpin family C member 1 Homo sapiens 76-81 16940049-4 2006 This change suggested that Tyr(131) might serve as a switch for ATIII conformational activation. Tyrosine 27-30 serpin family C member 1 Homo sapiens 64-69 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Tyrosine 16-19 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Tyrosine 16-19 serpin family C member 1 Homo sapiens 305-310 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Asparagine 25-28 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Asparagine 25-28 serpin family C member 1 Homo sapiens 305-310 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Leucine 34-37 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Leucine 34-37 serpin family C member 1 Homo sapiens 305-310 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Leucine 43-46 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Leucine 43-46 serpin family C member 1 Homo sapiens 305-310 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Serine 52-55 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Serine 52-55 serpin family C member 1 Homo sapiens 305-310 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Tyrosine 208-216 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Tyrosine 208-216 serpin family C member 1 Homo sapiens 305-310 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Heparin 233-240 serpin family C member 1 Homo sapiens 114-126 16940049-8 2006 Thus, the tight Tyr(131)-Asn(127)-Leu(130)-Leu(140)-Ser(142) cluster at the helix D-strand 2A interface of native antithrombin contributes significantly to the stability of the ground state conformation, and tyrosine 131 serves as a heparin-responsive molecular switch during the allosteric activation of ATIII anticoagulant activity. Heparin 233-240 serpin family C member 1 Homo sapiens 305-310 16796563-0 2006 Conformational transitions induced in heparin octasaccharides by binding with antithrombin III. heparin octasaccharides 38-61 serpin family C member 1 Homo sapiens 78-94 17174877-6 2006 CASE REPORT: We present a case of recurrent acute in-stent thrombosis in a patient with mild antithrombin III (AT) deficiency despite the combined administration of clopidogrel and aspirin. Aspirin 181-188 serpin family C member 1 Homo sapiens 93-109 16880140-3 2006 Heparin concentration recovery, in vitro, was dependent on the plasma antithrombin concentration for all 3 assays. Heparin 0-7 serpin family C member 1 Homo sapiens 70-82 16938875-8 2006 We demonstrated the specificity of the antithrombin III functionalized sensor for the physiologically active pentasaccharide sequence. pentasaccharide 109-124 serpin family C member 1 Homo sapiens 39-55 17043951-6 2006 Anticoagulant heparan sulfate proteoglycans (aHSPG), like heparin, possess a pentasaccharide sequence which binds and activates antithrombin III. Heparin 58-65 serpin family C member 1 Homo sapiens 128-144 17043951-6 2006 Anticoagulant heparan sulfate proteoglycans (aHSPG), like heparin, possess a pentasaccharide sequence which binds and activates antithrombin III. pentasaccharide 77-92 serpin family C member 1 Homo sapiens 128-144 16880140-4 2006 The antithrombin-supplemented assay demonstrated improved heparin recovery in direct correlation to the heparin concentration in the plasma. Heparin 58-65 serpin family C member 1 Homo sapiens 4-16 16880140-4 2006 The antithrombin-supplemented assay demonstrated improved heparin recovery in direct correlation to the heparin concentration in the plasma. Heparin 104-111 serpin family C member 1 Homo sapiens 4-16 16880140-7 2006 Classification of the clinical adequacy of patient heparin levels showed agreement of 80% or more between the antithrombin-supplemented and nonsupplemented assays. Heparin 51-58 serpin family C member 1 Homo sapiens 110-122 16856890-0 2006 Comparison of the anticoagulant effect of a direct thrombin inhibitor and a low molecular weight heparin in an acquired antithrombin deficiency in children with acute lymphoblastic leukaemia treated with L-asparaginase: an in vitro study. Heparin 97-104 serpin family C member 1 Homo sapiens 120-132 16966848-8 2006 Heparin infusion was started when the antithrombin value was > 100% and remained stable for more than 12 hours and the amount of bleeding was < 2 ml/kg for more than 3 consecutive hours; then heparin infusion was started at 2 UI/kg/h via the oxygenator (target ACT was not < 150 seconds). Heparin 0-7 serpin family C member 1 Homo sapiens 38-50 16624472-2 2006 Two sesquiterpenolides of similar structures (atractylenolide I, AT-I; atractylenolide III, AT-III) were isolated from dried rhizome of Atractylodes ovata. sesquiterpenolides 4-22 serpin family C member 1 Homo sapiens 92-98 16884719-0 2006 Allosteric activation of antithrombin is independent of charge neutralization or reversal in the heparin binding site. Heparin 97-104 serpin family C member 1 Homo sapiens 25-37 16884719-1 2006 We investigate the hypothesis that heparin activates antithrombin (AT) by relieving electrostatic strain within helix D. Mutation of residues K125 and R129 to either Ala or Glu abrogated heparin binding, but did not activate AT towards inhibition of factors IXa or Xa. Heparin 35-42 serpin family C member 1 Homo sapiens 53-65 16884719-1 2006 We investigate the hypothesis that heparin activates antithrombin (AT) by relieving electrostatic strain within helix D. Mutation of residues K125 and R129 to either Ala or Glu abrogated heparin binding, but did not activate AT towards inhibition of factors IXa or Xa. Alanine 166-169 serpin family C member 1 Homo sapiens 53-65 16884719-1 2006 We investigate the hypothesis that heparin activates antithrombin (AT) by relieving electrostatic strain within helix D. Mutation of residues K125 and R129 to either Ala or Glu abrogated heparin binding, but did not activate AT towards inhibition of factors IXa or Xa. Glutamic Acid 173-176 serpin family C member 1 Homo sapiens 53-65 16954536-0 2006 Structural effects of a covalent linkage between antithrombin and heparin: covalent N-terminus attachment of heparin enhances the maintenance of antithrombin"s activated state. Heparin 66-73 serpin family C member 1 Homo sapiens 145-157 16954536-0 2006 Structural effects of a covalent linkage between antithrombin and heparin: covalent N-terminus attachment of heparin enhances the maintenance of antithrombin"s activated state. Heparin 109-116 serpin family C member 1 Homo sapiens 49-61 16954536-0 2006 Structural effects of a covalent linkage between antithrombin and heparin: covalent N-terminus attachment of heparin enhances the maintenance of antithrombin"s activated state. Heparin 109-116 serpin family C member 1 Homo sapiens 145-157 16954536-2 2006 This study was designed to elucidate the covalent linkage point(s) for heparin on antithrombin and conformational properties of the ATH molecule. Heparin 71-78 serpin family C member 1 Homo sapiens 82-94 16954536-3 2006 ATH was produced using Schiff base/Amadori rearrangement by incubating antithrombin with unfractionated heparin for 14 d at 40 degrees C. ATH was then digested using Proteinase K, and the heparin-peptide was reacted with NaIO4/NaBH4/mild acid to degrade the heparin moiety. Schiff Bases 23-34 serpin family C member 1 Homo sapiens 71-83 16954536-8 2006 The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin. Heparin 25-32 serpin family C member 1 Homo sapiens 72-84 16954536-8 2006 The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin. Heparin 25-32 serpin family C member 1 Homo sapiens 183-195 16954536-8 2006 The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin. Heparin 157-164 serpin family C member 1 Homo sapiens 72-84 16954536-8 2006 The results suggest that heparin is conjugated to the amino terminal of antithrombin in the majority of ATH molecules, proximal to the previously determined heparin binding domain of antithrombin. Heparin 157-164 serpin family C member 1 Homo sapiens 183-195 16517611-0 2006 Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa. exosite 98-105 serpin family C member 1 Homo sapiens 58-70 16675258-10 2006 Heparin was given during cardiopulmonary bypass to maintain an activated clotting time above 480 s. RESULTS: Patients in the enoxaparin group needed more heparin to maintain an activated clotting time above 480 s, and had higher heparin concentrations and lower antithrombin values compared with control patients. Heparin 0-7 serpin family C member 1 Homo sapiens 262-274 16675258-10 2006 Heparin was given during cardiopulmonary bypass to maintain an activated clotting time above 480 s. RESULTS: Patients in the enoxaparin group needed more heparin to maintain an activated clotting time above 480 s, and had higher heparin concentrations and lower antithrombin values compared with control patients. Enoxaparin 125-135 serpin family C member 1 Homo sapiens 262-274 16672689-0 2006 Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin-independent mechanism. holothurian glycosaminoglycan 14-43 serpin family C member 1 Homo sapiens 105-117 16672689-0 2006 Depolymerized holothurian glycosaminoglycan and heparin inhibit the intrinsic tenase complex by a common antithrombin-independent mechanism. Heparin 48-55 serpin family C member 1 Homo sapiens 105-117 16672689-1 2006 Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chrondroitin sulfate that possesses antithrombin-independent antithrombotic properties and inhibits factor X activation by the intrinsic tenase complex (factor IXa-factor VIIIa). holothurian glycosaminoglycan 14-43 serpin family C member 1 Homo sapiens 103-115 16672689-1 2006 Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chrondroitin sulfate that possesses antithrombin-independent antithrombotic properties and inhibits factor X activation by the intrinsic tenase complex (factor IXa-factor VIIIa). dhg 45-48 serpin family C member 1 Homo sapiens 103-115 16672689-1 2006 Depolymerized holothurian glycosaminoglycan (DHG) is a fucosylated chrondroitin sulfate that possesses antithrombin-independent antithrombotic properties and inhibits factor X activation by the intrinsic tenase complex (factor IXa-factor VIIIa). chrondroitin sulfate 67-87 serpin family C member 1 Homo sapiens 103-115 16820297-3 2006 The regulatory advantages provided by structural mobility are best illustrated by the heparin activation mechanisms of the plasma serpins antithrombin and heparin cofactor II. Heparin 86-93 serpin family C member 1 Homo sapiens 138-150 16837886-11 2006 Oral E(2) with NETA reduced antithrombin III (P < 0.001) and protein C (P < 0.001) activity. Norethindrone Acetate 15-19 serpin family C member 1 Homo sapiens 28-44 16517611-0 2006 Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa. Heparin 125-132 serpin family C member 1 Homo sapiens 58-70 16517611-1 2006 We previously showed that conformational activation of the anticoagulant serpin, antithrombin, by heparin generates new exosites in strand 3 of beta-sheet C, which promote the reaction of the inhibitor with the target proteases, factor Xa and factor IXa. Heparin 98-105 serpin family C member 1 Homo sapiens 81-93 16619025-0 2006 Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. Heparin 29-36 serpin family C member 1 Homo sapiens 0-12 16619025-0 2006 Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. Heparin 29-36 serpin family C member 1 Homo sapiens 83-95 16619025-2 2006 One of the principal regulatory mechanisms involves heparin activation of the serpin antithrombin (AT). Heparin 52-59 serpin family C member 1 Homo sapiens 85-97 16685318-1 2006 BACKGROUND: Subcutaneous enoxaparin is increasingly employed as the antithrombin of choice in non-ST elevation myocardial infarction and in conjunction with various fibrinolytic regimens in acute ST elevation myocardial infarction (STEMI). Enoxaparin 25-35 serpin family C member 1 Homo sapiens 68-80 16676077-5 2006 In patients with no concomitant heparin, 28-day mortality was lower with antithrombin than with placebo (37.8% vs. 43.6%; absolute reduction: 5.8%; risk ratio: 0.860 [0.725-1.019]), which increased until day-90 (44.9% vs. 52.5%; absolute reduction: 7.6%; risk ratio: 0.851 [0.735-0.987]). Heparin 32-39 serpin family C member 1 Homo sapiens 73-85 16711739-2 2006 Only the twisted boat conformation allowed the biologically active pentasaccharide unit of heparin (DEFGH) to bind to antithrombin. pentasaccharide 67-82 serpin family C member 1 Homo sapiens 118-130 16711739-2 2006 Only the twisted boat conformation allowed the biologically active pentasaccharide unit of heparin (DEFGH) to bind to antithrombin. Heparin 91-98 serpin family C member 1 Homo sapiens 118-130 16676077-0 2006 Benefit/risk profile of high-dose antithrombin in patients with severe sepsis treated with and without concomitant heparin. Heparin 115-122 serpin family C member 1 Homo sapiens 34-46 16676077-10 2006 In the treatment of severe sepsis, high-dose antithrombin may sufficiently protect against development of venous thromboembolism when no concomitant heparin is given. Heparin 149-156 serpin family C member 1 Homo sapiens 45-57 16289605-0 2006 A novel application of multi-wavelength TIRF spectroscopy for real time monitoring of antithrombin interactions with immobilized heparin. Heparin 129-136 serpin family C member 1 Homo sapiens 86-98 16618121-0 2006 Pentasaccharide enhances the inactivation of factor Xa by antithrombin by promoting the assembly of a Michaelis-type intermediate complex. pentasaccharide 0-15 serpin family C member 1 Homo sapiens 58-70 16442510-0 2006 Thrombin inhibition by antithrombin in the presence of oversulfated dermatan sulfates. Dermatan Sulfate 68-85 serpin family C member 1 Homo sapiens 23-35 16442510-2 2006 DSS1 and DSS2 both enhanced the rate at which antithrombin (AT) inactivates thrombin according to a concentration dependent manner. dss2 9-13 serpin family C member 1 Homo sapiens 46-58 16567083-0 2006 Heparin coating durability on artificial heart valves studied by XPS and antithrombin binding capacity. Heparin 0-7 serpin family C member 1 Homo sapiens 73-85 16567083-1 2006 The durability and functionality of a heparin coating on artificial heart valve leaflets were evaluated with X-ray photoelectron spectroscopy (XPS) and by the coatings" capacity to bind antithrombin. Heparin 38-45 serpin family C member 1 Homo sapiens 186-198 16567083-4 2006 It was found that the heparin coating was stable and wear resistant enough to still be present after 3 weeks and to have about the same antithrombin uptake as coatings not exposed to circulating plasma. Heparin 22-29 serpin family C member 1 Homo sapiens 136-148 16289605-1 2006 Real time interactions of antithrombin (AT) with Corline Heparin Surfaces (CHS) with one and two layers of heparin conjugate have been examined using a multi-wavelength TIRF spectroscopy technique with continuous flow. corline heparin 49-64 serpin family C member 1 Homo sapiens 26-38 16289605-1 2006 Real time interactions of antithrombin (AT) with Corline Heparin Surfaces (CHS) with one and two layers of heparin conjugate have been examined using a multi-wavelength TIRF spectroscopy technique with continuous flow. corline heparin 49-64 serpin family C member 1 Homo sapiens 40-42 16289605-1 2006 Real time interactions of antithrombin (AT) with Corline Heparin Surfaces (CHS) with one and two layers of heparin conjugate have been examined using a multi-wavelength TIRF spectroscopy technique with continuous flow. Heparin 107-114 serpin family C member 1 Homo sapiens 26-38 16289605-1 2006 Real time interactions of antithrombin (AT) with Corline Heparin Surfaces (CHS) with one and two layers of heparin conjugate have been examined using a multi-wavelength TIRF spectroscopy technique with continuous flow. Heparin 107-114 serpin family C member 1 Homo sapiens 40-42 16289605-2 2006 Fluorescently labeled AT, adsorbed from citrated human blood plasma, showed significantly higher signals on CHS compared to the cationic surface used to attach the heparin conjugate. Heparin 164-171 serpin family C member 1 Homo sapiens 22-24 16289605-3 2006 The AT binding to CHS was very stable, also after exposure to soluble heparin at a concentration of 1.5 IU/mL. Heparin 70-77 serpin family C member 1 Homo sapiens 4-6 16289605-5 2006 In contrast, larger amounts of the freshly added AT had adsorbed to the surfaces, especially to the surface with two layers of heparin conjugate, indicating the presence of unsaturated AT binding sites. Heparin 127-134 serpin family C member 1 Homo sapiens 49-51 16360204-4 2006 The entrapment of heparin molecules was confirmed by a negatively increased zeta potential value and the specific binding affinity to antithrombin III. Heparin 18-25 serpin family C member 1 Homo sapiens 134-150 16613771-3 2006 Up-to-date antithrombin therapy consists of vitamin K antagonists, unfractionated and low molecular heparins, direct thrombin inhibitors and selective inhibitors of factor Xa. Vitamin K 44-53 serpin family C member 1 Homo sapiens 11-23 16613771-3 2006 Up-to-date antithrombin therapy consists of vitamin K antagonists, unfractionated and low molecular heparins, direct thrombin inhibitors and selective inhibitors of factor Xa. Heparin 100-108 serpin family C member 1 Homo sapiens 11-23 16368135-4 2006 The capacity of surface bound heparin to promote ATIII-mediated thrombin inactivation was investigated in a parallel plate flow chamber under simulated venous and arterial wall shear rates of 50 and 500 s(-1), respectively. Heparin 30-37 serpin family C member 1 Homo sapiens 49-54 16337041-5 2006 RESULTS: After 1 week of treatment, a significant increase of ATIII (p < 0.05), fV (p < 0.01) and vWF (p < 0.05) was found in the control group, but not in atorvastatin-treated group. Atorvastatin 165-177 serpin family C member 1 Homo sapiens 62-67 16290930-2 2006 A naphthylsulfonamide analogue showed excellent antithrombin activity. naphthylsulfonamide 2-21 serpin family C member 1 Homo sapiens 48-60 16542481-5 2006 Preclinical research has demonstrated partial interference of heparin--administered even at low doses--with the therapeutic effects of antithrombin, and has confirmed--at the level of cellular mechanisms--a regulatory role for antithrombin in DIC. Heparin 62-69 serpin family C member 1 Homo sapiens 135-147 16475045-6 2006 Fondaparinux is a synthetic pentasaccharide, which binds to antithrombin, thereby indirectly selectively inhibiting factor Xa. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 60-72 16575261-0 2006 Antithrombin Nagasaki (Ser 116 to Pro): a rare antithrombin variant with abnormal heparin binding presenting during pregnancy. Heparin 82-89 serpin family C member 1 Homo sapiens 0-12 16575261-0 2006 Antithrombin Nagasaki (Ser 116 to Pro): a rare antithrombin variant with abnormal heparin binding presenting during pregnancy. Heparin 82-89 serpin family C member 1 Homo sapiens 47-59 16575261-2 2006 Studies suggest, however, that individuals heterozygous for missense mutations involving the heparin-binding site of antithrombin do not have a significantly increased thrombotic risk. Heparin 93-100 serpin family C member 1 Homo sapiens 117-129 16575261-4 2006 We report here the case of a pregnant woman with an exceptionally rare Type II heparin-binding site antithrombin variant. Heparin 79-86 serpin family C member 1 Homo sapiens 100-112 16542495-1 2006 INTRODUCTION: Acquired antithrombin III (AT) deficiency may induce heparin resistance and premature membrane clotting during continuous renal replacement therapy (CRRT). Heparin 67-74 serpin family C member 1 Homo sapiens 23-39 16413239-1 2006 We hypothesized that infusion of recombinant human antithrombin without concomitant heparin would have dose-dependent anticoagulant properties and potentially decrease endotoxin (lipopolysaccharide [LPS])-induced cytokine production. Heparin 84-91 serpin family C member 1 Homo sapiens 51-63 16310167-5 2006 Surface plasmon resonance was used to measure the interaction of each member of this polysaccharide library with antithrombin III (ATIII), to afford structural information on sulfo groups required for this HP/HS-protein interaction. Polysaccharides 85-99 serpin family C member 1 Homo sapiens 113-129 16310167-5 2006 Surface plasmon resonance was used to measure the interaction of each member of this polysaccharide library with antithrombin III (ATIII), to afford structural information on sulfo groups required for this HP/HS-protein interaction. Polysaccharides 85-99 serpin family C member 1 Homo sapiens 131-136 16344381-11 2005 These data suggest that LMWH should be the preferred antithrombin in this setting. Heparin, Low-Molecular-Weight 24-28 serpin family C member 1 Homo sapiens 53-65 16394262-3 2006 Heparan sulfate enables growth factor function and modifies enzyme/inhibitor functions, such as antithrombin III and heparin cofactor II. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 96-112 17124098-8 2006 Fondaparinux is a synthetic pentasaccharide, which binds to antithrombin, thereby indirectly selectively inhibiting factor Xa. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 60-72 16192735-4 2006 Those women receiving intranasal estradiol showed a mild increment in plasminogen activator inhibitor-1 (PAI-I) (from 6.8 +/- 3.5 to 9.6 +/- 3.9 U/ml, p < 0.01); however, fibrinogen, factor VII-tissue factor complex (VIIa-rTF), antithrombin III (ATIII), protein C (PC) activity, protein S (PS) activity, plasminogen (PLG), and tissue-type plasminogen activator antigen (t-PA) were unchanged. Estradiol 33-42 serpin family C member 1 Homo sapiens 249-254 16244492-4 2006 Our case shows that a combined treatment with antithrombin substitution and a prophylactic, body-weight-adjusted dose of low-molecular-weight heparin may be successful in preventing pregnancy loss and thromboembolism in antithrombin deficiency during pregnancy, although other complications, such as preeclampsia and intrauterine growth restriction cannot always be prevented. Heparin 142-149 serpin family C member 1 Homo sapiens 220-232 17323590-1 2006 The antithrombin binding sequence of heparin, a pentasaccharide, has been synthesized as fondaparinux, an indirect, selective, and reversible factor Xa inhibitor. Heparin 37-44 serpin family C member 1 Homo sapiens 4-16 17323590-1 2006 The antithrombin binding sequence of heparin, a pentasaccharide, has been synthesized as fondaparinux, an indirect, selective, and reversible factor Xa inhibitor. pentasaccharide 48-63 serpin family C member 1 Homo sapiens 4-16 16260789-4 2005 By selecting appropriate enzymatic modification steps, an inactive precursor has been converted to the heparan sulfate having three distinct biological activities, associated with binding to antithrombin, fibroblast growth factor-2, and herpes simplex virus envelope glycoprotein D. Because the recombinant sulfotransferases are expressed in bacteria, and the method uses a low cost sulfo donor, it can be readily utilized to synthesize large quantities of anticoagulant heparin drug or other biologically active heparan sulfates. Heparitin Sulfate 103-118 serpin family C member 1 Homo sapiens 191-203 16051347-5 2005 This ATIII adsorption was mediated by the heparin layer, since surfaces modified with PEG only did not adsorb significant quantities of AT. Heparin 42-49 serpin family C member 1 Homo sapiens 5-10 16305899-12 2005 International normalized ratio (p = 0.03) and antithrombin III (p = 0.04) levels were elevated during CPB in the CCPB group, most likely owing to differences of the intraoperative anticoagulation management. ccpb 113-117 serpin family C member 1 Homo sapiens 46-62 16310443-9 2005 Systemic oxygen saturation correlated positively with the levels of anticoagulants (protein C, protein S, antithrombin III) and procoagulants (factors II, V, VII, and X) (all with p<0.05, r=0.33 to 0.61). Oxygen 9-15 serpin family C member 1 Homo sapiens 106-122 16051347-5 2005 This ATIII adsorption was mediated by the heparin layer, since surfaces modified with PEG only did not adsorb significant quantities of AT. Polyethylene Glycols 86-89 serpin family C member 1 Homo sapiens 5-10 16109780-3 2005 Fondaparinux, a synthetic anticoagulant modeled after the antithrombin-binding pentasaccharide, is believed to be nonimmunogenic. pentasaccharide 79-94 serpin family C member 1 Homo sapiens 58-70 16146701-0 2005 Insights into the induced fit mechanism in antithrombin-heparin interaction using molecular dynamics simulations. Heparin 56-63 serpin family C member 1 Homo sapiens 43-55 16202731-6 2005 Compared with placebo, raloxifene 60 mg decreased total protein S (-8.2%, P = .009) after 4 weeks and antithrombin (-6.0%, P = .034) and fibrinogen (-18.1%, P = .007) after 12 weeks. Raloxifene Hydrochloride 23-33 serpin family C member 1 Homo sapiens 102-114 16277716-12 2005 Low antithrombin concentrations before certoparin were independently correlated with underdosing of certoparin. certoparin 100-110 serpin family C member 1 Homo sapiens 4-16 16437314-2 2005 UFH is still the recommended antithrombin as soon as percutaneous coronary interventions (PCI) are performed, although the results of different trials clearly have demonstrated the benefit of enoxaparin also in interventional cardiology. Heparin 0-3 serpin family C member 1 Homo sapiens 29-41 16234627-3 2005 There are developments in the role of low-molecular-weight heparin agents in management of acute coronary syndromes in the modern treatment era, in which early coronary revascularization and use of other potent antiplatelet and antithrombin agents are common. Heparin 59-66 serpin family C member 1 Homo sapiens 228-240 16022574-2 2005 It is a chemically synthesised pentasaccharide mimicking the site of heparin that binds to antithrombin. pentasaccharide 31-46 serpin family C member 1 Homo sapiens 91-103 16128566-0 2005 Importance of tryptophan 49 of antithrombin in heparin binding and conformational activation. Tryptophan 14-24 serpin family C member 1 Homo sapiens 31-43 16128566-0 2005 Importance of tryptophan 49 of antithrombin in heparin binding and conformational activation. Heparin 47-54 serpin family C member 1 Homo sapiens 31-43 16128566-1 2005 Tryptophan 49 of antithrombin, the primary inhibitor of blood clotting proteinases, has previously been implicated in binding the allosteric activator, heparin, by chemical modification and mutagenesis studies. Tryptophan 0-10 serpin family C member 1 Homo sapiens 17-29 16128566-1 2005 Tryptophan 49 of antithrombin, the primary inhibitor of blood clotting proteinases, has previously been implicated in binding the allosteric activator, heparin, by chemical modification and mutagenesis studies. Heparin 152-159 serpin family C member 1 Homo sapiens 17-29 16128566-3 2005 Here, we provide a detailed thermodynamic and kinetic characterization of heparin binding to a Trp49 to Lys variant of antithrombin and suggest a model for how Trp49 participates in heparin binding and activation. Heparin 74-81 serpin family C member 1 Homo sapiens 119-131 16128566-5 2005 Rapid kinetics analyses showed that the mutation minimally affected the initial weak binding of heparin to antithrombin or the rate constant for the subsequent conformational activation of the serpin. Heparin 96-103 serpin family C member 1 Homo sapiens 107-119 15905187-2 2005 Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin"s ability to inhibit proliferation, migration, capillary-like tube formation, basic fibroblast growth factor (bFGF) signaling, and perlecan gene expression in bFGF-stimulated human umbilical vein endothelial cells. Heparin 13-20 serpin family C member 1 Homo sapiens 55-67 15905187-2 2005 Blocking the heparin-binding site of cleaved or latent antithrombin by complexation with a high-affinity heparin pentasaccharide abolished the serpin"s ability to inhibit proliferation, migration, capillary-like tube formation, basic fibroblast growth factor (bFGF) signaling, and perlecan gene expression in bFGF-stimulated human umbilical vein endothelial cells. pentasaccharide 113-128 serpin family C member 1 Homo sapiens 55-67 15905187-4 2005 Surprisingly, mutation of Lys114, which blocks anticoagulant activation of antithrombin by heparin, caused the native protein to acquire antiproliferative activity without the need for conformational change. Heparin 91-98 serpin family C member 1 Homo sapiens 75-87 15905187-5 2005 Together, these results indicate that the heparin-binding site of antithrombin is of crucial importance for mediating the serpin"s antiangiogenic activity and that heparin activation of native antithrombin constitutes an antiangiogenic switch that is responsible for turning off the antiangiogenic activity of the native serpin. Heparin 42-49 serpin family C member 1 Homo sapiens 66-78 15905187-5 2005 Together, these results indicate that the heparin-binding site of antithrombin is of crucial importance for mediating the serpin"s antiangiogenic activity and that heparin activation of native antithrombin constitutes an antiangiogenic switch that is responsible for turning off the antiangiogenic activity of the native serpin. Heparin 164-171 serpin family C member 1 Homo sapiens 193-205 16085538-4 2005 Fondaparinux is a novel synthetic heparin pentasaccharide capable of inhibiting factor Xa via the action of antithrombin (AT) but devoid of anti-factor IIa (thrombin) activity. IC 831423 34-57 serpin family C member 1 Homo sapiens 108-120 15970714-0 2005 Antithrombin efficiency is maintained in vitro in human plasma following dilution with hydroxyethyl starches. hydroxyethyl starches 87-108 serpin family C member 1 Homo sapiens 0-12 16145710-1 2005 The glycan structures of the major and more than ten minor populated isoforms of antithrombin (AT) were determined after separation of the isoforms by IEF using IPG strips. Polysaccharides 4-10 serpin family C member 1 Homo sapiens 81-93 16145710-1 2005 The glycan structures of the major and more than ten minor populated isoforms of antithrombin (AT) were determined after separation of the isoforms by IEF using IPG strips. 2-Isopropoxyethanol 161-164 serpin family C member 1 Homo sapiens 81-93 16270635-1 2005 Heparin is the current mainstay drug for anticoagulation during cardiac surgery, but it requires normal levels of antithrombin (AT) for optimal anticoagulation. Heparin 0-7 serpin family C member 1 Homo sapiens 114-126 16078853-0 2005 Mechanism of poly(acrylic acid) acceleration of antithrombin inhibition of thrombin: implications for the design of novel heparin mimics. carbopol 940 13-31 serpin family C member 1 Homo sapiens 48-60 16078853-0 2005 Mechanism of poly(acrylic acid) acceleration of antithrombin inhibition of thrombin: implications for the design of novel heparin mimics. Heparin 122-129 serpin family C member 1 Homo sapiens 48-60 16078853-1 2005 The bridging mechanism of antithrombin inhibition of thrombin is a dominant mechanism contributing a massive approximately 2500-fold acceleration in the reaction rate and is also a key reason for the clinical usage of heparin. Heparin 218-225 serpin family C member 1 Homo sapiens 26-38 16078853-2 2005 Our recent study of the antithrombin-activating properties of a carboxylic acid-based polymer, poly(acrylic acid) (PAA), demonstrated a surprisingly high acceleration in thrombin inhibition (Monien, B. H.; Desai, U. R. J. Med. carboxylic acid-based polymer 64-93 serpin family C member 1 Homo sapiens 24-36 16078853-2 2005 Our recent study of the antithrombin-activating properties of a carboxylic acid-based polymer, poly(acrylic acid) (PAA), demonstrated a surprisingly high acceleration in thrombin inhibition (Monien, B. H.; Desai, U. R. J. Med. carbopol 940 95-113 serpin family C member 1 Homo sapiens 24-36 16078853-2 2005 Our recent study of the antithrombin-activating properties of a carboxylic acid-based polymer, poly(acrylic acid) (PAA), demonstrated a surprisingly high acceleration in thrombin inhibition (Monien, B. H.; Desai, U. R. J. Med. carbopol 940 115-118 serpin family C member 1 Homo sapiens 24-36 16078853-6 2005 Competitive binding studies with low-affinity heparin and a heparin tetrasaccharide suggest that PAA binds antithrombin in both the pentasaccharide- and the extended heparin-binding sites, and these results are corroborated by molecular modeling. heparin tetrasaccharide 60-83 serpin family C member 1 Homo sapiens 107-119 16078853-6 2005 Competitive binding studies with low-affinity heparin and a heparin tetrasaccharide suggest that PAA binds antithrombin in both the pentasaccharide- and the extended heparin-binding sites, and these results are corroborated by molecular modeling. carbopol 940 97-100 serpin family C member 1 Homo sapiens 107-119 16078853-6 2005 Competitive binding studies with low-affinity heparin and a heparin tetrasaccharide suggest that PAA binds antithrombin in both the pentasaccharide- and the extended heparin-binding sites, and these results are corroborated by molecular modeling. pentasaccharide 132-147 serpin family C member 1 Homo sapiens 107-119 16078853-7 2005 The salt-dependence of the K(D) of the PAA-antithrombin interaction shows the formation of five ionic interactions. Salts 4-8 serpin family C member 1 Homo sapiens 43-55 16078853-9 2005 A bell-shaped profile of the observed rate constant for antithrombin inhibition of thrombin as a function of PAA concentration was observed, suggesting that inhibition proceeds through the "bridging" mechanism. carbopol 940 109-112 serpin family C member 1 Homo sapiens 56-68 16026276-8 2005 Some patients with very low AT levels may be resistant to heparin therapy and may require increased doses of heparin or AT concentrates. Heparin 58-65 serpin family C member 1 Homo sapiens 28-30 16026276-8 2005 Some patients with very low AT levels may be resistant to heparin therapy and may require increased doses of heparin or AT concentrates. Heparin 109-116 serpin family C member 1 Homo sapiens 28-30 16102051-2 2005 Novel parenteral agents include synthetic analogs of the pentasaccharide sequence of heparin that mediates its interaction with antithrombin. pentasaccharide 57-72 serpin family C member 1 Homo sapiens 128-140 16102051-2 2005 Novel parenteral agents include synthetic analogs of the pentasaccharide sequence of heparin that mediates its interaction with antithrombin. Heparin 85-92 serpin family C member 1 Homo sapiens 128-140 15967359-0 2005 QCM-FIA with PGMA coating for dynamic interaction study of heparin and antithrombin III. polyglycidyl methacrylate 13-17 serpin family C member 1 Homo sapiens 71-87 15967359-1 2005 In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III). polyglycidyl methacrylate 68-95 serpin family C member 1 Homo sapiens 336-352 15967359-1 2005 In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III). polyglycidyl methacrylate 68-95 serpin family C member 1 Homo sapiens 354-360 15967359-1 2005 In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III). pgma) polymer 97-110 serpin family C member 1 Homo sapiens 336-352 15967359-1 2005 In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III). pgma) polymer 97-110 serpin family C member 1 Homo sapiens 354-360 15967359-1 2005 In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III). Heparin 226-233 serpin family C member 1 Homo sapiens 336-352 15967359-1 2005 In this work, we describe a method of constructing a film of linear poly(glycidyl methacrylate) (PGMA) polymer onto the surface of quartz crystal microbalance (QCM) electrode as a coating material that allows easy coupling of heparin molecules onto the electrode and facilitates the determination of the interaction between heparin and antithrombin III (AT III). Heparin 226-233 serpin family C member 1 Homo sapiens 354-360 15967359-5 2005 The interactions between immobilized heparin and AT III were studied with various concentrations under various conditions. Heparin 37-44 serpin family C member 1 Homo sapiens 49-55 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 25-29 serpin family C member 1 Homo sapiens 83-88 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin 38-45 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin 38-45 serpin family C member 1 Homo sapiens 83-88 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 83-88 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 65-81 16004430-3 2005 The interactions between LMWH and the heparin-binding regions of antithrombin III (ATIII) or the heparin interacting protein (HIP) have been characterized via heparin affinity chromatography and surface plasmon resonance (SPR); results indicate that the two peptides have slightly different affinities for heparin and LMWH, and bind LMWH with micromolar affinity. Heparin, Low-Molecular-Weight 318-322 serpin family C member 1 Homo sapiens 83-88 16142016-5 2005 Furthermore, repaglinide administration resulted in a significant decrease in fasting plasma free fatty acids, fibrinogen, thrombin-antithrombin complex and reaction product of malondialdehyde with thiobarbituric acid (TBARS) levels, in absence of significant difference in fasting plasma insulin levels. repaglinide 13-24 serpin family C member 1 Homo sapiens 132-144 16013610-1 2005 The paper presents data on the primary structure of the glycan variants present in human antithrombin (AT) isoforms obtained from a plasma pool. Polysaccharides 56-62 serpin family C member 1 Homo sapiens 89-101 16013610-1 2005 The paper presents data on the primary structure of the glycan variants present in human antithrombin (AT) isoforms obtained from a plasma pool. Polysaccharides 56-62 serpin family C member 1 Homo sapiens 103-105 16013610-8 2005 In total, the variability in the carbohydrate structure of plasma derived AT appears as being quite limited. Carbohydrates 33-45 serpin family C member 1 Homo sapiens 74-76 16296580-9 2005 MANAGEMENT OF THROMBOPHILIA: Treatment of patients with congenital AT III deficiency includes intravenous heparin and AT III concentrate (dosage 50 U/ kgbw). Heparin 106-113 serpin family C member 1 Homo sapiens 67-73 15922935-2 2005 Inspired by the ternary complex formation of heparin with antithrombin III and thrombin, the active pentasaccharide fondaparinux has been succeeded by several clinical candidates, such as SR123781, that have tailor-made factor Xa and thrombin inhibitory activities combined with less aspecific binding (e.g. binding to platelet factor 4 involved in thrombocytopenia). Heparin 45-52 serpin family C member 1 Homo sapiens 58-74 15922935-2 2005 Inspired by the ternary complex formation of heparin with antithrombin III and thrombin, the active pentasaccharide fondaparinux has been succeeded by several clinical candidates, such as SR123781, that have tailor-made factor Xa and thrombin inhibitory activities combined with less aspecific binding (e.g. binding to platelet factor 4 involved in thrombocytopenia). pentasaccharide 100-115 serpin family C member 1 Homo sapiens 58-74 15922935-2 2005 Inspired by the ternary complex formation of heparin with antithrombin III and thrombin, the active pentasaccharide fondaparinux has been succeeded by several clinical candidates, such as SR123781, that have tailor-made factor Xa and thrombin inhibitory activities combined with less aspecific binding (e.g. binding to platelet factor 4 involved in thrombocytopenia). sr123781 188-196 serpin family C member 1 Homo sapiens 58-74 15999048-0 2005 Recombinant human antithrombin III restores heparin responsiveness and decreases activation of coagulation in heparin-resistant patients during cardiopulmonary bypass. Heparin 44-51 serpin family C member 1 Homo sapiens 18-34 15999048-0 2005 Recombinant human antithrombin III restores heparin responsiveness and decreases activation of coagulation in heparin-resistant patients during cardiopulmonary bypass. Heparin 110-117 serpin family C member 1 Homo sapiens 18-34 15999048-1 2005 OBJECTIVES: We sought to evaluate the efficacy of recombinant human antithrombin III for restoration of heparin responsiveness in heparin-resistant patients scheduled for cardiac surgery. Heparin 104-111 serpin family C member 1 Homo sapiens 68-84 15999048-1 2005 OBJECTIVES: We sought to evaluate the efficacy of recombinant human antithrombin III for restoration of heparin responsiveness in heparin-resistant patients scheduled for cardiac surgery. Heparin 130-137 serpin family C member 1 Homo sapiens 68-84 15999048-13 2005 CONCLUSION: Treatment with recombinant human antithrombin III in a dose of 75 U/kg is effective in restoring heparin responsiveness and promoting therapeutic anticoagulation for cardiopulmonary bypass in the majority of heparin-resistant patients. Heparin 109-116 serpin family C member 1 Homo sapiens 45-61 15999048-13 2005 CONCLUSION: Treatment with recombinant human antithrombin III in a dose of 75 U/kg is effective in restoring heparin responsiveness and promoting therapeutic anticoagulation for cardiopulmonary bypass in the majority of heparin-resistant patients. Heparin 220-227 serpin family C member 1 Homo sapiens 45-61 16113788-4 2005 Heparin, however, partially relieves this protective effect and at the same time it facilitates the inhibition of the intrinsic thrombin activity by antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 149-161 16142016-8 2005 At time 120" of meal test, repaglinide vs glimepiride administration was associated with a significant decline in plasma triglycerides, free fatty acids, fibrinogen, Plasminogen Activator Inhibitor-1, plasmin-alpha(2)-antiplasmin complex, thrombin-antithrombin complex, TBARS levels and increase in plasma HDL-cholesterol levels. repaglinide 27-38 serpin family C member 1 Homo sapiens 248-260 15957976-2 2005 It is one of a group of glycosaminoglycan compounds that accelerate the inactivation of factor Xa by inducing a conformational change in antithrombin. Glycosaminoglycans 24-41 serpin family C member 1 Homo sapiens 137-149 15957976-5 2005 Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned. Heparin, Low-Molecular-Weight 26-30 serpin family C member 1 Homo sapiens 0-12 15957976-5 2005 Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned. Heparin 34-37 serpin family C member 1 Homo sapiens 0-12 15957976-5 2005 Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned. Enoxaparin 204-214 serpin family C member 1 Homo sapiens 0-12 15957976-5 2005 Antithrombin therapy with LMWH or UFH has the highest-level recommendation (IA) in the 2002 professional guidelines for the management of unstable angina and non-ST-elevation myocardial infarction, where enoxaparin has a IIA recommendation over UFH unless early coronary artery bypass surgery is planned. Heparin 245-248 serpin family C member 1 Homo sapiens 0-12 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Heparitin Sulfate 97-113 serpin family C member 1 Homo sapiens 63-75 16052399-5 2005 Eight women with pregnancy-induced antithrombin deficiency, including three women with gestational thrombocytopenia, were significantly more likely to develop perinatal elevations of AST, lactate dehydrogenase, serum creatinine, fibrin/fibrinogen degradation products, and D-dimer than were those without pregnancy-induced antithrombin deficiency. Creatinine 217-227 serpin family C member 1 Homo sapiens 35-47 15882280-5 2005 After adjustment for illness severity, antithrombin-III levels increased significantly more over the period of study in the citrate as compared to the heparin group (P= 0.038). Citric Acid 124-131 serpin family C member 1 Homo sapiens 39-55 15882280-5 2005 After adjustment for illness severity, antithrombin-III levels increased significantly more over the period of study in the citrate as compared to the heparin group (P= 0.038). Heparin 151-158 serpin family C member 1 Homo sapiens 39-55 15882280-6 2005 Moreover, after adjustment for antithrombin-III levels and illness severity score, the relative risk of hemorrhage with citrate anticoagulation was significantly lower than that with heparin (relative risk of 0.14; 95% CI 0.02 to 0.96, P= 0.05). Citric Acid 120-127 serpin family C member 1 Homo sapiens 31-47 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Heparitin Sulfate 97-113 serpin family C member 1 Homo sapiens 148-160 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Superoxides 199-215 serpin family C member 1 Homo sapiens 63-75 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Superoxides 199-215 serpin family C member 1 Homo sapiens 148-160 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Adenosine Diphosphate 262-283 serpin family C member 1 Homo sapiens 63-75 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Adenosine Diphosphate 262-283 serpin family C member 1 Homo sapiens 148-160 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Adenosine Triphosphate 288-310 serpin family C member 1 Homo sapiens 63-75 15968398-3 2005 In this study, we report that platelets express syndecan-4, an antithrombin-binding cell surface heparan sulphate proteoglycan, whose ligation with antithrombin inhibits activated platelet-dependent superoxide anion release from neutrophils by the limitation of adenosine diphosphate and adenosine triphosphate secretion in activated platelets. Adenosine Triphosphate 288-310 serpin family C member 1 Homo sapiens 148-160 15968398-4 2005 Adenosine triphosphate-induced platelet aggregation is reduced after treatment of platelets with antithrombin, which is reversed by blockade of syndecan-4. Adenosine Triphosphate 0-22 serpin family C member 1 Homo sapiens 97-109 15968398-5 2005 We further observed that antithrombin limits CD40 ligand expression in adenosine diphosphate-activated platelets and inhibits the shedding of syndecan-4 from activated platelets. Adenosine Diphosphate 71-92 serpin family C member 1 Homo sapiens 25-37 15968398-7 2005 We suggest that antithrombin might exert beneficial effects in disseminated intravascular coagulation by reducing platelet activation, observed as inhibited CD40 ligand expression, syndecan-4 shedding, and adenosine diphosphate- and adenosine triphosphate-release from activated platelets with subsequent inhibition of neutrophil respiratory burst. Adenosine Diphosphate 206-227 serpin family C member 1 Homo sapiens 16-28 15968398-7 2005 We suggest that antithrombin might exert beneficial effects in disseminated intravascular coagulation by reducing platelet activation, observed as inhibited CD40 ligand expression, syndecan-4 shedding, and adenosine diphosphate- and adenosine triphosphate-release from activated platelets with subsequent inhibition of neutrophil respiratory burst. triphosphoric acid 243-255 serpin family C member 1 Homo sapiens 16-28 15968411-0 2005 Inihibition of cytokine response by methylprednisolone attenuates antithrombin reduction following hepatic resection. Methylprednisolone 36-54 serpin family C member 1 Homo sapiens 66-78 15839662-5 2005 Therefore, this case is different than that described for the controversial recognition of heparin-like saccharides by AT-III, which seems to recognize just one conformation of the iduronic acid residues. Heparin 91-98 serpin family C member 1 Homo sapiens 119-125 15924156-9 2005 Antithrombin concentrate is used in patients with antithrombin deficiency treated with heparin for acute venous thrombosis or embolism, extracorporeal circulation procedures or other invasive procedures. Heparin 87-94 serpin family C member 1 Homo sapiens 0-12 15924156-9 2005 Antithrombin concentrate is used in patients with antithrombin deficiency treated with heparin for acute venous thrombosis or embolism, extracorporeal circulation procedures or other invasive procedures. Heparin 87-94 serpin family C member 1 Homo sapiens 50-62 15924157-5 2005 Treatment with antithrombin and heparin resulted in a considerable increase in bleeding complications and on the other hand, may have antagonized the expected effect of antithrombin on the patient"s prognosis. Heparin 32-39 serpin family C member 1 Homo sapiens 169-181 15839662-5 2005 Therefore, this case is different than that described for the controversial recognition of heparin-like saccharides by AT-III, which seems to recognize just one conformation of the iduronic acid residues. Iduronic Acid 181-194 serpin family C member 1 Homo sapiens 119-125 15787598-4 2005 The formation of polymers results in the failure to secrete mutants of other members of the serpin superfamily: antithrombin, C1 inhibitor and alpha1-antichymotrypsin, to cause a plasma deficiency that results in the clinical syndromes of thrombosis, angio-oedema and emphysema respectively. Polymers 17-25 serpin family C member 1 Homo sapiens 112-124 15741074-5 2005 Consecutive binding of the thrombin inhibitors heparin, antithrombin III or the heparin-antithrombin III complex to the immobilized thrombin molecules, and binding of a ternary complex of heparin, anithrombin III, and thrombin to aptamers was evaluated. Heparin 80-87 serpin family C member 1 Homo sapiens 88-104 15741074-7 2005 Binding of heparin activated the formation of the inhibitory complex of antithrombin III with thrombin about 2.7-fold. Heparin 11-18 serpin family C member 1 Homo sapiens 72-88 15878740-5 2005 Minor amounts of particular a heparan sulfate (< 5% of the total arterial glycosaminoglycans) with high anticoagulant activity were also observed, as assessed by its retention on an antithrombin-affinity column. Heparitin Sulfate 30-45 serpin family C member 1 Homo sapiens 185-197 15878740-8 2005 One is based on antithrombin activation by the heparan sulfate expressed by the endothelial cells. Heparitin Sulfate 47-62 serpin family C member 1 Homo sapiens 16-28 15860994-6 2005 Fibrinolytic therapy, in combination with adjunctive antithrombin therapy that is simpler and quicker to administer (e.g., tenecteplase with enoxaparin), may be more efficacious and easier to use than regimens involving unfractionated heparin. Enoxaparin 141-151 serpin family C member 1 Homo sapiens 53-65 15860994-6 2005 Fibrinolytic therapy, in combination with adjunctive antithrombin therapy that is simpler and quicker to administer (e.g., tenecteplase with enoxaparin), may be more efficacious and easier to use than regimens involving unfractionated heparin. Heparin 235-242 serpin family C member 1 Homo sapiens 53-65 16124953-9 2005 A nonsignificant trend toward higher rates of major bleeding was seen at 7 days for enoxaparin-treated patients, in both the overall safety population and the population of patients who did not receive antithrombin treatment before randomization, but there was no difference in blood transfusions. Enoxaparin 84-94 serpin family C member 1 Homo sapiens 202-214 15736971-0 2005 The factor IXa heparin-binding exosite is a cofactor interactive site: mechanism for antithrombin-independent inhibition of intrinsic tenase by heparin. Heparin 15-22 serpin family C member 1 Homo sapiens 85-97 16161915-11 2005 Both simvastatin and atorvastatin markedly increased AT III (87%, 98%) in comparison to the initial values. Simvastatin 5-16 serpin family C member 1 Homo sapiens 53-59 16161915-11 2005 Both simvastatin and atorvastatin markedly increased AT III (87%, 98%) in comparison to the initial values. Atorvastatin 21-33 serpin family C member 1 Homo sapiens 53-59 15736971-1 2005 Therapeutic heparin concentrations selectively inhibit the intrinsic tenase complex in an antithrombin-independent manner. Heparin 12-19 serpin family C member 1 Homo sapiens 90-102 15804733-8 2005 Raloxifene decreased the levels of fibrinogen, from 354.7 to 302.0 g/l (p = 0.009) and the levels of antithrombin III, from 102.4 to 98.5% (p = 0.039). Raloxifene Hydrochloride 0-10 serpin family C member 1 Homo sapiens 101-117 15698795-4 2005 Most per-sulfated flavonoids studied are activators of antithrombin for accelerated inhibition of factor Xa, a key enzyme of the blood coagulation cascade. Flavonoids 18-28 serpin family C member 1 Homo sapiens 55-67 15715496-0 2005 Antithrombin activation by nonsulfated, non-polysaccharide organic polymer. Polysaccharides 44-58 serpin family C member 1 Homo sapiens 0-12 15715496-1 2005 Accelerated antithrombin inhibition of procoagulant enzymes has been exclusively achieved with polysulfated polysaccharides. Polysaccharides 108-123 serpin family C member 1 Homo sapiens 12-24 15715496-2 2005 We reasoned that antithrombin activation should be possible with nonsulfated activators based only on carboxylic acid groups. Carboxylic Acids 102-117 serpin family C member 1 Homo sapiens 17-29 15664348-5 2005 This column is highly specific as described by the dissociation constant of the complex of immobilized heparin and AT III, which was 2.83 x 10(-5)mol/L. Heparin 103-110 serpin family C member 1 Homo sapiens 115-121 15664348-3 2005 This heparin-viscose fiber material was used for purifying antithrombin III (AT III) from human plasma. Heparin 5-12 serpin family C member 1 Homo sapiens 59-75 15715496-3 2005 As a proof of the principle, linear poly(acrylic acid)s were found to bind to antithrombin and accelerate inhibition of factor Xa and thrombin. carbopol 940 36-55 serpin family C member 1 Homo sapiens 78-90 15664348-3 2005 This heparin-viscose fiber material was used for purifying antithrombin III (AT III) from human plasma. Heparin 5-12 serpin family C member 1 Homo sapiens 77-83 15664348-4 2005 The purity of the AT III from this one-step purification is 93% as measured by SDS-PAGE and the protein recovery yield is about 90%. Sodium Dodecyl Sulfate 79-82 serpin family C member 1 Homo sapiens 18-24 15715496-4 2005 Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators. Sulfates 58-65 serpin family C member 1 Homo sapiens 86-98 15715496-4 2005 Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators. Sulfates 58-65 serpin family C member 1 Homo sapiens 217-229 15715496-4 2005 Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators. carboxylate 199-210 serpin family C member 1 Homo sapiens 86-98 15715496-4 2005 Our work demonstrates that molecules completely devoid of sulfate groups can activate antithrombin effectively and, more importantly, suggests that it may be possible to develop orally bioavailable, carboxylate-based antithrombin activators. carboxylate 199-210 serpin family C member 1 Homo sapiens 217-229 15757405-8 2005 They include anti-Xa inhibitors, such as pentasaccharide, and antithrombin inhibitors, such as ximelagatran. ximelagatran 95-107 serpin family C member 1 Homo sapiens 62-74 15699163-7 2005 Fondaparinux, which is identical with the antithrombin III-binding pentasaccharide in heparin, did not bind to LBP or alter LBP function. pentasaccharide 67-82 serpin family C member 1 Homo sapiens 42-58 15699163-7 2005 Fondaparinux, which is identical with the antithrombin III-binding pentasaccharide in heparin, did not bind to LBP or alter LBP function. Heparin 86-93 serpin family C member 1 Homo sapiens 42-58 15652173-7 2005 The antithrombin-mediated anti-factor Xa activity of human liver heparan sulfate, however, was much lower than porcine intestinal (pharmaceutical) heparin but was comparable to standard porcine intestinal heparan sulfate. Heparitin Sulfate 65-80 serpin family C member 1 Homo sapiens 4-16 15749837-1 2005 Dermatan sulfate mediates the blood coagulation cascade by binding to heparin cofactor II and potentiating the antithrombin activity. Dermatan Sulfate 0-16 serpin family C member 1 Homo sapiens 111-123 15819171-4 2005 At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin. Heparin 15-22 serpin family C member 1 Homo sapiens 33-45 16156690-1 2005 Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin. Fondaparinux 0-19 serpin family C member 1 Homo sapiens 108-120 16156690-1 2005 Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin. Fondaparinux 21-33 serpin family C member 1 Homo sapiens 108-120 16156690-1 2005 Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin. pentasaccharide 59-74 serpin family C member 1 Homo sapiens 108-120 16156690-1 2005 Fondaparinux sodium (fondaparinux) is a synthetic sulfated pentasaccharide anticoagulant developed from the antithrombin binding moiety of heparin. Heparin 139-146 serpin family C member 1 Homo sapiens 108-120 16474289-4 2005 Prolonged hypothermic extracorporeal circulation and the high intraoperative blood loss (over 35 ml/kg bw) lead to an appreciable decrease in antithrombin III and protein C activity which results in activation of disseminated intravascular blood coagulation in the early postoperative period and ineffectiveness of heparin therapy. Heparin 315-322 serpin family C member 1 Homo sapiens 142-158 15743473-0 2005 Inhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis. Hyaluronic Acid 30-45 serpin family C member 1 Homo sapiens 14-26 15743473-5 2005 Various glycosaminoglycans, including HA, chondroitin sulfate, keratan sulfate, heparin, and heparan, were incubated with human antithrombin III in vitro. Glycosaminoglycans 8-26 serpin family C member 1 Homo sapiens 128-144 15743473-7 2005 HA concentrations ranging from 250 to 1000 mug/ml significantly blocked the ability of antithrombin to inhibit thrombin in the presence of Ca2+ or Fe3+, and chondroitin A, B and C also reduced this ability under the same conditions but to a lesser extent. ferric sulfate 147-151 serpin family C member 1 Homo sapiens 87-99 15819171-4 2005 At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin. Heparin 46-53 serpin family C member 1 Homo sapiens 33-45 15819171-4 2005 At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin. Heparin 46-53 serpin family C member 1 Homo sapiens 33-45 15819171-4 2005 At 0.2 U/ml of heparin, covalent antithrombin-heparin inhibited free thrombin generation to a greater degree than heparin and low molecular weight heparin. Heparin 46-53 serpin family C member 1 Homo sapiens 33-45 16218489-4 2005 This is the case of fondaparinux, a pentasaccharide which can interact with antithrombin, thus inhibiting factor Xa. pentasaccharide 36-51 serpin family C member 1 Homo sapiens 76-88 15604328-11 2005 CONCLUSION: Atorvastatin did not change the maximum hyperaemic flow, although it decreased plasma concentrations of antithrombin III, protein C, factor V, tPA, and PAI-1 in patients with heart failure. Atorvastatin 12-24 serpin family C member 1 Homo sapiens 116-132 15634277-5 2005 The mutation also significantly decreases (i) the catalytic activity of thrombin with a 9-fold reduction in catalytic efficiency of the mutant toward S-2238; (ii) the interaction with benzamidine; (iii) the rate of inhibition by TLCK and antithrombin; and (iv) the rate of hydrolysis of macromolecular substrates (fibrinogen, protein C). benzamidine 184-195 serpin family C member 1 Homo sapiens 238-250 15792676-8 2005 CONCLUSIONS: The correlation between TEG and PT, APTT and antithrombin level supports its value in providing a global measure of haemostasis. triethylene glycol 37-40 serpin family C member 1 Homo sapiens 58-70 16293985-6 2005 However, the complete loss of thrombin-induced VEGF production upon treatment with argatroban, a derivative of arginine and a potent anticoagulant/antithrombin agent, supports the notion that argatroban serves as a useful therapeutic tool for thrombin-associated pathologic conditions. argatroban 83-93 serpin family C member 1 Homo sapiens 147-159 16293985-6 2005 However, the complete loss of thrombin-induced VEGF production upon treatment with argatroban, a derivative of arginine and a potent anticoagulant/antithrombin agent, supports the notion that argatroban serves as a useful therapeutic tool for thrombin-associated pathologic conditions. argatroban 192-202 serpin family C member 1 Homo sapiens 147-159 15567465-7 2005 For both high and low coagulant challenges, clotting times increased and prothrombin fragment 1.2 and thrombin-antithrombin (TAT) formation decreased with melagatran in a concentration-dependent fashion in umbilical cord and adult plasma. melagatran 155-165 serpin family C member 1 Homo sapiens 111-123 15935830-1 2005 We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103. Methionine 205-215 serpin family C member 1 Homo sapiens 41-53 15608477-8 2005 AT III levels were positively correlated with plasma total cholesterol levels, plasma low density lipoprotein cholesterol levels, plasma triglycerides and D-dimer levels. Cholesterol 59-70 serpin family C member 1 Homo sapiens 0-6 15608477-8 2005 AT III levels were positively correlated with plasma total cholesterol levels, plasma low density lipoprotein cholesterol levels, plasma triglycerides and D-dimer levels. Triglycerides 137-150 serpin family C member 1 Homo sapiens 0-6 16521916-5 2005 Statistically significant relationship of AT III activity with age (Spearman"s rho=-0.23; p=0.002), trigliceride level (rho=0.17; p=0.03), Geriatric Depression Scale (rho=-0.17; p=0.03) and Instrumental Activities of Daily Living scale (rho=0.16; p=0.03) was found. trigliceride 100-112 serpin family C member 1 Homo sapiens 42-48 15567452-0 2005 Pharmacokinetics of UH and LMWH are similar with respect to antithrombin activity. Heparin, Low-Molecular-Weight 27-31 serpin family C member 1 Homo sapiens 60-72 15567452-4 2005 METHODS: We performed a clinical pharmacokinetic trial to compare the variability in peak antithrombin effect between subcutaneous unfractionated heparin and various LMWHs, all given in recommended weight-adjusted treatment doses. Heparin 146-153 serpin family C member 1 Homo sapiens 90-102 15935830-1 2005 We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103. Methionine 205-215 serpin family C member 1 Homo sapiens 55-57 15935830-1 2005 We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103. Methionine 217-220 serpin family C member 1 Homo sapiens 41-53 15578742-0 2004 Exact molecular mass determination of various forms of native and de-N-glycosylated human plasma-derived antithrombin by means of electrospray ionization ion trap mass spectrometry. Nitrogen 69-70 serpin family C member 1 Homo sapiens 105-117 15935830-1 2005 We studied a Japanese family with type I antithrombin (AT) deficiency and identified a novel in-frame deletion mutation (-ATG at nucleotide position of 2771-2773) in the AT gene, which predicted loss of a methionine (Met) at amino acid number of 103. Methionine 217-220 serpin family C member 1 Homo sapiens 55-57 15543318-0 2004 Accelerating ability of synthetic oligosaccharides on antithrombin inhibition of proteinases of the clotting and fibrinolytic systems. Oligosaccharides 34-50 serpin family C member 1 Homo sapiens 54-66 15371417-2 2004 The antithrombotic effect of heparin, however, is due primarily to the specific interaction of a fraction of heparin chains with the related serpin antithrombin (AT). Heparin 29-36 serpin family C member 1 Homo sapiens 148-160 15371417-2 2004 The antithrombotic effect of heparin, however, is due primarily to the specific interaction of a fraction of heparin chains with the related serpin antithrombin (AT). Heparin 109-116 serpin family C member 1 Homo sapiens 148-160 15543318-6 2004 A synthetic hexadecasaccharide, containing both the pentasaccharide sequence and a proteinase binding site, exerts its anticoagulant effect by accelerating antithrombin inactivation of both thrombin and factor Xa to rate constants of approximately 10(6) - 10(7) M(-1).s(-1), although thrombin appears to be the more important target. hexadecasaccharide 12-30 serpin family C member 1 Homo sapiens 156-168 15543318-6 2004 A synthetic hexadecasaccharide, containing both the pentasaccharide sequence and a proteinase binding site, exerts its anticoagulant effect by accelerating antithrombin inactivation of both thrombin and factor Xa to rate constants of approximately 10(6) - 10(7) M(-1).s(-1), although thrombin appears to be the more important target. pentasaccharide 52-67 serpin family C member 1 Homo sapiens 156-168 15543318-8 2004 The conformational change of antithrombin induced both by the pentasaccharides and longer heparins contributes substantially, approximately 150-500-fold, to accelerating the inactivation of factors Xa, IXa and VIIa and moderately, approximately 50-fold, to that of factor XIIa and tissue plasminogen activator inhibition. pentasaccharides 62-78 serpin family C member 1 Homo sapiens 29-41 15543318-8 2004 The conformational change of antithrombin induced both by the pentasaccharides and longer heparins contributes substantially, approximately 150-500-fold, to accelerating the inactivation of factors Xa, IXa and VIIa and moderately, approximately 50-fold, to that of factor XIIa and tissue plasminogen activator inhibition. Heparin 90-98 serpin family C member 1 Homo sapiens 29-41 15543318-9 2004 The bridging effect due to binding of antithrombin and proteinase to the same, long heparin chain is dominating, approximately 1000-3000-fold, for thrombin inhibition and is appreciably smaller, although up to approximately 250-350-fold, for the inactivation of factors IXa and XIa. Heparin 84-91 serpin family C member 1 Homo sapiens 38-50 15543318-2 2004 The abilities of three synthetic oligosaccharides to accelerate antithrombin inhibition of ten clotting or fibrinolytic proteinases were compared with those of unfractionated, fractionated high-affinity and low-molecular-weight heparins. Oligosaccharides 33-49 serpin family C member 1 Homo sapiens 64-76 15641292-7 2004 The great majority of the patients (99%) received oral antiplatelets during hospitalization and low molecular weight heparins were the preferred antithrombin therapy. Heparin 117-125 serpin family C member 1 Homo sapiens 145-157 15486847-5 2004 Although the presence of persistent antibody to phospholipids was the most common abnormal finding in the laboratory, evaluation of thrombophilia, cases of low levels of proteins C and S and antithrombin III, and elevated levels of factor VIII and homocysteine were also identified. Phospholipids 48-61 serpin family C member 1 Homo sapiens 191-207 15516868-4 2004 The APTT was prolonged on the PU-C-H and PU-P-H, suggesting the binding of immobilized heparin to the antithrombin III. Polyurethanes 30-32 serpin family C member 1 Homo sapiens 102-118 15516868-4 2004 The APTT was prolonged on the PU-C-H and PU-P-H, suggesting the binding of immobilized heparin to the antithrombin III. Polyurethanes 41-43 serpin family C member 1 Homo sapiens 102-118 15516868-4 2004 The APTT was prolonged on the PU-C-H and PU-P-H, suggesting the binding of immobilized heparin to the antithrombin III. Phosphorus 5-6 serpin family C member 1 Homo sapiens 102-118 15516868-4 2004 The APTT was prolonged on the PU-C-H and PU-P-H, suggesting the binding of immobilized heparin to the antithrombin III. Heparin 87-94 serpin family C member 1 Homo sapiens 102-118 15456490-7 2004 Interestingly, FXIa(WT) and FXIa-Glu555 cleave the small tripeptide substrate S-2366 with comparable k(cat)s. Modeling indicates that the side chain of Glu555 significantly alters the electrostatic charge around the active site, and would sterically interfere with the interaction between the FXIa S2" site and the P2" residues on factor IX and antithrombin. tripeptide K-26 57-67 serpin family C member 1 Homo sapiens 345-357 17491674-11 2004 The activity of ATIII was significantly lower in men with CAF/GF ratio >or= 1.17, as compared to those with CAF/GF < 1.17 (105.10 +/- 10.02 vs. 113.42 +/- 10.72 %, p < 0.05). Leu-Thr 119-121 serpin family C member 1 Homo sapiens 16-21 15325299-10 2004 We also focused our attention on di- and tetrasaccharidic species containing the 3-O-sulfated glucosamines taken as markers of the active sites for antithrombin III. Glucosamine 94-106 serpin family C member 1 Homo sapiens 148-164 15178583-1 2004 A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin. pentasaccharide 9-24 serpin family C member 1 Homo sapiens 75-87 15178583-1 2004 A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin. pentasaccharide 9-24 serpin family C member 1 Homo sapiens 262-274 15178583-1 2004 A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin. Heparin 37-44 serpin family C member 1 Homo sapiens 75-87 15178583-1 2004 A unique pentasaccharide fragment of heparin can enhance the reactivity of antithrombin with coagulation proteases factors IXa and Xa by 300- to 600-fold through a conformational activation of the serpin, without having a significant effect on the reactivity of antithrombin with thrombin. Heparin 37-44 serpin family C member 1 Homo sapiens 262-274 15231514-1 2004 Heparin is a major anticoagulant with activity mediated primarily through its interaction with antithrombin (AT). Heparin 0-7 serpin family C member 1 Homo sapiens 95-107 15178583-6 2004 These results suggest that structural differences in the autolysis loop of coagulation proteases play a key role in their differential reactivity with the native and heparin-activated conformations of antithrombin. Heparin 166-173 serpin family C member 1 Homo sapiens 201-213 15311268-1 2004 Antithrombin, the principal physiological inhibitor of the blood coagulation proteinase thrombin, requires heparin as a cofactor. Heparin 107-114 serpin family C member 1 Homo sapiens 0-12 15383472-2 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors. Heparin 0-3 serpin family C member 1 Homo sapiens 66-78 15383472-2 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 66-78 15383472-2 2004 UFH is a heterogeneous mixture of glycosaminoglycans that bind to antithrombin via a pentasaccharide, catalyzing the inactivation of thrombin and other clotting factors. pentasaccharide 85-100 serpin family C member 1 Homo sapiens 66-78 15311268-2 2004 We report the crystal structure of the rate-determining encounter complex formed between antithrombin, anhydrothrombin and an optimal synthetic 16-mer oligosaccharide. 16-mer oligosaccharide 144-166 serpin family C member 1 Homo sapiens 89-101 15311268-5 2004 The 16-mer oligosaccharide is just long enough to form the predicted bridge between the high-affinity pentasaccharide-binding site on antithrombin and the highly basic exosite 2 on thrombin, validating the design strategy for this synthetic heparin. 16-mer oligosaccharide 4-26 serpin family C member 1 Homo sapiens 134-146 15311268-5 2004 The 16-mer oligosaccharide is just long enough to form the predicted bridge between the high-affinity pentasaccharide-binding site on antithrombin and the highly basic exosite 2 on thrombin, validating the design strategy for this synthetic heparin. pentasaccharide 102-117 serpin family C member 1 Homo sapiens 134-146 15311268-5 2004 The 16-mer oligosaccharide is just long enough to form the predicted bridge between the high-affinity pentasaccharide-binding site on antithrombin and the highly basic exosite 2 on thrombin, validating the design strategy for this synthetic heparin. Heparin 241-248 serpin family C member 1 Homo sapiens 134-146 15311268-6 2004 The protein-protein and protein-oligosaccharide interactions together explain the basis for heparin activation of antithrombin as a thrombin inhibitor. Oligosaccharides 32-47 serpin family C member 1 Homo sapiens 114-126 15311269-0 2004 Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Heparin 39-46 serpin family C member 1 Homo sapiens 17-29 15311269-0 2004 Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. Heparin 103-110 serpin family C member 1 Homo sapiens 17-29 15311269-2 2004 Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans. Heparin 127-134 serpin family C member 1 Homo sapiens 0-12 15311269-2 2004 Antithrombin circulates at a high concentration, but only becomes capable of efficient thrombin inhibition on interaction with heparin or related glycosaminoglycans. Glycosaminoglycans 146-164 serpin family C member 1 Homo sapiens 0-12 15311269-3 2004 The anticoagulant properties of therapeutic heparin are mediated by its interaction with antithrombin, although the structural basis for this interaction is unclear. Heparin 44-51 serpin family C member 1 Homo sapiens 89-101 15311269-4 2004 Here we present the crystal structure at a resolution of 2.5 A of the ternary complex between antithrombin, thrombin and a heparin mimetic (SR123781). sr123781 140-148 serpin family C member 1 Homo sapiens 94-106 15311269-5 2004 The structure reveals a template mechanism with antithrombin and thrombin bound to the same heparin chain. Heparin 92-99 serpin family C member 1 Homo sapiens 48-60 15302778-1 2004 BACKGROUND: Unfractionated heparin (UFH) is the most widely used antithrombin during percutaneous coronary intervention (PCI). Heparin 27-34 serpin family C member 1 Homo sapiens 65-77 15339877-6 2004 These include fondaparinux and idraparinux, synthetic analogs of the pentasaccharide sequence that mediates the interaction of heparin and LMWH with antithrombin, and ximelagatran, an orally active inhibitor of thrombin. pentasaccharide 69-84 serpin family C member 1 Homo sapiens 149-161 15339877-6 2004 These include fondaparinux and idraparinux, synthetic analogs of the pentasaccharide sequence that mediates the interaction of heparin and LMWH with antithrombin, and ximelagatran, an orally active inhibitor of thrombin. Heparin 127-134 serpin family C member 1 Homo sapiens 149-161 15339877-6 2004 These include fondaparinux and idraparinux, synthetic analogs of the pentasaccharide sequence that mediates the interaction of heparin and LMWH with antithrombin, and ximelagatran, an orally active inhibitor of thrombin. Heparin, Low-Molecular-Weight 139-143 serpin family C member 1 Homo sapiens 149-161 15302778-1 2004 BACKGROUND: Unfractionated heparin (UFH) is the most widely used antithrombin during percutaneous coronary intervention (PCI). Heparin 36-39 serpin family C member 1 Homo sapiens 65-77 15334855-2 2004 When given intravenously, UFH quickly binds to and activates antithrombin, which then inhibits several activated factors in the clotting cascade. Heparin 26-29 serpin family C member 1 Homo sapiens 61-73 15326828-6 2004 Pharmaceutic research has developed new drugs, some of which are already on the market, such as fondaparinux, a pentasaccharide that can interact with antithrombin, thus inhibiting factor Xa. pentasaccharide 112-127 serpin family C member 1 Homo sapiens 151-163 15355575-0 2004 Determination of the stabilizer sucrose in a plasma-derived antithrombin process solution by hydrophilic interaction chromatography with evaporative light-scattering detection. Sucrose 32-39 serpin family C member 1 Homo sapiens 60-72 15355575-3 2004 A process sample of antithrombin (Atenativ) from Octapharma AB (Stockholm, Sweden) containing 20% sucrose is analyzed. Sucrose 98-105 serpin family C member 1 Homo sapiens 20-32 15194626-11 2004 The addition of antithrombin (0.2 units/ml) to heparinized blood samples further prolonged ACTs, but the difference was not statistically significant when compared with heparin alone. Heparin 47-54 serpin family C member 1 Homo sapiens 16-28 15282457-6 2004 Heparin bound nonspecifically to plasma proteins was measured after displacement with a chemically altered heparin with low affinity to antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 136-148 15282457-6 2004 Heparin bound nonspecifically to plasma proteins was measured after displacement with a chemically altered heparin with low affinity to antithrombin. Heparin 107-114 serpin family C member 1 Homo sapiens 136-148 15238596-0 2004 Efficacy and bleeding complications among patients randomized to enoxaparin or unfractionated heparin for antithrombin therapy in non-ST-Segment elevation acute coronary syndromes: a systematic overview. Enoxaparin 65-75 serpin family C member 1 Homo sapiens 106-118 15238596-0 2004 Efficacy and bleeding complications among patients randomized to enoxaparin or unfractionated heparin for antithrombin therapy in non-ST-Segment elevation acute coronary syndromes: a systematic overview. Heparin 94-101 serpin family C member 1 Homo sapiens 106-118 15219196-2 2004 The serpin antithrombin (AT) is an important physiological regulator of FXa activity in an inhibition reaction that is enhanced by heparin. Heparin 131-138 serpin family C member 1 Homo sapiens 11-23 15247982-2 2004 Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin. Heparin 128-135 serpin family C member 1 Homo sapiens 73-85 15247982-2 2004 Heparin cofactor II (HCII) is a serine protease inhibitor that resembles antithrombin (ATIII) in its ability to be activated by heparin. Heparin 128-135 serpin family C member 1 Homo sapiens 87-92 15219196-8 2004 These results support a theory that mutating individual Gla residues in FXa alters the calcium-induced conformational changes in the Gla region and affects the antithrombin-heparin inhibition reaction. Glutamic Acid 56-59 serpin family C member 1 Homo sapiens 160-172 15219196-0 2004 Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin. 1-Carboxyglutamic Acid 12-38 serpin family C member 1 Homo sapiens 116-128 15219196-0 2004 Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin. Calcium 87-94 serpin family C member 1 Homo sapiens 116-128 15219196-8 2004 These results support a theory that mutating individual Gla residues in FXa alters the calcium-induced conformational changes in the Gla region and affects the antithrombin-heparin inhibition reaction. Calcium 87-94 serpin family C member 1 Homo sapiens 160-172 15219196-0 2004 Role of the gamma-carboxyglutamic acid domain of activated factor X in the presence of calcium during inhibition by antithrombin-heparin. Heparin 129-136 serpin family C member 1 Homo sapiens 116-128 15372880-1 2004 A new assay based on using an original chromogenic substrate (z-Ala-Ala-Arg-pNa) and designed for the determination of antithrombin III is described in the paper. z-ala-ala-arg 62-75 serpin family C member 1 Homo sapiens 119-135 15060080-1 2004 Heparan sulfate interacts with antithrombin, a protease inhibitor, to regulate blood coagulation. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 31-43 15199558-0 2004 A synthetic antithrombin III binding pentasaccharide is now a drug! pentasaccharide 37-52 serpin family C member 1 Homo sapiens 12-28 15199558-3 2004 In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade. pentasaccharide 51-66 serpin family C member 1 Homo sapiens 107-123 15199558-3 2004 In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade. pentasaccharide 51-66 serpin family C member 1 Homo sapiens 125-131 15199558-3 2004 In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade. Heparin 82-89 serpin family C member 1 Homo sapiens 107-123 15199558-3 2004 In the early 1980s it was discovered that a unique pentasaccharide domain in some heparin chains activates antithrombin III (AT-III), a serine protease inhibitor that blocks thrombin and factor Xa in the coagulation cascade. Heparin 82-89 serpin family C member 1 Homo sapiens 125-131 15199558-5 2004 The resulting antithrombotic drug arixtra, which went on the market in the USA and Europe in 2002, shows superior antithrombotic activity and brings about AT-III-mediated activity against factor Xa exclusively. Fondaparinux 34-41 serpin family C member 1 Homo sapiens 155-161 15199558-6 2004 Structure-based design has subsequently led to analogues with longer-lasting activity, such as idraparinux, as well as novel conjugates and long oligosaccharides with specific anti-Xa and antithrombin activities. Oligosaccharides 145-161 serpin family C member 1 Homo sapiens 188-200 15317404-3 2004 Fondaparinux, a new, synthetic pentasaccharide, binds to antithrombin III and potentiates antithrombin III"s inhibition of factor Xa. pentasaccharide 31-46 serpin family C member 1 Homo sapiens 57-73 15317404-3 2004 Fondaparinux, a new, synthetic pentasaccharide, binds to antithrombin III and potentiates antithrombin III"s inhibition of factor Xa. pentasaccharide 31-46 serpin family C member 1 Homo sapiens 90-106 15060080-3 2004 This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin. Phosphoadenosine Phosphosulfate 54-91 serpin family C member 1 Homo sapiens 235-247 15060080-3 2004 This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin. Glucosamine 118-129 serpin family C member 1 Homo sapiens 235-247 15060080-3 2004 This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin. 3-o-sulfo glucosamine 150-171 serpin family C member 1 Homo sapiens 235-247 15060080-3 2004 This enzyme transfers the sulfuryl group (SO(3)) from 3"-phosphoadenosine 5"-phosphosulfate to the 3-OH position of a glucosamine residue to form the 3-O-sulfo glucosamine, a structural motif critical for binding of heparan sulfate to antithrombin. Heparitin Sulfate 216-231 serpin family C member 1 Homo sapiens 235-247 15140129-0 2004 Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis. Disulfides 71-80 serpin family C member 1 Homo sapiens 35-47 15170430-3 2004 Because of a severe antithombin deficiency, regular infusions of antithrombin concentrates were necessary until delivery to ensure effective anticoagulation by heparin. Heparin 160-167 serpin family C member 1 Homo sapiens 65-77 15164384-1 2004 Antithrombin (AT), the most important coagulation serine proteases inhibitor, plays an important role in maintaining the hemostatic balance. Serine 50-56 serpin family C member 1 Homo sapiens 0-12 15140129-11 2004 The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop. Disulfides 69-78 serpin family C member 1 Homo sapiens 13-25 15353914-4 2004 Hemodilution associated with ANH may reduce the effectiveness of heparin anticoagulation due to dilution of antithrombin. Heparin 65-72 serpin family C member 1 Homo sapiens 108-120 15140129-11 2004 The abnormal antithrombin purified from P80S carriers is an inactive disulfide-linked dimer of mutant antithrombin whose properties are consistent with head-to-head insertion of the reactive loop. Disulfides 69-78 serpin family C member 1 Homo sapiens 102-114 14996843-0 2004 Antithrombin-mediated anticoagulant activity of sulfated polysaccharides: different mechanisms for heparin and sulfated galactans. Polysaccharides 57-72 serpin family C member 1 Homo sapiens 0-12 14996843-7 2004 4) Possibly, it is the bulk structure of the sulfated galactan, and not a specific minor component as in heparin, that determines its interaction with antithrombin. Galactans 54-62 serpin family C member 1 Homo sapiens 151-163 14996843-10 2004 6) Sulfated galactan and heparin bind to different sites on antithrombin. Heparin 25-32 serpin family C member 1 Homo sapiens 60-72 14996843-11 2004 7) Sulfated galactans are less effective than heparin at promoting antithrombin conformational activation. Heparin 46-53 serpin family C member 1 Homo sapiens 67-79 14996843-14 2004 The conformational activation of antithrombin and the consequent formation of a covalent complex with thrombin appear to be less important for the anticoagulant activity of sulfated galactan than for heparin. Galactans 182-190 serpin family C member 1 Homo sapiens 33-45 14996843-15 2004 Our results demonstrate that the paradigm of heparin-antithrombin interaction cannot be extended to other sulfated polysaccharides. Polysaccharides 115-130 serpin family C member 1 Homo sapiens 53-65 15196003-5 2004 Low molecular weight heparin accelerates the inhibition of trypsin by antithrombin by a factor of 16 [d(t)=0.36 s]. Heparin 21-28 serpin family C member 1 Homo sapiens 70-82 15005625-1 2004 A unique pentasaccharide fragment of high-affinity heparin activates antithrombin (AT) to enhance its rate of complex formation with factor Xa (FXa) by 200-300-fold. pentasaccharide 9-24 serpin family C member 1 Homo sapiens 69-81 15186640-6 2004 We believe that malabsorption of vitamin K dependent proteins C, S and antithrombin due to bariatric surgery predisposed the patient to purpura fulminans and disseminated intravascular coagulation. Vitamin K 33-42 serpin family C member 1 Homo sapiens 71-83 15931699-1 2004 AIM: To analyse the correlation between coagulation tests (PT APTT fibrinogen, D-dimer) and albumin with AT-II in DHF as well to find the formula to calculate AT-III with the parameter of coagulation tests and albumin. dhf 114-117 serpin family C member 1 Homo sapiens 159-165 15931699-5 2004 RESULTS: A significant correlation was found between PT and AT-III (r= -0.631; p=0.000), between D-dimer and AT-III (r= -0.337; p=0.021) and between albumin and AT-III (r= 0.291; p-0.045). Platinum 53-55 serpin family C member 1 Homo sapiens 60-66 15931699-8 2004 PT, D-dimer and AT-III were correlated with the grading severity of the DHF. dhf 72-75 serpin family C member 1 Homo sapiens 16-22 15168893-1 2004 Clinical practice over the past decade has evolved to include new agents, LMWH and synthetic polysaccharides, that bind to and enhance the activity of antithrombin similar to UFH. Heparin, Low-Molecular-Weight 74-78 serpin family C member 1 Homo sapiens 151-163 15168893-1 2004 Clinical practice over the past decade has evolved to include new agents, LMWH and synthetic polysaccharides, that bind to and enhance the activity of antithrombin similar to UFH. Polysaccharides 93-108 serpin family C member 1 Homo sapiens 151-163 15073698-0 2004 Decreased concentration of antithrombin after preoperative therapeutic heparin does not cause heparin resistance during cardiopulmonary bypass. Heparin 71-78 serpin family C member 1 Homo sapiens 27-39 15073698-1 2004 OBJECTIVE: To determine if preoperative heparin therapy causes an increase in the incidence of intraoperative heparin resistance by reducing the concentration of antithrombin in plasma. Heparin 40-47 serpin family C member 1 Homo sapiens 162-174 15073698-1 2004 OBJECTIVE: To determine if preoperative heparin therapy causes an increase in the incidence of intraoperative heparin resistance by reducing the concentration of antithrombin in plasma. Heparin 110-117 serpin family C member 1 Homo sapiens 162-174 15073698-9 2004 Comparison of heparin-resistant and heparin-responsive POHI patients showed that the concentration of antithrombin did not differ before bypass (82.4% and 79.8%, respectively, p = 0.53) or during bypass (51.8% and 51.4%, respectively, p = 0.91). Heparin 36-43 serpin family C member 1 Homo sapiens 102-114 15073698-10 2004 In fact, antithrombin concentrations were slightly higher in the heparin-resistant POHI patients (not significant). Heparin 65-72 serpin family C member 1 Homo sapiens 9-21 15073698-12 2004 CONCLUSIONS: Preoperative heparin causes an increased incidence of heparin resistance and reduced antithrombin concentrations. Heparin 26-33 serpin family C member 1 Homo sapiens 98-110 15162900-2 2004 Unfractionated heparin and low-molecular-weight heparins may not provide effective anticoagulation since they require antithrombin for activity. Heparin 48-56 serpin family C member 1 Homo sapiens 118-130 15162900-10 2004 Direct thrombin inhibitors, such as argatroban, seem to be suitable alternatives for acute anticoagulation in patients with antithrombin deficiency. argatroban 36-46 serpin family C member 1 Homo sapiens 124-136 15116263-0 2004 Binding of heparin to plasma proteins and endothelial surfaces is inhibited by covalent linkage to antithrombin. Heparin 11-18 serpin family C member 1 Homo sapiens 99-111 15116263-3 2004 Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH. Heparin 36-43 serpin family C member 1 Homo sapiens 20-32 15116263-3 2004 Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH. Heparin 114-117 serpin family C member 1 Homo sapiens 20-32 15116263-3 2004 Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH. Heparin, Low-Molecular-Weight 122-126 serpin family C member 1 Homo sapiens 20-32 15116263-3 2004 Covalent linkage of antithrombin to heparin gave a complex (ATH) with superior anticoagulant activity compared to UFH and LMWH, and longer intravenous half-life compared to UFH. Heparin 173-176 serpin family C member 1 Homo sapiens 20-32 15116263-8 2004 Although ATH is polydisperse, the covalently-linked antithrombin may shield a portion of the heparin chain from association with plasma or endothelial cell surface proteins. Heparin 93-100 serpin family C member 1 Homo sapiens 52-64 15210403-13 2004 In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity. Heparin, Low-Molecular-Weight 18-22 serpin family C member 1 Homo sapiens 157-169 15210403-13 2004 In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity. Dalteparin 24-34 serpin family C member 1 Homo sapiens 157-169 15210403-13 2004 In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity. Enoxaparin 36-46 serpin family C member 1 Homo sapiens 157-169 15210403-13 2004 In most instances LMWH (dalteparin, enoxaparin, nadroparin) treatment for DVT may be given once daily at a fixed dose without any harm, based on a prolonged antithrombin activity. Nadroparin 48-58 serpin family C member 1 Homo sapiens 157-169 15171962-1 2004 Argatroban represents the first antithrombin agent that was approved for clinical use. argatroban 0-10 serpin family C member 1 Homo sapiens 32-44 14707039-8 2004 The functionality of immobilized heparin was confirmed by specific uptake of antithrombin, 13.5+/-4.7 pmol/cm2 and 1.95+/-0.21 pmol/cm2 for mildly and heavily periodated heparin, respectively. Heparin 33-40 serpin family C member 1 Homo sapiens 77-89 14707039-8 2004 The functionality of immobilized heparin was confirmed by specific uptake of antithrombin, 13.5+/-4.7 pmol/cm2 and 1.95+/-0.21 pmol/cm2 for mildly and heavily periodated heparin, respectively. Heparin 170-177 serpin family C member 1 Homo sapiens 77-89 15171962-3 2004 Unlike the other antithrombin drugs, such as hirudins and hirulogs, argatroban is a reversible antithrombin agent and therefore exhibits a considerably different pharmacological profile. argatroban 68-78 serpin family C member 1 Homo sapiens 17-29 15171962-3 2004 Unlike the other antithrombin drugs, such as hirudins and hirulogs, argatroban is a reversible antithrombin agent and therefore exhibits a considerably different pharmacological profile. argatroban 68-78 serpin family C member 1 Homo sapiens 95-107 14711523-0 2004 Separation of latent, prelatent, and native forms of human antithrombin by heparin affinity high-performance liquid chromatography. Heparin 75-82 serpin family C member 1 Homo sapiens 59-71 14694355-7 2004 Specifically mutant alleles of antithrombin, C1-inhibitor and alpha(1)-antichymotrypsin have been reported that favour the spontaneous formation of polymers and the retention of protein within hepatocytes. Polymers 148-156 serpin family C member 1 Homo sapiens 31-43 14687916-4 2004 The inhibitory activity of antithrombin is controlled by its interaction with the co-factor, heparin, which accelerates its interaction with target proteases. Heparin 93-100 serpin family C member 1 Homo sapiens 27-39 14705167-3 2004 Heparin-based anticoagulants are indirect inhibitors that enhance the proteinase inhibitory activity of a natural anticoagulant, antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 129-141 14705167-12 2004 synthetic non-sugar antithrombin activators. Sugars 14-19 serpin family C member 1 Homo sapiens 20-32 15000687-2 2004 Heparin and pentosan polysulfate stabilized antithrombin III; this resulted in decrease in ultrasonic-induced formation of the aggregate and latent forms. Heparin 0-7 serpin family C member 1 Homo sapiens 44-60 15000687-2 2004 Heparin and pentosan polysulfate stabilized antithrombin III; this resulted in decrease in ultrasonic-induced formation of the aggregate and latent forms. Pentosan Sulfuric Polyester 12-32 serpin family C member 1 Homo sapiens 44-60 15259286-0 2004 Low-dose oral combination of 17beta-estradiol and norethisterone acetate in postmenopausal women decreases factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1. Estradiol 29-45 serpin family C member 1 Homo sapiens 131-143 15259286-0 2004 Low-dose oral combination of 17beta-estradiol and norethisterone acetate in postmenopausal women decreases factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1. Norethindrone Acetate 50-72 serpin family C member 1 Homo sapiens 131-143 15259286-5 2004 RESULTS: The two low doses of E2-NETA induced significantly lower plasma levels of factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1 (PAI-1), compared with placebo treatmen CONCLUSIONS: Low-dose E2 (1 mg) in combination with NETA resulted in favorable changes of factor VII activity and fibrinogen, compared with placebo. e2-neta 30-37 serpin family C member 1 Homo sapiens 107-119 15259286-5 2004 RESULTS: The two low doses of E2-NETA induced significantly lower plasma levels of factor VII, fibrinogen, antithrombin and plasminogen activator inhibitor-1 (PAI-1), compared with placebo treatmen CONCLUSIONS: Low-dose E2 (1 mg) in combination with NETA resulted in favorable changes of factor VII activity and fibrinogen, compared with placebo. Norethindrone Acetate 33-37 serpin family C member 1 Homo sapiens 107-119 14623882-0 2004 The influence of hinge region residue Glu-381 on antithrombin allostery and metastability. Glutamic Acid 38-41 serpin family C member 1 Homo sapiens 49-61 14623882-1 2004 Antithrombin becomes an efficient inhibitor of factor Xa and thrombin by binding a specific pentasaccharide sequence found on a small fraction of the heparan sulfate proteoglycans lining the microvaculature. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 0-12 14623882-2 2004 In the structure of native antithrombin, the reactive center loop is restrained due to the insertion of its hinge region into the main beta-sheet A, whereas in the heparin-activated state the reactive center loop is freed from beta-sheet A. Heparin 164-171 serpin family C member 1 Homo sapiens 27-39 14759471-3 2004 In our case, due to the poor reversibility of the antithrombin agents, argatroban was chosen as a heparin substitute due to its short half-life and its anticoagulation assessment using the activated clotting time (ACT). argatroban 71-81 serpin family C member 1 Homo sapiens 50-62 14679575-1 2003 The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods. polyacrylamide 156-170 serpin family C member 1 Homo sapiens 46-62 15085469-1 2004 The 87-year history of heparin began in 1916 when a 26-year-old medical student named Jay McLean startled his mentor William Howell, Professor of Physiology at Johns Hopkins University, by proclaiming that he had discovered "antithrombin." Heparin 23-30 serpin family C member 1 Homo sapiens 225-237 15085469-12 2004 The first synthetic product was called the pentasaccharide, named for the five critical sugar units in heparin that bind to antithrombin (1983). pentasaccharide 43-58 serpin family C member 1 Homo sapiens 124-136 15085469-12 2004 The first synthetic product was called the pentasaccharide, named for the five critical sugar units in heparin that bind to antithrombin (1983). Sugars 88-93 serpin family C member 1 Homo sapiens 124-136 15085469-12 2004 The first synthetic product was called the pentasaccharide, named for the five critical sugar units in heparin that bind to antithrombin (1983). Heparin 103-110 serpin family C member 1 Homo sapiens 124-136 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Heparin 0-7 serpin family C member 1 Homo sapiens 214-230 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Iduronic Acid 18-31 serpin family C member 1 Homo sapiens 214-230 15513323-4 2004 RESULTS: Pretreatment plasminogen activator inhibitor 1 (PAI-1) levels correlated negatively to SHBG and antithrombin III (AT III) negatively to total and free cortisol. Hydrocortisone 160-168 serpin family C member 1 Homo sapiens 105-121 15513323-4 2004 RESULTS: Pretreatment plasminogen activator inhibitor 1 (PAI-1) levels correlated negatively to SHBG and antithrombin III (AT III) negatively to total and free cortisol. Hydrocortisone 160-168 serpin family C member 1 Homo sapiens 123-129 14519763-5 2003 We have demonstrated the feasibility of this new approach to rapidly assemble antithrombin III-binding classical and non-classical anticoagulant polysaccharide structures for the first time. Polysaccharides 145-159 serpin family C member 1 Homo sapiens 78-94 14532267-1 2003 We have previously shown that exosites in antithrombin outside the P6-P3" reactive loop region become available upon heparin activation to promote rapid inhibition of the target proteases, factor Xa and factor IXa. Heparin 117-124 serpin family C member 1 Homo sapiens 42-54 14532267-3 2003 All chimeras bound heparin with a high affinity similar to wild-type, underwent heparin-induced fluorescence changes indicative of normal conformational activation, and were able to form SDS-stable complexes with thrombin, factor Xa, and factor IXa and inhibit these proteases with stoichiometries minimally altered from those of wild-type antithrombin. Heparin 19-26 serpin family C member 1 Homo sapiens 340-352 14532267-3 2003 All chimeras bound heparin with a high affinity similar to wild-type, underwent heparin-induced fluorescence changes indicative of normal conformational activation, and were able to form SDS-stable complexes with thrombin, factor Xa, and factor IXa and inhibit these proteases with stoichiometries minimally altered from those of wild-type antithrombin. Sodium Dodecyl Sulfate 187-190 serpin family C member 1 Homo sapiens 340-352 14730971-0 2004 Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change. Heparin 79-86 serpin family C member 1 Homo sapiens 63-75 14730971-0 2004 Roles of N-terminal region residues Lys11, Arg13, and Arg24 of antithrombin in heparin recognition and in promotion and stabilization of the heparin-induced conformational change. Heparin 141-148 serpin family C member 1 Homo sapiens 63-75 14730971-1 2004 The N-terminal region residues, Lys11, Arg13, and Arg24, of the plasma coagulation inhibitor, antithrombin, have been implicated in binding of the anticoagulant polysaccharide, heparin, from the identification of natural mutants with impaired heparin binding or by the X-ray structure of a complex of the inhibitor with a high-affinity heparin pentasaccharide. Polysaccharides 161-175 serpin family C member 1 Homo sapiens 94-106 14730971-1 2004 The N-terminal region residues, Lys11, Arg13, and Arg24, of the plasma coagulation inhibitor, antithrombin, have been implicated in binding of the anticoagulant polysaccharide, heparin, from the identification of natural mutants with impaired heparin binding or by the X-ray structure of a complex of the inhibitor with a high-affinity heparin pentasaccharide. Heparin 177-184 serpin family C member 1 Homo sapiens 94-106 14730971-1 2004 The N-terminal region residues, Lys11, Arg13, and Arg24, of the plasma coagulation inhibitor, antithrombin, have been implicated in binding of the anticoagulant polysaccharide, heparin, from the identification of natural mutants with impaired heparin binding or by the X-ray structure of a complex of the inhibitor with a high-affinity heparin pentasaccharide. Heparin 243-250 serpin family C member 1 Homo sapiens 94-106 14730971-1 2004 The N-terminal region residues, Lys11, Arg13, and Arg24, of the plasma coagulation inhibitor, antithrombin, have been implicated in binding of the anticoagulant polysaccharide, heparin, from the identification of natural mutants with impaired heparin binding or by the X-ray structure of a complex of the inhibitor with a high-affinity heparin pentasaccharide. IC 831423 336-359 serpin family C member 1 Homo sapiens 94-106 14730971-6 2004 The N-terminal region of antithrombin is thus critical for high-affinity heparin binding, Lys11 and Arg24 being responsible for maintaining appreciable and comparable binding energy, whereas Arg13 is less important. Heparin 73-80 serpin family C member 1 Homo sapiens 25-37 14730971-10 2004 Together, these findings show that N-terminal residues of antithrombin make markedly different contributions to the energetics and dynamics of binding of the pentasaccharide ligand to the native and activated conformational states of the inhibitor that could not have been predicted from the X-ray structure. pentasaccharide 158-173 serpin family C member 1 Homo sapiens 58-70 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Glycosaminoglycans 43-61 serpin family C member 1 Homo sapiens 214-230 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Glycosaminoglycans 63-66 serpin family C member 1 Homo sapiens 214-230 15078125-1 2004 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate 76-92 serpin family C member 1 Homo sapiens 214-230 15233593-1 2004 Fondaparinux sodium (Arixtra; fondaparinux) is the first of a new class of synthetic pentasaccharide anticoagulants that bind to antithrombin and inhibit the action of factor Xa. Fondaparinux 0-19 serpin family C member 1 Homo sapiens 129-141 15233593-1 2004 Fondaparinux sodium (Arixtra; fondaparinux) is the first of a new class of synthetic pentasaccharide anticoagulants that bind to antithrombin and inhibit the action of factor Xa. Fondaparinux 21-28 serpin family C member 1 Homo sapiens 129-141 15233593-1 2004 Fondaparinux sodium (Arixtra; fondaparinux) is the first of a new class of synthetic pentasaccharide anticoagulants that bind to antithrombin and inhibit the action of factor Xa. pentasaccharide 85-100 serpin family C member 1 Homo sapiens 129-141 12907439-0 2003 Heparin-induced substrate behavior of antithrombin Cambridge II. Heparin 0-7 serpin family C member 1 Homo sapiens 38-50 12907439-3 2003 Antithrombin Cambridge II was found to be normal in its affinity for heparin, its ability to form sodium dodecyl sulfate-stable complexes with factor Xa and thrombin, and its uncatalyzed stoichiometries and rates of inhibition. Heparin 69-76 serpin family C member 1 Homo sapiens 0-12 12907439-3 2003 Antithrombin Cambridge II was found to be normal in its affinity for heparin, its ability to form sodium dodecyl sulfate-stable complexes with factor Xa and thrombin, and its uncatalyzed stoichiometries and rates of inhibition. Sodium Dodecyl Sulfate 98-120 serpin family C member 1 Homo sapiens 0-12 12907439-5 2003 The stoichiometries were not affected by pentasaccharides, indicating that the inhibitory mechanism of antithrombin Cambridge II is perturbed only in the presence of a bridging glycosaminoglycan. Glycosaminoglycans 177-194 serpin family C member 1 Homo sapiens 103-115 14679575-1 2003 The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods. 2-Isopropoxyethanol 207-210 serpin family C member 1 Homo sapiens 64-69 14679575-4 2003 ATIII-alpha and ATIII-beta-fractions preseparated by heparin affinity chromatography showed an analogous but shifted spot pattern consisting each of one major and three minor isoforms. Heparin 53-60 serpin family C member 1 Homo sapiens 0-5 14679575-4 2003 ATIII-alpha and ATIII-beta-fractions preseparated by heparin affinity chromatography showed an analogous but shifted spot pattern consisting each of one major and three minor isoforms. Heparin 53-60 serpin family C member 1 Homo sapiens 16-21 14679575-5 2003 The main isoforms of ATIII-alpha and ATIII-beta exhibit pI values of 5.18 and 5.32, respectively, both values determined in the presence of high concentrations of urea. Urea 163-167 serpin family C member 1 Homo sapiens 21-26 14679575-5 2003 The main isoforms of ATIII-alpha and ATIII-beta exhibit pI values of 5.18 and 5.32, respectively, both values determined in the presence of high concentrations of urea. Urea 163-167 serpin family C member 1 Homo sapiens 37-42 14679575-1 2003 The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods. polyacrylamide 156-170 serpin family C member 1 Homo sapiens 64-69 14679575-1 2003 The isoforms distribution of the glycoprotein antithrombin III (ATIII) derived from human plasma was investigated by means of isoelectric focusing (IEF) in polyacrylamide gels with immobilized pH gradients (IPG) and two-dimensional gel electrophoresis (2-DE) as well as capillary electrophoretic methods. 2-Isopropoxyethanol 207-210 serpin family C member 1 Homo sapiens 46-62 14652650-9 2003 Concomitant incubation with pentasaccharide abolished this effect of antithrombin. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 69-81 14719183-0 2003 Modulation of antithrombin-protease interactions by semisynthetic low-molecular-weight heparins with different sulfation patterns. Heparin 87-95 serpin family C member 1 Homo sapiens 14-26 14719183-3 2003 To gain insight into structure-activity relationships, we investigated the interaction of a homogeneous series of sulfated polysaccharides, derived from controlled desulfation of a supersulfated low-molecular-weight heparin (LMWH) with the target enzymes human antithrombin (AT) and thrombin (T). Polysaccharides 123-138 serpin family C member 1 Homo sapiens 261-273 14652650-13 2003 From our results, we can conclude that endotoxin-induced adhesion of leukocytes to endothelium can be reversed by ligation of syndecan-4 with antithrombin"s heparin-binding site and interferences with stress response signaling events in endothelium. Heparin 157-164 serpin family C member 1 Homo sapiens 142-154 14607764-3 2003 It is a pentasaccharide mimicking the site where heparin binds to antithrombin III (1). pentasaccharide 8-23 serpin family C member 1 Homo sapiens 66-82 14650860-5 2003 Inhibition of factor Xa via antithrombin (AT) by fondaparinux has been studied extensively. Fondaparinux 49-61 serpin family C member 1 Homo sapiens 28-40 14575696-0 2003 Platelet factor 4 neutralizes heparan sulfate-enhanced antithrombin inactivation of factor Xa by preventing interaction(s) of enzyme with polysaccharide. Heparitin Sulfate 30-45 serpin family C member 1 Homo sapiens 55-67 14575696-0 2003 Platelet factor 4 neutralizes heparan sulfate-enhanced antithrombin inactivation of factor Xa by preventing interaction(s) of enzyme with polysaccharide. Polysaccharides 138-152 serpin family C member 1 Homo sapiens 55-67 14607764-3 2003 It is a pentasaccharide mimicking the site where heparin binds to antithrombin III (1). Heparin 49-56 serpin family C member 1 Homo sapiens 66-82 14502551-6 2003 We show here that, similar to antithrombin, a member of the FGF family, FGF7, selectively captures anti-Factor Xa and anti-Factor IIa activity from commercially and clinically applied heparin mixtures. Heparin 184-191 serpin family C member 1 Homo sapiens 30-42 14528313-0 2003 Enzymatic synthesis of antithrombin III-binding heparan sulfate pentasaccharide. heparan sulfate pentasaccharide 48-79 serpin family C member 1 Homo sapiens 23-39 14528313-4 2003 We rapidly and efficiently assembled the antithrombin III-binding pentasaccharide in just 6 steps, in contrast to the approximately 60 steps needed for its chemical synthesis, with an overall yield at least twofold greater and a completion time at least 100 times faster than for the chemical process. pentasaccharide 66-81 serpin family C member 1 Homo sapiens 41-57 13679071-1 2003 Antithrombin (AT) circulates in two isoforms, alpha- (90-95%) and beta-AT (5-10%). methylphenyl carbinol 46-52 serpin family C member 1 Homo sapiens 0-12 13679071-1 2003 Antithrombin (AT) circulates in two isoforms, alpha- (90-95%) and beta-AT (5-10%). beta-at 66-73 serpin family C member 1 Homo sapiens 0-12 14564303-1 2003 BACKGROUND: Unfractionated heparin has been the cornerstone of antithrombin therapy in the treatment of non-ST-segment elevation acute coronary syndromes for more than a decade. Heparin 27-34 serpin family C member 1 Homo sapiens 63-75 14502551-8 2003 This may provide a novel cost-effective, bioaffinity-based alternative to antithrombin for concurrent enrichment and recovery of anticoagulant and nonanticoagulant heparin from the same heparin mixture. Heparin 164-171 serpin family C member 1 Homo sapiens 74-86 14566786-4 2003 We demonstrate that the blood compatibility of a surface with regard to coagulation, complement, and platelet activation can be improved by increasing the heparin surface concentration in the 6-12 pmol antithrombin/cm2 concentration interval. Heparin 155-162 serpin family C member 1 Homo sapiens 202-214 14566788-0 2003 Interactions of antithrombin and proteins in the plasma contact activation system with immobilized functional heparin. Heparin 110-117 serpin family C member 1 Homo sapiens 16-28 15199446-4 2003 Larger clinical studies are needed to confirm the safety and efficacy of LMWH as an antithrombin for the treatment across the spectrum of ACS. Heparin, Low-Molecular-Weight 73-77 serpin family C member 1 Homo sapiens 84-96 14511765-1 2003 In the blood coagulation cascade, human antithrombin III (hAT III) acts as an inhibitor of serine proteases such as thrombin and factor Xa, and this anticoagulatory glycoprotein requires the binding of heparin for its activation. Heparin 202-209 serpin family C member 1 Homo sapiens 40-56 14511765-1 2003 In the blood coagulation cascade, human antithrombin III (hAT III) acts as an inhibitor of serine proteases such as thrombin and factor Xa, and this anticoagulatory glycoprotein requires the binding of heparin for its activation. Heparin 202-209 serpin family C member 1 Homo sapiens 58-65 14511765-2 2003 In this study, we synthesized the polypeptides corresponding to the proposed heparin-binding sites including the (41-49), (286-301) and (123-139) regions of hAT III, and examined their interactions with heparin by means of physicochemical and biochemical methods. Heparin 77-84 serpin family C member 1 Homo sapiens 157-164 14511765-2 2003 In this study, we synthesized the polypeptides corresponding to the proposed heparin-binding sites including the (41-49), (286-301) and (123-139) regions of hAT III, and examined their interactions with heparin by means of physicochemical and biochemical methods. Heparin 203-210 serpin family C member 1 Homo sapiens 157-164 14511765-4 2003 In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin. Heparin 56-63 serpin family C member 1 Homo sapiens 13-20 14511765-4 2003 In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin. Heparin 56-63 serpin family C member 1 Homo sapiens 85-92 14511765-4 2003 In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin. Heparin 56-63 serpin family C member 1 Homo sapiens 85-92 14511765-4 2003 In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin. Heparin 200-207 serpin family C member 1 Homo sapiens 13-20 14511765-4 2003 In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin. Heparin 200-207 serpin family C member 1 Homo sapiens 85-92 14511765-4 2003 In addition, hAT III (123-139) attenuated the effect of heparin on the activation of hAT III, whereas other HBPs did not, suggesting that only hAT III (123-139) could interact with the active site of heparin. Heparin 200-207 serpin family C member 1 Homo sapiens 85-92 14511765-5 2003 On the basis of these results, we prepared novel hAT III (123-139)-related derivatives as potent heparin antagonist candidates, and examined the influence of several modifications on their activity in vitro. Heparin 97-104 serpin family C member 1 Homo sapiens 49-56 14511765-6 2003 The results provided new findings about the structure-activity relationship of hAT III (123-139), and led us to the successful development of a potent antagonist for heparin. Heparin 166-173 serpin family C member 1 Homo sapiens 79-86 12920045-2 2003 To explore how glycosaminoglycan changes could influence the thrombogenicity of atherosclerotic lesions, water-transfer reactions were examined during activation of antithrombin by CS. Chondroitin Sulfates 181-183 serpin family C member 1 Homo sapiens 165-177 12920045-5 2003 Oversulfated CS functionally bound antithrombin with a dissociation constant of 3.3+/-1.9 micromol/L. Chondroitin Sulfates 13-15 serpin family C member 1 Homo sapiens 35-47 14519117-5 2003 M27 blocked the ability of antithrombin to inhibit thrombin as well as antithrombin cleavage, both in the presence and absence of heparin. Heparin 130-137 serpin family C member 1 Homo sapiens 27-39 12860985-1 2003 The serpin antithrombin is a slow thrombin inhibitor that requires heparin to enhance its reaction rate. Heparin 67-74 serpin family C member 1 Homo sapiens 11-23 12860985-2 2003 In contrast, alpha1-proteinase inhibitor (alpha1PI) Pittsburgh (P1 Met --> Arg natural variant) inhibits thrombin 17 times faster than pentasaccharide heparin-activated antithrombin. pentasaccharide 138-153 serpin family C member 1 Homo sapiens 172-184 12832413-0 2003 Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide. Heparin 86-93 serpin family C member 1 Homo sapiens 54-66 12837765-7 2003 A fraction of these fragments contains the specific pentasaccharide sequence required for high affinity binding to antithrombin implicated with anticoagulant activity. pentasaccharide 52-67 serpin family C member 1 Homo sapiens 115-127 12837765-10 2003 Commercial heparin was found to be a powerful inhibitor (I50 approximately 20 nM expressed as disaccharide unit, approximately 0.7 nM polysaccharide) of heparanase action toward antithrombin-binding oligosaccharides. Heparin 11-18 serpin family C member 1 Homo sapiens 178-190 12832413-0 2003 Mechanism of catalysis of inhibition of factor IXa by antithrombin in the presence of heparin or pentasaccharide. pentasaccharide 97-112 serpin family C member 1 Homo sapiens 54-66 12837765-10 2003 Commercial heparin was found to be a powerful inhibitor (I50 approximately 20 nM expressed as disaccharide unit, approximately 0.7 nM polysaccharide) of heparanase action toward antithrombin-binding oligosaccharides. Disaccharides 94-106 serpin family C member 1 Homo sapiens 178-190 12837765-10 2003 Commercial heparin was found to be a powerful inhibitor (I50 approximately 20 nM expressed as disaccharide unit, approximately 0.7 nM polysaccharide) of heparanase action toward antithrombin-binding oligosaccharides. Polysaccharides 134-148 serpin family C member 1 Homo sapiens 178-190 12832413-3 2003 This result demonstrates that antithrombin is the predominant inhibitor of f.IXa in plasma, and that the activity of antithrombin is promoted by pentasaccharide. pentasaccharide 145-160 serpin family C member 1 Homo sapiens 117-129 12837765-10 2003 Commercial heparin was found to be a powerful inhibitor (I50 approximately 20 nM expressed as disaccharide unit, approximately 0.7 nM polysaccharide) of heparanase action toward antithrombin-binding oligosaccharides. Oligosaccharides 199-215 serpin family C member 1 Homo sapiens 178-190 12837765-12 2003 These findings strongly suggest that the intracellular processing of the heparin proteoglycan polysaccharide chains is catalyzed by heparanase, which primarily cleaves target structures distinct from the antithrombin-binding sequence. Polysaccharides 94-108 serpin family C member 1 Homo sapiens 204-216 12832413-4 2003 Kinetic experiments reveal that pentasaccharide increases the rates of antithrombin-mediated inhibition of both f.IXa and f.Xa by 2 orders of magnitude. pentasaccharide 32-47 serpin family C member 1 Homo sapiens 71-83 12832413-5 2003 These findings indicate that pentasaccharide-induced conformational changes in antithrombin enhance its capacity to inhibit both f.IXa and f.Xa. pentasaccharide 29-44 serpin family C member 1 Homo sapiens 79-91 12832413-9 2003 Thus, Ca2+ promotes heparin-catalyzed inhibition of f.IXa and f.Xa by antithrombin by augmenting the template mechanism. Heparin 20-27 serpin family C member 1 Homo sapiens 70-82 12832413-10 2003 These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa. Heparin 28-35 serpin family C member 1 Homo sapiens 78-90 12832413-10 2003 These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa. Heparin 28-35 serpin family C member 1 Homo sapiens 185-197 12832413-10 2003 These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa. pentasaccharide 105-120 serpin family C member 1 Homo sapiens 78-90 12832413-10 2003 These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa. Heparin 156-163 serpin family C member 1 Homo sapiens 78-90 12832413-10 2003 These results indicate that heparin-mediated catalysis of f.IXa inhibition by antithrombin reflects both pentasaccharide-induced conformational changes and heparin-mediated bridging of antithrombin to f.IXa. Heparin 156-163 serpin family C member 1 Homo sapiens 185-197 12941037-2 2003 The aim of this work was to study the inhibition of clot-bound FXa and clot-bound thrombin by SanOrg123781A, a synthetic hexadecasaccharide that enhances the inhibition of thrombin and FXa by antithrombin (AT). hexadecasaccharide 121-139 serpin family C member 1 Homo sapiens 192-204 12939144-0 2003 Introduction of a mutation in the shutter region of antithrombin (Phe77 --> Leu) increases affinity for heparin and decreases thermal stability. Leucine 79-82 serpin family C member 1 Homo sapiens 52-64 12939144-0 2003 Introduction of a mutation in the shutter region of antithrombin (Phe77 --> Leu) increases affinity for heparin and decreases thermal stability. Heparin 107-114 serpin family C member 1 Homo sapiens 52-64 12939144-8 2003 Previous studies on shutter region mutations that destabilize antithrombin revealed that such variants possess enhanced affinity for both heparin pentasaccharide and full-length heparin. IC 831423 138-161 serpin family C member 1 Homo sapiens 62-74 12939144-8 2003 Previous studies on shutter region mutations that destabilize antithrombin revealed that such variants possess enhanced affinity for both heparin pentasaccharide and full-length heparin. Heparin 138-145 serpin family C member 1 Homo sapiens 62-74 12939144-10 2003 We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions. Arginine 137-145 serpin family C member 1 Homo sapiens 101-113 12939144-10 2003 We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions. Arginine 137-145 serpin family C member 1 Homo sapiens 195-207 12939144-10 2003 We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions. Heparin 208-215 serpin family C member 1 Homo sapiens 101-113 12939144-10 2003 We suggest that the Phe77Leu mutation causes conformational changes around the top of the D-helix in antithrombin, in particular, to the arginine 132 and 133 residues that may mediate additional antithrombin/heparin interactions. Heparin 208-215 serpin family C member 1 Homo sapiens 195-207 12886459-5 2003 On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin 19-26 serpin family C member 1 Homo sapiens 135-147 14531265-6 2003 Several recent articles have reported that heparin resistance was corrected with antithrombin III concentrates, fresh frozen plasma, or argatroban. Heparin 43-50 serpin family C member 1 Homo sapiens 81-97 13677267-13 2003 In patients who have hereditary antithrombin deficiency, antiphospholipid antibodies, a combined abnormality or a history of a severe thrombotic event (pulmonary embolism, extended deep vein thrombosis) should be advised to use prophylactic heparin during pregnancy, starting during the first trimester. Heparin 241-248 serpin family C member 1 Homo sapiens 32-44 12886459-5 2003 On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparitin Sulfate 28-43 serpin family C member 1 Homo sapiens 135-147 12886459-5 2003 On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 microM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Dermatan Sulfate 65-81 serpin family C member 1 Homo sapiens 135-147 12721300-6 2003 By contrast, Arg143 and Lys147 mutants reacted normally with antithrombin (AT) in both the absence and presence of the cofactor, heparin. Heparin 129-136 serpin family C member 1 Homo sapiens 61-73 14760212-2 2003 Two subcutaneously injected synthetic pentasaccharide anticoagulants, fondaparinux and idraparinux, employ the minimal chain length required to bind to antithrombin and confer a conformational change, increasing its ability to catalyze inactivation of activated factor X (Xa). pentasaccharide 38-53 serpin family C member 1 Homo sapiens 152-164 12911595-8 2003 Both H483-K497 and G486-K502 were effective in neutralizing the accelerated inhibition by heparin of thrombin by antithrombin in the absence of Zn++. Heparin 90-97 serpin family C member 1 Homo sapiens 113-125 12873131-0 2003 Crystal structure of antithrombin in a heparin-bound intermediate state. Heparin 39-46 serpin family C member 1 Homo sapiens 21-33 12873131-1 2003 Antithrombin is activated as an inhibitor of the coagulation proteases through its specific interaction with a heparin pentasaccharide. IC 831423 111-134 serpin family C member 1 Homo sapiens 0-12 12873131-2 2003 The binding of heparin induces a global conformational change in antithrombin which results in the freeing of its reactive center loop for interaction with target proteases and a 1000-fold increase in heparin affinity. Heparin 15-22 serpin family C member 1 Homo sapiens 65-77 12873131-2 2003 The binding of heparin induces a global conformational change in antithrombin which results in the freeing of its reactive center loop for interaction with target proteases and a 1000-fold increase in heparin affinity. Heparin 201-208 serpin family C member 1 Homo sapiens 65-77 12873131-3 2003 The allosteric mechanism by which the properties of antithrombin are altered by its interactions with the specific pentasaccharide sequence of heparin is of great interest to the medical and protein biochemistry communities. pentasaccharide 115-130 serpin family C member 1 Homo sapiens 52-64 12873131-3 2003 The allosteric mechanism by which the properties of antithrombin are altered by its interactions with the specific pentasaccharide sequence of heparin is of great interest to the medical and protein biochemistry communities. Heparin 143-150 serpin family C member 1 Homo sapiens 52-64 12873131-4 2003 Heparin binding has previously been characterized as a two-step, three-state mechanism where, after an initial weak interaction, antithrombin undergoes a conformational change to its high-affinity state. Heparin 0-7 serpin family C member 1 Homo sapiens 129-141 12873131-6 2003 Here we present the structure of an intermediate pentasaccharide-bound conformation of antithrombin which has undergone all of the conformational changes associated with activation except loop expulsion and helix D elongation. pentasaccharide 49-64 serpin family C member 1 Homo sapiens 87-99 12873131-7 2003 We conclude that the basis of the high-affinity state is not improved interaction with the pentasaccharide but a lowering of the global free energy due to conformational changes elsewhere in antithrombin. pentasaccharide 91-106 serpin family C member 1 Homo sapiens 191-203 12846563-0 2003 Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites. Heparin 0-7 serpin family C member 1 Homo sapiens 46-58 12846563-0 2003 Heparin and calcium ions dramatically enhance antithrombin reactivity with factor IXa by generating new interaction exosites. Calcium 12-19 serpin family C member 1 Homo sapiens 46-58 12846563-2 2003 Here we show that antithrombin is essentially unreactive with factor IXa in the absence of heparin (k(ass) approximately 10 M(-1) s(-1)) but undergoes a remarkable approximately 1 million-fold enhancement in reactivity with this proteinase to the physiologically relevant range (k(ass) approximately 10(7) M(-1) s(-1)) when activated by heparin in the presence of physiologic levels of calcium. Heparin 91-98 serpin family C member 1 Homo sapiens 18-30 12846563-2 2003 Here we show that antithrombin is essentially unreactive with factor IXa in the absence of heparin (k(ass) approximately 10 M(-1) s(-1)) but undergoes a remarkable approximately 1 million-fold enhancement in reactivity with this proteinase to the physiologically relevant range (k(ass) approximately 10(7) M(-1) s(-1)) when activated by heparin in the presence of physiologic levels of calcium. Heparin 337-344 serpin family C member 1 Homo sapiens 18-30 12846563-2 2003 Here we show that antithrombin is essentially unreactive with factor IXa in the absence of heparin (k(ass) approximately 10 M(-1) s(-1)) but undergoes a remarkable approximately 1 million-fold enhancement in reactivity with this proteinase to the physiologically relevant range (k(ass) approximately 10(7) M(-1) s(-1)) when activated by heparin in the presence of physiologic levels of calcium. Calcium 386-393 serpin family C member 1 Homo sapiens 18-30 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). IC 831423 126-149 serpin family C member 1 Homo sapiens 90-102 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). IC 831423 126-149 serpin family C member 1 Homo sapiens 265-277 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). Calcium 210-217 serpin family C member 1 Homo sapiens 90-102 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). Calcium 210-217 serpin family C member 1 Homo sapiens 265-277 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). Heparin 126-133 serpin family C member 1 Homo sapiens 90-102 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). Heparin 126-133 serpin family C member 1 Homo sapiens 265-277 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). Calcium 306-313 serpin family C member 1 Homo sapiens 90-102 12846563-3 2003 This rate enhancement is shown to derive from three sources: (i) allosteric activation of antithrombin by a sequence-specific heparin pentasaccharide (300-500-fold), (ii) allosteric activation of factor IXa by calcium ions (4-8-fold), and (iii) heparin bridging of antithrombin and factor IXa augmented by calcium ions (130-1000-fold depending on heparin chain length). Heparin 245-252 serpin family C member 1 Homo sapiens 90-102 12846563-4 2003 Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity. p6-p3 15-20 serpin family C member 1 Homo sapiens 48-60 12846563-4 2003 Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity. Arginine 162-165 serpin family C member 1 Homo sapiens 48-60 12846563-4 2003 Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity. Heparin 258-265 serpin family C member 1 Homo sapiens 48-60 12846563-4 2003 Mutagenesis of P6-P3" reactive loop residues of antithrombin further reveals that the reactivity of the unactivated inhibitor is principally determined by the P1 Arg residue, whereas exosites outside the loop which are present on the activated serpin and on heparin are responsible for heparin enhancement of this reactivity. Heparin 286-293 serpin family C member 1 Homo sapiens 48-60 12695507-1 2003 Covalent antithrombin-heparin (ATH) complexes, formed spontaneously between antithrombin (AT) and unfractionated standard heparin (H), have a potent ability to catalyze the inhibition of factor Xa (or thrombin) by added AT. Heparin 22-29 serpin family C member 1 Homo sapiens 9-21 12695507-1 2003 Covalent antithrombin-heparin (ATH) complexes, formed spontaneously between antithrombin (AT) and unfractionated standard heparin (H), have a potent ability to catalyze the inhibition of factor Xa (or thrombin) by added AT. Heparin 22-29 serpin family C member 1 Homo sapiens 76-88 12783932-10 2003 Several blood biomarkers showed dose-response relationships with tamoxifen, including decreased insulin-like growth factor-I, increased sex hormone-binding globulin, and decreased low-density lipoprotein-cholesterol, ultrasensitive C-reactive protein, fibrinogen, and antithrombin-III levels. Tamoxifen 65-74 serpin family C member 1 Homo sapiens 268-284 12841884-9 2003 CONCLUSIONS: The results of this prospective study show for the first time that raloxifene use is associated with a significant reduction in plasma antithrombin activity. Raloxifene Hydrochloride 80-90 serpin family C member 1 Homo sapiens 148-160 12871328-1 2003 Antithrombin and its cofactor, heparin, target both the product of prothrombin activation by prothrombinase, thrombin, as well as the enzyme responsible for the reaction, factor (F)Xa. Heparin 31-38 serpin family C member 1 Homo sapiens 0-12 12871328-9 2003 Therefore, in the presence of unfractionated heparin, fondaparinux, or enoxaparin, prothrombinase is profoundly protected from antithrombin. Heparin 45-52 serpin family C member 1 Homo sapiens 127-139 12556442-0 2003 Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation. Phenylalanine 17-31 serpin family C member 1 Homo sapiens 0-16 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 78-85 serpin family C member 1 Homo sapiens 24-31 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 24-31 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 156-163 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 156-163 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 24-31 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 156-163 12948833-5 2003 Of all the tested HBPs, hAT III (123-139) exhibited the highest affinity with heparin and showed an inhibitory effect on the heparin-induced enhancement of hAT III activity toward factor Xa, indicating that hAT III (123-139) specifically interacts with the active region in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 156-163 12948833-6 2003 We prepared a synthetic hAT III (123-139)-coupled affinity chromatography system, and demonstrated that this novel affinity chromatography is useful for fractionation of highly active moieties in LMW-heparins. 2-(4-Amino-N-ethylanilino)ethanol 196-199 serpin family C member 1 Homo sapiens 24-31 12948833-6 2003 We prepared a synthetic hAT III (123-139)-coupled affinity chromatography system, and demonstrated that this novel affinity chromatography is useful for fractionation of highly active moieties in LMW-heparins. Heparin 200-208 serpin family C member 1 Homo sapiens 24-31 12948833-1 2003 In the blood coagulation cascade, heparin activates human plasma antithrombin III (hAT III), resulting in the inhibition of factor Xa. Heparin 34-41 serpin family C member 1 Homo sapiens 65-81 12948833-1 2003 In the blood coagulation cascade, heparin activates human plasma antithrombin III (hAT III), resulting in the inhibition of factor Xa. Heparin 34-41 serpin family C member 1 Homo sapiens 83-90 12865952-5 2003 Antithrombin binds to endothelial glycosaminoglycans and then significantly increases anticoagulant activity. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 0-12 12556442-0 2003 Antithrombin III phenylalanines 122 and 121 contribute to its high affinity for heparin and its conformational activation. Heparin 80-87 serpin family C member 1 Homo sapiens 0-16 12556442-1 2003 The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor"s binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contribute approximately 40 and approximately 60% of the binding free energy, respectively. Heparin 42-49 serpin family C member 1 Homo sapiens 61-77 12556442-1 2003 The dissociation equilibrium constant for heparin binding to antithrombin III (ATIII) is a measure of the cofactor"s binding to and activation of the proteinase inhibitor, and its salt dependence indicates that ionic and non-ionic interactions contribute approximately 40 and approximately 60% of the binding free energy, respectively. Heparin 42-49 serpin family C member 1 Homo sapiens 79-84 12556442-5 2003 Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide. Phenylalanine 51-54 serpin family C member 1 Homo sapiens 153-158 12556442-5 2003 Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide. Lysine 63-66 serpin family C member 1 Homo sapiens 153-158 12556442-5 2003 Kinetic and structural considerations suggest that Phe-122 and Lys-114 act cooperatively through non-ionic interactions to promote P-helix formation and ATIII binding to the pentasaccharide. pentasaccharide 174-189 serpin family C member 1 Homo sapiens 153-158 12556442-6 2003 In summary, although hydrophobic residues Phe-122 and Phe-121 make minimal contact with the pentasaccharide, they play a critical role in heparin binding and activation of antithrombin by coordinating the P-helix-mediated conformational change and organizing an extensive network of ionic and non-ionic interactions between positively charged heparin binding site residues and the cofactor. Phenylalanine 42-45 serpin family C member 1 Homo sapiens 172-184 12556442-6 2003 In summary, although hydrophobic residues Phe-122 and Phe-121 make minimal contact with the pentasaccharide, they play a critical role in heparin binding and activation of antithrombin by coordinating the P-helix-mediated conformational change and organizing an extensive network of ionic and non-ionic interactions between positively charged heparin binding site residues and the cofactor. Phenylalanine 54-57 serpin family C member 1 Homo sapiens 172-184 12556442-6 2003 In summary, although hydrophobic residues Phe-122 and Phe-121 make minimal contact with the pentasaccharide, they play a critical role in heparin binding and activation of antithrombin by coordinating the P-helix-mediated conformational change and organizing an extensive network of ionic and non-ionic interactions between positively charged heparin binding site residues and the cofactor. Heparin 138-145 serpin family C member 1 Homo sapiens 172-184 12556442-6 2003 In summary, although hydrophobic residues Phe-122 and Phe-121 make minimal contact with the pentasaccharide, they play a critical role in heparin binding and activation of antithrombin by coordinating the P-helix-mediated conformational change and organizing an extensive network of ionic and non-ionic interactions between positively charged heparin binding site residues and the cofactor. Heparin 343-350 serpin family C member 1 Homo sapiens 172-184 12701115-4 2003 Moreover, eosinophil peroxidase by itself functioned as a powerful procoagulant and also inhibited the anticoagulant actions of heparin in a chromogenic assay for antithrombin III/factor Xa activity. Heparin 128-135 serpin family C member 1 Homo sapiens 163-179 12871355-4 2003 We also calculated the molar concentration of A-domain with 12 sugar units at its non-reducing end, i.e. the structure that carries antithrombin activity (C-domain). Sugars 63-68 serpin family C member 1 Homo sapiens 132-144 12739991-3 2003 Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases. Heparin 0-7 serpin family C member 1 Homo sapiens 165-177 12739991-3 2003 Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases. Heparin 50-58 serpin family C member 1 Homo sapiens 165-177 12739991-3 2003 Heparin and its derivatives (low molecular weight heparins and the active pentasaccharide) inhibit thrombin and/or other coagulation serine proteases indirectly via antithrombin, and the warfarin-type drugs interfere with the synthesis of the precursors of the coagulation serine proteases. pentasaccharide 74-89 serpin family C member 1 Homo sapiens 165-177 12845799-0 2003 [Synthesis and antithrombin activity of phosphoalanine-containing peptides]. phosphoalanine 40-54 serpin family C member 1 Homo sapiens 15-27 12871355-5 2003 RESULTS: The antithrombin activity and the effects on TG and APTT are primarily determined by the concentration of C-domain and independent of the source material (UFH or LMWH) or Mr. High Mr fractions (>15 000) are less active, probably through interaction with non-antithrombin plasma proteins. Heparin 164-167 serpin family C member 1 Homo sapiens 13-25 12871355-5 2003 RESULTS: The antithrombin activity and the effects on TG and APTT are primarily determined by the concentration of C-domain and independent of the source material (UFH or LMWH) or Mr. High Mr fractions (>15 000) are less active, probably through interaction with non-antithrombin plasma proteins. Heparin, Low-Molecular-Weight 171-175 serpin family C member 1 Homo sapiens 13-25 12689824-2 2003 An affinity capillary electrophoresis method has been developed to evidence the complex formation and to determine the binding properties between an anticoagulant polysaccharide of marine origin, fucoidan, and a potential target protein, antithrombin. Polysaccharides 163-177 serpin family C member 1 Homo sapiens 238-250 12768169-7 2003 The most important mechanism responsible of the anti-inflammatory properties of AT is the binding to the glycosaminoglycans of the endothelial cells and the consequent release of prostacyclin. Glycosaminoglycans 105-123 serpin family C member 1 Homo sapiens 80-82 12768169-7 2003 The most important mechanism responsible of the anti-inflammatory properties of AT is the binding to the glycosaminoglycans of the endothelial cells and the consequent release of prostacyclin. Epoprostenol 179-191 serpin family C member 1 Homo sapiens 80-82 12754837-2 2003 Polymeric systems with antithrombin activity and LCST were prepared via a reaction of amino groups of hirudin with phthalimide groups of the copolymers. phthalimide 115-126 serpin family C member 1 Homo sapiens 23-35 12754837-4 2003 The antithrombin activity of polymeric systems obtained by hirudin immobilization on copolymer carriers was inversely related to the content of the copolymer, amounting to 6% of the activity of native hirudin. copolymer 85-94 serpin family C member 1 Homo sapiens 4-16 12754837-4 2003 The antithrombin activity of polymeric systems obtained by hirudin immobilization on copolymer carriers was inversely related to the content of the copolymer, amounting to 6% of the activity of native hirudin. copolymer 148-157 serpin family C member 1 Homo sapiens 4-16 12578831-2 2003 Exposure of this histidine in antithrombin, which has a partially opened sheet, allows polymerization and peptide insertion to occur at pH 6 or less when His-334 will be predictably protonated with disruption of the H-bond network. Histidine 17-26 serpin family C member 1 Homo sapiens 30-42 12578831-2 2003 Exposure of this histidine in antithrombin, which has a partially opened sheet, allows polymerization and peptide insertion to occur at pH 6 or less when His-334 will be predictably protonated with disruption of the H-bond network. Histidine 154-157 serpin family C member 1 Homo sapiens 30-42 12578831-3 2003 Similarly, thermal stability of antithrombin is pH-dependent with a single unfolding transition at pH 6, but there is no such transition when His-334 is buried by a fully closed A-sheet in heparin-complexed antithrombin or in alpha(1)-antitrypsin. Histidine 142-145 serpin family C member 1 Homo sapiens 32-44 12578831-4 2003 Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH. Histidine 15-18 serpin family C member 1 Homo sapiens 157-169 12578831-4 2003 Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH. Serine 52-58 serpin family C member 1 Homo sapiens 157-169 12578831-4 2003 Replacement of His-334 in alpha(1)-antitrypsin by a serine or alanine at pH 7.4 results in the same polymerization and loop-peptide acceptance observed with antithrombin at low pH. Alanine 62-69 serpin family C member 1 Homo sapiens 157-169 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. galactopyranosyl-1-4-paragloboside 12-14 serpin family C member 1 Homo sapiens 35-47 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. galactopyranosyl-1-4-paragloboside 12-14 serpin family C member 1 Homo sapiens 57-69 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. Arginine 15-23 serpin family C member 1 Homo sapiens 35-47 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. Arginine 15-23 serpin family C member 1 Homo sapiens 57-69 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. Heparin 121-128 serpin family C member 1 Homo sapiens 35-47 12591924-0 2003 Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. Heparin 121-128 serpin family C member 1 Homo sapiens 57-69 12591924-2 2003 Sequencing of the antithrombin genes of the patient revealed that one of the two alleles was abnormal due to an in-frame deletion of the codon for the P1 arginine residue. Arginine 154-162 serpin family C member 1 Homo sapiens 18-30 12591924-3 2003 The abnormal antithrombin was separated from the normal inhibitor by complexing the latter with thrombin followed by heparin-agarose affinity chromatography. Heparin 117-124 serpin family C member 1 Homo sapiens 13-25 12591924-3 2003 The abnormal antithrombin was separated from the normal inhibitor by complexing the latter with thrombin followed by heparin-agarose affinity chromatography. Sepharose 125-132 serpin family C member 1 Homo sapiens 13-25 12591924-4 2003 The purified variant, antithrombin London, was completely inactive as a thrombin or factor Xa inhibitor even after heparin activation. Heparin 115-122 serpin family C member 1 Homo sapiens 22-34 12591924-7 2003 Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction. Heparin 39-46 serpin family C member 1 Homo sapiens 70-82 12591924-7 2003 Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction. Heparin 134-141 serpin family C member 1 Homo sapiens 70-82 12591924-7 2003 Consistent with its higher than normal heparin affinity, the inactive antithrombin variant was a potent competitive antagonist of the heparin-catalyzed reaction of normal antithrombin with thrombin but did not affect the uncatalyzed reaction. Heparin 134-141 serpin family C member 1 Homo sapiens 171-183 12591924-9 2003 The unusually severe thrombosis associated with the heterozygous mutation may be explained by the ability of antithrombin London to bind endogenous heparan sulfate or heparin molecules with high affinity and to thereby block activation of the normal inhibitor. Heparitin Sulfate 148-163 serpin family C member 1 Homo sapiens 109-121 12591924-9 2003 The unusually severe thrombosis associated with the heterozygous mutation may be explained by the ability of antithrombin London to bind endogenous heparan sulfate or heparin molecules with high affinity and to thereby block activation of the normal inhibitor. Heparin 167-174 serpin family C member 1 Homo sapiens 109-121 12480701-0 2003 Antithrombin reduces ischemia/reperfusion-induced renal injury in rats by inhibiting leukocyte activation through promotion of prostacyclin production. Epoprostenol 127-139 serpin family C member 1 Homo sapiens 0-12 12689824-5 2003 The effective mobility data of the protein were processed according to classical linearization treatments to obtain the binding constant for the polysaccharide/antithrombin complex. Polysaccharides 145-159 serpin family C member 1 Homo sapiens 160-172 12689824-6 2003 The results indicate that fucoidan binds to antithrombin in a 1:1 stoichiometry and with an affinity depending on the molecular weight of the polysaccharide. Polysaccharides 142-156 serpin family C member 1 Homo sapiens 44-56 12871411-5 2003 The CVBETWEEN was significantly higher for antithrombin and protein S for samples with low levels similar to heterozygous deficiencies. cvbetween 4-13 serpin family C member 1 Homo sapiens 43-55 12581643-0 2003 Structure of beta-antithrombin and the effect of glycosylation on antithrombin"s heparin affinity and activity. Heparin 81-88 serpin family C member 1 Homo sapiens 18-30 12889361-3 2003 Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen. Heparin 297-304 serpin family C member 1 Homo sapiens 67-83 12889361-3 2003 Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen. thiotriasoline 306-320 serpin family C member 1 Homo sapiens 67-83 12889361-3 2003 Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen. prednizolon 370-381 serpin family C member 1 Homo sapiens 67-83 12889361-3 2003 Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen. Heparin 383-390 serpin family C member 1 Homo sapiens 67-83 12889361-3 2003 Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen. thiotriasoline 392-406 serpin family C member 1 Homo sapiens 67-83 12633766-3 2003 Results Using D-BUT-CHT-lys-pNA as a plasmin-specific substrate, we show that incubation of plasma with fructose, glyceraldehyde or MG but not glucose decreases plasminogen activity reaching more than 40% in 16 h. A parallel dose-dependent decrease in heparin activation of AT III by up to a 50% was demonstrated using SAR-PRO-ARG-pNA as a specific thrombin substrate. Fructose 104-112 serpin family C member 1 Homo sapiens 274-280 12633766-3 2003 Results Using D-BUT-CHT-lys-pNA as a plasmin-specific substrate, we show that incubation of plasma with fructose, glyceraldehyde or MG but not glucose decreases plasminogen activity reaching more than 40% in 16 h. A parallel dose-dependent decrease in heparin activation of AT III by up to a 50% was demonstrated using SAR-PRO-ARG-pNA as a specific thrombin substrate. Glyceraldehyde 114-128 serpin family C member 1 Homo sapiens 274-280 12633766-3 2003 Results Using D-BUT-CHT-lys-pNA as a plasmin-specific substrate, we show that incubation of plasma with fructose, glyceraldehyde or MG but not glucose decreases plasminogen activity reaching more than 40% in 16 h. A parallel dose-dependent decrease in heparin activation of AT III by up to a 50% was demonstrated using SAR-PRO-ARG-pNA as a specific thrombin substrate. Magnesium 132-134 serpin family C member 1 Homo sapiens 274-280 12889361-3 2003 Convincing, statistically significant data have been obtained that antithrombin III gets increased in AVM patients undergoing complex therapy: in those patients running a mild course of the illness, a mild one presenting with elevated indices for homeostasis, a medium gravity course (diclofenac, heparin, thiotriasoline, quick-frozen plasma), and grave course as well (prednizolon, heparin, thiotriasoline, quick-frozen plasma), which fact can be taken account of in choosing a therapeutic regimen. Diclofenac 285-295 serpin family C member 1 Homo sapiens 67-83 12623072-0 2003 N-linked oligosaccharide processing, but not association with calnexin/calreticulin is highly correlated with endoplasmic reticulum-associated degradation of antithrombin Glu313-deleted mutant. n-linked oligosaccharide 0-24 serpin family C member 1 Homo sapiens 158-170 12623072-7 2003 These results indicate that, besides proteasome inhibitors, inhibitors of ER mannosidase I and protein synthesis suppress ERAD of the antithrombin deltaGlu mutant at different stages, and processing of N-linked oligosaccharides highly correlated with the efficiency of ERAD. n-linked oligosaccharides 202-227 serpin family C member 1 Homo sapiens 134-146 12651125-0 2003 Separation between the alpha and beta forms of human antithrombin by hydroxyapatite high-performance liquid chromatography. Durapatite 69-83 serpin family C member 1 Homo sapiens 53-65 12651125-2 2003 The predominant form of AT in plasma is ATalpha, which contains four glycosylated asparagine residues, and the minor form is ATbeta, which lacks the Asn-135 glycosylation. Asparagine 82-92 serpin family C member 1 Homo sapiens 24-26 12651125-5 2003 Two analyzed commercial AT products both contained about 2% ATbeta. atbeta 60-66 serpin family C member 1 Homo sapiens 24-26 12581643-0 2003 Structure of beta-antithrombin and the effect of glycosylation on antithrombin"s heparin affinity and activity. Heparin 81-88 serpin family C member 1 Homo sapiens 66-78 12581643-3 2003 Activation of antithrombin is brought about by a conformational change initiated upon binding heparin or heparan sulphate. Heparin 94-101 serpin family C member 1 Homo sapiens 14-26 12581643-3 2003 Activation of antithrombin is brought about by a conformational change initiated upon binding heparin or heparan sulphate. Heparitin Sulfate 105-121 serpin family C member 1 Homo sapiens 14-26 12581643-5 2003 Of the two forms, beta-antithrombin has the higher affinity for heparin and thus functions as the major inhibitor in vivo even though it is the less abundant form. Heparin 64-71 serpin family C member 1 Homo sapiens 23-35 12581643-7 2003 Here, we describe the most accurate structures of alpha-antithrombin and alpha-antithrombin+heparin pentasaccharide reported to date (2.6A and 2.9A resolution, respectively, both re-refinements using old data), and the structure of beta-antithrombin (2.6A resolution). Heparin 92-99 serpin family C member 1 Homo sapiens 79-91 12639557-0 2003 Exploring new non-sugar sulfated molecules as activators of antithrombin. Sugars 18-23 serpin family C member 1 Homo sapiens 60-72 12639557-1 2003 New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa. Sugars 8-13 serpin family C member 1 Homo sapiens 163-175 12581643-7 2003 Here, we describe the most accurate structures of alpha-antithrombin and alpha-antithrombin+heparin pentasaccharide reported to date (2.6A and 2.9A resolution, respectively, both re-refinements using old data), and the structure of beta-antithrombin (2.6A resolution). Heparin 92-99 serpin family C member 1 Homo sapiens 79-91 12581643-7 2003 Here, we describe the most accurate structures of alpha-antithrombin and alpha-antithrombin+heparin pentasaccharide reported to date (2.6A and 2.9A resolution, respectively, both re-refinements using old data), and the structure of beta-antithrombin (2.6A resolution). pentasaccharide 100-115 serpin family C member 1 Homo sapiens 79-91 12581643-7 2003 Here, we describe the most accurate structures of alpha-antithrombin and alpha-antithrombin+heparin pentasaccharide reported to date (2.6A and 2.9A resolution, respectively, both re-refinements using old data), and the structure of beta-antithrombin (2.6A resolution). pentasaccharide 100-115 serpin family C member 1 Homo sapiens 79-91 12639557-1 2003 New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa. epicatechin sulfate 93-116 serpin family C member 1 Homo sapiens 163-175 12639557-1 2003 New non-sugar, small, sulfated molecules, based on our de novo rationally designed activator (-)-epicatechin sulfate (ECS), were investigated to bind and activate antithrombin, an inhibitor of plasma coagulation enzyme factor Xa. epicatechin sulfate 118-121 serpin family C member 1 Homo sapiens 163-175 12581643-8 2003 The new structures have a remarkable degree of ordered carbohydrate and include parts of the antithrombin chain not modeled before. Carbohydrates 55-67 serpin family C member 1 Homo sapiens 93-105 12581643-10 2003 They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135. Heparin 62-69 serpin family C member 1 Homo sapiens 79-91 12581643-10 2003 They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135. Heparin 62-69 serpin family C member 1 Homo sapiens 102-114 12581643-10 2003 They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135. Heparin 168-175 serpin family C member 1 Homo sapiens 79-91 12639557-2 2003 For the activators studied, the equilibrium dissociation constant (K(D)) of the interaction with plasma antithrombin varies nearly 53-fold, with the highest affinity of 1.8 microM observed for morin sulfate, while the acceleration in factor Xa inhibition varies 2.6-fold. NSC676013 193-206 serpin family C member 1 Homo sapiens 104-116 12581643-10 2003 They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135. Heparin 168-175 serpin family C member 1 Homo sapiens 102-114 12581643-10 2003 They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135. Carbohydrates 250-262 serpin family C member 1 Homo sapiens 79-91 12581643-10 2003 They show that the structural basis of the lower affinity for heparin of alpha-antithrombin over beta-antithrombin is due to the conformational change that occurs upon heparin binding being sterically hindered by the presence of the additional bulky carbohydrate at Asn135. Carbohydrates 250-262 serpin family C member 1 Homo sapiens 102-114 12627673-3 2003 Antithrombin drugs such as argatroban and hirudin are already approved for alternative management of heparin-compromised patients. argatroban 27-37 serpin family C member 1 Homo sapiens 0-12 12627673-15 2003 In addition, binding oligosaccharides are conjugated with antithrombin agents to mimic the anti-Xa/anti-IIa activities of heparin. Oligosaccharides 21-37 serpin family C member 1 Homo sapiens 58-70 12627673-15 2003 In addition, binding oligosaccharides are conjugated with antithrombin agents to mimic the anti-Xa/anti-IIa activities of heparin. Heparin 122-129 serpin family C member 1 Homo sapiens 58-70 14593356-4 2003 AIM: To study changes of markers of coagulation and platelet activation during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin. Ticlopidine 97-108 serpin family C member 1 Homo sapiens 170-182 12871518-0 2003 Two new antithrombin variants support a role for K114 and R13 in heparin binding. Heparin 65-72 serpin family C member 1 Homo sapiens 8-20 12765778-0 2003 1976-1983, a critical period in the history of heparin: the discovery of the antithrombin binding site. Heparin 47-54 serpin family C member 1 Homo sapiens 77-89 12765778-1 2003 Heparin inhibits blood coagulation by binding to the protease inhibitor antithrombin, thus promoting inactivation of the protease "factors" of the coagulation cascade mechanism. Heparin 0-7 serpin family C member 1 Homo sapiens 72-84 12765778-2 2003 The article provides an overview of the studies, by different research groups, that led to the structural elucidation of the antithrombin-binding region of heparin. Heparin 156-163 serpin family C member 1 Homo sapiens 125-137 12765778-3 2003 These studies were triggered by the finding that only a fraction of heparin molecules were capable of binding with high affinity to antithrombin, and further that this fraction essentially accounted for the anticoagulant activity of the unfractionated material. Heparin 68-75 serpin family C member 1 Homo sapiens 132-144 12765778-5 2003 The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide. pentasaccharide 90-105 serpin family C member 1 Homo sapiens 60-72 12765778-5 2003 The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide. Glucosamine 152-163 serpin family C member 1 Homo sapiens 60-72 12765778-5 2003 The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide. Sugars 185-190 serpin family C member 1 Homo sapiens 60-72 12765778-5 2003 The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide. Sulfates 143-150 serpin family C member 1 Homo sapiens 60-72 12765778-5 2003 The results were interpreted in terms of a binding site for antithrombin constituted by a pentasaccharide sequence with an internal unique 3-O-sulfated glucosamine unit, in addition to sugar residues and sulfate groups present elsewhere also in the polysaccharide. Polysaccharides 249-263 serpin family C member 1 Homo sapiens 60-72 12765779-1 2003 We have synthesized three new antithrombin activating pentasaccharides displaying various sulfation patterns on the reducing end unit (H). pentasaccharides 54-70 serpin family C member 1 Homo sapiens 30-42 14556453-3 2003 In a further step, we have designed and synthesised oligosaccharides (pentadeca--to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain. pentadeca--to eicosasaccharides 70-101 serpin family C member 1 Homo sapiens 118-130 14556454-3 2003 We determined the molar concentration of material (HAM) containing the antithrombin (AT) binding pentasaccharide (A-domain), the specific catalytic activity in thrombin- and factor Xa inactivation and the capacity to inhibit thrombin generation (TG). pentasaccharide 97-112 serpin family C member 1 Homo sapiens 71-83 14521318-9 2003 The use of antithrombin III is one way of preventing heparin resistance. Heparin 53-60 serpin family C member 1 Homo sapiens 11-27 12535860-2 2003 Here, we report that treatment of coronary artery patients with 100 mg/day of aspirin does not attenuate thrombin generation, but reduces free thrombin by favouring the formation of thrombin/antithrombin (TAT) complexes. Aspirin 78-85 serpin family C member 1 Homo sapiens 191-203 12535860-3 2003 Antithrombin hyperactivation is mediated by inhibition of platelet factor 4 release from alpha-granules, leading to higher heparin availability. Heparin 123-130 serpin family C member 1 Homo sapiens 0-12 14587291-7 2003 Sequential crystallographic structures now provide clear depictions of the way antithrombin is activated on binding to the heparans of the microcirculation, and how evolution has utilized this mobile mechanism for subtle variations in activity. heparans 123-131 serpin family C member 1 Homo sapiens 79-91 12492585-6 2003 Among tamoxifen-treated women, antithrombin and protein S, but not protein C or APC ratio were reduced. Tamoxifen 6-15 serpin family C member 1 Homo sapiens 31-43 12492585-7 2003 Sequential antithrombin concentrations with tamoxifen were 114% and 104% (P = 0.001 compared with placebo). Tamoxifen 44-53 serpin family C member 1 Homo sapiens 11-23 12492585-10 2003 Reductions of antithrombin and protein S, but not protein C or APC resistance, might relate to the increased risk of venous thrombosis associated with tamoxifen treatment. Tamoxifen 151-160 serpin family C member 1 Homo sapiens 14-26 14556453-1 2003 In the early eighties, following breakthroughs in oligosaccharide chemistry, we achieved the total chemical synthesis of pentasaccharides related to the antithrombin-binding domain in heparin. Oligosaccharides 50-65 serpin family C member 1 Homo sapiens 153-165 14556453-1 2003 In the early eighties, following breakthroughs in oligosaccharide chemistry, we achieved the total chemical synthesis of pentasaccharides related to the antithrombin-binding domain in heparin. pentasaccharides 121-137 serpin family C member 1 Homo sapiens 153-165 14556453-3 2003 In a further step, we have designed and synthesised oligosaccharides (pentadeca--to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain. Oligosaccharides 52-68 serpin family C member 1 Homo sapiens 118-130 14515016-7 2003 After 1200 s of clotting, purified antithrombin III (22 microM) reduced PCF by 74%. PHENYL CHLOROFORMATE 72-75 serpin family C member 1 Homo sapiens 35-51 12891293-3 2003 AIM: To study changes of parameters of fibrinolysis during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin. Ticlopidine 77-88 serpin family C member 1 Homo sapiens 150-162 12891293-3 2003 AIM: To study changes of parameters of fibrinolysis during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin. Clopidogrel 93-104 serpin family C member 1 Homo sapiens 150-162 14593356-4 2003 AIM: To study changes of markers of coagulation and platelet activation during short term use of ticlopidine and clopidogrel in NSTEACS patients treated with aspirin and antithrombin. Clopidogrel 113-124 serpin family C member 1 Homo sapiens 170-182 14593356-15 2003 Both ticlopidine and clopidogrel used in regimes with loading doses in NSTEACS patients treated with aspirin and antithrombin prevented acute phase elevation of vWF. Ticlopidine 5-16 serpin family C member 1 Homo sapiens 113-125 14593356-15 2003 Both ticlopidine and clopidogrel used in regimes with loading doses in NSTEACS patients treated with aspirin and antithrombin prevented acute phase elevation of vWF. Clopidogrel 21-32 serpin family C member 1 Homo sapiens 113-125 12540961-2 2003 Here, the anti-fXa and anti-prothrombinase activities of DX-9065a which is an active-site directed inhibitor of fXa, and therapeutic heparins which are dependent on antithrombin (AT) for their anticoagulant function, were studied in amidolytic and proteolytic activity assays. (2S)-2-(4-(((3S)-1-acetimidoyl-3-pyrrolidinyl)oxy)phenyl)-3-(7-amidino-2-naphtyl)propanoic acid 57-65 serpin family C member 1 Homo sapiens 165-177 12876681-9 2003 The strategy allows the fast identification of methionine- and methionine-sulfoxide-containing peptides even in complex tryptic digests, as demonstrated here for the glycoprotein antithrombin. Methionine 47-57 serpin family C member 1 Homo sapiens 179-191 12876681-9 2003 The strategy allows the fast identification of methionine- and methionine-sulfoxide-containing peptides even in complex tryptic digests, as demonstrated here for the glycoprotein antithrombin. Methionine 63-73 serpin family C member 1 Homo sapiens 179-191 12876681-9 2003 The strategy allows the fast identification of methionine- and methionine-sulfoxide-containing peptides even in complex tryptic digests, as demonstrated here for the glycoprotein antithrombin. sulfoxide 74-83 serpin family C member 1 Homo sapiens 179-191 12679126-1 2003 Fondaparinux (Arixtra) is the first of a new class of selective indirect antithrombin-dependent factor Xa inhibitors, which inhibits thrombin generation. Fondaparinux 0-12 serpin family C member 1 Homo sapiens 73-85 12679126-1 2003 Fondaparinux (Arixtra) is the first of a new class of selective indirect antithrombin-dependent factor Xa inhibitors, which inhibits thrombin generation. Fondaparinux 14-21 serpin family C member 1 Homo sapiens 73-85 12540961-2 2003 Here, the anti-fXa and anti-prothrombinase activities of DX-9065a which is an active-site directed inhibitor of fXa, and therapeutic heparins which are dependent on antithrombin (AT) for their anticoagulant function, were studied in amidolytic and proteolytic activity assays. Heparin 133-141 serpin family C member 1 Homo sapiens 165-177 12433487-6 2002 Our results indicate that a 2-sulfated, 3-linked alpha-L-galactan, but not an alpha-L-fucan, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II. sulfated 30-38 serpin family C member 1 Homo sapiens 136-148 15013282-0 2003 Antithrombin activity of lepirudin adsorbed to silicone (polydimethylsiloxane) tubing. Silicones 47-55 serpin family C member 1 Homo sapiens 0-12 15013282-0 2003 Antithrombin activity of lepirudin adsorbed to silicone (polydimethylsiloxane) tubing. baysilon 57-77 serpin family C member 1 Homo sapiens 0-12 12397068-5 2002 Similarly, antithrombin inactivated FIXa derivatives with a similar second-order association rate constant (k(2)) in both the absence and presence of pentasaccharide. pentasaccharide 150-165 serpin family C member 1 Homo sapiens 11-23 12441904-8 2002 Anti-inflammatory properties of AT independent of coagulation involve direct interactions with cells leading to the release of, for instance, prostacyclin. Epoprostenol 142-154 serpin family C member 1 Homo sapiens 32-34 12441904-12 2002 Accordingly, the supplementation of AT without concomitant heparin may be beneficial in disorders with inflammatory characteristics, which has to be demonstrated in further clinical studies. Heparin 59-66 serpin family C member 1 Homo sapiens 36-38 12433487-6 2002 Our results indicate that a 2-sulfated, 3-linked alpha-L-galactan, but not an alpha-L-fucan, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II. 3-linked alpha-l-galactan 40-65 serpin family C member 1 Homo sapiens 136-148 12433488-3 2002 1D 1H NMR showed two-thirds of the N-acetyl groups were lost on periodate cleavage, suggesting cleavage had occurred at the glucopyranosyluronic acid (GlcpA) and idopyranosyluronic acid (IdopA) residues located within and adjacent to the antithrombin III (ATIII) binding site. metaperiodate 64-73 serpin family C member 1 Homo sapiens 238-254 12433488-3 2002 1D 1H NMR showed two-thirds of the N-acetyl groups were lost on periodate cleavage, suggesting cleavage had occurred at the glucopyranosyluronic acid (GlcpA) and idopyranosyluronic acid (IdopA) residues located within and adjacent to the antithrombin III (ATIII) binding site. metaperiodate 64-73 serpin family C member 1 Homo sapiens 256-261 12433488-5 2002 The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue. glcpa 4-9 serpin family C member 1 Homo sapiens 30-35 12433488-5 2002 The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue. n-sulfo 85-92 serpin family C member 1 Homo sapiens 30-35 12433488-5 2002 The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue. 3, 6-o-sulfo glycopyranosylamine 94-126 serpin family C member 1 Homo sapiens 30-35 12433488-5 2002 The GlcpA residue, within the ATIII binding site, is on the non-reducing side of the N-sulfo, 3, 6-O-sulfo glycopyranosylamine (GlcpNS3S6S) residue. glcpns3s6s 128-138 serpin family C member 1 Homo sapiens 30-35 12421140-10 2002 The diagnosis of antithrombin deficiency should be established only after other acquired causes of antithrombin deficiency, such as liver disease, consumptive coagulopathy, or heparin therapy, are excluded. Heparin 176-183 serpin family C member 1 Homo sapiens 17-29 12536119-0 2002 Heparin activates antithrombin anticoagulant function by generating new interaction sites (exosites) for blood clotting proteinases. Heparin 0-7 serpin family C member 1 Homo sapiens 18-30 12501872-7 2002 RESULTS: Fondaparinux is a synthetic pentasaccharide that selectively binds to antithrombin III, inducing a conformational change that increases anti-factor Xa activity. pentasaccharide 37-52 serpin family C member 1 Homo sapiens 79-95 12536119-2 2002 Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex. Heparin 0-7 serpin family C member 1 Homo sapiens 18-30 12536119-2 2002 Heparin activates antithrombin both by inducing conformational changes in the protein that specifically enhances factor Xa binding and by providing a surface to promote thrombin or factor Xa binding alongside antithrombin in a ternary bridging complex. Heparin 0-7 serpin family C member 1 Homo sapiens 209-221 12536119-3 2002 Although x-ray structures of antithrombin, free and complexed with heparin, have suggested that exposure of a reactive proteinase binding loop is a key feature of conformational activation, mutagenesis of reactive loop residues indicates that the function of this structural change is not to present an optimal loop sequence to target clotting proteinases. Heparin 67-74 serpin family C member 1 Homo sapiens 29-41 12244069-3 2002 Our results indicate that a 2-O-sulfated, 3-linked alpha-L-galactan, but not a alpha-L-fucan with a similar molecular size, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II. 2-o-sulfated 28-40 serpin family C member 1 Homo sapiens 167-179 12138164-2 2002 The 3-O-sulfated glucosamine residue contributes to two important biological functions of HS: binding to antithrombin and thereby carrying anticoagulant activity, and binding to herpes simplex viral envelope glycoprotein D to serve as an entry receptor for herpes simplex virus 1. Glucosamine 17-28 serpin family C member 1 Homo sapiens 105-117 12357148-11 2002 The generation of fibrin even in the presence of high heparin concentrations most likely has to be attributed to the reduced antithrombin III concentrations or reduced inhibition of clot-bound thrombin. Heparin 54-61 serpin family C member 1 Homo sapiens 125-141 12368161-10 2002 Plasma TpP levels correlated significantly with other DIC parameters including platelet count, fibrinogen, antithrombin and TAT, and correlated weakly with D-dimer. tpp 7-10 serpin family C member 1 Homo sapiens 107-119 12369826-0 2002 Specificity of the basic side chains of Lys114, Lys125, and Arg129 of antithrombin in heparin binding. Heparin 86-93 serpin family C member 1 Homo sapiens 70-82 12369826-1 2002 The anticoagulant polysaccharide heparin binds and activates the plasma proteinase inhibitor antithrombin through a pentasaccharide sequence. polysaccharide heparin 18-40 serpin family C member 1 Homo sapiens 93-105 12369826-1 2002 The anticoagulant polysaccharide heparin binds and activates the plasma proteinase inhibitor antithrombin through a pentasaccharide sequence. pentasaccharide 116-131 serpin family C member 1 Homo sapiens 93-105 12369826-5 2002 However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114. Arginine 70-73 serpin family C member 1 Homo sapiens 151-163 12369826-5 2002 However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114. pentasaccharide 196-211 serpin family C member 1 Homo sapiens 151-163 12369826-5 2002 However, a loss of approximately one ionic interaction on mutation to Arg indicates that the optimal configuration of the network of basic residues of antithrombin that together interact with the pentasaccharide requires a Lys in position 114. Lysine 223-226 serpin family C member 1 Homo sapiens 151-163 12369826-10 2002 This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor. Arginine 54-57 serpin family C member 1 Homo sapiens 93-105 12369826-10 2002 This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor. Arginine 181-184 serpin family C member 1 Homo sapiens 93-105 12369826-10 2002 This requirement is most likely due to the ability of Arg to interact with other residues of antithrombin, primarily, Glu414 and Thr44, in a manner that appropriately positions the Arg side chain for keeping the pentasaccharide anchored to the activated state of the inhibitor. pentasaccharide 212-227 serpin family C member 1 Homo sapiens 93-105 12359224-6 2002 Dimethylsphingosine also inhibited leukocyte chemotaxis toward antithrombin, indicating that similar mechanisms may be involved upon syndecan-4 ligation. dimethylsphingosine 0-19 serpin family C member 1 Homo sapiens 63-75 12244069-3 2002 Our results indicate that a 2-O-sulfated, 3-linked alpha-L-galactan, but not a alpha-L-fucan with a similar molecular size, is a potent thrombin inhibitor mediated by antithrombin or heparin cofactor II. 3-linked alpha-l-galactan 42-67 serpin family C member 1 Homo sapiens 167-179 12244069-5 2002 The occurrence of 2,4-di-O-sulfated units is an amplifying motif for 3-linked alpha-fucan-enhanced thrombin inhibition by antithrombin. 2,4-di-o 18-26 serpin family C member 1 Homo sapiens 122-134 12244069-5 2002 The occurrence of 2,4-di-O-sulfated units is an amplifying motif for 3-linked alpha-fucan-enhanced thrombin inhibition by antithrombin. sulfated 27-35 serpin family C member 1 Homo sapiens 122-134 12244069-6 2002 If we replace antithrombin by heparin cofactor II, then the major structural requirement for the activity becomes single 4-O-sulfated fucose units. 4-o-sulfated fucose 121-140 serpin family C member 1 Homo sapiens 14-26 12425373-2 2002 This pentasaccharide selectively and specifically inhibits coagulation factor Xa, and requires antithrombin as co-factor It is entirely synthetic, in contrast to conventional heparin and low molecular heparins which are derived from animal tissues. pentasaccharide 5-20 serpin family C member 1 Homo sapiens 95-107 12238925-1 2002 Recently, we designed (-)-epicatechin sulfate (ECS), the first small nonsaccharide molecule, as an activator of antithrombin for the accelerated inhibition of factor Xa, a key proteinase of the coagulation cascade (Gunnarsson, G. T.; Desai, U. R. J. Med. epicatechin sulfate 22-45 serpin family C member 1 Homo sapiens 112-124 12238925-1 2002 Recently, we designed (-)-epicatechin sulfate (ECS), the first small nonsaccharide molecule, as an activator of antithrombin for the accelerated inhibition of factor Xa, a key proteinase of the coagulation cascade (Gunnarsson, G. T.; Desai, U. R. J. Med. epicatechin sulfate 47-50 serpin family C member 1 Homo sapiens 112-124 12238925-1 2002 Recently, we designed (-)-epicatechin sulfate (ECS), the first small nonsaccharide molecule, as an activator of antithrombin for the accelerated inhibition of factor Xa, a key proteinase of the coagulation cascade (Gunnarsson, G. T.; Desai, U. R. J. Med. nonsaccharide 69-82 serpin family C member 1 Homo sapiens 112-124 12238925-6 2002 (+)-Catechin sulfate (CS), a chiral stereoisomer of ECS, bound plasma antithrombin with a 3-fold higher affinity (K(D) = 3.5 microM) and a 2-fold higher second-order rate constant for factor Xa inhibition (k(ACT) = 6750 M(-1) s(-1)). catechin sulfate 0-20 serpin family C member 1 Homo sapiens 70-82 12238925-6 2002 (+)-Catechin sulfate (CS), a chiral stereoisomer of ECS, bound plasma antithrombin with a 3-fold higher affinity (K(D) = 3.5 microM) and a 2-fold higher second-order rate constant for factor Xa inhibition (k(ACT) = 6750 M(-1) s(-1)). catechin sulfate 22-24 serpin family C member 1 Homo sapiens 70-82 12236772-4 2002 In this study a series of silyl-heparins were synthesized and each of the analogues found to function similar to unmodified heparin relative to their binding of antithrombin III and also the binding of bFGF. Heparin 32-39 serpin family C member 1 Homo sapiens 161-177 12172461-2 2002 The drug replicates the sulphated antithrombin-binding pentasaccharide sequence in heparin and induces potent and specific antithrombin-mediated anti-Xa activity with excellent bioavailability and a long circulating half-life of 18 hours that makes it ideal for once-daily subcutaneous dosing. pentasaccharide 55-70 serpin family C member 1 Homo sapiens 34-46 12236772-4 2002 In this study a series of silyl-heparins were synthesized and each of the analogues found to function similar to unmodified heparin relative to their binding of antithrombin III and also the binding of bFGF. silyl-heparins 26-40 serpin family C member 1 Homo sapiens 161-177 12172461-2 2002 The drug replicates the sulphated antithrombin-binding pentasaccharide sequence in heparin and induces potent and specific antithrombin-mediated anti-Xa activity with excellent bioavailability and a long circulating half-life of 18 hours that makes it ideal for once-daily subcutaneous dosing. Heparin 83-90 serpin family C member 1 Homo sapiens 34-46 12009311-2 2002 Antithrombin III (ATIII) was purified from ostrich plasma by heparin-Sepharose and Super Q-650S chromatography. Heparin 61-68 serpin family C member 1 Homo sapiens 18-23 12009311-2 2002 Antithrombin III (ATIII) was purified from ostrich plasma by heparin-Sepharose and Super Q-650S chromatography. Sepharose 69-78 serpin family C member 1 Homo sapiens 18-23 12121115-9 2002 Finally, the current methodology was applied to the characterization of the biologically important ATIII binding pentasaccharide and its precursors, which differ from each other by sulfation pattern and/or degree of sulfation. pentasaccharide 113-128 serpin family C member 1 Homo sapiens 99-104 13679662-1 2002 Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III. Dermatan Sulfate 0-17 serpin family C member 1 Homo sapiens 151-167 13679662-1 2002 Dermatan sulphate (DS) is a glycosaminoglycan which selectively catalyzes the inactivation of thrombin by Heparin Cofactor II without interacting with Antithrombin III. Dermatan Sulfate 19-21 serpin family C member 1 Homo sapiens 151-167 13679666-15 2002 In patients who have hereditary antithrombin deficiency, antiphospholipid antibodies, a combined abnormality or a history of a severe thrombotic event (pulmonary embolism, extended deep vein thrombosis) should be advised to use prophylactic heparin during pregnancy, starting during the first trimester. Heparin 241-248 serpin family C member 1 Homo sapiens 32-44 12353072-1 2002 We investigated the effect of various oligosaccharides (OS) on the inhibition of factor IXa by antithrombin (AT) in a purified system. Oligosaccharides 38-54 serpin family C member 1 Homo sapiens 95-107 12353072-1 2002 We investigated the effect of various oligosaccharides (OS) on the inhibition of factor IXa by antithrombin (AT) in a purified system. Oligosaccharides 56-58 serpin family C member 1 Homo sapiens 95-107 12353073-0 2002 Antithrombin "DREUX" (Lys 114Glu): a variant with complete loss of heparin affinity. Heparin 67-74 serpin family C member 1 Homo sapiens 0-12 12353073-1 2002 Here we report the finding of a new natural antithrombin mutation that confirms the critical contribution of lysine 114 to the binding of the core heparin pentasaccharide, with the replacement of lysine 114 by glutamate causing a complete loss in affinity. Lysine 109-115 serpin family C member 1 Homo sapiens 44-56 12353073-1 2002 Here we report the finding of a new natural antithrombin mutation that confirms the critical contribution of lysine 114 to the binding of the core heparin pentasaccharide, with the replacement of lysine 114 by glutamate causing a complete loss in affinity. IC 831423 147-170 serpin family C member 1 Homo sapiens 44-56 12353073-3 2002 The variant forms SDS-stable complexes with activated factor X (fXa) and its thermal stability and rate of factor Xa inhibition in the absence of heparin are identical to those of normal antithrombin. Sodium Dodecyl Sulfate 18-21 serpin family C member 1 Homo sapiens 187-199 12353073-4 2002 Normal antithrombin binds to the high affinity heparin pentasaccharide with a Kd of 1nM, as detected by a 45% change in intrinsic fluorescence, resulting in a 230-fold increase in rate of factor Xa inhibition. IC 831423 47-70 serpin family C member 1 Homo sapiens 7-19 12195696-0 2002 Adverse effect of heparin on antithrombin action during endotoxemia: microhemodynamic and cellular mechanisms. Heparin 18-25 serpin family C member 1 Homo sapiens 29-41 12195696-1 2002 A recent clinical sepsis trial reported a significant reduction in 90-day mortality by antithrombin (AT) exclusively in the subgroup of patients without simultaneous heparin prophylaxis. Heparin 166-173 serpin family C member 1 Homo sapiens 87-99 12145015-6 2002 CONCLUSION: Percentage enrichment at 3 d (but not at 6 h) can be used to evaluate vitamin A body stores in humans. Vitamin A 82-91 serpin family C member 1 Homo sapiens 34-40 12211411-3 2002 Understanding the heparin structure led to the development of LMWHs, synthetic heparinomimetics, antithrombin and anti-Factor Xa agents. Heparin 18-25 serpin family C member 1 Homo sapiens 97-109 12244479-1 2002 NMR determination of the conformation of heparin sequences complexed with antithrombin and fibroblast growth factors in solution. Heparin 41-48 serpin family C member 1 Homo sapiens 74-86 12244479-4 2002 The pentasaccharide corresponding to the active site of heparin/heparan sulfate for antithrombin (AT) adopts in the complex with the protein a conformation different from that in the absence of the protein. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 84-96 12244479-4 2002 The pentasaccharide corresponding to the active site of heparin/heparan sulfate for antithrombin (AT) adopts in the complex with the protein a conformation different from that in the absence of the protein. Heparin 56-63 serpin family C member 1 Homo sapiens 84-96 12244479-4 2002 The pentasaccharide corresponding to the active site of heparin/heparan sulfate for antithrombin (AT) adopts in the complex with the protein a conformation different from that in the absence of the protein. Heparitin Sulfate 64-79 serpin family C member 1 Homo sapiens 84-96 12244482-0 2002 Effects of calcium ions on the interactions between antithrombin and factor Xa mediated by variously sulfated, semisynthetic low-molecular-weight heparins. Calcium 11-18 serpin family C member 1 Homo sapiens 52-64 12244482-0 2002 Effects of calcium ions on the interactions between antithrombin and factor Xa mediated by variously sulfated, semisynthetic low-molecular-weight heparins. Heparin 146-154 serpin family C member 1 Homo sapiens 52-64 12244482-1 2002 A homogeneous set of low-molecular weight heparins, chemically modified to yield different degrees of sulfation, were investigated for their ability to interfere with the antithrombin (AT)-factor Xa (FXa) interaction process in the presence or absence of physiological concentrations of calcium ions. Heparin 42-50 serpin family C member 1 Homo sapiens 171-183 12361208-0 2002 Direct antithrombin agents ameliorate disseminated intravascular coagulation in suspected heparin-induced thrombocytopenia thrombosis syndrome. Heparin 90-97 serpin family C member 1 Homo sapiens 7-19 11971909-0 2002 Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition. Arginine 18-26 serpin family C member 1 Homo sapiens 97-113 11971909-0 2002 Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition. Glutamic Acid 59-72 serpin family C member 1 Homo sapiens 97-113 11971909-1 2002 The mechanism for heparin activation of antithrombin III has been postulated to involve disruption of interactions between its reactive loop P1 residue and Glu(255) on the underlying protein surface. Glutamic Acid 156-159 serpin family C member 1 Homo sapiens 40-56 12413592-1 2002 Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans. Glycosaminoglycans 235-253 serpin family C member 1 Homo sapiens 0-12 12413592-1 2002 Antithrombin (ATIII), heparin cofactor II (HCII) and protein C inhibitor (PCI; also named plasminogen activator inhibitor-3) are serine protease inhibitors (serpins) whose thrombin inhibition activity is accelerated in the presence of glycosaminoglycans. Glycosaminoglycans 235-253 serpin family C member 1 Homo sapiens 14-19 12413592-7 2002 These results suggest that PCI is similar to ATIII and depends upon ternary complex formation with heparin and these specific thrombin exosite-2 residues to accelerate thrombin inhibition. Heparin 99-106 serpin family C member 1 Homo sapiens 45-50 12361208-1 2002 This is a case series of 5 patients who were treated with the direct antithrombin agents (lepirudin or argatroban) for known or suspected heparin-induced thrombocytopenia thrombosis syndrome (HITTs). argatroban 103-113 serpin family C member 1 Homo sapiens 69-81 12361208-1 2002 This is a case series of 5 patients who were treated with the direct antithrombin agents (lepirudin or argatroban) for known or suspected heparin-induced thrombocytopenia thrombosis syndrome (HITTs). Heparin 138-145 serpin family C member 1 Homo sapiens 69-81 12361208-4 2002 These observations provide evidence that the direct antithrombin inhibitors, lepirudin and argatroban, can improve DIC. argatroban 91-101 serpin family C member 1 Homo sapiens 52-64 12124681-2 2002 Their action is in contrast to heparin and its derivatives, which inhibit thrombin and other coagulation serine proteases via antithrombin, and to the warfarin-type drugs that interfere with synthesis of the precursors of the coagulation serine proteases. Heparin 31-38 serpin family C member 1 Homo sapiens 126-138 12645893-2 2002 Protein sequence comparisons with the other 10 known antithrombin sequences and with sequences of other serpins have provided striking evidence for the conservation of the heparin activation mechanism and new insight into those residues important for heparin binding, for heparin activation, and for reactive center loop function, as well as an indication of which glycosylation sites might be needed for function. Heparin 172-179 serpin family C member 1 Homo sapiens 53-65 12645893-2 2002 Protein sequence comparisons with the other 10 known antithrombin sequences and with sequences of other serpins have provided striking evidence for the conservation of the heparin activation mechanism and new insight into those residues important for heparin binding, for heparin activation, and for reactive center loop function, as well as an indication of which glycosylation sites might be needed for function. Heparin 251-258 serpin family C member 1 Homo sapiens 53-65 12645893-2 2002 Protein sequence comparisons with the other 10 known antithrombin sequences and with sequences of other serpins have provided striking evidence for the conservation of the heparin activation mechanism and new insight into those residues important for heparin binding, for heparin activation, and for reactive center loop function, as well as an indication of which glycosylation sites might be needed for function. Heparin 251-258 serpin family C member 1 Homo sapiens 53-65 12022882-6 2002 The reactivities of Arg(143) and Lys(147) mutants were improved approximately 2-fold with antithrombin in the absence but not in the presence of heparin cofactors. Arginine 20-23 serpin family C member 1 Homo sapiens 90-102 12161073-0 2002 Identification of critical molecular interactions mediating heparin activation of antithrombin: implications for the design of improved heparin anticoagulants. Heparin 60-67 serpin family C member 1 Homo sapiens 82-94 12161073-2 2002 The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin. Heparin 67-74 serpin family C member 1 Homo sapiens 104-116 12161073-2 2002 The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin. Heparin 227-234 serpin family C member 1 Homo sapiens 104-116 12161073-2 2002 The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin. pentasaccharide 305-320 serpin family C member 1 Homo sapiens 104-116 12161073-2 2002 The relative importance of the molecular interactions that mediate heparin binding to and activation of antithrombin, and the dynamics of how they are established, have recently been revealed from the effects of mutagenesis of heparin-binding residues of antithrombin and of modifications of the specific pentasaccharide-binding region in heparin. Heparin 227-234 serpin family C member 1 Homo sapiens 104-116 12161073-3 2002 One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex. Lysine 13-16 serpin family C member 1 Homo sapiens 37-49 12161073-3 2002 One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex. Trisaccharides 92-105 serpin family C member 1 Homo sapiens 37-49 12161073-3 2002 One residue, Lys 125, is pivotal for antithrombin to recognize and bind the nonreducing-end trisaccharide of the pentasaccharide in an initial low-affinity complex. pentasaccharide 113-128 serpin family C member 1 Homo sapiens 37-49 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. Lysine 20-23 serpin family C member 1 Homo sapiens 203-215 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. Arginine 32-35 serpin family C member 1 Homo sapiens 203-215 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. Lysine 61-64 serpin family C member 1 Homo sapiens 203-215 12161073-4 2002 Two other residues, Lys 114 and Arg 129, then cooperate with Lys 125 to induce the low-affinity complex into an activated, high-affinity complex, in which a network of electrostatic interactions between antithrombin and the entire pentasaccharide is established. pentasaccharide 231-246 serpin family C member 1 Homo sapiens 203-215 12161073-5 2002 The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active. Trisaccharides 74-87 serpin family C member 1 Homo sapiens 147-159 12161073-5 2002 The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active. Heparin 91-98 serpin family C member 1 Homo sapiens 147-159 12161073-5 2002 The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active. Heparin 125-132 serpin family C member 1 Homo sapiens 55-67 12161073-5 2002 The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active. Heparin 125-132 serpin family C member 1 Homo sapiens 147-159 12161073-5 2002 The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active. Heparin 125-132 serpin family C member 1 Homo sapiens 55-67 12161073-5 2002 The identification of three critical basic residues in antithrombin and a trisaccharide in heparin as principal mediators of heparin activation of antithrombin may stimulate the design of small-molecule anticoagulants that mimic the action of heparin and are orally active. Heparin 125-132 serpin family C member 1 Homo sapiens 147-159 12010802-8 2002 The observation that chemically modified AT III that lacks heparin-binding capacity had no effect on NF-kappaB activation supports the current understanding that the inhibitory potency of AT III depends on the interaction of AT III with heparinlike cell surface glycosaminoglycans. Glycosaminoglycans 262-280 serpin family C member 1 Homo sapiens 188-194 12010802-8 2002 The observation that chemically modified AT III that lacks heparin-binding capacity had no effect on NF-kappaB activation supports the current understanding that the inhibitory potency of AT III depends on the interaction of AT III with heparinlike cell surface glycosaminoglycans. Glycosaminoglycans 262-280 serpin family C member 1 Homo sapiens 188-194 12010802-9 2002 This hypothesis was underscored by the finding that the AT III beta-isoform, known to have higher affinity for glycosaminoglycans, is more effective in preventing NF-kappaB transactivation than alpha-AT III. Glycosaminoglycans 111-129 serpin family C member 1 Homo sapiens 56-62 12073179-6 2002 Based on studies of the heparin binding site of antithrombin, this novel pentasaccharide has superior pharmacokinetics and bioavailability when compared with LMWH and can be administered once daily. Heparin 24-31 serpin family C member 1 Homo sapiens 48-60 12073179-6 2002 Based on studies of the heparin binding site of antithrombin, this novel pentasaccharide has superior pharmacokinetics and bioavailability when compared with LMWH and can be administered once daily. pentasaccharide 73-88 serpin family C member 1 Homo sapiens 48-60 27264755-2 2002 It is a synthetic pentasaccharide mimicking the site of heparin that binds to antithrombin III (AT). pentasaccharide 18-33 serpin family C member 1 Homo sapiens 78-94 27264755-2 2002 It is a synthetic pentasaccharide mimicking the site of heparin that binds to antithrombin III (AT). Heparin 56-63 serpin family C member 1 Homo sapiens 78-94 12022882-6 2002 The reactivities of Arg(143) and Lys(147) mutants were improved approximately 2-fold with antithrombin in the absence but not in the presence of heparin cofactors. Lysine 33-36 serpin family C member 1 Homo sapiens 90-102 12022882-7 2002 On the other hand, the pentasaccharide-catalyzed reactivity of antithrombin with the Arg(150) mutant was impaired by an order of magnitude. pentasaccharide 23-38 serpin family C member 1 Homo sapiens 63-75 12022882-7 2002 On the other hand, the pentasaccharide-catalyzed reactivity of antithrombin with the Arg(150) mutant was impaired by an order of magnitude. Arginine 85-88 serpin family C member 1 Homo sapiens 63-75 12022882-8 2002 These results suggest that Arg(150) of the autolysis loop may specifically interact with the activated conformation of antithrombin. Arginine 27-30 serpin family C member 1 Homo sapiens 119-131 12004255-7 2002 Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces. pentasaccharides 31-47 serpin family C member 1 Homo sapiens 0-12 11854268-0 2002 Molecular determinants of the mechanism underlying acceleration of the interaction between antithrombin and factor Xa by heparin pentasaccharide. IC 831423 121-144 serpin family C member 1 Homo sapiens 91-103 11854268-2 2002 Antithrombin requires the co-factor, heparin, to efficiently inhibit target proteinases. Heparin 37-44 serpin family C member 1 Homo sapiens 0-12 11854268-3 2002 A specific pentasaccharide sequence (H5) in high affinity heparin induces a conformational change in antithrombin that is particularly important for factor Xa (fXa) inhibition. pentasaccharide 11-26 serpin family C member 1 Homo sapiens 101-113 11854268-3 2002 A specific pentasaccharide sequence (H5) in high affinity heparin induces a conformational change in antithrombin that is particularly important for factor Xa (fXa) inhibition. Heparin 58-65 serpin family C member 1 Homo sapiens 101-113 11854268-4 2002 Thus, synthetic H5 accelerates the interaction between antithrombin and fXa 100-fold as compared with only 2-fold versus thrombin. h5 16-18 serpin family C member 1 Homo sapiens 55-67 11854268-8 2002 The x-ray crystal structure of fXa reveals that Gln(61) forms part of the S1" and S3" pocket, suggesting that the P" region of the reactive center loop of antithrombin is crucial for mediating the acceleration in the rate of inhibition of fXa by H5-activated antithrombin. Glutamine 48-51 serpin family C member 1 Homo sapiens 155-167 11854268-8 2002 The x-ray crystal structure of fXa reveals that Gln(61) forms part of the S1" and S3" pocket, suggesting that the P" region of the reactive center loop of antithrombin is crucial for mediating the acceleration in the rate of inhibition of fXa by H5-activated antithrombin. Glutamine 48-51 serpin family C member 1 Homo sapiens 259-271 12004255-7 2002 Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces. Heparin 61-68 serpin family C member 1 Homo sapiens 0-12 12004255-7 2002 Antithrombin binds to specific pentasaccharides expressed on heparin, glycosaminoglycans, and related proteoglycans within the circulation and along endothelial surfaces. Glycosaminoglycans 70-88 serpin family C member 1 Homo sapiens 0-12 12004255-10 2002 In addition, antithrombin exerts anti-inflammatory properties by both prostacyclin-dependent and prostacyclin-independent actions; heparin interferes with these anti-inflammatory properties. Epoprostenol 70-82 serpin family C member 1 Homo sapiens 13-25 12004255-10 2002 In addition, antithrombin exerts anti-inflammatory properties by both prostacyclin-dependent and prostacyclin-independent actions; heparin interferes with these anti-inflammatory properties. Epoprostenol 97-109 serpin family C member 1 Homo sapiens 13-25 12004255-12 2002 The results of a recent phase 3 clinical trials with high-dose antithrombin in sepsis suggested a beneficial effect in patients who did not concomitantly receive heparin, thereby generating new challenges in the understanding of interactions between antithrombin and heparin or heparin-like proteoglycans. Heparin 162-169 serpin family C member 1 Homo sapiens 63-75 12004255-12 2002 The results of a recent phase 3 clinical trials with high-dose antithrombin in sepsis suggested a beneficial effect in patients who did not concomitantly receive heparin, thereby generating new challenges in the understanding of interactions between antithrombin and heparin or heparin-like proteoglycans. Heparin 267-274 serpin family C member 1 Homo sapiens 63-75 12029263-6 2002 Moreover, patients pre-treated with heparin reach the operating theater with reduced levels of circulating antithrombin III; this may lead to the heparin resistance phenomenon and may further increase the risk for postoperative thrombotic complications. Heparin 36-43 serpin family C member 1 Homo sapiens 107-123 11981148-1 2002 BACKGROUND: Acquired antithrombin III (AT) deficiency may render heparin less effective during cardiac surgery and cardiopulmonary bypass (CPB). Heparin 65-72 serpin family C member 1 Homo sapiens 21-37 12029263-6 2002 Moreover, patients pre-treated with heparin reach the operating theater with reduced levels of circulating antithrombin III; this may lead to the heparin resistance phenomenon and may further increase the risk for postoperative thrombotic complications. Heparin 146-153 serpin family C member 1 Homo sapiens 107-123 11939772-0 2002 Importance of lysine 125 for heparin binding and activation of antithrombin. Lysine 14-20 serpin family C member 1 Homo sapiens 63-75 12017388-2 2002 Its aetiology often recognizes a decrease in circulating antithrombin III (AT III) due to a preoperative heparin treatment. Heparin 105-112 serpin family C member 1 Homo sapiens 57-73 12017388-2 2002 Its aetiology often recognizes a decrease in circulating antithrombin III (AT III) due to a preoperative heparin treatment. Heparin 105-112 serpin family C member 1 Homo sapiens 75-81 12017388-8 2002 This subgroup significantly differs from the AT III-dependent heparin-resistant group being affected by a less severe degree of HR and including less patients pretreated with heparin. Heparin 62-69 serpin family C member 1 Homo sapiens 45-51 12017388-8 2002 This subgroup significantly differs from the AT III-dependent heparin-resistant group being affected by a less severe degree of HR and including less patients pretreated with heparin. Heparin 175-182 serpin family C member 1 Homo sapiens 45-51 11939772-1 2002 The anticoagulant sulfated polysaccharide, heparin, binds to the plasma coagulation proteinase inhibitor, antithrombin, and activates it by a conformational change that results in a greatly increased rate of inhibition of target proteinases. Polysaccharides 27-41 serpin family C member 1 Homo sapiens 106-118 11939772-1 2002 The anticoagulant sulfated polysaccharide, heparin, binds to the plasma coagulation proteinase inhibitor, antithrombin, and activates it by a conformational change that results in a greatly increased rate of inhibition of target proteinases. Heparin 43-50 serpin family C member 1 Homo sapiens 106-118 11939772-2 2002 Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin. pentasaccharide 194-209 serpin family C member 1 Homo sapiens 10-22 11939772-2 2002 Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin. pentasaccharide 194-209 serpin family C member 1 Homo sapiens 175-187 11939772-2 2002 Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin. pentasaccharide 194-209 serpin family C member 1 Homo sapiens 175-187 11939772-2 2002 Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin. Heparin 258-265 serpin family C member 1 Homo sapiens 10-22 11939772-2 2002 Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin. Heparin 258-265 serpin family C member 1 Homo sapiens 175-187 11939772-2 2002 Lys125 of antithrombin has previously been implicated in this binding by chemical modification and site-directed mutagenesis and by the crystal structure of a complex between antithrombin and a pentasaccharide constituting the antithrombin-binding region of heparin. Heparin 258-265 serpin family C member 1 Homo sapiens 175-187 11939772-3 2002 Replacement of Lys125 with Met or Gln in this work reduced the affinity of antithrombin for full-length heparin or the pentasaccharide by 150-600-fold at I = 0.15, corresponding to a loss of 25-33% of the total binding energy. Heparin 104-111 serpin family C member 1 Homo sapiens 75-87 11939772-3 2002 Replacement of Lys125 with Met or Gln in this work reduced the affinity of antithrombin for full-length heparin or the pentasaccharide by 150-600-fold at I = 0.15, corresponding to a loss of 25-33% of the total binding energy. pentasaccharide 119-134 serpin family C member 1 Homo sapiens 75-87 11939772-4 2002 The affinity decrease was due both to disruption of approximately three ionic interactions, indicating that Lys125 and two other basic residues of antithrombin act cooperatively in binding to heparin, and to weakened nonionic interactions. Heparin 192-199 serpin family C member 1 Homo sapiens 147-159 11939772-5 2002 The mutations caused a 10-17-fold decrease in the affinity of the initial, weak binding step of the two-step mechanism of heparin binding to antithrombin. Heparin 122-129 serpin family C member 1 Homo sapiens 141-153 11939772-7 2002 Lys125 is thus a major heparin-binding residue of antithrombin, contributing an amount of binding energy comparable to that of Arg129, but less energy than Lys114. Heparin 23-30 serpin family C member 1 Homo sapiens 50-62 11939772-8 2002 It is the first residue identified so far that has a critical role in the initial recognition of heparin by antithrombin, but also appreciably stabilizes the heparin-induced activated state of the inhibitor. Heparin 97-104 serpin family C member 1 Homo sapiens 108-120 11939772-8 2002 It is the first residue identified so far that has a critical role in the initial recognition of heparin by antithrombin, but also appreciably stabilizes the heparin-induced activated state of the inhibitor. Heparin 158-165 serpin family C member 1 Homo sapiens 108-120 12182916-0 2002 Separation of active and inactive forms of human antithrombin by heparin affinity chromatography. Heparin 65-72 serpin family C member 1 Homo sapiens 49-61 11951068-8 2002 In the patient group (with AT III and/or PC and/or PS decrease) statistically significant reduction of kaolin-kephalin time in comparison with controls was observed (a<0. kaolin-kephalin 103-118 serpin family C member 1 Homo sapiens 27-33 11934350-2 2002 Fondaparinux is a synthetic polysaccharide that selectively binds to antithrombin, the primary endogenous regulator of blood coagulation. Polysaccharides 28-42 serpin family C member 1 Homo sapiens 69-81 11870603-4 2002 Elevation of expression level by selection for increased drug resistance in Chinese hamster ovary cells stably expressing ATIII resulted in formation of disulfide-bonded aggregates of ATIII. Disulfides 153-162 serpin family C member 1 Homo sapiens 122-127 11870603-4 2002 Elevation of expression level by selection for increased drug resistance in Chinese hamster ovary cells stably expressing ATIII resulted in formation of disulfide-bonded aggregates of ATIII. Disulfides 153-162 serpin family C member 1 Homo sapiens 184-189 11870603-8 2002 However, the amount of ATIII-synthesized per L-glutamine consumed did not seem to increase steadily with expression level for ATIII, indicating that secretion of ATIII may be limited by the capacity of the cell to utilize L-glutamine. Glutamine 45-56 serpin family C member 1 Homo sapiens 23-28 11895775-13 2002 Some antibodies reacted strongly with the pentasaccharide, which interacts with antithrombin III. pentasaccharide 42-57 serpin family C member 1 Homo sapiens 80-96 11919156-5 2002 We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding. 3-o, 6-o 36-44 serpin family C member 1 Homo sapiens 100-116 11919156-5 2002 We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding. 3-o, 6-o 36-44 serpin family C member 1 Homo sapiens 118-124 11919156-5 2002 We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding. Oligosaccharides 80-95 serpin family C member 1 Homo sapiens 100-116 11919156-5 2002 We demonstrated the requirements of 3-O, 6-O sulfates and the minimal length of oligosaccharide for antithrombin III (AT-III) binding. Oligosaccharides 80-95 serpin family C member 1 Homo sapiens 118-124 11919156-6 2002 We regenerated the binding sites for AT-III on completely desulfated N-resulfated heparin and revealed the critical modification enzymes. Nitrogen 69-70 serpin family C member 1 Homo sapiens 37-43 11919156-6 2002 We regenerated the binding sites for AT-III on completely desulfated N-resulfated heparin and revealed the critical modification enzymes. Heparin 82-89 serpin family C member 1 Homo sapiens 37-43 11741963-4 2002 To investigate the role of helix D elongation in the allosteric activation of antithrombin, we substituted a proline residue for Lys(133). Proline 109-116 serpin family C member 1 Homo sapiens 78-90 11881992-1 2002 Conformational activation of antithrombin is a critical mechanism for the inhibition of factor Xa, a proteinase of the blood coagulation cascade, and is typically achieved with heparin, a polyanionic polysaccharide clinically used for anticoagulation. Heparin 177-184 serpin family C member 1 Homo sapiens 29-41 11881992-1 2002 Conformational activation of antithrombin is a critical mechanism for the inhibition of factor Xa, a proteinase of the blood coagulation cascade, and is typically achieved with heparin, a polyanionic polysaccharide clinically used for anticoagulation. polyanionic polysaccharide 188-214 serpin family C member 1 Homo sapiens 29-41 11741963-1 2002 Antithrombin requires allosteric activation by heparin for efficient inhibition of its target protease, factor Xa. Heparin 47-54 serpin family C member 1 Homo sapiens 0-12 11881992-7 2002 HINT suggested a comparable antithrombin-binding geometry and interaction profile for ECS and trisaccharide DEF. Trisaccharides 94-107 serpin family C member 1 Homo sapiens 28-40 12091056-1 2002 Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a specific pentasaccharide sequence. Heparin 50-57 serpin family C member 1 Homo sapiens 0-12 12091056-1 2002 Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a specific pentasaccharide sequence. Heparin 59-62 serpin family C member 1 Homo sapiens 0-12 12091056-1 2002 Antithrombin (AT) high affinity of unfractionated heparin (UFH) resides in a specific pentasaccharide sequence. pentasaccharide 86-101 serpin family C member 1 Homo sapiens 0-12 11741963-4 2002 To investigate the role of helix D elongation in the allosteric activation of antithrombin, we substituted a proline residue for Lys(133). Lysine 129-132 serpin family C member 1 Homo sapiens 78-90 11741963-2 2002 A pentasaccharide sequence found in heparin activates antithrombin by inducing conformational changes that affect the reactive center of the inhibitor resulting in optimal recognition by factor Xa. pentasaccharide 2-17 serpin family C member 1 Homo sapiens 54-66 12532174-3 2002 Its structure is the copy of the heparin pentasaccharide sequence, the shortest chain required for antithrombin inhibition of activated factor X without antithrombin action. IC 831423 33-56 serpin family C member 1 Homo sapiens 99-111 11741963-2 2002 A pentasaccharide sequence found in heparin activates antithrombin by inducing conformational changes that affect the reactive center of the inhibitor resulting in optimal recognition by factor Xa. Heparin 36-43 serpin family C member 1 Homo sapiens 54-66 11866668-2 2002 It is a chemically synthetic pentasaccharide mimicking the site of heparin that binds to antithrombin III (AT). pentasaccharide 29-44 serpin family C member 1 Homo sapiens 89-105 11846379-6 2002 Similar experiments with alpha(1)-proteinase inhibitor and antithrombin, two inhibitory serpins that exhibit reactive center loop insertion, show a decrease in ANS fluorescence on cleavage with porcine pancreatic elastase and thrombin, respectively. 1-anilino-8-naphthalenesulfonate 160-163 serpin family C member 1 Homo sapiens 59-71 12532174-3 2002 Its structure is the copy of the heparin pentasaccharide sequence, the shortest chain required for antithrombin inhibition of activated factor X without antithrombin action. IC 831423 33-56 serpin family C member 1 Homo sapiens 153-165 12491369-2 2002 Heparin is widely used as an anticoagulant drug based on its ability to accelerate the rate at which antithrombin inhibits serine proteases in the blood coagulation cascade. Heparin 0-7 serpin family C member 1 Homo sapiens 101-113 11985057-2 2002 When measured in the presence of heparin, plasma antithrombin activity includes heparin cofactor II activity as about 20-30% of the total activity. Heparin 33-40 serpin family C member 1 Homo sapiens 49-61 11806943-0 2002 Hydration effects of heparin on antithrombin probed by osmotic stress. Heparin 21-28 serpin family C member 1 Homo sapiens 32-44 11806943-7 2002 Analytical characterization of water-permeable volumes in x-ray-derived bound and free antithrombin structures were correlated with the volumes measured in solution. Water 31-36 serpin family C member 1 Homo sapiens 87-99 11806943-2 2002 Heparin binding to antithrombin induces conformational transitions distal to the binding site. Heparin 0-7 serpin family C member 1 Homo sapiens 19-31 12168569-4 2002 Antithrombin III stimulates prostacyclin generation in endothelial cells by interacting with heparan sulfate of endothelial cells and inhibits cytokine and tissue factor production in endothelial cells and monocytes. Epoprostenol 28-40 serpin family C member 1 Homo sapiens 0-16 11836169-10 2002 INTERPRETATION AND CONCLUSIONS: Lower than expected thrombin inhibition by endogenous antithrombin action after full activation by heparin addition was found to be a common feature in patients who suffered from previous venous thrombotic events, and may reflect a hitherto unrecognized thrombophilic alteration. Heparin 131-138 serpin family C member 1 Homo sapiens 86-98 11828278-0 2002 Antithrombin III concentrate to treat heparin resistance in patients undergoing cardiac surgery. Heparin 38-45 serpin family C member 1 Homo sapiens 0-16 11828278-1 2002 OBJECTIVE: The purpose of this report is to describe the clinical use of antithrombin III concentrate in 53 patients who were found, in the operating room before cardiopulmonary bypass, to be heparin resistant. Heparin 192-199 serpin family C member 1 Homo sapiens 73-89 11828278-7 2002 Administration of antithrombin III concentrate (500 U in 45 patients and 1000 U in 8 patients) resulted in prolongation of the mean activated clotting time from 492 to 789 seconds without additional heparin. Heparin 199-206 serpin family C member 1 Homo sapiens 18-34 11828278-8 2002 The mean heparin dose response increased from 36.5 to 69.3 s x U(-1) x mL(-1) with antithrombin III treatment. Heparin 9-16 serpin family C member 1 Homo sapiens 83-99 11828278-10 2002 CONCLUSIONS: On the basis of the criterion used in this report, most of the patients defined as being heparin resistant had subnormal plasma antithrombin III activity. Heparin 102-109 serpin family C member 1 Homo sapiens 141-157 11828278-11 2002 Treatment with antithrombin III concentrate resulted in potentiation of the heparin effect to meet predetermined activated clotting time thresholds and allow for cardiopulmonary bypass. Heparin 76-83 serpin family C member 1 Homo sapiens 15-31 11707451-1 2002 Native antithrombin (AT) has an inactive reactive site loop conformation unless it is activated by a unique pentasaccharide fragment of heparin (H(5)). pentasaccharide 108-123 serpin family C member 1 Homo sapiens 7-19 11707451-1 2002 Native antithrombin (AT) has an inactive reactive site loop conformation unless it is activated by a unique pentasaccharide fragment of heparin (H(5)). Heparin 136-143 serpin family C member 1 Homo sapiens 7-19 11812067-12 2002 These findings regarding enoxaparin add to the data to be considered by clinicians when selecting an antithrombin for the acute phase of management of unstable angina/non-ST elevation myocardial infarction. Enoxaparin 25-35 serpin family C member 1 Homo sapiens 101-113 11831754-5 2002 The buffer, 25 mM Tris-HCl pH 8.0; the eluting agent, 2 M (NH4)2SO4; and 100% expansion of settled bed were determined to be the optimum conditions for the purification of antithrombin by ion-exchange expanded bed chromatography. Tris hydrochloride 18-26 serpin family C member 1 Homo sapiens 172-184 11831754-5 2002 The buffer, 25 mM Tris-HCl pH 8.0; the eluting agent, 2 M (NH4)2SO4; and 100% expansion of settled bed were determined to be the optimum conditions for the purification of antithrombin by ion-exchange expanded bed chromatography. Ammonium Sulfate 58-67 serpin family C member 1 Homo sapiens 172-184 12168569-4 2002 Antithrombin III stimulates prostacyclin generation in endothelial cells by interacting with heparan sulfate of endothelial cells and inhibits cytokine and tissue factor production in endothelial cells and monocytes. Heparitin Sulfate 93-108 serpin family C member 1 Homo sapiens 0-16 11677228-1 2001 Measurement of water transfer during antithrombin activation by heparin. Water 15-20 serpin family C member 1 Homo sapiens 37-49 12383040-4 2002 OBJECTIVE: To investigate the in vitro binding of fondaparinux sodium to purified antithrombin III (ATIII) and other plasma proteins. Fondaparinux 50-69 serpin family C member 1 Homo sapiens 82-98 12383040-4 2002 OBJECTIVE: To investigate the in vitro binding of fondaparinux sodium to purified antithrombin III (ATIII) and other plasma proteins. Fondaparinux 50-69 serpin family C member 1 Homo sapiens 100-105 12383040-5 2002 METHODS: Fondaparinux sodium was incubated with human plasma, antithrombin-depleted plasma or purified human plasma proteins, including antithrombin, alpha1-acid glycoprotein, serum albumin and immunoglobulin. Fondaparinux 9-28 serpin family C member 1 Homo sapiens 62-74 12383040-5 2002 METHODS: Fondaparinux sodium was incubated with human plasma, antithrombin-depleted plasma or purified human plasma proteins, including antithrombin, alpha1-acid glycoprotein, serum albumin and immunoglobulin. Fondaparinux 9-28 serpin family C member 1 Homo sapiens 136-148 12383040-7 2002 RESULTS: At steady state, fondaparinux sodium at therapeutic concentrations [i.e. those attainable in the prevention (0.14 to 0.50 mg/L) and treatment (up to approximately 2 mg/L) of VTE] was extensively bound (>97%) to plasma proteins and specifically bound (>94%) to purified ATIII. Fondaparinux 26-45 serpin family C member 1 Homo sapiens 284-289 12811008-0 2002 Development of argatroban as an anticoagulant and antithrombin agent in Japan. argatroban 15-25 serpin family C member 1 Homo sapiens 50-62 12811008-2 2002 In patients with chronic arterial occlusion, argatroban increased the skin temperature, reduced the size of skin ulcers, and decreased the thrombin-antithrombin complex. argatroban 45-55 serpin family C member 1 Homo sapiens 148-160 12811013-1 2002 Argatroban was the very first antithrombin agent that was approved for clinical use. argatroban 0-10 serpin family C member 1 Homo sapiens 30-42 12811013-3 2002 Unlike other antithrombin drugs, argatroban is a reversible antithrombin agent. argatroban 33-43 serpin family C member 1 Homo sapiens 13-25 12811013-3 2002 Unlike other antithrombin drugs, argatroban is a reversible antithrombin agent. argatroban 33-43 serpin family C member 1 Homo sapiens 60-72 12811013-6 2002 At a comparable ACT (300 s), argatroban produces much stronger inhibition of thrombin generation as measured by F(1.2) and thrombin-antithrombin complex generation. argatroban 29-39 serpin family C member 1 Homo sapiens 132-144 12811013-8 2002 The pharmacological profile of argatroban is unique as this antithrombin drug not only inhibits thrombogenesis but also modulates cellular functions. argatroban 31-41 serpin family C member 1 Homo sapiens 60-72 11867875-7 2002 Our standard anticoagulant is unfractionated heparin, where the primary mode of action is potentiation of endogenous AT-III. Heparin 45-52 serpin family C member 1 Homo sapiens 117-123 12096932-5 2002 A small, preliminary clinical trial has suggested that antithrombin therapy with intravenously administered argatroban may be useful in treatment of ICH. argatroban 108-118 serpin family C member 1 Homo sapiens 55-67 11801740-10 2002 Effects of antithrombin were abolished by pretreating cells with heparinase-1, chondroitinase, sodium chlorate and anti-syndecan-4 antibodies. sodium chlorate 95-110 serpin family C member 1 Homo sapiens 11-23 11801740-12 2002 In the presence of pentasaccharide, antithrombin lost its effect on cells. pentasaccharide 19-34 serpin family C member 1 Homo sapiens 36-48 11801740-13 2002 Data indicate that antithrombin directly inhibits chemokine-stimulated migration of monocytes and lymphocytes via the effects of its heparin-binding site on cell surface syndecan-4 by activation of protein kinase C and Rho signaling. Heparin 133-140 serpin family C member 1 Homo sapiens 19-31 12494145-5 2002 Multifactorial regression analysis showed that gender was independently (of age, duration of hypertension, smoking, body mass index, and total cholesterol level) related to only antithrombin III and protein C levels. Cholesterol 143-154 serpin family C member 1 Homo sapiens 178-194 11677228-1 2001 Measurement of water transfer during antithrombin activation by heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 37-49 11677228-3 2001 Heparin triggers conformational changes in, and the functional activation of, the serine proteinase inhibitor antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 110-122 11677228-4 2001 We investigated water-transfer reactions during the activation process to explore the possibility that functional interaction between antithrombin and sulfated glycosaminoglycans can be regulated by osmotic potentials. Water 16-21 serpin family C member 1 Homo sapiens 134-146 11677228-6 2001 Osmotic stress was induced with chemically inert probes that are geometrically excluded from the water-permeable spaces of antithrombin and from intermolecular spaces formed during the association reaction. Water 97-102 serpin family C member 1 Homo sapiens 123-135 11677228-7 2001 The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa. Heparin 54-61 serpin family C member 1 Homo sapiens 41-53 11677228-7 2001 The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa. Heparin 54-61 serpin family C member 1 Homo sapiens 173-185 11677228-7 2001 The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa. Heparin 160-167 serpin family C member 1 Homo sapiens 41-53 11677228-7 2001 The free energy change, Delta G, for the antithrombin/heparin interaction was calculated from the dissociation constant, determined by functional titrations of heparin with antithrombin at fixed concentrations of the coagulation protease factor Xa. Heparin 160-167 serpin family C member 1 Homo sapiens 173-185 11677228-11 2001 Analytical characterization of water-permeable volumes in x-ray-derived bound and free antithrombin structures revealed complex surfaces with smaller hydration volumes in the bound relative to the free conformation. Water 31-36 serpin family C member 1 Homo sapiens 87-99 11755958-10 2001 Antithrombin inhibited protein C activation with an IC(50) value of 290+/-10 nmol/l, which was enhanced fourfold (IC(50) 60 nmol/l) by the addition of heparin 0.5 U/ml. Heparin 151-158 serpin family C member 1 Homo sapiens 0-12 11806438-5 2001 This acquired heparin resistance was attributed to an antithrombin (AT III) deficiency, and was treated with fresh frozen plasma (FFP) to restore adequate anticoagulation. Heparin 14-21 serpin family C member 1 Homo sapiens 54-66 11735695-1 2001 Hirudin is one of the new synthetic antithrombin agents, which is most commonly used in patients with type II heparin-induced thrombocytopenia and in patients with hypersensitivity reactions to unfractionated heparin as well as low-molecular-weight heparins. Heparin 110-117 serpin family C member 1 Homo sapiens 36-48 11735695-1 2001 Hirudin is one of the new synthetic antithrombin agents, which is most commonly used in patients with type II heparin-induced thrombocytopenia and in patients with hypersensitivity reactions to unfractionated heparin as well as low-molecular-weight heparins. Heparin 209-216 serpin family C member 1 Homo sapiens 36-48 11748680-8 2001 Their binding activity to antithrombin III was not proportional to the content of heparin immobilized, and heparin-PGMA-I was the most efficient affinity medium for antithrombin III. Heparin 107-114 serpin family C member 1 Homo sapiens 165-181 11748680-8 2001 Their binding activity to antithrombin III was not proportional to the content of heparin immobilized, and heparin-PGMA-I was the most efficient affinity medium for antithrombin III. pgma-i 115-121 serpin family C member 1 Homo sapiens 165-181 11748680-10 2001 All the three heparin-PGMA beads were exploited for the separation of antithrombin III from human plasma. Heparin 14-21 serpin family C member 1 Homo sapiens 70-86 11748680-10 2001 All the three heparin-PGMA beads were exploited for the separation of antithrombin III from human plasma. pgma 22-26 serpin family C member 1 Homo sapiens 70-86 11755953-3 2001 We have estimated the concentration of circulating thrombin-antithrombin (TAT) complex in patients subjected to transperitoneal nephrectomy and randomized into controls and who received 40-mg enoxaparin 12 h before and 12 h after the operation and then once daily for 7 days. Enoxaparin 192-202 serpin family C member 1 Homo sapiens 60-72 11806438-8 2001 Future treatment with AT III concentrate rather than FFP may reduce heparin requirements that will, in turn, reduce protamine reversal dose, postoperative bleeding attributable to heparin rebound, and its associated complications. Heparin 68-75 serpin family C member 1 Homo sapiens 22-28 11806438-8 2001 Future treatment with AT III concentrate rather than FFP may reduce heparin requirements that will, in turn, reduce protamine reversal dose, postoperative bleeding attributable to heparin rebound, and its associated complications. Heparin 180-187 serpin family C member 1 Homo sapiens 22-28 11597289-13 2001 In patients receiving antithrombin III and concomitant heparin, a significantly increased bleeding incidence was observed (23.8% for antithrombin III group vs 13.5% for placebo group; P<.001). Heparin 55-62 serpin family C member 1 Homo sapiens 133-149 11798464-7 2001 To date, we cannot provide a mechanism to explain the AT III-promoted modulation of TNF-alpha and IL-1beta generation in VSMC. vsmc 121-125 serpin family C member 1 Homo sapiens 54-60 11567021-0 2001 Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding. Lysine 0-6 serpin family C member 1 Homo sapiens 14-26 11567021-0 2001 Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding. IC 831423 85-108 serpin family C member 1 Homo sapiens 14-26 11567021-1 2001 Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin. Heparin 138-145 serpin family C member 1 Homo sapiens 57-69 11567021-1 2001 Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin. Heparin 138-145 serpin family C member 1 Homo sapiens 211-223 11567021-1 2001 Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin. pentasaccharide 251-266 serpin family C member 1 Homo sapiens 57-69 11567021-1 2001 Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin. pentasaccharide 251-266 serpin family C member 1 Homo sapiens 211-223 11567021-1 2001 Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin. Heparin 275-282 serpin family C member 1 Homo sapiens 57-69 11567021-1 2001 Lys(114) of the plasma coagulation proteinase inhibitor, antithrombin, has been implicated in binding of the glycosaminoglycan activator, heparin, by previous mutagenesis studies and by the crystal structure of antithrombin in complex with the active pentasaccharide unit of heparin. Heparin 275-282 serpin family C member 1 Homo sapiens 211-223 11567021-2 2001 In the present work, substitution of Lys(114) by Ala or Met was shown to decrease the affinity of antithrombin for heparin and the pentasaccharide by approximately 10(5)-fold at I 0.15, corresponding to a reduction in binding energy of approximately 50%. Heparin 115-122 serpin family C member 1 Homo sapiens 98-110 11567021-2 2001 In the present work, substitution of Lys(114) by Ala or Met was shown to decrease the affinity of antithrombin for heparin and the pentasaccharide by approximately 10(5)-fold at I 0.15, corresponding to a reduction in binding energy of approximately 50%. pentasaccharide 131-146 serpin family C member 1 Homo sapiens 98-110 11567021-4 2001 The mutation minimally affected the initial, weak binding of the two-step mechanism of pentasaccharide binding to antithrombin but appreciably (>40-fold) decreased the forward rate constant of the conformational change in the second step and greatly (>1000-fold) increased the reverse rate constant of this step. pentasaccharide 87-102 serpin family C member 1 Homo sapiens 114-126 11567021-8 2001 However, its major effect, also larger than that of these two residues, is in maintaining antithrombin in the activated state by interactions that most likely involve the reducing end disaccharide unit. Disaccharides 184-196 serpin family C member 1 Homo sapiens 90-102 11794963-2 2001 The new anticoagulants are as follows: saccharide structures such as danaparoid and the pentasaccharide of antithrombin binding, and direct thrombin inhibitors, such as recombinating hirudines (desirudine, lepirudine), bivalirudine, melagatran.... Other molecular targets are possible, both at platelet and blood clotting levels but, for the moment, the dilemma remains and reinforcement of antithrombotic activity goes hand in hand with a greater decrease in the defensive mechanisms against bleeding. pentasaccharide 88-103 serpin family C member 1 Homo sapiens 107-119 11728442-4 2001 The serpin antithrombin III (ATIII) and the thrombin inhibitor hirudin both inhibited nuclear factor (NF)-kappaB activation by LPS and Lipid A. Lipid A 135-142 serpin family C member 1 Homo sapiens 11-27 11728442-4 2001 The serpin antithrombin III (ATIII) and the thrombin inhibitor hirudin both inhibited nuclear factor (NF)-kappaB activation by LPS and Lipid A. Lipid A 135-142 serpin family C member 1 Homo sapiens 29-34 11763451-0 2001 Synthesis of conformationally locked L-iduronic acid derivatives: direct evidence for a critical role of the skew-boat 2S0 conformer in the activation of antithrombin by heparin. Iduronic Acid 37-52 serpin family C member 1 Homo sapiens 154-166 11763451-0 2001 Synthesis of conformationally locked L-iduronic acid derivatives: direct evidence for a critical role of the skew-boat 2S0 conformer in the activation of antithrombin by heparin. Heparin 170-177 serpin family C member 1 Homo sapiens 154-166 11763451-1 2001 We have used organic synthesis to understand the role of L-iduronic acid conformational flexibility in the activation of antithrombin by heparin. Iduronic Acid 57-72 serpin family C member 1 Homo sapiens 121-133 11763451-1 2001 We have used organic synthesis to understand the role of L-iduronic acid conformational flexibility in the activation of antithrombin by heparin. Heparin 137-144 serpin family C member 1 Homo sapiens 121-133 11763451-2 2001 Among known synthetic analogues of the genuine pentasaccharidic sequence representing the antithrombin binding site of heparin, we have selected as a reference compound the methylated anti-factor Xa pentasaccharide 1. Heparin 119-126 serpin family C member 1 Homo sapiens 90-102 11763451-11 2001 These results clearly establish the critical importance of the 2S0 conformation of L-iduronic acid in the activation of antithrombin by heparin. Iduronic Acid 83-98 serpin family C member 1 Homo sapiens 120-132 11763451-11 2001 These results clearly establish the critical importance of the 2S0 conformation of L-iduronic acid in the activation of antithrombin by heparin. Heparin 136-143 serpin family C member 1 Homo sapiens 120-132 11722589-3 2001 We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI). Tritium 22-26 serpin family C member 1 Homo sapiens 174-190 11722589-3 2001 We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI). Estradiol 57-66 serpin family C member 1 Homo sapiens 174-190 11722589-3 2001 We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI). Progesterone 68-80 serpin family C member 1 Homo sapiens 174-190 11722589-3 2001 We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI). Testosterone 82-94 serpin family C member 1 Homo sapiens 174-190 11722589-3 2001 We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI). Hydrocortisone 96-104 serpin family C member 1 Homo sapiens 174-190 11722589-3 2001 We studied binding of (3)H-labeled hydrophobic hormones (estradiol, progesterone, testosterone, cortisol, aldosterone, and all-trans-retinoic acid) to the inhibitory serpins antithrombin III, heparin cofactor II, plasminogen activator inhibitor-1, and protein C inhibitor (PCI). Aldosterone 106-117 serpin family C member 1 Homo sapiens 174-190 11583572-0 2001 Conformation of heparin pentasaccharide bound to antithrombin III. IC 831423 16-39 serpin family C member 1 Homo sapiens 49-65 11597289-15 2001 High-dose antithrombin III was associated with an increased risk of hemorrhage when administered with heparin. Heparin 102-109 serpin family C member 1 Homo sapiens 10-26 11668418-5 2001 This indicates that heparins can influence cellular signaling in SMC via an antithrombin-II (AT-III)-independent mechanism. Heparin 20-28 serpin family C member 1 Homo sapiens 76-91 12004145-8 2001 Activity of AT III and protein C within 72 hours after introduction of steroids increased without any marked alterations in the clinical and biochemical course of the nephrotic syndrome. Steroids 71-79 serpin family C member 1 Homo sapiens 12-18 11669429-14 2001 A predictable drop of AT III (24.2%) occurred with saline dilution, while AT III levels in the AT III/Saline group were similar to the undiluted control. Sodium Chloride 51-57 serpin family C member 1 Homo sapiens 22-28 11669429-14 2001 A predictable drop of AT III (24.2%) occurred with saline dilution, while AT III levels in the AT III/Saline group were similar to the undiluted control. Sodium Chloride 102-108 serpin family C member 1 Homo sapiens 74-80 11669429-14 2001 A predictable drop of AT III (24.2%) occurred with saline dilution, while AT III levels in the AT III/Saline group were similar to the undiluted control. Sodium Chloride 102-108 serpin family C member 1 Homo sapiens 74-80 11668417-0 2001 Effects of sulfation on antithrombin-thrombin/factor Xa interactions in semisynthetic low molecular weight heparins. Heparin 107-115 serpin family C member 1 Homo sapiens 24-36 11668417-2 2001 To gain insight into structure-activity relationships, we investigated quantitatively the interactions of a series of sulfated LMW heparins of similar molecular weights (derived from statistical desulfation of a supersulfated heparin) with the target enzymes human antithrombin (AT) and thrombin (T). Heparin, Low-Molecular-Weight 127-139 serpin family C member 1 Homo sapiens 265-277 11668417-2 2001 To gain insight into structure-activity relationships, we investigated quantitatively the interactions of a series of sulfated LMW heparins of similar molecular weights (derived from statistical desulfation of a supersulfated heparin) with the target enzymes human antithrombin (AT) and thrombin (T). Heparin 131-138 serpin family C member 1 Homo sapiens 265-277 11668418-5 2001 This indicates that heparins can influence cellular signaling in SMC via an antithrombin-II (AT-III)-independent mechanism. Heparin 20-28 serpin family C member 1 Homo sapiens 93-99 11522012-3 2001 Binding to the cell blocked acceleration of the thrombin:antithrombin interaction by heparin. Heparin 85-92 serpin family C member 1 Homo sapiens 57-69 11686316-1 2001 We report 5 children from 3 families with homozygous antithrombin deficiency type II affecting the heparin binding site (99 Leu to Phe mutation). Heparin 99-106 serpin family C member 1 Homo sapiens 53-65 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 56-72 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 74-79 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 151-156 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate 32-35 serpin family C member 1 Homo sapiens 151-156 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Heparin 113-120 serpin family C member 1 Homo sapiens 56-72 11551226-8 2001 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Heparin 113-120 serpin family C member 1 Homo sapiens 74-79 11549250-3 2001 In vitro effects of antithrombin on human neutrophil migration in modified Boyden chambers were abolished by pretreating cells with heparinase-1, chondroitinase, sodium chlorate, and anti-syndecan-4 antibodies. sodium chlorate 162-177 serpin family C member 1 Homo sapiens 20-32 11549250-5 2001 In the presence of pentasaccharide, antithrombin lost its activity on the cells. pentasaccharide 19-34 serpin family C member 1 Homo sapiens 36-48 11549250-6 2001 Data suggest that antithrombin regulates neutrophil migration via effects of its heparin-binding site on cell surface syndecan-4. Heparin 81-88 serpin family C member 1 Homo sapiens 18-30 11575948-3 2001 Atherospermidine and squamolone exhibited cytotoxicity against hepatocarcinoma cancer cell lines (Hep G(2) and 2,2,15), and the activity of some of the alkaloids in an antithrombin assay is also discussed. atherospermidine 0-16 serpin family C member 1 Homo sapiens 168-180 11575948-3 2001 Atherospermidine and squamolone exhibited cytotoxicity against hepatocarcinoma cancer cell lines (Hep G(2) and 2,2,15), and the activity of some of the alkaloids in an antithrombin assay is also discussed. squamolone 21-31 serpin family C member 1 Homo sapiens 168-180 11479487-6 2001 RESULTS: The more recently developed synthetic pentasaccharide Org31540/SR90107A provides potent antithrombotic activity through selective inhibition of Factor Xa by high-affinity binding to antithrombin III. pentasaccharide 47-62 serpin family C member 1 Homo sapiens 191-207 11778099-5 2001 The pentasaccharide binds specifically to antithrombin III (ATIII) thus potentiating its inhibitory activity on factor Xa. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 42-58 11778099-5 2001 The pentasaccharide binds specifically to antithrombin III (ATIII) thus potentiating its inhibitory activity on factor Xa. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 60-65 11522012-7 2001 The release of these proteins from cells within the necrotic core of a tumour or from cells killed during chemotherapy may abrogate the heparan sulphate/antithrombin system and possibly contribute to the idiopathic thromboembolism often associated with cancer (Trousseau"s syndrome). Heparitin Sulfate 136-152 serpin family C member 1 Homo sapiens 153-165 11380262-2 2001 Heparin has been proposed to conformationally activate the serpin, antithrombin, by making the reactive center loop P1 arginine residue accessible to proteinases. Heparin 0-7 serpin family C member 1 Homo sapiens 67-79 11429331-15 2001 Antithrombin effects may explain the inhibition of shear activation of platelets by both heparin and protamine. Heparin 89-96 serpin family C member 1 Homo sapiens 0-12 11487039-9 2001 The efficacy and safety of pentasaccharide (the smallest antithrombin binding sequence of heparin) in the treatment and prevention of venous thromboembolic disorders is currently under investigation. pentasaccharide 27-42 serpin family C member 1 Homo sapiens 57-69 11487041-8 2001 Antithrombin has been shown in vitro to increase prostacyclin responses and activated protein C has been shown to inhibit a variety of cellular responses including endotoxin induced calcium fluxes in monocytes and the nuclear translocation of NFKB, a key step in the generation of the inflammatory response. Calcium 182-189 serpin family C member 1 Homo sapiens 0-12 11389017-4 2001 The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond. Arginine 179-182 serpin family C member 1 Homo sapiens 75-91 11389017-4 2001 The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond. Arginine 179-182 serpin family C member 1 Homo sapiens 133-149 11521878-4 2001 Micellar electrokinetic chromatography was used to analytically separate these AT III variants, which differ in their affinity to the polysaccharide heparin. Polysaccharides 134-148 serpin family C member 1 Homo sapiens 79-85 11521878-4 2001 Micellar electrokinetic chromatography was used to analytically separate these AT III variants, which differ in their affinity to the polysaccharide heparin. Heparin 149-156 serpin family C member 1 Homo sapiens 79-85 11441984-12 2001 Furthermore, the release of TFPI by heparin is mediated by non-antithrombin III binding fragments. Heparin 36-43 serpin family C member 1 Homo sapiens 63-79 11389017-4 2001 The antibody-bound prothrombin formed a stable stoichiometric complex with antithrombin III, consisting of intact prothrombin and an antithrombin III molecule cleaved at the (393)Arg-(394)Ser bond. Serine 188-191 serpin family C member 1 Homo sapiens 75-91 11380262-2 2001 Heparin has been proposed to conformationally activate the serpin, antithrombin, by making the reactive center loop P1 arginine residue accessible to proteinases. Arginine 119-127 serpin family C member 1 Homo sapiens 67-79 11380262-3 2001 To evaluate this proposal, we determined the effect of mutating the P1 arginine on antithrombin"s specificity for target and nontarget proteinases in both native and heparin-activated states of the serpin. Arginine 71-79 serpin family C member 1 Homo sapiens 83-95 11380262-3 2001 To evaluate this proposal, we determined the effect of mutating the P1 arginine on antithrombin"s specificity for target and nontarget proteinases in both native and heparin-activated states of the serpin. Heparin 166-173 serpin family C member 1 Homo sapiens 83-95 11380262-4 2001 As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)). Arginine 32-40 serpin family C member 1 Homo sapiens 120-132 11380262-4 2001 As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)). Tryptophan 44-54 serpin family C member 1 Homo sapiens 120-132 11380262-4 2001 As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)). Histidine 56-65 serpin family C member 1 Homo sapiens 120-132 11380262-4 2001 As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)). Leucine 67-74 serpin family C member 1 Homo sapiens 120-132 11380262-4 2001 As expected, mutation of the P1 arginine to tryptophan, histidine, leucine, and methionine converted the specificity of antithrombin from a trypsin inhibitor (k(assoc) = 2 x 10(5) M(-1) s(-1)) to a chymotrypsin inhibitor (k(assoc) = 10(3)-10(5) M(-1) s(-1)). Methionine 80-90 serpin family C member 1 Homo sapiens 120-132 11380262-6 2001 Mutation of the P1 arginine greatly reduced k(assoc) for antithrombin inhibition of thrombin and factor Xa from 40- to 5000-fold, but heparin normally accelerated the reactions of the variant antithrombins with these enzymes to make them reasonably efficient inhibitors (k(assoc) = 10(3)-10(4) M(-1) s(-1)). Arginine 19-27 serpin family C member 1 Homo sapiens 57-69 11380262-10 2001 Together, these findings suggest that the P1 arginine residue is similarly accessible to proteinases in both native and heparin-activated states of the serpin and contributes similarly to the specificity of antithrombin for thrombin and factor Xa in the two serpin conformational states. Arginine 45-53 serpin family C member 1 Homo sapiens 207-219 11380262-11 2001 Consequently, determinants other than the P1 residue are responsible for enhancing the specificity of antithrombin for the two proteinases when activated by heparin. Heparin 157-164 serpin family C member 1 Homo sapiens 102-114 11380263-1 2001 Activation of antithrombin by high-affinity heparin as an inhibitor of factor Xa has been ascribed to an allosteric switch between two conformations of the reactive center loop. Heparin 44-51 serpin family C member 1 Homo sapiens 14-26 11322919-2 2001 Hirudin is a powerful, direct, and specific antithrombin agent that can be used in many therapeutic scenarios in which heparin is routinely used. Heparin 119-126 serpin family C member 1 Homo sapiens 44-56 11278943-5 2001 The kinetics of inhibition of factor Xa (FXa) by antithrombin (AT) and AT-heparin were measured by monitoring activation of II(S525C)-fluorescein and the hydrolysis of the chromogenic substrate S2222 in the presence of AT. Fluorescein 134-145 serpin family C member 1 Homo sapiens 49-61 11278930-0 2001 Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the reactive center loop sequence. Heparin 0-7 serpin family C member 1 Homo sapiens 36-48 11278930-2 2001 Heparin activates the primary serpin inhibitor of blood clotting proteinases, antithrombin, both by an allosteric conformational change mechanism that specifically enhances factor Xa inactivation and by a ternary complex bridging mechanism that promotes the inactivation of thrombin and other target proteinases. Heparin 0-7 serpin family C member 1 Homo sapiens 78-90 11278930-4 2001 Evaluation of 12 such antithrombin variants showed that the thrombin specificity of the serpin allosterically activated by a heparin pentasaccharide could be enhanced as much as 55-fold by changing P3, P2, and P2" residues to a consensus thrombin recognition sequence. IC 831423 125-148 serpin family C member 1 Homo sapiens 22-34 11559998-5 2001 Administration of a standard heparin is accompanied by exhaustion of the antithrombin activity of the blood and depression of fibrinolysis, which event comes to be especially dangerous in the arterial vessels. Heparin 29-36 serpin family C member 1 Homo sapiens 73-85 11290592-3 2001 There are conflicting results as to whether anticoagulant heparins can catalyze the antithrombin inhibition of factor Xa in the prothrombinase complex (factor Va, negatively charged membrane surfaces, and calcium ion), which is the physiologically relevant form of the proteinase responsible for the activation of prothrombin to thrombin during the blood coagulation process. Heparin 58-66 serpin family C member 1 Homo sapiens 84-96 11350186-6 2001 Short-term low-dose oral mannose supplementation improved her transferrin IEF pattern and normalized her antithrombin III activity, further substantiating the beneficial effect of mannose in CDG-Ib. Mannose 25-32 serpin family C member 1 Homo sapiens 105-121 11290592-4 2001 In this study, a novel assay system was developed to compare the catalytic effect of different molecular-weight heparins in the antithrombin inhibition of factor Xa, either in free form or assembled into the prothrombinase complex during the process of prothrombin activation. Heparin 112-120 serpin family C member 1 Homo sapiens 128-140 11290592-5 2001 This assay takes advantage of the unique property of a recombinant mutant antithrombin, which, similar to the wild-type antithrombin, rapidly inhibits factor Xa, but not thrombin, in the presence of heparin. Heparin 199-206 serpin family C member 1 Homo sapiens 74-86 11290592-5 2001 This assay takes advantage of the unique property of a recombinant mutant antithrombin, which, similar to the wild-type antithrombin, rapidly inhibits factor Xa, but not thrombin, in the presence of heparin. Heparin 199-206 serpin family C member 1 Homo sapiens 120-132 11231699-2 2001 Important new antiplatelet drugs (glycoprotein IIb-IIIa inhibitors) and antithrombin agents (low-molecular-weight heparin) are currently recommended for patients with unstable angina pectoris/non-ST-segment elevation MI who are at high or intermediate risk on the basis of symptoms, electrocardiographic findings, and the presence or absence of serum markers (eg, troponin I, troponin T, and creatine kinase-MB). Heparin 114-121 serpin family C member 1 Homo sapiens 72-84 11287128-0 2001 Antithrombin binding of low molecular weight heparins and inhibition of factor Xa. Heparin 45-53 serpin family C member 1 Homo sapiens 0-12 11287128-1 2001 Fluorescence and stopped flow methods were used to compare clinically used heparins with regard to their ability to bind to antithrombin and to accelerate the inactivation of factor Xa. Heparin 75-83 serpin family C member 1 Homo sapiens 124-136 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 57-64 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 57-64 serpin family C member 1 Homo sapiens 248-260 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin, Low-Molecular-Weight 66-70 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin, Low-Molecular-Weight 66-70 serpin family C member 1 Homo sapiens 248-260 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Enoxaparin 73-83 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Dalteparin 85-92 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. ardeparin 97-106 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. ardeparin 97-106 serpin family C member 1 Homo sapiens 248-260 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 127-134 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 127-134 serpin family C member 1 Homo sapiens 248-260 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 136-139 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 136-139 serpin family C member 1 Homo sapiens 248-260 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 127-134 serpin family C member 1 Homo sapiens 13-25 11287128-2 2001 Titration of antithrombin with both low molecular weight heparin (LMWH) (enoxaparin, fragmin and ardeparin) and unfractionated heparin (UFH) produced an equivalent fluorescence increase and indicates similar affinity of all heparin preparations to antithrombin. Heparin 127-134 serpin family C member 1 Homo sapiens 248-260 11287128-4 2001 The rate of factor Xa inhibition by antithrombin increased with the concentration of the examined heparins to the same limiting value, but the concentration required for maximal acceleration depended on the preparation. Heparin 98-106 serpin family C member 1 Homo sapiens 36-48 11287128-6 2001 In contrast, in the presence of Ca UFH accelerated the inhibition of factor Xa by antithrombin 10-fold more efficiently than comparable concentrations of the high affinity fractions of enoxaparin and fragmin. Heparin 35-38 serpin family C member 1 Homo sapiens 82-94 11287128-8 2001 In conclusion, under physiologic conditions the anti-factor Xa activity of heparin results from a composite effect of chain length and the content of material with high affinity to antithrombin. Heparin 75-82 serpin family C member 1 Homo sapiens 181-193 11254909-1 2001 As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF). Heparin 167-170 serpin family C member 1 Homo sapiens 118-130 11337927-2 2001 The purpose of this study is to elucidate efficacy and safety of a combined approach using a bolus injection of low dose of mutant tissue plasminogen activator (mt-PA) with heparin and aspirin to ensure definite antithrombin and antiplatelet efficacy, followed by back-up percutaneous transluminal coronary angioplasty(PTCA). mt-pa 161-166 serpin family C member 1 Homo sapiens 212-224 11337927-2 2001 The purpose of this study is to elucidate efficacy and safety of a combined approach using a bolus injection of low dose of mutant tissue plasminogen activator (mt-PA) with heparin and aspirin to ensure definite antithrombin and antiplatelet efficacy, followed by back-up percutaneous transluminal coronary angioplasty(PTCA). Aspirin 185-192 serpin family C member 1 Homo sapiens 212-224 11260565-6 2001 RESULTS: We found that high-dose methotrexate administration adversely affected both the coagulation system (prolonged prothrombin time and activated partial thromboplastin time and decreased fibrinogen levels) and coagulation inhibitors (decreased protein C, protein S, antithrombin III) on day 1 after chemotherapy compared to the baseline values. Methotrexate 33-45 serpin family C member 1 Homo sapiens 271-287 11134031-0 2001 Hypersulfated low molecular weight heparin with reduced affinity for antithrombin acts as an anticoagulant by inhibiting intrinsic tenase and prothrombinase. Heparin 35-42 serpin family C member 1 Homo sapiens 69-81 11134031-2 2001 Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold. Heparin, Low-Molecular-Weight 34-38 serpin family C member 1 Homo sapiens 66-78 11134031-2 2001 Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold. la-lmwh 80-87 serpin family C member 1 Homo sapiens 66-78 11134031-2 2001 Although chemical modification of LMWH, to lower its affinity for antithrombin (LA-LMWH) has no effect on its ability to inhibit intrinsic tenase, N-desulfation of LMWH reduces its activity 12-fold. Heparin, Low-Molecular-Weight 83-87 serpin family C member 1 Homo sapiens 66-78 11323006-1 2001 In the presence of glycosaminoglycans, thrombin is rapidly inactivated by two natural inhibitors secreted from liver: antithrombin (AT) is presumed to be the principal thrombin inhibitor in circulating blood, while for heparin cofactor II (HCII), a role outside circulation has been proposed. Glycosaminoglycans 19-37 serpin family C member 1 Homo sapiens 118-130 11278631-0 2001 A novel anti-angiogenic form of antithrombin with retained proteinase binding ability and heparin affinity. Heparin 90-97 serpin family C member 1 Homo sapiens 32-44 11254909-1 2001 As thrombin stimulates P-selectin expression on platelets and its release into plasma, we hypothesized that enhancing antithrombin activity by unfractionated heparin (UFH) could decrease plasma levels of circulating (c)P-selectin, (c)E-selectin, and von Willebrand Factor (vWF). Heparin 158-165 serpin family C member 1 Homo sapiens 118-130 11238089-6 2001 Initially it was hypothesized that the cause of the disease in this family could be an antithrombin III (AT3) mutation that resulted in a constitutively active AT3 in the absence of heparin binding. Heparin 182-189 serpin family C member 1 Homo sapiens 87-103 11238089-6 2001 Initially it was hypothesized that the cause of the disease in this family could be an antithrombin III (AT3) mutation that resulted in a constitutively active AT3 in the absence of heparin binding. Heparin 182-189 serpin family C member 1 Homo sapiens 105-108 11159540-4 2001 Preincubation in vitro of neutrophils with Kybernin P or immune-adsorbed AT III significantly deactivated migration toward fMet-Leu-Phe, or interleukin-8 (IL-8), in a concentration-dependent manner. Leucine 128-131 serpin family C member 1 Homo sapiens 73-79 11304663-10 2001 In children treated with prednisone alone, a marked increase in plasma AT-III (by 76%, P < 0.001) and alpha 2-A (36%, P < 0.019) activity, and a significant decrease of the plasma fibrinogen concentration (6.07 +/- 1.66 vs. 3.17 +/- 1.64 g/L, P < 0.001), and APTT (45.1 +/- 7.6 vs. 33.8 +/- 4.4 s, P < 0.001) were found. Prednisone 25-35 serpin family C member 1 Homo sapiens 71-77 11304663-11 2001 Prednisone plus EACA therapy resulted in a significant increase in plasma AT-III activity (by 53%, P < 0.003), whereas plasma fibrinogen concentration and APTT remained unchanged. Prednisone 0-10 serpin family C member 1 Homo sapiens 74-80 11087737-4 2001 However, the rate of inhibition by antithrombin III in the presence of submaximal concentrations of heparin is reduced for all the enzymes. Heparin 100-107 serpin family C member 1 Homo sapiens 35-51 11159540-4 2001 Preincubation in vitro of neutrophils with Kybernin P or immune-adsorbed AT III significantly deactivated migration toward fMet-Leu-Phe, or interleukin-8 (IL-8), in a concentration-dependent manner. Phenylalanine 132-135 serpin family C member 1 Homo sapiens 73-79 11159540-7 2001 Analyses revealed that the AT III heparin-binding site interacts with neutrophil membrane-associated heparan sulfate proteoglycan receptors. Heparin 34-41 serpin family C member 1 Homo sapiens 27-33 11159540-8 2001 Mechanisms of intracellular signaling differed; the deactivation of IL-8-induced chemotaxis resulted from tyrphostin-sensitive interactions of AT III-signaling with the IL-8 signal transduction pathway, whereas AT III-induced chemotaxis involved protein kinase C and phosphodiesterases. Tyrphostins 106-116 serpin family C member 1 Homo sapiens 143-149 11133602-16 2001 In Group A patients with decreased AT activity, 18% demonstrated an inadequate ACT response-defined as ACT <400 s-to the first bolus injection of heparin. Heparin 149-156 serpin family C member 1 Homo sapiens 35-37 11133602-0 2001 Low preoperative antithrombin activity causes reduced response to heparin in adult but not in infant cardiac-surgical patients. Heparin 66-73 serpin family C member 1 Homo sapiens 17-29 11133602-1 2001 UNLABELLED: We evaluated the interaction of preoperative antithrombin (AT) activity and intraoperative response to heparin in cardiac surgery. Heparin 115-122 serpin family C member 1 Homo sapiens 57-69 11133602-1 2001 UNLABELLED: We evaluated the interaction of preoperative antithrombin (AT) activity and intraoperative response to heparin in cardiac surgery. Heparin 115-122 serpin family C member 1 Homo sapiens 71-73 11133602-3 2001 Heparin itself has no anticoagulant properties, however it causes a conformational change of the physiologic plasma inhibitor AT that converts this slow-acting serine protease inhibitor into a fast acting one. Heparin 0-7 serpin family C member 1 Homo sapiens 126-128 11133602-4 2001 Thus, adequate AT activity is a prerequisite for sufficient heparin anticoagulation. Heparin 60-67 serpin family C member 1 Homo sapiens 15-17 11197503-1 2001 Heparin is a potent anticoagulant agent that interacts strongly with antithrombin III to prevent the formation of fibrin clot. Heparin 0-7 serpin family C member 1 Homo sapiens 69-85 11162400-6 2001 Antithrombin was eluted at about 13 min, and L-AT, at 30 min, corresponding to about 4.2 and 1.6 mol/L sodium chloride, respectively. Sodium Chloride 103-118 serpin family C member 1 Homo sapiens 0-12 14728009-1 2001 Enoxaparin (enoxaparin sodium) is a low-molecular-weight heparin that binds to and increases the activity of antithrombin III. Enoxaparin 0-10 serpin family C member 1 Homo sapiens 109-125 14728009-1 2001 Enoxaparin (enoxaparin sodium) is a low-molecular-weight heparin that binds to and increases the activity of antithrombin III. Enoxaparin 12-29 serpin family C member 1 Homo sapiens 109-125 14728009-1 2001 Enoxaparin (enoxaparin sodium) is a low-molecular-weight heparin that binds to and increases the activity of antithrombin III. Heparin 57-64 serpin family C member 1 Homo sapiens 109-125 11133602-5 2001 AT activity is reduced by long-term heparin therapy. Heparin 36-43 serpin family C member 1 Homo sapiens 0-2 11133602-19 2001 These results suggest that preoperative diminished AT activity causes reduced response to heparin in adult but not in infant patients. Heparin 90-97 serpin family C member 1 Homo sapiens 51-53 11133602-13 2001 In adult patients, preoperative AT activity depended predominantly on preoperative heparin treatment: 62% of the patients with an AT activity <80% were pretreated with heparin. Heparin 83-90 serpin family C member 1 Homo sapiens 32-34 11133602-13 2001 In adult patients, preoperative AT activity depended predominantly on preoperative heparin treatment: 62% of the patients with an AT activity <80% were pretreated with heparin. Heparin 171-178 serpin family C member 1 Homo sapiens 32-34 11133602-21 2001 Measurement of preoperative AT activity identifies adult patients at risk of reduced sensitivity to heparin. Heparin 100-107 serpin family C member 1 Homo sapiens 28-30 11133602-24 2001 In contrast, in patients older than one year of age and adult patients decreased preoperative AT activity is mainly caused by preoperative heparin therapy and causes insufficient response to heparin anticoagulation with a standard heparin dosage. Heparin 139-146 serpin family C member 1 Homo sapiens 94-96 11133602-24 2001 In contrast, in patients older than one year of age and adult patients decreased preoperative AT activity is mainly caused by preoperative heparin therapy and causes insufficient response to heparin anticoagulation with a standard heparin dosage. Heparin 191-198 serpin family C member 1 Homo sapiens 94-96 11133602-24 2001 In contrast, in patients older than one year of age and adult patients decreased preoperative AT activity is mainly caused by preoperative heparin therapy and causes insufficient response to heparin anticoagulation with a standard heparin dosage. Heparin 191-198 serpin family C member 1 Homo sapiens 94-96 11190907-1 2001 A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism. pentasaccharide 12-27 serpin family C member 1 Homo sapiens 65-81 11777389-6 2001 The adsorptivity and its stability in buffer solution, complexation compatibility with antithrombin III (ATIII), were enhanced with larger alkyl-group-derivatized heparins. Heparin 163-171 serpin family C member 1 Homo sapiens 87-103 11777389-6 2001 The adsorptivity and its stability in buffer solution, complexation compatibility with antithrombin III (ATIII), were enhanced with larger alkyl-group-derivatized heparins. Heparin 163-171 serpin family C member 1 Homo sapiens 105-110 11288878-1 2001 Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex. Heparin 74-81 serpin family C member 1 Homo sapiens 42-54 11288878-1 2001 Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex. Heparin 74-81 serpin family C member 1 Homo sapiens 147-159 11288878-1 2001 Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex. Heparin 116-123 serpin family C member 1 Homo sapiens 42-54 11288878-1 2001 Kinetic studies of thrombin inhibition by antithrombin in the presence of heparin have shown that thrombin binds to heparin in a preformed heparin-antithrombin complex. Heparin 116-123 serpin family C member 1 Homo sapiens 147-159 11288878-2 2001 To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics, which structurally are very similar to the genuine polysaccharide. Heparin 103-110 serpin family C member 1 Homo sapiens 70-82 11288878-2 2001 To study the relative position of the thrombin binding domain and the antithrombin binding domain on a heparin molecule we have designed and synthesized heparin mimetics, which structurally are very similar to the genuine polysaccharide. Heparin 153-160 serpin family C member 1 Homo sapiens 70-82 11936856-5 2001 Our results confirmed, in opposition to almost all early literature, that under very strict conditions of pH 6.0, calcium chloride concentration (2 mM), and very low ionic strength (25 mM), the first component of the human complement cascade recognize heparin fractions "enriched" in the high affinity sequence for the antithrombin III. Heparin 252-259 serpin family C member 1 Homo sapiens 319-335 11190907-1 2001 A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism. pentasaccharide 12-27 serpin family C member 1 Homo sapiens 83-88 11190907-1 2001 A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism. PENTA 29-36 serpin family C member 1 Homo sapiens 65-81 11190907-1 2001 A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism. PENTA 29-36 serpin family C member 1 Homo sapiens 83-88 11190907-1 2001 A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism. Heparin 110-117 serpin family C member 1 Homo sapiens 65-81 11190907-1 2001 A synthetic pentasaccharide (SR90107/ ORG31540) representing the antithrombin III (ATIII) binding sequence in heparin is under clinical development for the prophylaxis and management of venous thromboembolism. Heparin 110-117 serpin family C member 1 Homo sapiens 83-88 11465877-1 2001 UNLABELLED: Reviparin (reviparin sodium) is a low molecular weight heparin (LMWH) that catalyses the inactivation of factors Xa and IIa by binding to antithrombin, which ultimately leads to the inhibition of the clotting cascade. Heparin 67-74 serpin family C member 1 Homo sapiens 150-162 11465877-1 2001 UNLABELLED: Reviparin (reviparin sodium) is a low molecular weight heparin (LMWH) that catalyses the inactivation of factors Xa and IIa by binding to antithrombin, which ultimately leads to the inhibition of the clotting cascade. reviparin 12-21 serpin family C member 1 Homo sapiens 150-162 11465877-1 2001 UNLABELLED: Reviparin (reviparin sodium) is a low molecular weight heparin (LMWH) that catalyses the inactivation of factors Xa and IIa by binding to antithrombin, which ultimately leads to the inhibition of the clotting cascade. reviparin 23-39 serpin family C member 1 Homo sapiens 150-162 11465877-1 2001 UNLABELLED: Reviparin (reviparin sodium) is a low molecular weight heparin (LMWH) that catalyses the inactivation of factors Xa and IIa by binding to antithrombin, which ultimately leads to the inhibition of the clotting cascade. Heparin, Low-Molecular-Weight 76-80 serpin family C member 1 Homo sapiens 150-162 11853380-3 2001 The APTT was prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III. pu-hep 26-32 serpin family C member 1 Homo sapiens 83-99 11734954-1 2001 The aim of this study was to assess in vivo patency of seven commonly used non-ferromagnetic plain stents as regards demonstration of the contained lumen at 3D gadolinium-enhanced MRA in a 0.5-T MR environment. Gadolinium 160-170 serpin family C member 1 Homo sapiens 154-159 11853380-3 2001 The APTT was prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III. Heparin 72-79 serpin family C member 1 Homo sapiens 83-99 11099716-5 2000 Percent activity of AT-III was significantly decreased in CEI patients for 3 weeks compared to this activity in controls, LI and ATI (P<0.001). 4-Amino-2,2,5,5-tetramethyl-3-imidazoli-ne-1-yloxyl free radical 129-132 serpin family C member 1 Homo sapiens 20-26 11824259-3 2001 Administration of AT III in septic patients (KYBERSEPT) reduced the mortality rate solely in patients which were not treated with heparin. Heparin 130-137 serpin family C member 1 Homo sapiens 18-24 11154130-0 2000 Antithrombin niigata: a novel missense mutation (Thr194-Ile) of the antithrombin gene results in type I deficiency. niigata 13-20 serpin family C member 1 Homo sapiens 0-12 11150580-2 2000 Heparin is known to exert its antithrombotic effects by accelerating the effect of antithrombin (AT) and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation from vascular endothelium. Heparin 0-7 serpin family C member 1 Homo sapiens 83-95 11150584-0 2000 Rebound activation of coagulation after treatment with unfractionated heparin and not with low molecular weight heparin is associated with partial depletion of tissue factor pathway inhibitor and antithrombin. Heparin 70-77 serpin family C member 1 Homo sapiens 196-208 11154130-0 2000 Antithrombin niigata: a novel missense mutation (Thr194-Ile) of the antithrombin gene results in type I deficiency. niigata 13-20 serpin family C member 1 Homo sapiens 68-80 10973949-9 2000 Antithrombin binds to Xa-calcium with a approximately 4-fold faster rate, to sodium-Xa with a approximately 24-fold faster rate and to sodium-Xa-calcium with a approximately 28-fold faster rate. sodium-xa 77-86 serpin family C member 1 Homo sapiens 0-12 10973949-9 2000 Antithrombin binds to Xa-calcium with a approximately 4-fold faster rate, to sodium-Xa with a approximately 24-fold faster rate and to sodium-Xa-calcium with a approximately 28-fold faster rate. sodium-xa-calcium 135-152 serpin family C member 1 Homo sapiens 0-12 11006120-0 2000 Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III. Heparitin Sulfate 26-41 serpin family C member 1 Homo sapiens 85-101 11127851-3 2000 The treatment decision involves continuation or discontinuation of vitamin K antagonists in patients with a first spontaneous or secondary venous thromboembolism and an antithrombin, protein C or S deficiency. Vitamin K 67-76 serpin family C member 1 Homo sapiens 169-181 11009624-2 2000 Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa. Heparin 0-7 serpin family C member 1 Homo sapiens 49-61 11009624-2 2000 Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa. Heparin 146-153 serpin family C member 1 Homo sapiens 49-61 11009624-2 2000 Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa. Calcium 248-255 serpin family C member 1 Homo sapiens 49-61 11009624-2 2000 Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa. Calcium 270-277 serpin family C member 1 Homo sapiens 49-61 11009624-2 2000 Heparin catalyzes the inhibition of factor Xa by antithrombin mainly through an allosteric activation of the serpin inhibitor, but an alternative heparin bridging mechanism has been suggested to enhance the catalysis in the presence of physiologic calcium levels due to calcium interactions with the Gla domain exposing a heparin binding exosite in factor Xa. gamma-Linolenic Acid 300-303 serpin family C member 1 Homo sapiens 49-61 11009624-3 2000 To provide direct evidence for this bridging mechanism, we studied the heparin-catalyzed reaction of antithrombin with factor Xa, Gla-domainless factor Xa (GDFXa), and a heparin binding exosite mutant of GDFXa in the absence and presence of calcium using rapid kinetic methods. Heparin 71-78 serpin family C member 1 Homo sapiens 101-113 11009624-3 2000 To provide direct evidence for this bridging mechanism, we studied the heparin-catalyzed reaction of antithrombin with factor Xa, Gla-domainless factor Xa (GDFXa), and a heparin binding exosite mutant of GDFXa in the absence and presence of calcium using rapid kinetic methods. gdfxa 156-161 serpin family C member 1 Homo sapiens 101-113 11009624-3 2000 To provide direct evidence for this bridging mechanism, we studied the heparin-catalyzed reaction of antithrombin with factor Xa, Gla-domainless factor Xa (GDFXa), and a heparin binding exosite mutant of GDFXa in the absence and presence of calcium using rapid kinetic methods. Calcium 241-248 serpin family C member 1 Homo sapiens 101-113 11009624-4 2000 The pseudo-first-order rate constant for factor Xa inhibition by antithrombin complexed with a long-chain approximately 70-saccharide heparin showed a saturable dependence on inhibitor concentration in the presence but not in the absence of 2.5 mM Ca(2+), indicating the formation of an intermediate heparin-serpin-proteinase encounter complex with a dissociation constant of approximately 90 nM prior to formation of the stable serpin-proteinase complex with a rate constant of approximately 20 s(-1). Carbohydrates 123-133 serpin family C member 1 Homo sapiens 65-77 11009624-4 2000 The pseudo-first-order rate constant for factor Xa inhibition by antithrombin complexed with a long-chain approximately 70-saccharide heparin showed a saturable dependence on inhibitor concentration in the presence but not in the absence of 2.5 mM Ca(2+), indicating the formation of an intermediate heparin-serpin-proteinase encounter complex with a dissociation constant of approximately 90 nM prior to formation of the stable serpin-proteinase complex with a rate constant of approximately 20 s(-1). Heparin 134-141 serpin family C member 1 Homo sapiens 65-77 11009624-5 2000 Similar saturation kinetics were observed for the inhibition of GDFXa by the antithrombin-heparin complex, except that Ca(2+) was not required for the effect. gdfxa 64-69 serpin family C member 1 Homo sapiens 77-89 11009624-7 2000 These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism. Heparin 51-58 serpin family C member 1 Homo sapiens 232-244 11009624-7 2000 These findings suggest that binding of full-length heparin chains to an exosite of factor Xa in the presence of Ca(2+) produces a chain-length-dependent lowering of the dissociation constant for assembly of the intermediate heparin-antithrombin-factor Xa encounter complex, resulting in a several 100-fold rate enhancement by a heparin bridging mechanism. Heparin 224-231 serpin family C member 1 Homo sapiens 232-244 10906682-4 2000 To decrease their thrombogenicity, which remains the major obstacle, we have developed polymeric materials endowed with a specific affinity for antithrombin III (ATIII) and thus able, like heparin, to catalyze the inhibition of thrombin by ATIII. Heparin 189-196 serpin family C member 1 Homo sapiens 240-245 11124600-7 2000 Serum anti-Xa activity is better than activated partial thromboplastin time and antithrombin in assessing the optimal dose of LMWH. Heparin, Low-Molecular-Weight 126-130 serpin family C member 1 Homo sapiens 80-92 11065253-2 2000 In our previous study, the antithrombin drug argatroban t ameliorated the neurological exacerbations in a BD patient with antiphospholipid antibody syndrome. argatroban 45-55 serpin family C member 1 Homo sapiens 27-39 11131221-2 2000 Binding of AT-III to heparin dramatically increases its inhibitory effect. Heparin 21-28 serpin family C member 1 Homo sapiens 11-17 11131221-3 2000 AT-III deficiency during cardiopulmonary bypass (CPB) can lead to insufficient anticoagulation which cannot be treated by higher doses of heparin. Heparin 138-145 serpin family C member 1 Homo sapiens 0-6 11131221-8 2000 Heparinization was performed with 400 IU/kg of porcine mucosal heparin, increasing the activated coagulation time (ACT) from a baseline of 115 to 549 s. AT-III activity at that time was above 100% and the plasma D-dimer concentration was 230 ng/l. Heparin 63-70 serpin family C member 1 Homo sapiens 153-159 11131221-11 2000 Heparin was reversed with 3 mg/kg protamine chloride, decreasing the ACT to 155 s. In the intensive care unit (ICU), the patientreceived prophylactic Fraxiparine and 1500 IU AT-III, increasing the AT-III activity to 84%. Heparin 0-7 serpin family C member 1 Homo sapiens 174-180 11131221-11 2000 Heparin was reversed with 3 mg/kg protamine chloride, decreasing the ACT to 155 s. In the intensive care unit (ICU), the patientreceived prophylactic Fraxiparine and 1500 IU AT-III, increasing the AT-III activity to 84%. Heparin 0-7 serpin family C member 1 Homo sapiens 197-203 11131221-11 2000 Heparin was reversed with 3 mg/kg protamine chloride, decreasing the ACT to 155 s. In the intensive care unit (ICU), the patientreceived prophylactic Fraxiparine and 1500 IU AT-III, increasing the AT-III activity to 84%. Nadroparin 150-161 serpin family C member 1 Homo sapiens 197-203 11369259-2 2000 Binding of a full-length heparin chain to this site of factor Xa in the presence of calcium makes a significant contribution to acceleration of the proteinase inhibition by antithrombin through a ternary complex bridging or template mechanism. Heparin 25-32 serpin family C member 1 Homo sapiens 173-185 11369259-2 2000 Binding of a full-length heparin chain to this site of factor Xa in the presence of calcium makes a significant contribution to acceleration of the proteinase inhibition by antithrombin through a ternary complex bridging or template mechanism. Calcium 84-91 serpin family C member 1 Homo sapiens 173-185 11009624-0 2000 Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Calcium 0-7 serpin family C member 1 Homo sapiens 42-54 11009624-0 2000 Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Calcium 0-7 serpin family C member 1 Homo sapiens 127-139 11009624-0 2000 Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Heparin 17-24 serpin family C member 1 Homo sapiens 42-54 11009624-0 2000 Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by promoting the assembly of an intermediate heparin-antithrombin-factor Xa bridging complex. Heparin 17-24 serpin family C member 1 Homo sapiens 127-139 11006120-2 2000 Surface plasmon resonance spectroscopy showed a low affinity interaction with antithrombin III (ATIII) when it was flowed over a surface containing heparan sulfate. Heparitin Sulfate 148-163 serpin family C member 1 Homo sapiens 78-94 11006120-2 2000 Surface plasmon resonance spectroscopy showed a low affinity interaction with antithrombin III (ATIII) when it was flowed over a surface containing heparan sulfate. Heparitin Sulfate 148-163 serpin family C member 1 Homo sapiens 96-101 11006120-3 2000 ATIII bound tightly with high affinity when the same surface was enzymatically modified to using 3-O-sulfotransferase isoform 1 (3-OST-1) in the presence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS). Phosphoadenosine Phosphosulfate 157-194 serpin family C member 1 Homo sapiens 0-5 10974350-3 2000 The interaction of plasminogen was significantly (>90%) inhibited by lysine, indicating the involvement of kringles in binding antithrombin III. Lysine 72-78 serpin family C member 1 Homo sapiens 130-146 10974350-6 2000 Using carboxypeptidase B digestion, the plasminogen-binding site of antithrombin III was localized to the carboxy-terminus lysine of the anticoagulant protein. Lysine 123-129 serpin family C member 1 Homo sapiens 68-84 11006120-3 2000 ATIII bound tightly with high affinity when the same surface was enzymatically modified to using 3-O-sulfotransferase isoform 1 (3-OST-1) in the presence of 3"-phosphoadenosine 5"-phosphosulfate (PAPS). Phosphoadenosine Phosphosulfate 196-200 serpin family C member 1 Homo sapiens 0-5 10974350-7 2000 Tissue plasminogen activator also interacted with antithrombin III in a time- and concentration-dependent manner and its binding was also significantly (>90%) inhibited by lysine. Lysine 175-181 serpin family C member 1 Homo sapiens 50-66 11006120-4 2000 The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII. Heparitin Sulfate 34-49 serpin family C member 1 Homo sapiens 220-225 11006120-4 2000 The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII. 3-o-sulfo 89-98 serpin family C member 1 Homo sapiens 220-225 11006120-4 2000 The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII. Glycosaminoglycans 115-132 serpin family C member 1 Homo sapiens 220-225 11006120-4 2000 The 3-OST-1 enzyme is involved in heparan sulfate biosynthesis and introduces a critical 3-O-sulfo group into this glycosaminoglycan affording the appropriate pentasaccharide sequence capable of high affinity binding to ATIII. pentasaccharide 159-174 serpin family C member 1 Homo sapiens 220-225 10825225-5 2000 The adsorption of ATIII increased with increasing heparin on the surface. Heparin 50-57 serpin family C member 1 Homo sapiens 18-23 10984531-0 2000 Sequencing of 3-O sulfate containing heparin decasaccharides with a partial antithrombin III binding site. 3-o sulfate 14-25 serpin family C member 1 Homo sapiens 76-92 10984531-0 2000 Sequencing of 3-O sulfate containing heparin decasaccharides with a partial antithrombin III binding site. heparin decasaccharides 37-60 serpin family C member 1 Homo sapiens 76-92 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. IC 831423 29-52 serpin family C member 1 Homo sapiens 0-6 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. IC 831423 29-52 serpin family C member 1 Homo sapiens 161-167 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. 3-o sulfate 85-96 serpin family C member 1 Homo sapiens 0-6 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. 3-o sulfate 85-96 serpin family C member 1 Homo sapiens 161-167 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. 6-o 114-117 serpin family C member 1 Homo sapiens 0-6 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. 6-o 114-117 serpin family C member 1 Homo sapiens 161-167 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. Glucosamine 127-138 serpin family C member 1 Homo sapiens 0-6 10984531-3 2000 AT-III binding to a specific heparin pentasaccharide sequence, containing an unusual 3-O sulfate on a N-sulfated, 6-O sulfated glucosamine, increases 1,000-fold AT-III"s ability to inhibit specific proteases in the coagulation cascade. Glucosamine 127-138 serpin family C member 1 Homo sapiens 161-167 10966821-1 2000 The mechanism of activation of antithrombin by heparin. Heparin 47-54 serpin family C member 1 Homo sapiens 31-43 10966821-4 2000 Here we compare the structures of the circulating inactive form of antithrombin with the activated structure in complex with heparin pentasaccharide. IC 831423 125-148 serpin family C member 1 Homo sapiens 67-79 11016326-0 2000 A randomized trial of antithrombin concentrate for treatment of heparin resistance. Heparin 64-71 serpin family C member 1 Homo sapiens 22-34 11016326-6 2000 All patients who failed heparin therapy were successfully treated with AT. Heparin 24-31 serpin family C member 1 Homo sapiens 71-73 11776053-3 2000 The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system. Glycosaminoglycans 30-33 serpin family C member 1 Homo sapiens 4-16 11776053-3 2000 The antithrombin mechanism of GAG was checked by assaying its effects on the thrombin activity in normal human pooled plasma, purified human heparin cofactor II system and antithrombin III system. Glycosaminoglycans 30-33 serpin family C member 1 Homo sapiens 172-184 11776053-16 2000 GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin. Glycosaminoglycans 0-3 serpin family C member 1 Homo sapiens 83-95 11776053-16 2000 GAG was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin. Dermatan Sulfate 19-35 serpin family C member 1 Homo sapiens 83-95 11014724-5 2000 It remains to be seen whether the new antithrombin agents reduce the rate of periprocedural complications if used in combination with aspirin and new antiplatelet therapies. Aspirin 134-141 serpin family C member 1 Homo sapiens 38-50 10992803-8 2000 In the ArT patient group, there was 1 patient (5.88%) with AT III, 3 (17.64%) with PC deficiency, 1 (5.88%) with PS deficiency and no APC resistant patients, while there was one (2.08%) with PC deficiency and one (2.08%) with APC resistance in the control group (49 persons, mean age 41 years). art 7-10 serpin family C member 1 Homo sapiens 59-65 10913257-0 2000 The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139. Heparin 56-63 serpin family C member 1 Homo sapiens 14-26 10913257-0 2000 The region of antithrombin interacting with full-length heparin chains outside the high-affinity pentasaccharide sequence extends to Lys136 but not to Lys139. pentasaccharide 97-112 serpin family C member 1 Homo sapiens 14-26 10913257-1 2000 The interaction of a well-defined pentasaccharide sequence of heparin with a specific binding site on antithrombin activates the inhibitor through a conformational change. pentasaccharide 34-49 serpin family C member 1 Homo sapiens 102-114 10913257-1 2000 The interaction of a well-defined pentasaccharide sequence of heparin with a specific binding site on antithrombin activates the inhibitor through a conformational change. Heparin 62-69 serpin family C member 1 Homo sapiens 102-114 10913257-3 2000 An extended heparin binding site of antithrombin outside the specific pentasaccharide site has been proposed to account for the higher affinity of the inhibitor for full-length heparin chains by interacting with saccharides adjacent to the pentasaccharide sequence. pentasaccharide 70-85 serpin family C member 1 Homo sapiens 36-48 10913257-3 2000 An extended heparin binding site of antithrombin outside the specific pentasaccharide site has been proposed to account for the higher affinity of the inhibitor for full-length heparin chains by interacting with saccharides adjacent to the pentasaccharide sequence. Heparin 12-19 serpin family C member 1 Homo sapiens 36-48 10913257-3 2000 An extended heparin binding site of antithrombin outside the specific pentasaccharide site has been proposed to account for the higher affinity of the inhibitor for full-length heparin chains by interacting with saccharides adjacent to the pentasaccharide sequence. pentasaccharide 240-255 serpin family C member 1 Homo sapiens 36-48 10913257-10 2000 Together, these results show that Lys136 forms part of the extended heparin binding site of antithrombin that participates in the binding of full-length heparin chains, whereas Lys139 is located outside this site. Heparin 68-75 serpin family C member 1 Homo sapiens 92-104 10913257-10 2000 Together, these results show that Lys136 forms part of the extended heparin binding site of antithrombin that participates in the binding of full-length heparin chains, whereas Lys139 is located outside this site. Heparin 153-160 serpin family C member 1 Homo sapiens 92-104 10809774-4 2000 We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region. Fluorescein 86-97 serpin family C member 1 Homo sapiens 52-64 10809774-4 2000 We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region. Fluorescein 103-114 serpin family C member 1 Homo sapiens 52-64 10809774-4 2000 We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region. Heparin 183-190 serpin family C member 1 Homo sapiens 52-64 10809774-4 2000 We determined the crystal structure of an activated antithrombin variant, N135Q S380C-fluorescein (P14-fluorescein), in order to see how full activation is achieved in the absence of heparin and how the structural effects of the substitution in the hinge region are translated to the heparin binding region. Heparin 284-291 serpin family C member 1 Homo sapiens 52-64 10809774-5 2000 The crystal structure resembles native antithrombin except in the hinge and heparin binding regions. Heparin 76-83 serpin family C member 1 Homo sapiens 39-51 10822073-11 2000 While neither drug had any effect on the percutaneous transluminal coronary angioplasty-induced inflammatory response, argatroban may more effectively inhibit the generated thrombin and prevent antithrombin consumption during and after percutaneous transluminal coronary angioplasty. argatroban 119-129 serpin family C member 1 Homo sapiens 194-206 10824912-2 2000 Partial thrombotic obstruction of the pulmonary trunk secondary to Antithrombin III (homozygous defect of heparin binding site) deficiency was subsequently diagnosed. Heparin 106-113 serpin family C member 1 Homo sapiens 67-83 10850803-7 2000 Substitutions of the lysine at equivalent positions in two other inhibitory serpins, human alpha1-antichymotrypsin and human antithrombin III, also increased stability and decreased inhibitory activity toward alpha-chymotrypsin and thrombin, respectively. Lysine 21-27 serpin family C member 1 Homo sapiens 125-141 10715105-3 2000 The mutation was selective as demonstrated by normal activation and inhibition, except in the presence of subsaturating heparin where the rate of inhibition by antithrombin III (ATIII) was 15% of normal. Heparin 120-127 serpin family C member 1 Homo sapiens 160-176 10715105-3 2000 The mutation was selective as demonstrated by normal activation and inhibition, except in the presence of subsaturating heparin where the rate of inhibition by antithrombin III (ATIII) was 15% of normal. Heparin 120-127 serpin family C member 1 Homo sapiens 178-183 10898273-7 2000 These data suggest that (a) in patients with diabetes, antiplatelet therapy with sarpogrelate hydrochloride is a useful antithrombin therapy because it suppresses the production of intrinsic coagulants by activated platelets; and (b) sarpogrelate hydrochloride decreases endothelial cell damage via adhesion molecules. sarpogrelate hydrochloride 81-107 serpin family C member 1 Homo sapiens 120-132 10898281-3 2000 A continuous infusion of antithrombin concentrate was used successfully, following failure of plasma, to correct the heparin resistance. Heparin 117-124 serpin family C member 1 Homo sapiens 25-37 10898281-7 2000 This antithrombin variant has been previously reported (antithrombin Budapest 3) and results in reduced binding of heparin to antithrombin. Heparin 115-122 serpin family C member 1 Homo sapiens 5-17 10898281-7 2000 This antithrombin variant has been previously reported (antithrombin Budapest 3) and results in reduced binding of heparin to antithrombin. Heparin 115-122 serpin family C member 1 Homo sapiens 56-68 10898281-7 2000 This antithrombin variant has been previously reported (antithrombin Budapest 3) and results in reduced binding of heparin to antithrombin. Heparin 115-122 serpin family C member 1 Homo sapiens 56-68 10899490-9 2000 Tibolone showed a stronger reduction of factor VII activity; less reduction of AT-III, protein C activity, and protein S activity; stronger increase of the activated partial thromboplastin time, plasminogen and plasminogen-antiplasminogen complexes; and less increase of D-Dimer than ccHRT. tibolone 0-8 serpin family C member 1 Homo sapiens 79-85 11060763-6 2000 There are two general classes of FXa inhibitors in development, of which SR90107A/ORG31540, an antithrombin-III-dependent pentasaccharide and DX-9065a, a small molecule direct FXa inhibitor, have published clinical data. PENTA 73-81 serpin family C member 1 Homo sapiens 95-111 11060763-6 2000 There are two general classes of FXa inhibitors in development, of which SR90107A/ORG31540, an antithrombin-III-dependent pentasaccharide and DX-9065a, a small molecule direct FXa inhibitor, have published clinical data. pentasaccharide 122-137 serpin family C member 1 Homo sapiens 95-111 10764763-0 2000 Role of arginine 129 in heparin binding and activation of antithrombin. Arginine 8-16 serpin family C member 1 Homo sapiens 58-70 10764763-1 2000 The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln. Arginine 20-23 serpin family C member 1 Homo sapiens 44-56 10764763-1 2000 The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln. Heparin 118-125 serpin family C member 1 Homo sapiens 44-56 10764763-1 2000 The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln. Histidine 192-195 serpin family C member 1 Homo sapiens 44-56 10764763-1 2000 The contribution of Arg(129) of the serpin, antithrombin, to the mechanism of allosteric activation of the protein by heparin was determined from the effect of mutating this residue to either His or Gln. Glutamine 199-202 serpin family C member 1 Homo sapiens 44-56 10764763-2 2000 R129H and R129Q antithrombins bound pentasaccharide and full-length heparins containing the antithrombin recognition sequence with similar large reductions in affinity ranging from 400- to 2500-fold relative to the control serpin, corresponding to a loss of 28-35% of the binding free energy. pentasaccharide 36-51 serpin family C member 1 Homo sapiens 16-28 10764763-2 2000 R129H and R129Q antithrombins bound pentasaccharide and full-length heparins containing the antithrombin recognition sequence with similar large reductions in affinity ranging from 400- to 2500-fold relative to the control serpin, corresponding to a loss of 28-35% of the binding free energy. Heparin 68-76 serpin family C member 1 Homo sapiens 16-28 10764763-4 2000 Rapid kinetic studies showed that the mutation minimally affected the initial low affinity binding of heparin to antithrombin, but greatly affected the subsequent conformational activation of the serpin leading to high affinity heparin binding, although not enough to disfavor activation. Heparin 102-109 serpin family C member 1 Homo sapiens 113-125 10764763-4 2000 Rapid kinetic studies showed that the mutation minimally affected the initial low affinity binding of heparin to antithrombin, but greatly affected the subsequent conformational activation of the serpin leading to high affinity heparin binding, although not enough to disfavor activation. Heparin 228-235 serpin family C member 1 Homo sapiens 113-125 10764763-5 2000 Consistent with these findings, the mutant antithrombin was normally activated by heparin for accelerated inhibition of factor Xa and thrombin. Heparin 82-89 serpin family C member 1 Homo sapiens 43-55 10764763-6 2000 These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state. Arginine 44-47 serpin family C member 1 Homo sapiens 106-118 10764763-6 2000 These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state. Heparin 84-91 serpin family C member 1 Homo sapiens 106-118 10764763-6 2000 These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state. Arginine 177-180 serpin family C member 1 Homo sapiens 106-118 10764763-6 2000 These results support an important role for Arg(129) in an induced-fit mechanism of heparin activation of antithrombin wherein conformational activation of the serpin positions Arg(129) and other residues for cooperative interactions with the heparin pentasaccharide so as to lock the serpin in the activated state. IC 831423 243-266 serpin family C member 1 Homo sapiens 106-118 10872794-7 2000 Based on its known anticoagulative function in endothelial cells and effects on the production of prostacyclin, it is reasonable to speculate that antithrombin III present in aqueous humor might influence the physiology of the trabecular and uveoscleral meshwork and thereby regulate intraocular pressure. Epoprostenol 98-110 serpin family C member 1 Homo sapiens 147-163 10781455-0 2000 The in vitro effects of antithrombin III on the activated coagulation time in patients on heparin therapy. Heparin 90-97 serpin family C member 1 Homo sapiens 24-40 10781455-1 2000 UNLABELLED: Heparin requires antithrombin III (AT) to achieve anticoagulation, and patients on continuous small-dose heparin preoperatively experience decreased levels of AT-causing heparin resistance. Heparin 12-19 serpin family C member 1 Homo sapiens 29-45 10781455-11 2000 IMPLICATIONS: In vitro addition of antithrombin III (0.2 U/mL) to heparinized blood samples (4.1-6.8 units of heparin/mL) from patients on previous heparin therapy increases sensitivity to supplemental heparin as reflected by significantly prolonged activated clotting time. Heparin 66-73 serpin family C member 1 Homo sapiens 35-51 10781455-11 2000 IMPLICATIONS: In vitro addition of antithrombin III (0.2 U/mL) to heparinized blood samples (4.1-6.8 units of heparin/mL) from patients on previous heparin therapy increases sensitivity to supplemental heparin as reflected by significantly prolonged activated clotting time. Heparin 110-117 serpin family C member 1 Homo sapiens 35-51 10781455-11 2000 IMPLICATIONS: In vitro addition of antithrombin III (0.2 U/mL) to heparinized blood samples (4.1-6.8 units of heparin/mL) from patients on previous heparin therapy increases sensitivity to supplemental heparin as reflected by significantly prolonged activated clotting time. Heparin 110-117 serpin family C member 1 Homo sapiens 35-51 10904927-4 2000 This process also occurs in other members of the serine proteinase inhibitor (serpin) superfamily, antithrombin, C1-inhibitor and alpha 1-antichymotrypsin, in association with thrombosis, angioedema and chronic obstructive pulmonary disease, respectively, and we have recently shown that it underlies a novel inclusion body dementia. Serine 49-55 serpin family C member 1 Homo sapiens 99-111 10766996-4 2000 The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N). Glycosaminoglycans 126-129 serpin family C member 1 Homo sapiens 62-65 10766996-4 2000 The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N). Glutamic Acid 134-137 serpin family C member 1 Homo sapiens 62-65 10766996-4 2000 The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N). Lysine 234-237 serpin family C member 1 Homo sapiens 62-65 10766996-4 2000 The DNA sequencing demonstrated novel mutations in exon 3A of AT3: a G to T substitution at nucleotide position 5333 in codon GAG for Glu 113, causing a stop codon (E113X), and an A to T substitution at position 5338 in codon AAA for Lys 114, forming Asn (K114N). Asparagine 251-254 serpin family C member 1 Homo sapiens 62-65 10810875-4 2000 Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes. Epoprostenol 24-36 serpin family C member 1 Homo sapiens 0-12 10810875-4 2000 Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes. Heparitin Sulfate 91-106 serpin family C member 1 Homo sapiens 0-12 10810875-4 2000 Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes. Epoprostenol 142-154 serpin family C member 1 Homo sapiens 0-12 10722716-0 2000 The effect of a reducing-end extension on pentasaccharide binding by antithrombin. pentasaccharide 42-57 serpin family C member 1 Homo sapiens 69-81 10722716-1 2000 Antithrombin requires heparin for efficient inhibition of the final two proteinases of the blood coagulation cascade, factor Xa and thrombin. Heparin 22-29 serpin family C member 1 Homo sapiens 0-12 10722716-2 2000 Antithrombin binds heparin via a specific pentasaccharide domain in a two-step mechanism whereby initial weak binding is followed by a conformational change and subsequent tight binding. Heparin 19-26 serpin family C member 1 Homo sapiens 0-12 10722716-2 2000 Antithrombin binds heparin via a specific pentasaccharide domain in a two-step mechanism whereby initial weak binding is followed by a conformational change and subsequent tight binding. pentasaccharide 42-57 serpin family C member 1 Homo sapiens 0-12 10722716-7 2000 This conclusion supports the likely presence of a range of sequences that can bind to and activate antithrombin in the natural heparan sulfates that line the vascular endothelium. Heparitin Sulfate 127-143 serpin family C member 1 Homo sapiens 99-111 10712595-0 2000 Salmon antithrombin has only three carbohydrate side chains, and shows functional similarities to human beta-antithrombin. Carbohydrates 35-47 serpin family C member 1 Homo sapiens 7-19 10759005-8 2000 The thrombin-based assays also overestimated antithrombin activity in patients under high-dose heparin. Heparin 95-102 serpin family C member 1 Homo sapiens 45-57 10712595-3 2000 Due to a single nucleotide replacement, Asn135 of the antithrombin in higher vertebrates is substituted by Asp in the salmon homolog. Aspartic Acid 107-110 serpin family C member 1 Homo sapiens 54-66 10712595-5 2000 The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135. Nitrogen 28-29 serpin family C member 1 Homo sapiens 129-141 10712595-5 2000 The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135. Nitrogen 28-29 serpin family C member 1 Homo sapiens 357-369 10712595-5 2000 The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135. Carbohydrates 97-109 serpin family C member 1 Homo sapiens 129-141 10712595-5 2000 The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135. Heparin 196-203 serpin family C member 1 Homo sapiens 129-141 10712595-5 2000 The existence of only three N-linked side chains is evidenced by the sequential removal of three carbohydrate chains from salmon antithrombin during timed-digestion with N-glycosidase F. The high heparin binding affinity of the salmon inhibitor, Kd of 2.2 and 48 nM at I = 0.15 and 0.3, respectively, is very similar to that of the minor human isoform beta-antithrombin, which is not glycosylated at Asn135. Heparin 196-203 serpin family C member 1 Homo sapiens 357-369 10712595-6 2000 Furthermore, the invariant third-position Ser137 at this glycosylation site of mammalian and chicken antithrombins is substituted by Thr in the salmon, a replacement that has been shown to induce full glycosylation in human antithrombin. Threonine 133-136 serpin family C member 1 Homo sapiens 101-113 10712595-8 2000 Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid. Oligosaccharides 50-65 serpin family C member 1 Homo sapiens 7-19 10712595-8 2000 Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid. N-Acetylneuraminic Acid 89-100 serpin family C member 1 Homo sapiens 7-19 10712595-8 2000 Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid. Galactose 133-142 serpin family C member 1 Homo sapiens 7-19 10712595-8 2000 Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 179-185 serpin family C member 1 Homo sapiens 7-19 10712595-8 2000 Salmon antithrombin appears to have three complex oligosaccharide side chains containing sialic acid terminally linked alpha(2-3) to galactose, while trace amounts of Galbeta(1-4)GlcNAc suggest microheterogeneity due to partial loss of sialic acid. N-Acetylneuraminic Acid 236-247 serpin family C member 1 Homo sapiens 7-19 10709911-5 2000 Unlike heparin-induced stimulation of antithrombin-thrombin interaction, the heparin-induced stimulation of tissue plasminogen activator did not seem to follow a template model. Heparin 7-14 serpin family C member 1 Homo sapiens 38-50 10660568-0 2000 Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa. Serine 0-6 serpin family C member 1 Homo sapiens 53-65 10660541-0 2000 The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III. Aspartic Acid 4-7 serpin family C member 1 Homo sapiens 185-201 10660568-0 2000 Serine 380 (P14) --> glutamate mutation activates antithrombin as an inhibitor of factor Xa. Glutamic Acid 24-33 serpin family C member 1 Homo sapiens 53-65 10660541-0 2000 The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III. Glutamic Acid 13-16 serpin family C member 1 Homo sapiens 185-201 10660541-0 2000 The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III. Heparin 81-88 serpin family C member 1 Homo sapiens 185-201 10660568-1 2000 Heparin regulates the inhibitory activity of antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 45-57 10660541-0 2000 The Asp(272)-Glu(282) region of platelet glycoprotein Ibalpha interacts with the heparin-binding site of alpha-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III. Heparin 153-160 serpin family C member 1 Homo sapiens 185-201 10660568-2 2000 It has been proposed that residues P15 and P14 are expelled from beta-sheet A of antithrombin by heparin binding, permitting better interaction of the reactive center loop with factor Xa. Heparin 97-104 serpin family C member 1 Homo sapiens 81-93 10660568-4 2000 There is minimal further increase in antithrombin fluorescence upon heparin binding. Heparin 68-75 serpin family C member 1 Homo sapiens 37-49 10660568-7 2000 This is comparable to that of antithrombin activated by high affinity heparin pentasaccharide. IC 831423 70-93 serpin family C member 1 Homo sapiens 30-42 10652320-1 2000 We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site. Heparin 91-98 serpin family C member 1 Homo sapiens 146-158 10652320-1 2000 We recently demonstrated that a template mechanism makes a significant contribution to the heparin-accelerated inactivation of factor Xa (FXa) by antithrombin at physiologic Ca(2+), suggesting that FXa has a potential heparin-binding site. Heparin 218-225 serpin family C member 1 Homo sapiens 146-158 10652320-5 2000 Antithrombin inactivated FXa derivatives with a similar second-order association rate constant (k(2)) in both the absence and presence of pentasaccharide. pentasaccharide 138-153 serpin family C member 1 Homo sapiens 0-12 10644732-0 2000 Critical role of the linker region between helix D and strand 2A in heparin activation of antithrombin. Heparin 68-75 serpin family C member 1 Homo sapiens 90-102 11096650-7 2000 On the other hand, available data suggest that serious bleeding should not be problematic despite difficulties measuring that antithrombin effect among patients receiving LMWH, even when it is combined with potent platelet inhibitor therapy. Heparin, Low-Molecular-Weight 171-175 serpin family C member 1 Homo sapiens 126-138 10644732-1 2000 The binding of pentasaccharide heparin to antithrombin induces a conformational change that is transmitted to the reactive center loop and increases the rate of inhibition of factor Xa by approximately 300-fold. pentasaccharide heparin 15-38 serpin family C member 1 Homo sapiens 42-54 10632394-7 2000 In the experiment with plasma proteins, the PRT and APTT were significantly prolonged for both the heparin-immobilized PET (PET-He) and the PET-I-H, suggesting the binding of immobilized heparin to antithrombin III. Heparin 99-106 serpin family C member 1 Homo sapiens 198-214 10632394-7 2000 In the experiment with plasma proteins, the PRT and APTT were significantly prolonged for both the heparin-immobilized PET (PET-He) and the PET-I-H, suggesting the binding of immobilized heparin to antithrombin III. Heparin 187-194 serpin family C member 1 Homo sapiens 198-214 11011802-21 2000 The FDA has approved a recombinant hirudin (Refludan) and a synthetic antithrombin agent, argatroban (Novastan), for this indication. argatroban 90-100 serpin family C member 1 Homo sapiens 70-82 10736978-10 2000 ), of the reduced stay in the Intensive Care Unit, of the riduced risk involved with problems of bleeding and the need of repeated operative procedures make this method fundamental in patients with reduced plasma levels of ATIII such as coronary patients who are under heparin treatment for several days. Heparin 269-276 serpin family C member 1 Homo sapiens 223-228 10617008-1 1999 BACKGROUND: To evaluate the effectiveness of intraoperative administration of antithrombin III (AT III) to improve anticoagulation and preserve the hemostatic mechanisms during cardiopulmonary bypass (CPB) in patients with unstable angina under heparin treatment. Heparin 245-252 serpin family C member 1 Homo sapiens 78-94 10574918-10 1999 We generated a carboxyl-terminal histidine-tagged recombinant antithrombin III to study the tag on another serpin. Histidine 33-42 serpin family C member 1 Homo sapiens 62-78 10577463-2 1999 Antithrombin therapy with unfractionated heparin has several important disadvantages, such as a variable anticoagulant effect, sensitivity to platelet factor 4, an inability to inhibit clot-bound thrombin, and the potential to cause thrombocytopenia. Heparin 41-48 serpin family C member 1 Homo sapiens 0-12 10611948-6 1999 Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities. Heparin 65-72 serpin family C member 1 Homo sapiens 33-38 10611948-6 1999 Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities. Heparin 65-72 serpin family C member 1 Homo sapiens 84-89 10611948-6 1999 Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities. Heparin 129-136 serpin family C member 1 Homo sapiens 33-38 10611948-6 1999 Crossed immunoelectrophoresis of ATIII, performed in presence of heparin, evidenced ATIII forms with reduced binding capacity to heparin and TAT complexes of various electrophoretic mobilities. Heparin 129-136 serpin family C member 1 Homo sapiens 84-89 10617008-1 1999 BACKGROUND: To evaluate the effectiveness of intraoperative administration of antithrombin III (AT III) to improve anticoagulation and preserve the hemostatic mechanisms during cardiopulmonary bypass (CPB) in patients with unstable angina under heparin treatment. Heparin 245-252 serpin family C member 1 Homo sapiens 96-102 10726029-9 1999 This was soon followed by experiments with antithrombin drugs such as hirudin and argatroban as replacements for heparin in the HIT-HITT syndrome. argatroban 82-92 serpin family C member 1 Homo sapiens 43-55 10636462-3 1999 The efficacy of UTM on thromboplastin-induced disseminated intravascular coagulation produced in ATIII-decreased rats was almost the same as that in normal rats, whereas unfractionated (UF)-heparin remarkably diminished its effect in ATIII-decreased rats. Heparin 190-197 serpin family C member 1 Homo sapiens 234-239 10569284-7 1999 These values are lower than those reported for low-molecular-weight heparins and are consistent with the requirement of an antithrombin III pentasaccharide binding site for anti-factor Xa activity. pentasaccharide 140-155 serpin family C member 1 Homo sapiens 123-139 11212344-8 1999 Heparan sulfate thus binds and regulates the activity of growth factors, cytokines, superoxide dismutase and antithrombin, which contribute to aberrant cell proliferation, migration and matrix production, scavenging of reactive oxygen radicals and thrombosis. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 109-121 11212344-8 1999 Heparan sulfate thus binds and regulates the activity of growth factors, cytokines, superoxide dismutase and antithrombin, which contribute to aberrant cell proliferation, migration and matrix production, scavenging of reactive oxygen radicals and thrombosis. reactive oxygen radicals 219-243 serpin family C member 1 Homo sapiens 109-121 11094330-4 1999 The anticoagulant activity of this polysaccharide is mediated by both antithrombin and heparin cofactor II; it has antithrombotic activity when targeted at the intrinsic coagulation pathway. Polysaccharides 35-49 serpin family C member 1 Homo sapiens 70-82 10502216-3 1999 Efegatran is a new direct antithrombin, which in experimental animals has been shown to enhance thrombolysis, reduce rate of reocclusion, and limit infarct size. efegatran 0-9 serpin family C member 1 Homo sapiens 26-38 10607857-8 1999 The biological potencies of these compounds were assessed in ex vivo experiments where their ability to compete with antithrombin for binding heparin was determined. Heparin 142-149 serpin family C member 1 Homo sapiens 117-129 10844407-5 1999 Serum 17beta-oestradiol exhibited a direct correlation with endogenous thrombin potential extrinsic pathway (R = 0.42, p = 0.01) and prothrombin fragments 1 and 2 (R = 0.37, p = 0.03) and an inverse correlation with antithrombin III (R = -0.36, p = 0.03) and alpha(2)-antiplasmin (R = -0.45, p = 0.005). Estradiol 6-23 serpin family C member 1 Homo sapiens 216-232 10585151-6 1999 Heparin resistance was defined as at least one activated clotting time < 400 s after heparinization and/or the need for purified antithrombin III (AT-III) administration. Heparin 0-7 serpin family C member 1 Homo sapiens 132-148 10585151-6 1999 Heparin resistance was defined as at least one activated clotting time < 400 s after heparinization and/or the need for purified antithrombin III (AT-III) administration. Heparin 0-7 serpin family C member 1 Homo sapiens 150-156 10726029-9 1999 This was soon followed by experiments with antithrombin drugs such as hirudin and argatroban as replacements for heparin in the HIT-HITT syndrome. Heparin 113-120 serpin family C member 1 Homo sapiens 43-55 10726036-4 1999 Argatroban represents the first clinically approved antithrombin agent, which was made available in Japan several years ago. argatroban 0-10 serpin family C member 1 Homo sapiens 52-64 10497166-4 1999 Surprisingly, the enhanced thrombin specificity of the mutant antithrombin was attenuated when a full-length bridging heparin was the activator, due both to a reduced rate of covalent reaction of the mutant serpin and thrombin and preferred reaction of the mutant serpin as a substrate. Heparin 118-125 serpin family C member 1 Homo sapiens 62-74 10596996-8 1999 RESULTS: In the Hepcon group, the sensitivity to heparin was correlated with coagulation time (r = -0.78) and antithrombin III levels (r = 0.70), and individual difference of sensitivity resulted in a wide range of dosage (160 to 490 IU/kg). Heparin 49-56 serpin family C member 1 Homo sapiens 110-126 10497166-0 1999 Importance of the P2 glycine of antithrombin in target proteinase specificity, heparin activation, and the efficiency of proteinase trapping as revealed by a P2 Gly --> Pro mutation. Glycine 21-28 serpin family C member 1 Homo sapiens 32-44 10497166-5 1999 These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex. Glycine 197-200 serpin family C member 1 Homo sapiens 120-132 10497166-0 1999 Importance of the P2 glycine of antithrombin in target proteinase specificity, heparin activation, and the efficiency of proteinase trapping as revealed by a P2 Gly --> Pro mutation. Heparin 79-86 serpin family C member 1 Homo sapiens 32-44 10497166-5 1999 These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex. Glycine 197-200 serpin family C member 1 Homo sapiens 241-253 10497166-0 1999 Importance of the P2 glycine of antithrombin in target proteinase specificity, heparin activation, and the efficiency of proteinase trapping as revealed by a P2 Gly --> Pro mutation. Glycine 161-164 serpin family C member 1 Homo sapiens 32-44 10497166-5 1999 These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex. Glycine 197-200 serpin family C member 1 Homo sapiens 241-253 10497166-1 1999 A sequence-specific heparin pentasaccharide activates the serpin, antithrombin, to inhibit factor Xa through an allosteric mechanism, whereas full-length heparin chains containing this sequence further activate the serpin to inhibit thrombin by an alternative bridging mechanism. IC 831423 20-43 serpin family C member 1 Homo sapiens 66-78 10497166-5 1999 These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex. Heparin 282-289 serpin family C member 1 Homo sapiens 120-132 10497166-1 1999 A sequence-specific heparin pentasaccharide activates the serpin, antithrombin, to inhibit factor Xa through an allosteric mechanism, whereas full-length heparin chains containing this sequence further activate the serpin to inhibit thrombin by an alternative bridging mechanism. Heparin 20-27 serpin family C member 1 Homo sapiens 66-78 10497166-2 1999 To test whether the factor Xa specificity of allosterically activated antithrombin is encoded in the serpin reactive center loop, we mutated the factor Xa-preferred P2 Gly to the thrombin-preferred P2 Pro. Glycine 168-171 serpin family C member 1 Homo sapiens 70-82 10497166-3 1999 Kinetic studies revealed that the mutation maximally enhanced the reactivity of antithrombin with thrombin 15-fold and decreased its reactivity toward factor Xa 2-fold when the serpin was activated by heparin pentasaccharide, thereby transforming antithrombin into an allosterically activated inhibitor of both factor Xa and thrombin. IC 831423 201-224 serpin family C member 1 Homo sapiens 80-92 10497166-3 1999 Kinetic studies revealed that the mutation maximally enhanced the reactivity of antithrombin with thrombin 15-fold and decreased its reactivity toward factor Xa 2-fold when the serpin was activated by heparin pentasaccharide, thereby transforming antithrombin into an allosterically activated inhibitor of both factor Xa and thrombin. IC 831423 201-224 serpin family C member 1 Homo sapiens 247-259 10497166-5 1999 These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex. Heparin 282-289 serpin family C member 1 Homo sapiens 241-253 10497166-5 1999 These results demonstrate that the reactive center loop sequence determines the specificity of allosterically activated antithrombin for factor Xa and that the conformational flexibility of the P2 Gly may be critical for optimal bridging of antithrombin and thrombin by physiologic heparin and for preventing antithrombin from reacting as a substrate in the bridging complex. Heparin 282-289 serpin family C member 1 Homo sapiens 241-253 10656170-10 1999 Small fibrinogen (t0, t2, t6, t8), PAI-1 (t6) and AT III (t0-t8) increases were observed after gemfibrozil, while simvastatin did not significantly modify these parameters. Gemfibrozil 95-106 serpin family C member 1 Homo sapiens 50-56 10980840-2 1999 Heparin has limitations as an antithrombin agent, which has led to clinical investigation of alternative agents. Heparin 0-7 serpin family C member 1 Homo sapiens 30-42 10467078-4 1999 However, local delivery of heparin further increased coronary sinus ATIII activity (P = 0.003, period III vs. period IV). Heparin 27-34 serpin family C member 1 Homo sapiens 68-73 10468144-4 1999 Recent data are reviewed here from clinical trials supporting the use of the specific antithrombin agents in the treatment of acute cardiac ischemic syndromes, the prevention and treatment of venous thromboembolism, and the management of heparin-induced thrombocytopenia. Heparin 238-245 serpin family C member 1 Homo sapiens 86-98 10530936-3 1999 Conjugates VI and VIII show a remarkable increase in antithrombin activity compared to the structurally related conjugates with persulfated TBDs (i.e. compounds IV and V), whereas compound VII displays a diminished activity. H-D-Ser(tBu)-OH 140-144 serpin family C member 1 Homo sapiens 53-65 10688418-0 1999 Clinical laboratory monitoring of a synthetic antithrombin agent, argatroban, using high performance liquid chromatography and functional methods. argatroban 66-76 serpin family C member 1 Homo sapiens 46-58 10433728-1 1999 Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 49-61 10499652-0 1999 Gabexate mesilate and antithrombin III for intraoperative anticoagulation in heparin pretreated patients. Heparin 77-84 serpin family C member 1 Homo sapiens 22-38 10499652-7 1999 The total heparin dosage was less in group GA than in groups A and C. Purified AT-III administration is recommended in heparin pretreated patients; the addition of gabexate mesilate to this protocol decreases the heparin requirement and increases the AT-III preservation. Gabexate 164-181 serpin family C member 1 Homo sapiens 251-257 10441134-0 1999 Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin. Disulfides 8-17 serpin family C member 1 Homo sapiens 111-123 10460149-11 1999 In contrast, VIIaQ217A association with antithrombin III in the presence of heparin was the fastest among the variants with a second-order rate constant of 2.31 (x10(3) M(-)(1) min(-)(1)), as compared to 0.47 and 1.47 for VIIaQ217E and wild-type VIIa, respectively. Heparin 76-83 serpin family C member 1 Homo sapiens 40-56 10433728-1 1999 Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 185-197 10433728-1 1999 Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin. pentasaccharide 138-153 serpin family C member 1 Homo sapiens 49-61 10433728-1 1999 Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin. pentasaccharide 138-153 serpin family C member 1 Homo sapiens 185-197 10433728-1 1999 Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin. Heparin 166-173 serpin family C member 1 Homo sapiens 49-61 10433728-1 1999 Heparin greatly accelerates the reaction between antithrombin and its target proteinases, thrombin and factor Xa, by virtue of a specific pentasaccharide sequence of heparin binding to antithrombin. Heparin 166-173 serpin family C member 1 Homo sapiens 185-197 10433728-2 1999 The binding occurs in two steps, an initial weak interaction inducing a conformational change of antithrombin that increases the affinity for heparin and activates the inhibitor. Heparin 142-149 serpin family C member 1 Homo sapiens 97-109 10433728-3 1999 Arg46 and Arg47 of antithrombin have been implicated in heparin binding by studies of natural and recombinant variants and by the crystal structure of a pentasaccharide-antithrombin complex. Heparin 56-63 serpin family C member 1 Homo sapiens 19-31 10433728-3 1999 Arg46 and Arg47 of antithrombin have been implicated in heparin binding by studies of natural and recombinant variants and by the crystal structure of a pentasaccharide-antithrombin complex. Heparin 56-63 serpin family C member 1 Homo sapiens 169-181 10433728-3 1999 Arg46 and Arg47 of antithrombin have been implicated in heparin binding by studies of natural and recombinant variants and by the crystal structure of a pentasaccharide-antithrombin complex. pentasaccharide 153-168 serpin family C member 1 Homo sapiens 19-31 10433728-3 1999 Arg46 and Arg47 of antithrombin have been implicated in heparin binding by studies of natural and recombinant variants and by the crystal structure of a pentasaccharide-antithrombin complex. pentasaccharide 153-168 serpin family C member 1 Homo sapiens 169-181 10433728-10 1999 These results are in agreement with a previously proposed model, in which an initial low-affinity binding of the nonreducing-end trisaccharide of the heparin pentasaccharide induces the antithrombin conformational change. Trisaccharides 129-142 serpin family C member 1 Homo sapiens 186-198 10433728-10 1999 These results are in agreement with a previously proposed model, in which an initial low-affinity binding of the nonreducing-end trisaccharide of the heparin pentasaccharide induces the antithrombin conformational change. IC 831423 150-173 serpin family C member 1 Homo sapiens 186-198 10554832-1 1999 Based on heparin"s antithrombin and anti-FXa activity and its in vitro inhibition of activated factor VII (FVIIa) activity, we hypothesized that unfractionated heparin (UFH) may decrease plasma levels of FVIIa in humans. Heparin 9-16 serpin family C member 1 Homo sapiens 19-31 10466207-1 1999 Three hexasaccharides, having from low to very high affinity for antithrombin, were synthesised from disaccharide building block precursors. hexasaccharides 6-21 serpin family C member 1 Homo sapiens 65-77 10348900-4 1999 [3H]Heparin labeled with this reagent crosslinked to antithrombin III very specifically but not to ovalbumin, as analyzed by the Bio-imaging Analyzer System (BAS, Fuji Photo Film, Tokyo). Tritium 1-3 serpin family C member 1 Homo sapiens 53-69 10427858-1 1999 In the early eighties, following breakthroughs in oligosaccharide chemistry, the total chemical synthesis of pentasaccharides has been achieved, representing the antithrombin binding domain of heparin (the active site). Oligosaccharides 50-65 serpin family C member 1 Homo sapiens 162-174 10427858-1 1999 In the early eighties, following breakthroughs in oligosaccharide chemistry, the total chemical synthesis of pentasaccharides has been achieved, representing the antithrombin binding domain of heparin (the active site). pentasaccharides 109-125 serpin family C member 1 Homo sapiens 162-174 10427858-1 1999 In the early eighties, following breakthroughs in oligosaccharide chemistry, the total chemical synthesis of pentasaccharides has been achieved, representing the antithrombin binding domain of heparin (the active site). Heparin 193-200 serpin family C member 1 Homo sapiens 162-174 10427858-3 1999 In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group. Heparin 89-96 serpin family C member 1 Homo sapiens 62-74 10427858-3 1999 In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group. Heparin 89-96 serpin family C member 1 Homo sapiens 164-176 10427858-3 1999 In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group. Oligosaccharides 98-114 serpin family C member 1 Homo sapiens 62-74 10427858-3 1999 In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group. Oligosaccharides 98-114 serpin family C member 1 Homo sapiens 164-176 10427858-3 1999 In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group. pentadeca- to eicosasaccharides 116-147 serpin family C member 1 Homo sapiens 62-74 10427858-3 1999 In a further step, based on the knowledge of the mechanism of antithrombin activation by heparin, oligosaccharides (pentadeca- to eicosasaccharides), comprising an antithrombin binding domain prolonged by a thrombin binding domain, were designed and synthesised in the Sanofi group. pentadeca- to eicosasaccharides 116-147 serpin family C member 1 Homo sapiens 164-176 10215897-0 1999 Structure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts. heparin-derived tetrasaccharide 13-44 serpin family C member 1 Homo sapiens 77-89 10215897-1 1999 A complex of the synthetic tetrasaccharide AGA*IM [GlcN, 6-SO3-alpha(1-4)-GlcA-beta(1-4)-GlcN,3, 6-SO3-alpha(1-4)-IdoA-alphaOMe] and the plasma protein antithrombin has been studied by NMR spectroscopy. tetrasaccharide 27-42 serpin family C member 1 Homo sapiens 152-164 10215897-1 1999 A complex of the synthetic tetrasaccharide AGA*IM [GlcN, 6-SO3-alpha(1-4)-GlcA-beta(1-4)-GlcN,3, 6-SO3-alpha(1-4)-IdoA-alphaOMe] and the plasma protein antithrombin has been studied by NMR spectroscopy. polyethylene glycol-glutaminase-asparaginase 43-46 serpin family C member 1 Homo sapiens 152-164 10215897-3 1999 Considerable changes were observed at both 20 : 1 and 10 : 1 ratios (AGA*IM : antithrombin) in 1H as well as 13C chemical shifts. Hydrogen 95-97 serpin family C member 1 Homo sapiens 78-90 10215897-11 1999 All monitored NMR variables, 1H and 13C chemical shifts, 1JC-H couplings and transferred NOEs, indicated that the changes in conformation at the glycosidic linkage GlcN, 6-SO3-alpha(1-4)-GlcA were induced by the presence of antithrombin and suggested that the receptor selected a conformer different from that in the free state. Glucosamine 164-168 serpin family C member 1 Homo sapiens 224-236 10215897-11 1999 All monitored NMR variables, 1H and 13C chemical shifts, 1JC-H couplings and transferred NOEs, indicated that the changes in conformation at the glycosidic linkage GlcN, 6-SO3-alpha(1-4)-GlcA were induced by the presence of antithrombin and suggested that the receptor selected a conformer different from that in the free state. 6-so3-alpha(1-4)-glca 170-191 serpin family C member 1 Homo sapiens 224-236 10215897-15 1999 273, 7478-7487] for the interaction of heparin-derived oligosaccharides with antithrombin, but with a minor extension: in the first step a low-affinity recognition complex between ligand and receptor is formed, accompanied by a conformational change in the tetrasaccharide, possibly creating a complementary three-dimensional structure to fit the protein-binding site. Heparin 39-46 serpin family C member 1 Homo sapiens 77-89 10215897-15 1999 273, 7478-7487] for the interaction of heparin-derived oligosaccharides with antithrombin, but with a minor extension: in the first step a low-affinity recognition complex between ligand and receptor is formed, accompanied by a conformational change in the tetrasaccharide, possibly creating a complementary three-dimensional structure to fit the protein-binding site. Oligosaccharides 55-71 serpin family C member 1 Homo sapiens 77-89 10215897-15 1999 273, 7478-7487] for the interaction of heparin-derived oligosaccharides with antithrombin, but with a minor extension: in the first step a low-affinity recognition complex between ligand and receptor is formed, accompanied by a conformational change in the tetrasaccharide, possibly creating a complementary three-dimensional structure to fit the protein-binding site. tetrasaccharide 257-272 serpin family C member 1 Homo sapiens 77-89 10391608-1 1999 PURPOSE: To report three patients who developed heparin resistance during cardiac surgery which was successfully managed with 1000 U Antithrombin III (AT III). Heparin 48-55 serpin family C member 1 Homo sapiens 133-149 10391608-1 1999 PURPOSE: To report three patients who developed heparin resistance during cardiac surgery which was successfully managed with 1000 U Antithrombin III (AT III). Heparin 48-55 serpin family C member 1 Homo sapiens 151-157 10391608-12 1999 CONCLUSION: We recommend that AT III supplementation should be considered to manage heparin resistance prior or during CPB in patients undergoing open heart surgery. Heparin 84-91 serpin family C member 1 Homo sapiens 30-36 10348900-4 1999 [3H]Heparin labeled with this reagent crosslinked to antithrombin III very specifically but not to ovalbumin, as analyzed by the Bio-imaging Analyzer System (BAS, Fuji Photo Film, Tokyo). Heparin 4-11 serpin family C member 1 Homo sapiens 53-69 10375387-0 1999 Heparin induced thrombocytopenia: diagnosis and contemporary antithrombin management. Heparin 0-7 serpin family C member 1 Homo sapiens 61-73 10466207-1 1999 Three hexasaccharides, having from low to very high affinity for antithrombin, were synthesised from disaccharide building block precursors. Disaccharides 101-113 serpin family C member 1 Homo sapiens 65-77 10466208-4 1999 These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide. Heparin 32-39 serpin family C member 1 Homo sapiens 66-78 10466208-4 1999 These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide. pentadeca- 114-124 serpin family C member 1 Homo sapiens 66-78 10466208-4 1999 These results indicate that, in heparin, the sequence involved in antithrombin-catalyzed thrombin inhibition is a pentadeca- or a hexadecasaccharide. hexadecasaccharide 130-148 serpin family C member 1 Homo sapiens 66-78 10328304-1 1999 Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained. pentadeca-, heptadeca- and nonadecasaccharides 10-56 serpin family C member 1 Homo sapiens 72-88 9929104-8 1999 Included in this analysis is a linkage analysis of a trinucleotide repeat in intron 5 of the AT gene of the various family members, which also confirmed maternity and paternity. trinucleotide 53-66 serpin family C member 1 Homo sapiens 93-95 10328304-1 1999 Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained. pentadeca-, heptadeca- and nonadecasaccharides 10-56 serpin family C member 1 Homo sapiens 90-96 10328304-1 1999 Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained. pentasaccharide 106-121 serpin family C member 1 Homo sapiens 72-88 10328304-1 1999 Synthetic pentadeca-, heptadeca- and nonadecasaccharides, comprising an antithrombin III (AT III) binding pentasaccharide prolonged at the non-reducing end by a thrombin binding domain have been obtained. pentasaccharide 106-121 serpin family C member 1 Homo sapiens 90-96 10328304-2 1999 The pentadecasaccharide is the shortest oligosaccharide able to catalyse thrombin inhibition by AT III. pentadecasaccharide 4-23 serpin family C member 1 Homo sapiens 96-102 10328304-2 1999 The pentadecasaccharide is the shortest oligosaccharide able to catalyse thrombin inhibition by AT III. Oligosaccharides 40-55 serpin family C member 1 Homo sapiens 96-102 10510546-7 1999 sE-selectin levels in GDM correlated inversely with ATIII activity (r = -0.905, p = 0.0028). se-selectin 0-11 serpin family C member 1 Homo sapiens 52-57 10037709-1 1999 Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively. Heparin 29-36 serpin family C member 1 Homo sapiens 244-256 10037709-1 1999 Assembly of ternary thrombin-heparin-fibrin complexes, formed when fibrin binds to exosite 1 on thrombin and fibrin-bound heparin binds to exosite 2, produces a 58- and 247-fold reduction in the heparin-catalyzed rate of thrombin inhibition by antithrombin and heparin cofactor II, respectively. Heparin 122-129 serpin family C member 1 Homo sapiens 244-256 10037709-3 1999 Protection from inhibition by antithrombin and heparin cofactor II requires ligation of both exosites 1 and 2 because minimal protection is seen when exosite 1 variants (gamma-thrombin and thrombin Quick 1) or an exosite 2 variant (Arg93 --> Ala, Arg97 --> Ala, and Arg101 --> Ala thrombin) is substituted for thrombin. Alanine 245-248 serpin family C member 1 Homo sapiens 30-42 10037709-3 1999 Protection from inhibition by antithrombin and heparin cofactor II requires ligation of both exosites 1 and 2 because minimal protection is seen when exosite 1 variants (gamma-thrombin and thrombin Quick 1) or an exosite 2 variant (Arg93 --> Ala, Arg97 --> Ala, and Arg101 --> Ala thrombin) is substituted for thrombin. Alanine 263-266 serpin family C member 1 Homo sapiens 30-42 10037709-5 1999 In contrast, thrombin is protected from inhibition by a covalent antithrombin-heparin complex, suggesting that access of heparin to exosite 2 of thrombin is hampered when ternary complex formation occurs. Heparin 78-85 serpin family C member 1 Homo sapiens 65-77 10192656-8 1999 Levels of antithrombin decreased during treatment with oestradiol, whereas no changes were seen in levels of fibrinogen, von Willebrand factor, prothrombin fragment 1+2, protein S, protein C or resistance to activated protein C. In conclusion, oestrogen replacement therapy in postmenopausal women with NIDDM improved the fibrinolytic activity, while only clinically insignificant alterations in the clotting system were seen. Estradiol 55-65 serpin family C member 1 Homo sapiens 10-22 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. danaparoid 0-17 serpin family C member 1 Homo sapiens 24-36 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. Glycosaminoglycans 51-69 serpin family C member 1 Homo sapiens 24-36 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. Heparitin Sulfate 71-86 serpin family C member 1 Homo sapiens 24-36 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. Dermatan Sulfate 88-104 serpin family C member 1 Homo sapiens 24-36 10914239-1 1999 Danaparoid sodium is an antithrombin composed of 3 glycosaminoglycans: heparan sulfate, dermatan sulfate and chondroitin sulfate. Chondroitin Sulfates 109-128 serpin family C member 1 Homo sapiens 24-36 10914239-2 1999 Similar to heparin, danaparoid operates by activating antithrombin 3, but does not contain heparin or heparin fragments, and is therefore antigenically distinct. danaparoid 20-30 serpin family C member 1 Homo sapiens 54-66 10026234-8 1999 Double antibody techniques also demonstrated that the heparin binding domain of intraepithelial antithrombin was occupied. Heparin 54-61 serpin family C member 1 Homo sapiens 96-108 10026234-10 1999 These findings suggest that antithrombin, probably in association with heparin or heparan sulfate, is internalized by renal proximal epithelial cells. Heparin 71-78 serpin family C member 1 Homo sapiens 28-40 10026234-10 1999 These findings suggest that antithrombin, probably in association with heparin or heparan sulfate, is internalized by renal proximal epithelial cells. Heparitin Sulfate 82-97 serpin family C member 1 Homo sapiens 28-40 10226408-2 1999 We used an antithrombin agent, argatroban, as an alternative anticoagulant in left heart bypass with the Bio-Medicus centrifugal pump in 7 of 9 recent patients who underwent aortic repair using left heart bypass. argatroban 31-41 serpin family C member 1 Homo sapiens 11-23 9988693-4 1999 The neoepitope encompasses the motif DAFHK, located in native antithrombin on strand 4 of beta-sheet A, which becomes strand 5 of beta-sheet A in the RCL-cleaved and latent conformers. dafhk 37-42 serpin family C member 1 Homo sapiens 62-74 9950667-4 1999 METHODS AND RESULTS: Vasoflux is prepared by depolymerization of heparin, restricting molecular size to between 3000 and 8000 Da, and reducing antithrombin affinity by periodate oxidation. metaperiodate 168-177 serpin family C member 1 Homo sapiens 143-155 10187813-0 1999 Oxidation of methionine residues in antithrombin. Methionine 13-23 serpin family C member 1 Homo sapiens 36-48 10193724-0 1999 Antithrombin activity during the period of percutaneous coronary revascularization: relation to heparin use, thrombotic complications and restenosis. Heparin 96-103 serpin family C member 1 Homo sapiens 0-12 10193724-1 1999 OBJECTIVES: This study evaluated changes in antithrombin (AT) activity around the time of percutaneous transluminal coronary revascularization (PTCR) with unfractionated heparin anticoagulation and the effects these changes had on major thrombotic complications of PTCR. Heparin 170-177 serpin family C member 1 Homo sapiens 44-56 10401691-6 1999 Several carbohydrate-deficient isoforms were found in transferrin (four), alpha1-antitrypsin (three), antithrombin (two) and thyroxine-binding globulin (four). Carbohydrates 8-20 serpin family C member 1 Homo sapiens 102-114 10037709-0 1999 Exosites 1 and 2 are essential for protection of fibrin-bound thrombin from heparin-catalyzed inhibition by antithrombin and heparin cofactor II. Heparin 76-83 serpin family C member 1 Homo sapiens 108-120 10064272-0 1999 Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity. Aspartic Acid 17-20 serpin family C member 1 Homo sapiens 101-113 10064272-0 1999 Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity. Serine 21-24 serpin family C member 1 Homo sapiens 101-113 10064272-0 1999 Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity. Phenylalanine 25-28 serpin family C member 1 Homo sapiens 101-113 10064272-0 1999 Insertion of the Asp-Ser/Phe sequence in the P" position of hirutonin provides molecules having both antithrombin and disintegrin activity. hirutonin 60-69 serpin family C member 1 Homo sapiens 101-113 10093889-2 1999 The use of the current antithrombotic drugs, namely heparin + chronic aspirin (ASA) +/- oral anticoagulants, is based upon the assumptions that: i) heparin blocks thrombin generation and/or accelerates thrombin inhibition by antithrombin III (ATIII); ii) aspirin acetylates platelet cyclooxygenase, thereby preventing thromboxane A2 (TxA2) synthesis; and iii) oral anticoagulants reduce the availability of vitamin K-dependent procoagulants, thereby reducing the risk of thrombus formation. Heparin 148-155 serpin family C member 1 Homo sapiens 225-241 10093889-2 1999 The use of the current antithrombotic drugs, namely heparin + chronic aspirin (ASA) +/- oral anticoagulants, is based upon the assumptions that: i) heparin blocks thrombin generation and/or accelerates thrombin inhibition by antithrombin III (ATIII); ii) aspirin acetylates platelet cyclooxygenase, thereby preventing thromboxane A2 (TxA2) synthesis; and iii) oral anticoagulants reduce the availability of vitamin K-dependent procoagulants, thereby reducing the risk of thrombus formation. Heparin 148-155 serpin family C member 1 Homo sapiens 243-248 10629396-2 1999 Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin. Heparin 21-29 serpin family C member 1 Homo sapiens 143-155 10063994-2 1999 a sulfated pentasaccharide, which enhances specifically antithrombin III mediated inactivation of factor-Xa, in a clinical setting known to promote arterial thrombosis, i.e. coronary angioplasty. pentasaccharide 11-26 serpin family C member 1 Homo sapiens 56-72 9882436-0 1999 Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III. Disulfides 8-17 serpin family C member 1 Homo sapiens 116-132 10629396-2 1999 Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin. Heparin 21-28 serpin family C member 1 Homo sapiens 143-155 10629396-2 1999 Low-molecular-weight heparins (LMWHs), like unfractionated heparin (UFH), exert their action primarily by accelerating the interaction between antithrombin (AT) and thrombin. Heparin 68-71 serpin family C member 1 Homo sapiens 143-155 10050080-8 1999 Furthermore, antiplatelet therapy with cilostazol for diabetic patients may be useful as antithrombin therapy including antiplatelet therapy, since it suppresses the production of intrinsic coagulants produced by platelet activation. Cilostazol 39-49 serpin family C member 1 Homo sapiens 89-101 12080632-1 1999 OBJECTIVES: To partly elucidate the relationship between homocysteine(Hcy) and thrombosis, we observed Hcy"s effects on platelet aggregation and antithrombin activity of heparin cofactor in vitro. Homocysteine 103-106 serpin family C member 1 Homo sapiens 145-157 10421704-5 1999 Thus, it appears that dextran derivatives can mimic the action of heparin in regard to its interactions with antithrombin and serine proteases involved in blood coagulation. Dextrans 22-29 serpin family C member 1 Homo sapiens 109-121 10421704-5 1999 Thus, it appears that dextran derivatives can mimic the action of heparin in regard to its interactions with antithrombin and serine proteases involved in blood coagulation. Heparin 66-73 serpin family C member 1 Homo sapiens 109-121 21341006-0 1999 Characterization of heparin binding variants of antithrombin by crossed immunoelectrophoresis in the presence of heparin. Heparin 20-27 serpin family C member 1 Homo sapiens 48-60 21341006-0 1999 Characterization of heparin binding variants of antithrombin by crossed immunoelectrophoresis in the presence of heparin. Heparin 113-120 serpin family C member 1 Homo sapiens 48-60 21341006-4 1999 Thus, the last update of the antithrombin database listed 11 distinct molecular defects causing heparin binding abnormalities and nine defects having pleiotropic effects interfering with both thrombin inhibitory activity and heparin binding. Heparin 96-103 serpin family C member 1 Homo sapiens 29-41 21341006-4 1999 Thus, the last update of the antithrombin database listed 11 distinct molecular defects causing heparin binding abnormalities and nine defects having pleiotropic effects interfering with both thrombin inhibitory activity and heparin binding. Heparin 225-232 serpin family C member 1 Homo sapiens 29-41 10625206-11 1999 In women from symptomatic families with antithrombin deficiency, adjusted dose heparin throughout pregnancy is recommended and warfarin for at least 3 months post partum. Heparin 79-86 serpin family C member 1 Homo sapiens 40-52 10625206-11 1999 In women from symptomatic families with antithrombin deficiency, adjusted dose heparin throughout pregnancy is recommended and warfarin for at least 3 months post partum. Warfarin 127-135 serpin family C member 1 Homo sapiens 40-52 10537578-1 1998 A retrospective study examined the impact, in heparin resistant patients (HRP), of lyophilized antithrombin III (ATIII) upon five patient outcomes: intensive care unit stay (ICU-S), 24 hour chest tube drainage (CTD in ml), blood and blood product usage (BPU), development of postoperative coagulopathy (PO-Coag), and reoperation for bleeding (Re-Op). Heparin 46-53 serpin family C member 1 Homo sapiens 95-111 10065896-2 1999 Comparisons were made with a surface modified by endpoint attached heparin, which, like the endothelium, is negatively charged and exposes the specific antithrombin binding sequence and also binds FXII and antithrombin. Heparin 67-74 serpin family C member 1 Homo sapiens 152-164 10065896-2 1999 Comparisons were made with a surface modified by endpoint attached heparin, which, like the endothelium, is negatively charged and exposes the specific antithrombin binding sequence and also binds FXII and antithrombin. Heparin 67-74 serpin family C member 1 Homo sapiens 206-218 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparitin Sulfate 101-117 serpin family C member 1 Homo sapiens 21-33 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparitin Sulfate 101-117 serpin family C member 1 Homo sapiens 56-68 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparitin Sulfate 101-117 serpin family C member 1 Homo sapiens 56-68 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparitin Sulfate 101-117 serpin family C member 1 Homo sapiens 56-68 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparin 192-199 serpin family C member 1 Homo sapiens 21-33 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparin 192-199 serpin family C member 1 Homo sapiens 56-68 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparin 192-199 serpin family C member 1 Homo sapiens 56-68 10065896-7 1999 It is suggested that antithrombin bound by the specific antithrombin binding sequence of endothelial heparan sulphate, like antithrombin bound to the specific antithrombin binding sequence on heparin surface, inhibits alpha-FXIIa. Heparin 192-199 serpin family C member 1 Homo sapiens 56-68 19078327-4 1998 This test measures the ability of heparin, as a cofactor of antithrombin III, to inMbit the catalytic function of factor Xa in plasma. Heparin 34-41 serpin family C member 1 Homo sapiens 60-76 9930564-2 1999 Organic synthetic benzamidine derivatives were initially developed as direct antithrombin agents. benzamidine 18-29 serpin family C member 1 Homo sapiens 77-89 9856996-9 1998 Thus, ATH reacts directly with thrombin through a bridge mechanism and probably catalyzes the reaction of thrombin with antithrombin by a second binding sequence on its heparin chain. Heparin 169-176 serpin family C member 1 Homo sapiens 120-132 10537578-8 1998 However, significant reduction in CTD (p = 0.05) was seen in the aminocaproic acid patients who were treated with ATIII pre-CPB or within the first 20 minutes of CPB. Aminocaproic Acid 65-82 serpin family C member 1 Homo sapiens 114-119 10537578-8 1998 However, significant reduction in CTD (p = 0.05) was seen in the aminocaproic acid patients who were treated with ATIII pre-CPB or within the first 20 minutes of CPB. cpb 124-127 serpin family C member 1 Homo sapiens 114-119 9794814-5 1998 An antithrombin to papain inactivation stoichiometry of approximately 3 indicated extensive cleavage of the inhibitor concurrent with enzyme inactivation, a behaviour verified by SDS/PAGE. Sodium Dodecyl Sulfate 179-182 serpin family C member 1 Homo sapiens 3-15 9916505-4 1998 Affinity purified anti-HPS antibodies inhibited heparin dependent formation of thrombin-antithrombin III complexes. Heparin 48-55 serpin family C member 1 Homo sapiens 88-104 9916505-8 1998 Further, H16 mAb inhibited the binding of antithrombin III to heparin in a dose dependent manner. Heparin 62-69 serpin family C member 1 Homo sapiens 42-58 9916505-9 1998 These results indicate that this mAb could recognize antithrombin III-binding sites on vascular endothelial heparan sulfate, leading to procoagulant states through the inhibition of heparin/heparan sulfate dependent anticoagulant process. Heparitin Sulfate 108-123 serpin family C member 1 Homo sapiens 53-69 9916505-9 1998 These results indicate that this mAb could recognize antithrombin III-binding sites on vascular endothelial heparan sulfate, leading to procoagulant states through the inhibition of heparin/heparan sulfate dependent anticoagulant process. Heparin 182-189 serpin family C member 1 Homo sapiens 53-69 9916505-9 1998 These results indicate that this mAb could recognize antithrombin III-binding sites on vascular endothelial heparan sulfate, leading to procoagulant states through the inhibition of heparin/heparan sulfate dependent anticoagulant process. Heparitin Sulfate 190-205 serpin family C member 1 Homo sapiens 53-69 9813019-3 1998 Second order rate constants for inhibition in the absence of heparin were 1.57 x 10(3) and 0.91 x 10(3) M-1 s-1 for C1-INH and ATIII, respectively. Heparin 61-68 serpin family C member 1 Homo sapiens 127-132 9813019-4 1998 Therapeutic heparin concentrations (0.1-1.0 units/ml) enhanced inhibition by ATIII 20-55-fold compared with 0.1-7.0-fold for C1-INH. Heparin 12-19 serpin family C member 1 Homo sapiens 77-82 9813019-11 1998 Inhibition of FXIa by ATIII in the presence of heparin was decreased 4-fold by alanine substitution at Lys253 (A253), with smaller effects noted for mutants A255 and A252. Heparin 47-54 serpin family C member 1 Homo sapiens 22-27 9813019-18 1998 The data indicate that FXI/XIa must bind to heparin for optimal inhibition by ATIII and for autoactivation. Heparin 44-51 serpin family C member 1 Homo sapiens 78-83 10101569-4 1998 This phenomenon of heparin resistance was postulated to be due to consumption of circulating antithrombin III as a result of prior heparinisation. Heparin 19-26 serpin family C member 1 Homo sapiens 93-109 9794814-7 1998 The papain band in SDS/PAGE progressively disappeared on reaction of the enzyme with increasing amounts of antithrombin, but no band representing a stable antithrombin-papain complex appeared. Sodium Dodecyl Sulfate 19-22 serpin family C member 1 Homo sapiens 107-119 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Threonine 0-9 serpin family C member 1 Homo sapiens 119-131 9848674-1 1998 A new approach for separation, capillary affinity chromatography, is introduced for studying the interaction of heparin with antithrombin III and secretory leukocyte proteinase inhibitor. Heparin 112-119 serpin family C member 1 Homo sapiens 125-141 9855818-5 1998 Furthermore, alpha-thrombin-induced DNA synthesis could be inhibited by antithrombin III (2 units/ml) with heparin (2 units/ml) or D-Phe-Pro-ArgCH2Cl (50 micrograms/ml). Heparin 107-114 serpin family C member 1 Homo sapiens 72-88 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Threonine 0-9 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Threonine 0-9 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Threonine 0-9 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 119-131 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Lysine 108-114 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Methionine 322-332 serpin family C member 1 Homo sapiens 119-131 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Methionine 322-332 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Methionine 322-332 serpin family C member 1 Homo sapiens 175-187 9763552-2 1998 Threonine 85 underlies the opening of the main beta-sheet of the molecule and its replacement, by the polar lysine, in antithrombin Wobble, resulted in a plasma deficiency of antithrombin with an uncharacteristically severe onset of thrombosis at 10 years of age, whereas the replacement of the same residue by a nonpolar methionine, antithrombin Wibble, gave near-normal levels of plasma antithrombin and more typical adult thromboembolic disease. Methionine 322-332 serpin family C member 1 Homo sapiens 175-187 9763552-3 1998 Isolated antithrombin Wibble had a decreased thermal stability (Tm 56.2, normal 57.6 degreesC) but was fully stabilized by the heparin pentasaccharide (Tm 71.8, normal 71.0 degreesC), indicating that the prime abnormality is a laxity in the transition of the main sheet of the molecule from the 5- to 6-stranded form, as was confirmed by the ready conversion of antithrombin Wibble to the 6-stranded latent form on incubation. IC 831423 127-150 serpin family C member 1 Homo sapiens 9-21 9763552-6 1998 Both antithrombin variants had an exceptional (25-fold) increase in heparin affinity and this, together with an increased inhibitory activity against factor Xa, provides evidence of the direct linkage of A-sheet opening to the conformational basis of heparin binding and activation. Heparin 68-75 serpin family C member 1 Homo sapiens 5-17 9763552-6 1998 Both antithrombin variants had an exceptional (25-fold) increase in heparin affinity and this, together with an increased inhibitory activity against factor Xa, provides evidence of the direct linkage of A-sheet opening to the conformational basis of heparin binding and activation. Heparin 251-258 serpin family C member 1 Homo sapiens 5-17 9758732-7 1998 Methylprednisolone treatment effectively inhibited the increases in TNF-alpha and IL-6 and the decreases in AT-III and albumin, but did not inhibit the increases in PMN-elastase and TAT levels. Methylprednisolone 0-18 serpin family C member 1 Homo sapiens 108-114 9758732-9 1998 CONCLUSIONS: These results suggest that methylprednisolone pretreatment attenuates the decrease in AT-III by reducing IL-6 production postoperatively. Methylprednisolone 40-58 serpin family C member 1 Homo sapiens 99-105 9771845-6 1998 Allografts with depleted tubular antithrombin at transplantation (n=20) had significantly greater plasma creatinine concentrations at posttransplant days 3 (P < 0.001) and 5 (P < 0.03) than allografts with normal tubular antithrombin (n=21). Creatinine 105-115 serpin family C member 1 Homo sapiens 33-45 9737475-2 1998 The favorable pharmacologic properties of LMWHs include a binding affinity for antithrombin III, anti-factor IIa activity, excellent bioavailability, minimal protein binding, predictable anticoagulant response, and clinical tolerance by patients. Heparin, Low-Molecular-Weight 42-47 serpin family C member 1 Homo sapiens 79-91 9737884-1 1998 The anticoagulant activation of the serpin antithrombin by heparin pentasaccharide DEFGH was previously shown to involve trisaccharide DEF first binding and inducing activation of the serpin, followed by disaccharide GH binding and stabilizing the activated state [Petitou et al. pentasaccharide 67-82 serpin family C member 1 Homo sapiens 43-55 9737884-1 1998 The anticoagulant activation of the serpin antithrombin by heparin pentasaccharide DEFGH was previously shown to involve trisaccharide DEF first binding and inducing activation of the serpin, followed by disaccharide GH binding and stabilizing the activated state [Petitou et al. Trisaccharides 121-134 serpin family C member 1 Homo sapiens 43-55 9737884-1 1998 The anticoagulant activation of the serpin antithrombin by heparin pentasaccharide DEFGH was previously shown to involve trisaccharide DEF first binding and inducing activation of the serpin, followed by disaccharide GH binding and stabilizing the activated state [Petitou et al. Disaccharides 204-216 serpin family C member 1 Homo sapiens 43-55 9737884-7 1998 Perturbation of the conformational equilibrium of iduronate residue G through replacement of the nonessential 3-OH of this residue with -H resulted in parallel decreases in the fraction of residue G in the skew boat conformer (from 64 to 24%) and in the association constant for pentasaccharide binding to antithrombin [(2.6 +/- 0.3)-fold], consistent with selective binding of the skew boat conformer to the serpin. Iduronic Acid 50-59 serpin family C member 1 Homo sapiens 306-318 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. Salts 4-8 serpin family C member 1 Homo sapiens 78-90 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. pentasaccharide 91-106 serpin family C member 1 Homo sapiens 78-90 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. pentasaccharide 91-106 serpin family C member 1 Homo sapiens 299-311 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. pentasaccharide 183-198 serpin family C member 1 Homo sapiens 78-90 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. pentasaccharide 183-198 serpin family C member 1 Homo sapiens 299-311 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. Hydrogen 235-243 serpin family C member 1 Homo sapiens 78-90 9737884-9 1998 The salt dependence of binding, together with a recent X-ray structure of the antithrombin-pentasaccharide complex, suggested that the majority of the enhanced affinity of the latter pentasaccharide was due to direct electrostatic and hydrogen-bonding interactions of the H residue 3-O-sulfate with antithrombin. 3-o-sulfate 282-293 serpin family C member 1 Homo sapiens 78-90 9737884-10 1998 All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications. pentasaccharides 12-28 serpin family C member 1 Homo sapiens 62-74 9737884-10 1998 All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications. pentasaccharides 12-28 serpin family C member 1 Homo sapiens 216-228 9737884-10 1998 All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications. pentasaccharide 12-27 serpin family C member 1 Homo sapiens 62-74 9737884-10 1998 All variant pentasaccharides produced a normal enhancement of antithrombin fluoresence and normal acceleration of factor Xa inhibition by the serpin at saturating levels, indicating that conformational activation of antithrombin was not affected by the pentasaccharide modifications. pentasaccharide 12-27 serpin family C member 1 Homo sapiens 216-228 9737884-11 1998 Rapid kinetic studies were consistent with the altered affinities of the variant pentasaccharides resulting mostly from perturbed interactions of the reducing-end GH disaccharide with the activated antithrombin conformation and minimally to an altered binding of the nonreducing-end DEF trisaccharide to the native serpin conformation. pentasaccharides 81-97 serpin family C member 1 Homo sapiens 198-210 9737884-11 1998 Rapid kinetic studies were consistent with the altered affinities of the variant pentasaccharides resulting mostly from perturbed interactions of the reducing-end GH disaccharide with the activated antithrombin conformation and minimally to an altered binding of the nonreducing-end DEF trisaccharide to the native serpin conformation. Disaccharides 166-178 serpin family C member 1 Homo sapiens 198-210 9737884-12 1998 Together, these results support a model in which the conformational flexibility of the G residue facilitates conversion to the skew boat conformer and thereby allows charged groups of the GH disaccharide to bind and stabilize the activated antithrombin conformation that is induced by the DEF trisaccharide. gh disaccharide 188-203 serpin family C member 1 Homo sapiens 240-252 9730869-4 1998 Our results showed that stretch induced glycosaminoglycan production with increased antithrombin activity due to an increase in the concentration of active chondroitin sulfate. Chondroitin Sulfates 156-175 serpin family C member 1 Homo sapiens 84-96 9737884-12 1998 Together, these results support a model in which the conformational flexibility of the G residue facilitates conversion to the skew boat conformer and thereby allows charged groups of the GH disaccharide to bind and stabilize the activated antithrombin conformation that is induced by the DEF trisaccharide. Trisaccharides 293-306 serpin family C member 1 Homo sapiens 240-252 9748634-5 1998 PAI-1-ovalbumin, PAI-1-antithrombin III and PAI-1-P13 (Val-->Glu) revealed specific activities of 86+/-15%, 77+/-11%, and 100+/-30% respectively, towards t-PA and similar inhibitory properties towards u-PA. Valine 55-58 serpin family C member 1 Homo sapiens 23-39 9722560-0 1998 Deconvolution of the fluorescence emission spectrum of human antithrombin and identification of the tryptophan residues that are responsive to heparin binding. Heparin 143-150 serpin family C member 1 Homo sapiens 61-73 9722560-1 1998 Heparin causes an allosterically transmitted conformational change in the reactive center loop of antithrombin and a 40% enhancement of tryptophan fluorescence. Heparin 0-7 serpin family C member 1 Homo sapiens 98-110 9722560-2 1998 We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans. Tryptophan 61-64 serpin family C member 1 Homo sapiens 29-41 9722560-2 1998 We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans. Phenylalanine 72-75 serpin family C member 1 Homo sapiens 29-41 9722560-2 1998 We have expressed four human antithrombins containing single Trp --> Phe mutations and determined that the fluorescence of antithrombin is a linear combination of the four tryptophans. Tryptophan 175-186 serpin family C member 1 Homo sapiens 29-41 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 79-82 serpin family C member 1 Homo sapiens 44-56 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 95-98 serpin family C member 1 Homo sapiens 44-56 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 95-98 serpin family C member 1 Homo sapiens 44-56 9748565-0 1998 Mechanism of factor IXa inhibition by antithrombin in the presence of unfractionated and low molecular weight heparins and fucoidan. Heparin 110-118 serpin family C member 1 Homo sapiens 38-50 9748565-1 1998 Heparin exerts its anticoagulant activity by catalysing the inhibition of coagulation proteases by antithrombin (AT). Heparin 0-7 serpin family C member 1 Homo sapiens 99-111 9748565-3 1998 The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan. Polysaccharides 131-146 serpin family C member 1 Homo sapiens 82-94 9748565-3 1998 The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan. Heparin 181-188 serpin family C member 1 Homo sapiens 82-94 9748565-3 1998 The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan. Heparin 245-253 serpin family C member 1 Homo sapiens 82-94 9748565-3 1998 The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan. Heparin, Low-Molecular-Weight 255-259 serpin family C member 1 Homo sapiens 82-94 9748565-3 1998 The aim of this study was to compare the catalysis of inhibition of blood fIXa by antithrombin in the presence of several sulfated polysaccharides with anticoagulant activity, i.e. heparin, three widely used in therapeutics low molecular weight heparins (LMWH) and fucoidan. fucoidan 265-273 serpin family C member 1 Homo sapiens 82-94 9748565-4 1998 Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol. Heparin 106-113 serpin family C member 1 Homo sapiens 53-65 9748565-4 1998 Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol. Heparin 106-113 serpin family C member 1 Homo sapiens 190-202 9748565-4 1998 Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol. Heparin, Low-Molecular-Weight 118-122 serpin family C member 1 Homo sapiens 53-65 9748565-4 1998 Plots of the second-order rate constants of the fIXa-antithrombin reaction vs. the concentration of added heparin and LMWH are bell-shaped and fit the kinetic model established for thrombin-antithrombin reaction by Jordan R., Beeler D., Rosenberg R. (1979) J. Biol. Heparin, Low-Molecular-Weight 118-122 serpin family C member 1 Homo sapiens 190-202 9722560-3 1998 The contributions to the spectrum of native antithrombin at 340 nm were 8% for Trp-49, 10% for Trp-189, 19% for Trp-225, and 63% for Trp-307. Tryptophan 95-98 serpin family C member 1 Homo sapiens 44-56 9722560-5 1998 Trp-49 and Trp-225 underwent spectral shifts of 15 nm to blue and 5 nm to red, respectively, in the antithrombin-heparin complex. Tryptophan 0-3 serpin family C member 1 Homo sapiens 100-112 9804516-2 1998 The purpose of this study was to bind covalently a basecoat protein (canine serum albumin [CSAJ) and a potent antithrombin agent (recombinant hirudin [rHir]) to 4 mm inner diameter poly(carbonate urea) urethane grafts with reactive carboxylic acid groups (cPU). poly(carbonate urea) urethane 181-210 serpin family C member 1 Homo sapiens 110-122 9722560-5 1998 Trp-49 and Trp-225 underwent spectral shifts of 15 nm to blue and 5 nm to red, respectively, in the antithrombin-heparin complex. Tryptophan 11-14 serpin family C member 1 Homo sapiens 100-112 9722560-5 1998 Trp-49 and Trp-225 underwent spectral shifts of 15 nm to blue and 5 nm to red, respectively, in the antithrombin-heparin complex. Heparin 113-120 serpin family C member 1 Homo sapiens 100-112 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Tryptophan 56-67 serpin family C member 1 Homo sapiens 81-93 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Tryptophan 155-158 serpin family C member 1 Homo sapiens 81-93 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Tryptophan 167-170 serpin family C member 1 Homo sapiens 81-93 9722560-8 1998 The time-resolved fluorescence properties of individual tryptophans of wild-type antithrombin were also determined using the four variants and showed that Trp-225 and Trp-307 experienced the largest change in lifetime upon heparin binding, providing support for the steady-state fluorescence deconvolution. Heparin 223-230 serpin family C member 1 Homo sapiens 81-93 9801822-1 1998 We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom. c-pentasaccharide 65-82 serpin family C member 1 Homo sapiens 107-123 9801822-1 1998 We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom. c-pentasaccharide 65-82 serpin family C member 1 Homo sapiens 125-131 9801822-1 1998 We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom. Heparin 151-158 serpin family C member 1 Homo sapiens 107-123 9801822-1 1998 We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom. Heparin 151-158 serpin family C member 1 Homo sapiens 125-131 9801822-1 1998 We describe here the synthesis and the biological activity of a "C-pentasaccharide", a new analogue of the antithrombin III (AT III) binding region of heparin containing a methylene bridge in place of an interglycosidic oxygen atom. Oxygen 220-226 serpin family C member 1 Homo sapiens 125-131 9793617-4 1998 As this test is designed for heparin plasma levels, transformation of the chromophore occurred only after adding heparin AT III complex, which is usually present in plasma. Heparin 113-120 serpin family C member 1 Homo sapiens 121-127 9805364-2 1998 The polysaccharide, which is regarded as a homopolysaccharide, was 6-fold more antithrombin-active than the heparin standard. Heparin 108-115 serpin family C member 1 Homo sapiens 79-91 9702317-0 1998 Covalent linkage of recombinant hirudin to a novel ionic poly(carbonate) urethane polymer with protein binding sites: determination of surface antithrombin activity. poly(carbonate) urethane 57-81 serpin family C member 1 Homo sapiens 143-155 9805364-3 1998 The antithrombin activity was decreased, by desulfation, although the non-active product still retained 8% of the sulfate ester. sulfate ester 114-127 serpin family C member 1 Homo sapiens 4-16 10420071-1 1998 Unfractionated heparin (UFH) exerts its anticoagulant properties by increasing the inactivation of thrombin and activated factor X by antithrombin III. Heparin 15-22 serpin family C member 1 Homo sapiens 134-150 10420071-1 1998 Unfractionated heparin (UFH) exerts its anticoagulant properties by increasing the inactivation of thrombin and activated factor X by antithrombin III. Heparin 24-27 serpin family C member 1 Homo sapiens 134-150 9805364-0 1998 Chemical structure of antithrombin-active Rhamnan sulfate from Monostrom nitidum. rhamnan sulfate 42-57 serpin family C member 1 Homo sapiens 22-34 9805364-2 1998 The polysaccharide, which is regarded as a homopolysaccharide, was 6-fold more antithrombin-active than the heparin standard. Polysaccharides 4-18 serpin family C member 1 Homo sapiens 79-91 9805364-2 1998 The polysaccharide, which is regarded as a homopolysaccharide, was 6-fold more antithrombin-active than the heparin standard. homopolysaccharide 43-61 serpin family C member 1 Homo sapiens 79-91 9759611-3 1998 Heparin infusion, well known to inhibit thrombin generation by fostering antithrombin activity, inhibits the formation of platelet-derived procoagulant microparticles, probably by decreasing the formation of free thrombin, which, under our circumstances, is the main platelet activator. Heparin 0-7 serpin family C member 1 Homo sapiens 73-85 9736420-0 1998 Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy. Heparin 45-52 serpin family C member 1 Homo sapiens 105-117 9736420-0 1998 Differential effects of low molecular weight heparin and unfractionated heparin on circulating levels of antithrombin and tissue factor pathway inhibitor (TFPI): a possible mechanism for difference in therapeutic efficacy. Heparin 72-79 serpin family C member 1 Homo sapiens 105-117 9736420-2 1998 Heparin exerts its function by potentiating antithrombin and by mobilizing tissue factor pathway inhibitor (TFPI) into the circulation. Heparin 0-7 serpin family C member 1 Homo sapiens 44-56 9736420-6 1998 Infusion of UFH, but not subcutaneous LMWH, was found to attenuate the antithrombotic defense by a selective decrease of both circulating antithrombin (-21+/-7%, p<0.0001) and of free and endothelial-bound TFPI. Heparin 12-15 serpin family C member 1 Homo sapiens 138-150 9736420-8 1998 The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis. Heparin 27-30 serpin family C member 1 Homo sapiens 43-55 9736420-8 1998 The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis. Heparin, Low-Molecular-Weight 35-39 serpin family C member 1 Homo sapiens 43-55 9736420-8 1998 The differential effect of UFH and LMWH on antithrombin and TFPI may explain the superior efficacy of subcutaneous LMWH compared with conventional intravenous UFH for treatment of both arterial and venous thrombosis. Heparin, Low-Molecular-Weight 115-119 serpin family C member 1 Homo sapiens 43-55 9675160-6 1998 Hydration fingerprints of antithrombin (that is, water-permeable pockets) are analyzed to determine their location, volume, and size of access pores, using alpha shape-based methods from computational geometry. Water 49-54 serpin family C member 1 Homo sapiens 26-38 9675160-11 1998 This study demonstrates that conformational changes of antithrombin, including loop insertion, are linked to water transfer from antithrombin to bulk solution. Water 109-114 serpin family C member 1 Homo sapiens 55-67 9675160-11 1998 This study demonstrates that conformational changes of antithrombin, including loop insertion, are linked to water transfer from antithrombin to bulk solution. Water 109-114 serpin family C member 1 Homo sapiens 129-141 9702317-3 1998 The purpose of this study was to covalently immobilize the potent, specific antithrombin agent recombinant hirudin (rHir) onto a novel polyurethane polymer synthesized with carboxylic acid groups which served as protein attachment sites. polyurethane polymer 135-155 serpin family C member 1 Homo sapiens 76-88 9702317-12 1998 Thus, these results demonstrate that rHir can be covalently bound to this novel polyurethane surface and still maintain potent antithrombin activity. Polyurethanes 80-92 serpin family C member 1 Homo sapiens 127-139 9692954-11 1998 Homology modeling of PEDF based on the X-ray crystal structures of antithrombin III and ovalbumin shows a region at the center of beta-sheet A-strands 2 and 3- and helix F that has a basic electrostatic surface potential and is densely populated with lysines exposed to the surface (K134, K137, K189, K191, H212, and K214) that are available to interact with various glycosaminoglycans/polyanions. Lysine 251-258 serpin family C member 1 Homo sapiens 67-83 9724163-0 1998 Coagulation protein function V: diminution of antithrombin III function by acetaldehyde. Acetaldehyde 75-87 serpin family C member 1 Homo sapiens 46-62 9724163-1 1998 The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM. Acetaldehyde 153-165 serpin family C member 1 Homo sapiens 30-46 9724163-1 1998 The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM. Acetaldehyde 153-165 serpin family C member 1 Homo sapiens 48-53 9724163-1 1998 The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM. Acetaldehyde 167-170 serpin family C member 1 Homo sapiens 30-46 9724163-1 1998 The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM. Acetaldehyde 167-170 serpin family C member 1 Homo sapiens 48-53 9724163-4 1998 Clotting times of 20.9+/-1.0, 32.3+/-1.0, and 45.3+/-1.6 sec were obtained with 447, 89.4, and 17.9 mM AcH-ATIII mixtures, respectively. Acetaldehyde 103-106 serpin family C member 1 Homo sapiens 107-112 9724163-5 1998 These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant. Guanidine 60-72 serpin family C member 1 Homo sapiens 45-50 9724163-5 1998 These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant. aminos 74-80 serpin family C member 1 Homo sapiens 45-50 9724163-5 1998 These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant. Acetaldehyde 134-137 serpin family C member 1 Homo sapiens 45-50 9721974-8 1998 AT III supplementation prevented the continuous increase in sICAM-1 plasma concentration observed in control patients and led to a significant fall in soluble sE-selectin and CRP concentration (p < or = .01). se-selectin 159-170 serpin family C member 1 Homo sapiens 0-6 9784873-0 1998 Synthesis of a 3-deoxy-L-iduronic acid containing heparin pentasaccharide to probe the conformation of the antithrombin III binding sequence. 3-deoxy-l-iduronic acid 15-38 serpin family C member 1 Homo sapiens 107-123 9784873-0 1998 Synthesis of a 3-deoxy-L-iduronic acid containing heparin pentasaccharide to probe the conformation of the antithrombin III binding sequence. IC 831423 50-73 serpin family C member 1 Homo sapiens 107-123 9784873-2 1998 1H NMR studies demonstrated that, as anticipated, such a modification induces a shift of the conformational equilibrium toward 1C4 (contribution to the conformational equilibrium rises from 37% to 65%) and a substantial decrease of the affinity for antithrombin III (Kd 0.154 microM versus 0.050 microM). Hydrogen 0-2 serpin family C member 1 Homo sapiens 249-265 9692954-11 1998 Homology modeling of PEDF based on the X-ray crystal structures of antithrombin III and ovalbumin shows a region at the center of beta-sheet A-strands 2 and 3- and helix F that has a basic electrostatic surface potential and is densely populated with lysines exposed to the surface (K134, K137, K189, K191, H212, and K214) that are available to interact with various glycosaminoglycans/polyanions. Glycosaminoglycans 367-385 serpin family C member 1 Homo sapiens 67-83 9662467-7 1998 This preventive effect of antithrombin is mediated by the promotion of endothelial release of prostacyclin, an inhibitor of leukocyte activation. Epoprostenol 94-106 serpin family C member 1 Homo sapiens 26-38 9713170-1 1998 We investigated the effect of cell surface glycosaminoglycans (GAGs) on the inactivation of factor VIIa-tissue factor activity by antithrombin III (ATIII) on a human bladder carcinoma (J82) cell line and an ovarian carcinoma (OC-2008) cell line, two tumor cell lines which constitutively synthesize and express high levels of cell surface tissue factor. Glycosaminoglycans 43-61 serpin family C member 1 Homo sapiens 148-153 9713170-6 1998 In addition, we demonstrated that the ability of ATIII to inactivate factor VIIa-tissue factor activity was markedly reduced following treatment of cells with calcium ionophore (A23187). Calcium 159-166 serpin family C member 1 Homo sapiens 49-54 9713170-6 1998 In addition, we demonstrated that the ability of ATIII to inactivate factor VIIa-tissue factor activity was markedly reduced following treatment of cells with calcium ionophore (A23187). Calcimycin 178-184 serpin family C member 1 Homo sapiens 49-54 9684790-4 1998 The second order rate constant of the inactivation of FXIa by antithrombin was increased up to 6-fold by LMWH, whereas LMWdxs had no effect. Heparin, Low-Molecular-Weight 105-109 serpin family C member 1 Homo sapiens 62-74 9684790-7 1998 LMWH at maximal therapeutic plasma levels enhanced the contribution of antithrombin to the inactivation of FXIa in plasma up to 5-fold. Heparin, Low-Molecular-Weight 0-4 serpin family C member 1 Homo sapiens 71-83 9684790-9 1998 Furthermore, LMWH but not LMWdxs slightly enhanced FXIa inhibition by antithrombin. Heparin, Low-Molecular-Weight 13-17 serpin family C member 1 Homo sapiens 70-82 9642241-0 1998 Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Calcium 0-7 serpin family C member 1 Homo sapiens 42-54 9642241-0 1998 Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Heparin 17-24 serpin family C member 1 Homo sapiens 42-54 9642241-2 1998 It is believed that heparin accelerates factor Xa (FXa) inactivation by antithrombin (AT) by conformationally activating the inhibitor rather than by bridging AT and FXa in a ternary complex (template effect). Heparin 20-27 serpin family C member 1 Homo sapiens 72-84 9712292-7 1998 We found a clear relationship between the antithrombin binding capacity and the antithrombogenic potential of the heparin-coated stents. Heparin 114-121 serpin family C member 1 Homo sapiens 42-54 9641623-3 1998 We studied both their anticoagulant activity and the catalysis of thrombin (T) inhibition by heparin cofactor II (HCII) and antithrombin (AT) in the presence of these dextran derivatives relative to heparin and dextran sulfate (DXSu). Dextrans 167-174 serpin family C member 1 Homo sapiens 124-136 9765662-11 1998 ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin. Heparin 10-17 serpin family C member 1 Homo sapiens 93-109 9765662-11 1998 ACTION OF HEPARIN: The antithrombotic effect of heparin results from its catalytic effect on antithrombin III (AT) inhibition of thrombin. Heparin 48-55 serpin family C member 1 Homo sapiens 93-109 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. Heparin 98-105 serpin family C member 1 Homo sapiens 40-56 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. Heparin 98-105 serpin family C member 1 Homo sapiens 58-64 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. phyllophoran 107-119 serpin family C member 1 Homo sapiens 40-56 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. phyllophoran 107-119 serpin family C member 1 Homo sapiens 58-64 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. furcellaran 124-135 serpin family C member 1 Homo sapiens 40-56 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. furcellaran 124-135 serpin family C member 1 Homo sapiens 58-64 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. heparin-cellulose 252-269 serpin family C member 1 Homo sapiens 40-56 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. heparin-cellulose 252-269 serpin family C member 1 Homo sapiens 58-64 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. Heparin 252-259 serpin family C member 1 Homo sapiens 40-56 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. Heparin 252-259 serpin family C member 1 Homo sapiens 58-64 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. Sepharose 282-291 serpin family C member 1 Homo sapiens 40-56 9848182-2 1998 Biospecific adsorbents for thrombin and antithrombin III (AT III) isolation were synthesized with heparin, phyllophoran and furcellaran as ligands on aminopropylsilochrome and this proteins sorption characteristics on this sorbents in comparisons with heparin-cellulose and heparin-sepharose were investigated. Sepharose 282-291 serpin family C member 1 Homo sapiens 58-64 9539494-2 1998 The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex. Heparin 29-36 serpin family C member 1 Homo sapiens 75-91 9539494-2 1998 The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex. Heparin 29-36 serpin family C member 1 Homo sapiens 225-241 9662467-8 1998 An interaction between antithrombin and heparin-like glycosaminoglycans on the endothelial cell surface appears to be important for this effect. Glycosaminoglycans 53-71 serpin family C member 1 Homo sapiens 23-35 9662467-9 1998 Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans. Heparin 0-7 serpin family C member 1 Homo sapiens 45-57 9662467-9 1998 Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans. Heparin 114-121 serpin family C member 1 Homo sapiens 45-57 9662467-9 1998 Heparin inhibits such therapeutic effects of antithrombin by preventing it from interacting with the cell surface heparin-like glycosaminoglycans. Glycosaminoglycans 127-145 serpin family C member 1 Homo sapiens 45-57 9592979-5 1998 RESULTS: The industrial batches show a purity higher than 99% with approximately 95% native heparin binding ATIII. Heparin 92-99 serpin family C member 1 Homo sapiens 108-113 9516447-1 1998 Role of individual residues of the pentasaccharide activating sequence in the recognition of native and activated states of antithrombin. pentasaccharide 35-50 serpin family C member 1 Homo sapiens 124-136 9597517-2 1998 The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex. Heparin 29-36 serpin family C member 1 Homo sapiens 75-91 9597517-2 1998 The anticoagulant actions of heparin are severely limited by dependence on antithrombin III, neutralization by platelet factor 4, and the resistance of clot-bound thrombin and platelet membrane-bound factor Xa to the heparin-antithrombin III complex. Heparin 29-36 serpin family C member 1 Homo sapiens 225-241 9516447-2 1998 To determine the role of individual saccharide residues of a specific heparin pentasaccharide, denoted DEFGH, in the allosteric activation of the serpin, antithrombin, we studied the effect of deleting pentasaccharide residues on this activation. IC 831423 70-93 serpin family C member 1 Homo sapiens 154-166 9516447-2 1998 To determine the role of individual saccharide residues of a specific heparin pentasaccharide, denoted DEFGH, in the allosteric activation of the serpin, antithrombin, we studied the effect of deleting pentasaccharide residues on this activation. pentasaccharide 78-93 serpin family C member 1 Homo sapiens 154-166 9516447-4 1998 Rapid kinetic studies revealed that elimination of the reducing-end disaccharide marginally affected binding to the native low-heparin-affinity conformational state of antithrombin but greatly affected the conversion of the serpin to the activated high-heparin- affinity state, although the activated conformation was still favored. Disaccharides 68-80 serpin family C member 1 Homo sapiens 168-180 9516447-4 1998 Rapid kinetic studies revealed that elimination of the reducing-end disaccharide marginally affected binding to the native low-heparin-affinity conformational state of antithrombin but greatly affected the conversion of the serpin to the activated high-heparin- affinity state, although the activated conformation was still favored. Heparin 127-134 serpin family C member 1 Homo sapiens 168-180 9516447-6 1998 These results demonstrate that the nonreducing-end residues of the pentasaccharide function both to recognize the native low-heparin-affinity conformation of antithrombin and to induce and stabilize the activated high-heparin-affinity conformation. pentasaccharide 67-82 serpin family C member 1 Homo sapiens 158-170 9516447-6 1998 These results demonstrate that the nonreducing-end residues of the pentasaccharide function both to recognize the native low-heparin-affinity conformation of antithrombin and to induce and stabilize the activated high-heparin-affinity conformation. Heparin 125-132 serpin family C member 1 Homo sapiens 158-170 9516447-6 1998 These results demonstrate that the nonreducing-end residues of the pentasaccharide function both to recognize the native low-heparin-affinity conformation of antithrombin and to induce and stabilize the activated high-heparin-affinity conformation. Heparin 218-225 serpin family C member 1 Homo sapiens 158-170 9622211-1 1998 Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins. Heparin 19-27 serpin family C member 1 Homo sapiens 69-85 9521646-0 1998 Conformational conversion of antithrombin to a fully activated substrate of factor Xa without need for heparin. Heparin 103-110 serpin family C member 1 Homo sapiens 29-41 9521646-1 1998 Regulation of the inhibitory activity of antithrombin, the principal inhibitor of the blood-clotting proteinases factor Xa and thrombin, is accomplished by binding to heparin. Heparin 167-174 serpin family C member 1 Homo sapiens 41-53 9521646-2 1998 We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa. Serine 48-54 serpin family C member 1 Homo sapiens 18-30 9521646-2 1998 We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa. Cysteine 173-181 serpin family C member 1 Homo sapiens 18-30 9521646-2 1998 We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa. Heparin 214-221 serpin family C member 1 Homo sapiens 18-30 9521646-2 1998 We report here an antithrombin variant in which serine at position 380, 14 residues N-terminal from the reactive bond and at a hinge point in the structure, was replaced by cysteine to test a proposed mechanism of heparin activation of antithrombin as an inhibitor of factor Xa. Heparin 214-221 serpin family C member 1 Homo sapiens 236-248 9521646-3 1998 By derivatization of this cysteine with a bulky group, fluorescein, the antithrombin became permanently and fully activated toward reaction with factor Xa in a manner analogous to heparin activation, albeit as a substrate. Cysteine 26-34 serpin family C member 1 Homo sapiens 72-84 9521646-3 1998 By derivatization of this cysteine with a bulky group, fluorescein, the antithrombin became permanently and fully activated toward reaction with factor Xa in a manner analogous to heparin activation, albeit as a substrate. Fluorescein 55-66 serpin family C member 1 Homo sapiens 72-84 9521646-3 1998 By derivatization of this cysteine with a bulky group, fluorescein, the antithrombin became permanently and fully activated toward reaction with factor Xa in a manner analogous to heparin activation, albeit as a substrate. Heparin 180-187 serpin family C member 1 Homo sapiens 72-84 9521646-4 1998 These findings establish a structural basis for the mechanism of heparin activation of antithrombin against factor Xa in agreement with that proposed from an X-ray structure of antithrombin. Heparin 65-72 serpin family C member 1 Homo sapiens 87-99 9521646-4 1998 These findings establish a structural basis for the mechanism of heparin activation of antithrombin against factor Xa in agreement with that proposed from an X-ray structure of antithrombin. Heparin 65-72 serpin family C member 1 Homo sapiens 177-189 9622211-1 1998 Low-molecular-mass heparins (LMMHs) exert an anti-FXa effect through antithrombin III (ATIII) and tissue factor pathway inhibitor (TFPI) displaced from endothelium and lipoproteins. Heparin 19-27 serpin family C member 1 Homo sapiens 87-92 9622211-8 1998 At therapeutic subcutaneous doses, Bemiparin exerted an anti-FXa effect through TFPI during the first 2 h, through both ATIII and TFPI during the following 8 h (range 2-10 h) and through ATIII during the last 8 h (range 10-18 h). bemiparin 35-44 serpin family C member 1 Homo sapiens 120-125 9622211-8 1998 At therapeutic subcutaneous doses, Bemiparin exerted an anti-FXa effect through TFPI during the first 2 h, through both ATIII and TFPI during the following 8 h (range 2-10 h) and through ATIII during the last 8 h (range 10-18 h). bemiparin 35-44 serpin family C member 1 Homo sapiens 187-192 9651145-6 1998 Heparin strikingly enhanced antithrombin III"s inhibition of Xa and resulted in complete abrogation of the complex formation between h-rTFPI and Xa in the absence or presence of acidic phospholipids. Heparin 0-7 serpin family C member 1 Homo sapiens 28-44 9541411-0 1998 The N-terminal segment of antithrombin acts as a steric gate for the binding of heparin. Heparin 80-87 serpin family C member 1 Homo sapiens 26-38 9541411-1 1998 The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa. Heparin 15-22 serpin family C member 1 Homo sapiens 57-69 9541411-1 1998 The binding of heparin causes a conformational change in antithrombin to give an increased heparin binding affinity and activate the inhibition of thrombin and factor Xa. Heparin 91-98 serpin family C member 1 Homo sapiens 57-69 9541411-2 1998 The areas of antithrombin involved in binding heparin and stabilizing the interaction in the high-affinity form have been partially resolved through the study of both recombinant and natural variants. Heparin 46-53 serpin family C member 1 Homo sapiens 13-25 9541411-3 1998 The role of a section of the N-terminal segment of antithrombin, residues 22-46 (segment 22-46), in heparin binding was investigated using rapid kinetic analysis of the protein cleaved at residues 29-30 by limited proteolysis with thermolysin. Heparin 100-107 serpin family C member 1 Homo sapiens 51-63 9541411-4 1998 The cleaved antithrombin had 5.5-fold lowered affinity for heparin pentasaccharide and 1.8-fold for full-length, high-affinity heparin. IC 831423 59-82 serpin family C member 1 Homo sapiens 12-24 9541411-4 1998 The cleaved antithrombin had 5.5-fold lowered affinity for heparin pentasaccharide and 1.8-fold for full-length, high-affinity heparin. Heparin 59-66 serpin family C member 1 Homo sapiens 12-24 9541411-6 1998 This implies that the segment constituting residues 22-46 in the N terminus of antithrombin hinders access to the binding site for heparin, hence the increased initial binding for the cleaved form, whereas, when heparin is bound, segment 22-46 is involved in the stabilization of the binding interaction, as indicated by the increased dissociation constant. Heparin 131-138 serpin family C member 1 Homo sapiens 79-91 9541411-6 1998 This implies that the segment constituting residues 22-46 in the N terminus of antithrombin hinders access to the binding site for heparin, hence the increased initial binding for the cleaved form, whereas, when heparin is bound, segment 22-46 is involved in the stabilization of the binding interaction, as indicated by the increased dissociation constant. Heparin 212-219 serpin family C member 1 Homo sapiens 79-91 9541411-7 1998 When the heparin pentasaccharide is bound to antithrombin prior to incubation with thermolysin, it protects the N-terminal cleavage site, implying that segment 22-46 moves to interact with heparin in the conformational change and thus stabilizes the complex. Heparin 9-16 serpin family C member 1 Homo sapiens 45-57 9541411-7 1998 When the heparin pentasaccharide is bound to antithrombin prior to incubation with thermolysin, it protects the N-terminal cleavage site, implying that segment 22-46 moves to interact with heparin in the conformational change and thus stabilizes the complex. pentasaccharide 17-32 serpin family C member 1 Homo sapiens 45-57 9541411-7 1998 When the heparin pentasaccharide is bound to antithrombin prior to incubation with thermolysin, it protects the N-terminal cleavage site, implying that segment 22-46 moves to interact with heparin in the conformational change and thus stabilizes the complex. Heparin 189-196 serpin family C member 1 Homo sapiens 45-57 9651145-7 1998 Furthermore, antithrombin III induced dissociation of the preformed h-rTFPI/Xa complex in the presence of heparin. Heparin 106-113 serpin family C member 1 Homo sapiens 13-29 9651145-8 1998 These results suggest that in the presence of heparin, antithrombin III interferes with the catabolism of TFPI mediated via Xa. Heparin 46-53 serpin family C member 1 Homo sapiens 55-71 18370504-0 1998 Omega-3 Ethyl Ester Concentrate Decreases Total Apolipoprotein CIII and Increases Antithrombin III in Postmyocardial Infarction Patients. omega-3 ethyl ester 0-19 serpin family C member 1 Homo sapiens 82-98 9521111-0 1998 Reactivities of the S2 and S3 subsite residues of thrombin with the native and heparin-induced conformers of antithrombin. Heparin 79-86 serpin family C member 1 Homo sapiens 109-121 9521111-1 1998 A pentasaccharide (PS) fragment of heparin capable of activating antithrombin (AT) markedly accelerates the inhibition of factor Xa by AT, but has insignificant effect on inhibition of thrombin. pentasaccharide 2-17 serpin family C member 1 Homo sapiens 65-77 9521111-1 1998 A pentasaccharide (PS) fragment of heparin capable of activating antithrombin (AT) markedly accelerates the inhibition of factor Xa by AT, but has insignificant effect on inhibition of thrombin. ps 19-21 serpin family C member 1 Homo sapiens 65-77 9521111-1 1998 A pentasaccharide (PS) fragment of heparin capable of activating antithrombin (AT) markedly accelerates the inhibition of factor Xa by AT, but has insignificant effect on inhibition of thrombin. Heparin 35-42 serpin family C member 1 Homo sapiens 65-77 9839374-4 1998 As a drug AT III is separated from blood preparations by bioselective sorption on sorbents containing heparine as a complementary ligand interacting with AT III molecules. Heparin 102-110 serpin family C member 1 Homo sapiens 10-16 9839374-4 1998 As a drug AT III is separated from blood preparations by bioselective sorption on sorbents containing heparine as a complementary ligand interacting with AT III molecules. Heparin 102-110 serpin family C member 1 Homo sapiens 154-160 9514616-2 1998 GAG-UTM accelerates protein C activation by thrombin and also thrombin inhibition by antithrombin III (ATIII) in the buffer system. gag-utm 0-7 serpin family C member 1 Homo sapiens 85-101 9514616-2 1998 GAG-UTM accelerates protein C activation by thrombin and also thrombin inhibition by antithrombin III (ATIII) in the buffer system. gag-utm 0-7 serpin family C member 1 Homo sapiens 103-108 9493570-1 1998 Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution. Trichloroacetic Acid 167-170 serpin family C member 1 Homo sapiens 55-67 9493570-1 1998 Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution. Alanine 188-195 serpin family C member 1 Homo sapiens 55-67 9493570-1 1998 Thirty-one individuals from 18 unrelated families with antithrombin deficiency have been identified as having a single point mutation within codon 384 (13268 GCA-->TCA) resulting in an alanine to serine substitution. Serine 199-205 serpin family C member 1 Homo sapiens 55-67 9587911-0 1998 [Coefficient of linear correlation between levels of fibrinogen, antithrombin III, thrombin-antithrombin complex and lipid fractions in women exposed chronically to carbon disulfide]. Carbon Disulfide 165-181 serpin family C member 1 Homo sapiens 65-81 9466731-6 1998 The stimulatory effects of thrombin (10 U/ml) can be inhibited by antithrombin III (2 U/ml) (a natural thrombin inhibitor) with heparin (2 U/ml), PPACK (D-Phe-Pro-ArgCH2Cl) (20-50 microg/ml) (a serine protease inhibitor), and PGE2 (0.5-1.0 microg/ml). Heparin 128-135 serpin family C member 1 Homo sapiens 66-82 9466731-6 1998 The stimulatory effects of thrombin (10 U/ml) can be inhibited by antithrombin III (2 U/ml) (a natural thrombin inhibitor) with heparin (2 U/ml), PPACK (D-Phe-Pro-ArgCH2Cl) (20-50 microg/ml) (a serine protease inhibitor), and PGE2 (0.5-1.0 microg/ml). phenylalanyl-prolyl-arginine methyl chloride 153-171 serpin family C member 1 Homo sapiens 66-82 9466731-6 1998 The stimulatory effects of thrombin (10 U/ml) can be inhibited by antithrombin III (2 U/ml) (a natural thrombin inhibitor) with heparin (2 U/ml), PPACK (D-Phe-Pro-ArgCH2Cl) (20-50 microg/ml) (a serine protease inhibitor), and PGE2 (0.5-1.0 microg/ml). Dinoprostone 226-230 serpin family C member 1 Homo sapiens 66-82 10806853-6 1998 Simple linear regression analysis revealed a negative correlation between antithrombin III activity and fast blood glucose. Glucose 115-122 serpin family C member 1 Homo sapiens 74-90 9587911-0 1998 [Coefficient of linear correlation between levels of fibrinogen, antithrombin III, thrombin-antithrombin complex and lipid fractions in women exposed chronically to carbon disulfide]. Carbon Disulfide 165-181 serpin family C member 1 Homo sapiens 65-77 9515777-7 1998 Interaction of AT III with heparin-like glycosaminoglycans (GAGs) on the endothelial cell surface appears to be important for this effect. Heparin 27-34 serpin family C member 1 Homo sapiens 15-21 9515777-7 1998 Interaction of AT III with heparin-like glycosaminoglycans (GAGs) on the endothelial cell surface appears to be important for this effect. Glycosaminoglycans 40-58 serpin family C member 1 Homo sapiens 15-21 9515777-8 1998 Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs. Heparin 0-7 serpin family C member 1 Homo sapiens 46-52 9515777-8 1998 Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs. Heparin 0-7 serpin family C member 1 Homo sapiens 67-73 9515777-8 1998 Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs. Heparin 113-120 serpin family C member 1 Homo sapiens 46-52 9515777-8 1998 Heparin inhibits these therapeutic effects of AT III by preventing AT III from interacting with the cell surface heparin-like GAGs. Heparin 113-120 serpin family C member 1 Homo sapiens 67-73 9405673-0 1997 The anticoagulant activation of antithrombin by heparin. Heparin 48-55 serpin family C member 1 Homo sapiens 32-44 9610759-11 1998 It is concluded that surface-immobilized heparin, unlike heparin in solution, effectively inhibits the initial contact activation enzymes by an antithrombin-mediated mechanism, thereby suppressing the triggering of the intrinsic plasma coagulation pathway. Heparin 41-48 serpin family C member 1 Homo sapiens 144-156 9405673-1 1997 Antithrombin, a plasma serpin, is relatively inactive as an inhibitor of the coagulation proteases until it binds to the heparan side chains that line the microvasculature. heparan 121-128 serpin family C member 1 Homo sapiens 0-12 9405673-3 1997 The accompanying conformational change of antithrombin is revealed in a 2.9-A structure of a dimer of latent and active antithrombins, each in complex with the high-affinity pentasaccharide. pentasaccharide 174-189 serpin family C member 1 Homo sapiens 42-54 9405673-6 1997 Concomitant conformational changes at the heparin binding site explain both the initial tight binding of antithrombin to the heparans and the subsequent release of the antithrombin-protease complex into the circulation. Heparin 42-49 serpin family C member 1 Homo sapiens 105-117 9405673-6 1997 Concomitant conformational changes at the heparin binding site explain both the initial tight binding of antithrombin to the heparans and the subsequent release of the antithrombin-protease complex into the circulation. Heparin 42-49 serpin family C member 1 Homo sapiens 168-180 9405673-6 1997 Concomitant conformational changes at the heparin binding site explain both the initial tight binding of antithrombin to the heparans and the subsequent release of the antithrombin-protease complex into the circulation. heparans 125-133 serpin family C member 1 Homo sapiens 105-117 9405673-8 1997 This clear definition of the binding site will provide a structural basis for developing heparin analogues that are more specific toward their intended target antithrombin and therefore less likely to exhibit side effects. Heparin 89-96 serpin family C member 1 Homo sapiens 159-171 9395268-3 1997 Addition of LNA to porcine aortic endothelial cells reduced 125I-labeled antithrombin III binding to the cell surface heparan sulfate in a dose- and time-dependent fashion. Iodine-125 60-64 serpin family C member 1 Homo sapiens 73-89 9422339-6 1997 A chemically modified heparin with low affinity for antithrombin III was added ex vivo or in vivo to displace heparin bound nonspecifically to plasma proteins. Heparin 22-29 serpin family C member 1 Homo sapiens 52-68 9422339-6 1997 A chemically modified heparin with low affinity for antithrombin III was added ex vivo or in vivo to displace heparin bound nonspecifically to plasma proteins. Heparin 110-117 serpin family C member 1 Homo sapiens 52-68 9395268-3 1997 Addition of LNA to porcine aortic endothelial cells reduced 125I-labeled antithrombin III binding to the cell surface heparan sulfate in a dose- and time-dependent fashion. Heparitin Sulfate 118-133 serpin family C member 1 Homo sapiens 73-89 9395268-4 1997 Significant inhibition was observed with 1 mM LNA, and the maximal suppression (-50% of control) occurred at 10 mM LNA after 12 h. L-NAME (1 mM) and L-NMMA (1 mM) also significantly inhibited the antithrombin III binding. NG-Nitroarginine Methyl Ester 131-137 serpin family C member 1 Homo sapiens 196-212 9395268-4 1997 Significant inhibition was observed with 1 mM LNA, and the maximal suppression (-50% of control) occurred at 10 mM LNA after 12 h. L-NAME (1 mM) and L-NMMA (1 mM) also significantly inhibited the antithrombin III binding. omega-N-Methylarginine 149-155 serpin family C member 1 Homo sapiens 196-212 9395268-5 1997 The iron chelator desferrioxamine significantly prevented the reduction of antithrombin III binding to LNA-treated cells. Iron 4-8 serpin family C member 1 Homo sapiens 75-91 9395268-5 1997 The iron chelator desferrioxamine significantly prevented the reduction of antithrombin III binding to LNA-treated cells. Deferoxamine 18-33 serpin family C member 1 Homo sapiens 75-91 9499673-7 1997 Low-dose or very low-dose warfarin were subsequently demonstrated to be effective in patients with morbid obesity and decreased antithrombin III functional and antigenic levels, in patients with indwelling catheters, in patients undergoing gynecological surgery, as well as in patients with stage IV breast cancer. Warfarin 26-34 serpin family C member 1 Homo sapiens 128-144 9511991-0 1997 Capillary zone electrophoresis for the study of the binding of antithrombin to low-affinity heparin. Heparin 92-99 serpin family C member 1 Homo sapiens 63-75 9511991-2 1997 To evaluate the applicability of the CZE technique to this problem, we explored the interaction between antithrombin and low-affinity heparin. Heparin 134-141 serpin family C member 1 Homo sapiens 104-116 9511991-3 1997 In a series of CZE experiments we demonstrated that the mobility of antithrombin increases gradually as increased concentrations of low-affinity heparin were added to the electrolyte. Heparin 145-152 serpin family C member 1 Homo sapiens 68-80 9335355-6 1997 One of them, HAH, contained the specific antithrombin binding sequence and the other one, NAH, had a low affinity for antithrombin and had no anticoagulant activity. sodium bisulfide 90-93 serpin family C member 1 Homo sapiens 118-130 9361342-13 1997 AT III prevented the continuous rise in total serum bilirubin concentration observed in control patients and diminished the frequency of artificial renal support therapy (p < .05). Bilirubin 52-61 serpin family C member 1 Homo sapiens 0-6 9342999-9 1997 Therefore, our results challenge current practice of prescribing lifelong warfarin therapy after a first or second episode of venous thromboembolism in patients with antithrombin or protein C or S deficiency. Warfarin 74-82 serpin family C member 1 Homo sapiens 166-178 9374919-12 1997 The lack of a parallel increase of TAT with F1 + 2, in the presence of normal levels of antithrombin III (ATIII), indirectly suggests an impairment of the heparan sulphate-ATIII system which would favour thrombin generation. Heparitin Sulfate 155-171 serpin family C member 1 Homo sapiens 172-177 9342556-17 1997 Although toremifene decreases antithrombin III levels slightly, the incidence of thromboembolic complications is low. Toremifene 9-19 serpin family C member 1 Homo sapiens 30-46 9335347-0 1997 Inhibition of the plasma contact activation system of immobilized heparin: relation to surface density of functional antithrombin binding sites. Heparin 66-73 serpin family C member 1 Homo sapiens 117-129 9335347-2 1997 The present investigation was undertaken to determine what density of immobilized heparin molecules expressing functionally intact antithrombin binding sites is required to achieve these blood compatible properties. Heparin 82-89 serpin family C member 1 Homo sapiens 131-143 9335347-7 1997 Addition of heparin to the plasma phase reduced the capacity of the heparin surfaces to bind antithrombin, leading to a diminished ability of the surfaces to prevent contact activation. Heparin 12-19 serpin family C member 1 Homo sapiens 93-105 9335347-7 1997 Addition of heparin to the plasma phase reduced the capacity of the heparin surfaces to bind antithrombin, leading to a diminished ability of the surfaces to prevent contact activation. Heparin 68-75 serpin family C member 1 Homo sapiens 93-105 9335347-8 1997 This finding supports the hypothesis that antithrombin is the critical coagulation inhibitor for the suppression of contact activation on end-point immobilized heparin. Heparin 160-167 serpin family C member 1 Homo sapiens 42-54 9335355-7 1997 Our data demonstrate that in contrast to PU, PU-NAH and PU-HAH are strong mediators of factor XIa and factor IXa formation in normal and antithrombin-deficient plasma. pu-nah 45-51 serpin family C member 1 Homo sapiens 137-149 9335355-7 1997 Our data demonstrate that in contrast to PU, PU-NAH and PU-HAH are strong mediators of factor XIa and factor IXa formation in normal and antithrombin-deficient plasma. 1-(N-(2-hydroxy-5-azidobenzoyl)-2-aminoethyl)-4-(N-hydroxysuccinimidyl)succinate 59-62 serpin family C member 1 Homo sapiens 137-149 9288875-8 1997 In other clinical applications, heparin decreases antithrombin activity and causes intracircuit clot formation during extracorporeal circulation when the polymorphonuclear granulocyte elastase level is very high. Heparin 32-39 serpin family C member 1 Homo sapiens 50-62 9336303-2 1997 The aim of this work was to compare the extent of prothrombinase inhibition produced by two factor Xa inhibitors: the antithrombin III-dependent synthetic pentasaccharide (SR 90107/Org 31540) and DX-9065A, a direct factor Xa inhibitor. pentasaccharide 155-170 serpin family C member 1 Homo sapiens 118-134 9296400-0 1997 Antithrombin III during cardiac surgery: effect on response of activated clotting time to heparin and relationship to markers of hemostatic activation. Heparin 90-97 serpin family C member 1 Homo sapiens 0-16 9296400-1 1997 UNLABELLED: This study was designed to determine if, and to what extent, antithrombin III (AT) levels affect the response of the activated clotting time (ACT) to heparin in concentrations used during cardiac surgery, and to characterize the relationship between AT levels and markers of activation of coagulation during cardiopulmonary bypass (CPB). Heparin 162-169 serpin family C member 1 Homo sapiens 73-89 9309844-7 1997 Homocysteine inhibits the expression of thrombomodulin, the thrombin cofactor responsible for protein C activation, and inhibits antithrombin-III binding. Homocysteine 0-12 serpin family C member 1 Homo sapiens 129-145 9288875-9 1997 The antithrombin activity shows less decrease when argatroban is substituted for heparin. argatroban 51-61 serpin family C member 1 Homo sapiens 4-16 9288875-9 1997 The antithrombin activity shows less decrease when argatroban is substituted for heparin. Heparin 81-88 serpin family C member 1 Homo sapiens 4-16 9306621-5 1997 Following danazol administration, marked and sustained increases were noted in Free Protein S, Antithrombin, and Protein C. Platelet CD62 (P-selectin) positivity which was elevated before therapy, decreased to assay threshold limits within five weeks. Danazol 10-17 serpin family C member 1 Homo sapiens 95-107 9348117-0 1997 Mechanisms of antithrombin polymerisation and heparin activation probed by the insertion of synthetic reactive loop peptides. Peptides 116-124 serpin family C member 1 Homo sapiens 14-26 9348117-1 1997 Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation. Peptides 68-76 serpin family C member 1 Homo sapiens 14-26 9348117-1 1997 Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation. Peptides 68-76 serpin family C member 1 Homo sapiens 136-148 9348117-1 1997 Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation. Peptides 105-113 serpin family C member 1 Homo sapiens 14-26 9348117-1 1997 Incubation of antithrombin with a series of synthetic reactive loop peptides showed that 6-mer and 7-mer peptides, P14-P9 and P14-P8 of antithrombin respectively, induced loop-sheet polymerisation and binary complex formation. Peptides 105-113 serpin family C member 1 Homo sapiens 136-148 9348117-4 1997 Heparinised antithrombin was more resistant to polymerisation and peptide insertion, indicating that heparin induces a conformational change that closes the A-sheet and expels the reactive loop. Heparin 101-108 serpin family C member 1 Homo sapiens 12-24 9329410-8 1997 However, the use of heparin was associated with a lower antithrombin III activity level. Heparin 20-27 serpin family C member 1 Homo sapiens 56-72 9306621-6 1997 Both Prothrombin Fragment 1.2 and thrombin-antithrombin complexes were elevated post danazol therapy indicating continued clearance of generated thrombin. Danazol 85-92 serpin family C member 1 Homo sapiens 43-55 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. Arginine 35-38 serpin family C member 1 Homo sapiens 48-60 10322873-9 1997 After the infusion of TTMP the levels of PAdT, PagT, VIII:C, dWF and Fg were decreased significantly, while TXB2, 6-keto-PGF1 alpha, AT-III:a and AT-III:Ag remained unchanged. tetramethylpyrazine 22-26 serpin family C member 1 Homo sapiens 146-152 9242619-0 1997 Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity. Heparin 0-7 serpin family C member 1 Homo sapiens 66-78 9233715-5 1997 The presence of adenosine triphosphate, however, predicts a significantly better metabolic capacity to eliminate bilirubin, to synthesize fibrinogen and antithrombin III, and to maintain a better prothrombin time after transplantation. Adenosine Triphosphate 16-38 serpin family C member 1 Homo sapiens 153-169 9242619-0 1997 Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity. Arginine 54-62 serpin family C member 1 Homo sapiens 66-78 9242619-0 1997 Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity. Heparin 106-113 serpin family C member 1 Homo sapiens 66-78 9242619-2 1997 Recent crystallographic structures reveal the structural changes that occur when antithrombin is activated by the heparin pentasaccharide, with the exception of the final changes, which take place at the reactive center itself. IC 831423 114-137 serpin family C member 1 Homo sapiens 81-93 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. Arginine 43-46 serpin family C member 1 Homo sapiens 56-68 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. Arginine 43-46 serpin family C member 1 Homo sapiens 261-273 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. IC 831423 164-187 serpin family C member 1 Homo sapiens 56-68 9242619-3 1997 Here we show that the side chain of the P1 Arg of alpha-antithrombin is only accessible to modification by the enzyme peptidylarginine deiminase on addition of the heparin pentasaccharide, thereby inactivating the inhibitor, whereas the natural P1 His variant, antithrombin Glasgow, is unaffected, indicating that only the P1 Arg becomes accessible. Arginine 326-329 serpin family C member 1 Homo sapiens 56-68 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. Arginine 35-38 serpin family C member 1 Homo sapiens 238-250 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. IC 831423 107-130 serpin family C member 1 Homo sapiens 48-60 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. IC 831423 107-130 serpin family C member 1 Homo sapiens 238-250 9242619-4 1997 Furthermore, the deimination of P1 Arg converts antithrombin to a form with 4-fold higher affinity for the heparin pentasaccharide, similar to the affinity found for the P1 His variant, due to a lowered dissociation rate constant for the antithrombin-pentasaccharide complex. pentasaccharide 115-130 serpin family C member 1 Homo sapiens 48-60 9242619-5 1997 The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1 Arg. Arginine 165-168 serpin family C member 1 Homo sapiens 38-50 9242619-5 1997 The results support the proposal that antithrombin circulates in a constrained conformation, which when released, in this study by perturbation of the bonding of P1 Arg to the body of the molecule, allows the reactive site loop to take up the active inhibitory conformation with exposure of the P1 Arg. Arginine 298-301 serpin family C member 1 Homo sapiens 38-50 9301108-2 1997 Antithrombin activity appeared in this product was 6.5 times higher than that of standard heparin. Heparin 90-97 serpin family C member 1 Homo sapiens 0-12 9247347-3 1997 APTT was significantly prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III. pu-hep 36-42 serpin family C member 1 Homo sapiens 93-109 9247347-3 1997 APTT was significantly prolonged on PU-Hep, suggesting the binding of immobilized heparin to antithrombin III. Heparin 82-89 serpin family C member 1 Homo sapiens 93-109 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Heparin 8-15 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Lysine 34-37 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 42-45 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Lysine 66-69 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-6 1997 The key heparin binding residues, Lys-11, Arg-13, Arg-24, Arg-47, Lys-125, Arg-129, and Arg-145, line a 50-A long channel on the surface of ATIII. Arginine 50-53 serpin family C member 1 Homo sapiens 140-145 9235938-7 1997 Comparisons of binding residue positions in the structure of P14-inserted ATIII and models of native antithrombin, derived from the structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate antithrombin by breaking salt bridges that stabilize its native conformation. Heparin 205-212 serpin family C member 1 Homo sapiens 74-79 9235938-7 1997 Comparisons of binding residue positions in the structure of P14-inserted ATIII and models of native antithrombin, derived from the structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate antithrombin by breaking salt bridges that stabilize its native conformation. Heparin 205-212 serpin family C member 1 Homo sapiens 101-113 9235938-7 1997 Comparisons of binding residue positions in the structure of P14-inserted ATIII and models of native antithrombin, derived from the structures of native ovalbumin and native antichymotrypsin, suggest that heparin may activate antithrombin by breaking salt bridges that stabilize its native conformation. Heparin 205-212 serpin family C member 1 Homo sapiens 226-238 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 94-101 serpin family C member 1 Homo sapiens 113-129 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 94-101 serpin family C member 1 Homo sapiens 113-125 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 113-129 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 210-215 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 113-125 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 113-129 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 210-215 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 113-125 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 113-129 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 210-215 9235938-9 1997 In addition to providing a structural explanation for the conformational change observed upon heparin binding to antithrombin III, differences in the affinities of native, heparin-bound, complexed, and cleaved ATIII molecules for heparin can be explained based on the identified binding site and suggest why heparin functions catalytically and is released from antithrombin upon inhibitory complex formation. Heparin 172-179 serpin family C member 1 Homo sapiens 113-125 9184148-0 1997 The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Oligosaccharides 4-19 serpin family C member 1 Homo sapiens 51-63 9377090-9 1997 These results are in keeping with the observation that 2-O-sulfated pentasaccharides display a similar affinity for antithrombin III as their 2-N-sulfated counterparts. hippuric acid 55-58 serpin family C member 1 Homo sapiens 116-132 9377090-9 1997 These results are in keeping with the observation that 2-O-sulfated pentasaccharides display a similar affinity for antithrombin III as their 2-N-sulfated counterparts. sulfated 59-67 serpin family C member 1 Homo sapiens 116-132 9377090-9 1997 These results are in keeping with the observation that 2-O-sulfated pentasaccharides display a similar affinity for antithrombin III as their 2-N-sulfated counterparts. pentasaccharides 68-84 serpin family C member 1 Homo sapiens 116-132 9368910-10 1997 Magnesium infusion was associated with a significant elevation in ADP (+19.3%); ristocetin (+13.6%); and collagen-induced platelet aggregation (+14.2%); an increase in plasma antithrombin-III (+10.3%) and thromboxane (+49.4%) when compared to pre-infusion levels. Magnesium 0-9 serpin family C member 1 Homo sapiens 175-191 9198206-0 1997 Structural mobility of antithrombin and its modulation by heparin. Heparin 58-65 serpin family C member 1 Homo sapiens 23-35 9200692-3 1997 Kinetic analysis indicated that antithrombin (AT with P2 Gly) inhibited thrombin L99Y, 14.1- and 5.5-fold slower than thrombin in the absence and presence of heparin, respectively. Glycine 57-60 serpin family C member 1 Homo sapiens 32-44 9263656-2 1997 The standard antiplatelet and antithrombin agents used today in patients with acute coronary syndromes are aspirin and heparin. Aspirin 107-114 serpin family C member 1 Homo sapiens 30-42 9263656-2 1997 The standard antiplatelet and antithrombin agents used today in patients with acute coronary syndromes are aspirin and heparin. Heparin 119-126 serpin family C member 1 Homo sapiens 30-42 9253806-6 1997 The results showed that at lower concentration of the OSXP, the complexation of 125I-thrombin with heparin cofactor-II(HC-II) was enhanced, while at higher concentration of the compound, the complexation with both antithrombin-III(AT-III) and HC-II was enhanced. osxp 54-58 serpin family C member 1 Homo sapiens 214-230 9253806-6 1997 The results showed that at lower concentration of the OSXP, the complexation of 125I-thrombin with heparin cofactor-II(HC-II) was enhanced, while at higher concentration of the compound, the complexation with both antithrombin-III(AT-III) and HC-II was enhanced. osxp 54-58 serpin family C member 1 Homo sapiens 231-237 9184148-0 1997 The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Oligosaccharides 4-19 serpin family C member 1 Homo sapiens 80-92 9184148-0 1997 The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Asparagine 34-37 serpin family C member 1 Homo sapiens 51-63 9184148-0 1997 The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Asparagine 34-37 serpin family C member 1 Homo sapiens 80-92 9184148-0 1997 The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Heparin 108-115 serpin family C member 1 Homo sapiens 51-63 9184148-0 1997 The oligosaccharide side chain on Asn-135 of alpha-antithrombin, absent in beta-antithrombin, decreases the heparin affinity of the inhibitor by affecting the heparin-induced conformational change. Heparin 159-166 serpin family C member 1 Homo sapiens 51-63 9184148-1 1997 The beta-form of antithrombin, lacking a carbohydrate side chain on Asn-135, is known to bind heparin more tightly than the fully glycosylated alpha-form. Carbohydrates 41-53 serpin family C member 1 Homo sapiens 17-29 9184148-1 1997 The beta-form of antithrombin, lacking a carbohydrate side chain on Asn-135, is known to bind heparin more tightly than the fully glycosylated alpha-form. Asparagine 68-71 serpin family C member 1 Homo sapiens 17-29 9184148-1 1997 The beta-form of antithrombin, lacking a carbohydrate side chain on Asn-135, is known to bind heparin more tightly than the fully glycosylated alpha-form. Heparin 94-101 serpin family C member 1 Homo sapiens 17-29 9184148-2 1997 The molecular basis for this difference in affinity was elucidated by rapid-kinetic studies of the binding of heparin and the antithrombin-binding heparin pentasaccharide to plasma and recombinant forms of alpha- and beta-antithrombin. Heparin 110-117 serpin family C member 1 Homo sapiens 222-234 9184148-2 1997 The molecular basis for this difference in affinity was elucidated by rapid-kinetic studies of the binding of heparin and the antithrombin-binding heparin pentasaccharide to plasma and recombinant forms of alpha- and beta-antithrombin. IC 831423 147-170 serpin family C member 1 Homo sapiens 126-138 9184148-2 1997 The molecular basis for this difference in affinity was elucidated by rapid-kinetic studies of the binding of heparin and the antithrombin-binding heparin pentasaccharide to plasma and recombinant forms of alpha- and beta-antithrombin. IC 831423 147-170 serpin family C member 1 Homo sapiens 222-234 9184148-3 1997 The dissociation equilibrium constant for the first step of the two-step mechanism of binding of both heparin and pentasaccharide to alpha-antithrombin was only slightly higher than that for the binding to the beta-form. Heparin 102-109 serpin family C member 1 Homo sapiens 139-151 9184148-3 1997 The dissociation equilibrium constant for the first step of the two-step mechanism of binding of both heparin and pentasaccharide to alpha-antithrombin was only slightly higher than that for the binding to the beta-form. pentasaccharide 114-129 serpin family C member 1 Homo sapiens 139-151 9184148-4 1997 The oligosaccharide at Asn-135 thus at most moderately interferes with the initial, weak binding of heparin to alpha-antithrombin. Oligosaccharides 4-19 serpin family C member 1 Homo sapiens 117-129 9184148-4 1997 The oligosaccharide at Asn-135 thus at most moderately interferes with the initial, weak binding of heparin to alpha-antithrombin. asn-135 23-30 serpin family C member 1 Homo sapiens 117-129 9184148-4 1997 The oligosaccharide at Asn-135 thus at most moderately interferes with the initial, weak binding of heparin to alpha-antithrombin. Heparin 100-107 serpin family C member 1 Homo sapiens 117-129 9184148-5 1997 In contrast, the rate constant for the conformational change induced by heparin and pentasaccharide in the second binding step was substantially lower for alpha-antithrombin than for beta-antithrombin. Heparin 72-79 serpin family C member 1 Homo sapiens 161-173 9184148-5 1997 In contrast, the rate constant for the conformational change induced by heparin and pentasaccharide in the second binding step was substantially lower for alpha-antithrombin than for beta-antithrombin. Heparin 72-79 serpin family C member 1 Homo sapiens 188-200 9184148-5 1997 In contrast, the rate constant for the conformational change induced by heparin and pentasaccharide in the second binding step was substantially lower for alpha-antithrombin than for beta-antithrombin. pentasaccharide 84-99 serpin family C member 1 Homo sapiens 161-173 9184148-5 1997 In contrast, the rate constant for the conformational change induced by heparin and pentasaccharide in the second binding step was substantially lower for alpha-antithrombin than for beta-antithrombin. pentasaccharide 84-99 serpin family C member 1 Homo sapiens 188-200 9184148-7 1997 The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change. Carbohydrates 4-16 serpin family C member 1 Homo sapiens 82-94 9184148-7 1997 The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change. Asparagine 31-34 serpin family C member 1 Homo sapiens 82-94 9184148-7 1997 The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change. Heparin 56-63 serpin family C member 1 Homo sapiens 82-94 9184148-7 1997 The carbohydrate side chain at Asn-135 thus reduces the heparin affinity of alpha-antithrombin primarily by interfering with the heparin-induced conformational change. Heparin 129-136 serpin family C member 1 Homo sapiens 82-94 9184148-8 1997 These and previous results suggest a model in which the Asn-135 oligosaccharide of alpha-antithrombin is oriented away from the heparin binding site and does not interfere with the first step of heparin binding. asn-135 oligosaccharide 56-79 serpin family C member 1 Homo sapiens 89-101 9184148-8 1997 These and previous results suggest a model in which the Asn-135 oligosaccharide of alpha-antithrombin is oriented away from the heparin binding site and does not interfere with the first step of heparin binding. Heparin 128-135 serpin family C member 1 Homo sapiens 89-101 9184148-11 1997 This effect results in a higher energy for inducing the activated conformation in alpha-antithrombin, leading to a decrease in heparin binding affinity. Heparin 127-134 serpin family C member 1 Homo sapiens 88-100 9184748-6 1997 ATIII could be bound to the surface modified with alb-hep conjugate but not to a polystyrene surface modified with albumin. alb-hep 50-57 serpin family C member 1 Homo sapiens 0-5 9217177-5 1997 Serum cholesterol and triglyceride were associated with increases in factors VII and IX, as well as antithrombin, protein C and protein S; and with increased fibrinogen and factor VIII in women. Cholesterol 6-17 serpin family C member 1 Homo sapiens 100-112 9184748-7 1997 Rabbit anti-human ATIII did bind to the alb-hep surface previously exposed to ATIII, confirming the presence of surface bound ATIII. alb-hep 40-47 serpin family C member 1 Homo sapiens 18-23 9184748-7 1997 Rabbit anti-human ATIII did bind to the alb-hep surface previously exposed to ATIII, confirming the presence of surface bound ATIII. alb-hep 40-47 serpin family C member 1 Homo sapiens 78-83 9184748-7 1997 Rabbit anti-human ATIII did bind to the alb-hep surface previously exposed to ATIII, confirming the presence of surface bound ATIII. alb-hep 40-47 serpin family C member 1 Homo sapiens 78-83 9184748-8 1997 The alb-hep immobilized surface was able to bind much more thrombin than ATIII, which is probably due to the less specific heparin-thrombin interaction as compared to the heparin-ATIII interaction. epolamine 8-11 serpin family C member 1 Homo sapiens 73-78 9184748-8 1997 The alb-hep immobilized surface was able to bind much more thrombin than ATIII, which is probably due to the less specific heparin-thrombin interaction as compared to the heparin-ATIII interaction. epolamine 8-11 serpin family C member 1 Homo sapiens 179-184 9184748-8 1997 The alb-hep immobilized surface was able to bind much more thrombin than ATIII, which is probably due to the less specific heparin-thrombin interaction as compared to the heparin-ATIII interaction. Heparin 123-130 serpin family C member 1 Homo sapiens 73-78 9199820-8 1997 AT levels correlated with vWF (rs = - 0.73, P < 0.01) and creatinine (Rs = -0.70, P < 0.01). Creatinine 61-71 serpin family C member 1 Homo sapiens 0-2 9217177-5 1997 Serum cholesterol and triglyceride were associated with increases in factors VII and IX, as well as antithrombin, protein C and protein S; and with increased fibrinogen and factor VIII in women. Triglycerides 22-34 serpin family C member 1 Homo sapiens 100-112 9217177-7 1997 Smoking status and/or smoking markers were related to fibrinogen, factor IX, antithrombin and protein S. Alcohol intake was related to protein S, and inversely to fibrinogen and antithrombin in men. Alcohols 105-112 serpin family C member 1 Homo sapiens 178-190 9153200-4 1997 Zinc concentrations as low as 1.25 microM revealed HRG to be a powerful competitor of antithrombin for heparin in the purified component assays. Heparin 103-110 serpin family C member 1 Homo sapiens 86-98 9212075-3 1997 For example, it is well known that the sulfate groups are directly involved in the molecular interaction between heparin and antithrombin III. Sulfates 39-46 serpin family C member 1 Homo sapiens 125-141 9212075-3 1997 For example, it is well known that the sulfate groups are directly involved in the molecular interaction between heparin and antithrombin III. Heparin 113-120 serpin family C member 1 Homo sapiens 125-141 15619827-4 1997 The results suggested that plasma heparin may be one of factors resulting in decreased BPC and defect platelet function in HFRS patients with 80% AT-III: alpha or above. Heparin 34-41 serpin family C member 1 Homo sapiens 146-152 9169495-8 1997 These mechanisms include: first, heparin enhancement of antithrombin III-dependent inhibition of factor V activation by thrombin; second, the inactivation of membrane-bound FVa by APC; and third, the proteolytic inactivation of membrane-bound factor V by APC, which is enhanced by heparin. Heparin 33-40 serpin family C member 1 Homo sapiens 56-72 9153200-8 1997 The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded. Zinc 8-10 serpin family C member 1 Homo sapiens 45-57 9153200-8 1997 The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded. Zinc 8-10 serpin family C member 1 Homo sapiens 123-135 9153200-8 1997 The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded. Heparin 62-69 serpin family C member 1 Homo sapiens 45-57 9153200-8 1997 The HRG.Zn complex effectively competes with antithrombin for heparin, which restricts the availability of heparin to bind antithrombin and allows thrombin-mediated fibrinogenesis to proceed unimpeded. Heparin 62-69 serpin family C member 1 Homo sapiens 123-135 9153200-7 1997 Investigation of other divalent cations (copper and magnesium) indicated that augmentation of heparin binding by HRG in the presence of antithrombin was restricted to zinc. Heparin 94-101 serpin family C member 1 Homo sapiens 136-148 9187023-2 1997 Heparin augments the inhibitory activity of antithrombin (AT) towards thrombin, factor Xa (FXa) and other activated clotting enzymes. Heparin 0-7 serpin family C member 1 Homo sapiens 44-56 9169007-0 1997 Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity. Carbohydrates 21-33 serpin family C member 1 Homo sapiens 56-68 9169007-13 1997 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. Heparin 197-204 serpin family C member 1 Homo sapiens 67-79 9169007-0 1997 Effect of individual carbohydrate chains of recombinant antithrombin on heparin affinity and on the generation of glycoforms differing in heparin affinity. Heparin 72-79 serpin family C member 1 Homo sapiens 56-68 9158859-0 1997 Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): creation of a novel antithrombin surface. Polyethylene Terephthalates 43-71 serpin family C member 1 Homo sapiens 102-114 9169007-1 1997 Two major glycoforms of recombinant antithrombin which differ 10-fold in their affinity for the effector glycosaminoglycan, heparin, were previously shown to be expressed in BHK or CHO mammalian cell lines (I. Bjork, et al., 1992, Biochem. Glycosaminoglycans 105-122 serpin family C member 1 Homo sapiens 36-48 9169007-1 1997 Two major glycoforms of recombinant antithrombin which differ 10-fold in their affinity for the effector glycosaminoglycan, heparin, were previously shown to be expressed in BHK or CHO mammalian cell lines (I. Bjork, et al., 1992, Biochem. Heparin 124-131 serpin family C member 1 Homo sapiens 36-48 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Heparin 0-7 serpin family C member 1 Homo sapiens 43-55 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Sepharose 8-15 serpin family C member 1 Homo sapiens 43-55 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Glutamine 79-82 serpin family C member 1 Homo sapiens 43-55 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Glutamine 87-90 serpin family C member 1 Homo sapiens 43-55 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Glutamine 87-90 serpin family C member 1 Homo sapiens 43-55 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Heparin 152-159 serpin family C member 1 Homo sapiens 43-55 9169007-8 1997 Heparin-agarose chromatography of the four antithrombin variants revealed that Gln 96, Gln 135, and Gln 192 variants still displayed the two functional heparin-affinity forms previously observed with the wild-type inhibitor, whereas the Gln 155 variant showed only a single functional high heparin affinity form. Glutamine 87-90 serpin family C member 1 Homo sapiens 43-55 9169007-9 1997 These results demonstrate that heterogeneous glycosylation of Asn 155 of recombinant antithrombin is responsible for generating the low heparin affinity glycoform. Asparagine 62-65 serpin family C member 1 Homo sapiens 85-97 9169007-10 1997 Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity. Heparin 12-19 serpin family C member 1 Homo sapiens 226-238 9169007-10 1997 Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity. Heparin 42-49 serpin family C member 1 Homo sapiens 226-238 9169007-10 1997 Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity. Heparin 42-49 serpin family C member 1 Homo sapiens 226-238 9169007-10 1997 Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity. Heparin 42-49 serpin family C member 1 Homo sapiens 226-238 9169007-10 1997 Analysis of heparin binding to the higher heparin affinity forms of the four variants showed that all exhibited increased heparin affinities of two- to sevenfold compared to wild-type higher heparin affinity form or to plasma antithrombin, with the Gln 135 variant showing the largest effect on this affinity. Glutamine 249-252 serpin family C member 1 Homo sapiens 226-238 9169007-11 1997 The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin. Heparin 14-21 serpin family C member 1 Homo sapiens 173-185 9169007-11 1997 The extent of heparin-affinity enhancement was correlated with the distance of the mutated glycosylation site to the putative heparin-binding site in the X-ray structure of antithrombin. Heparin 126-133 serpin family C member 1 Homo sapiens 173-185 9169007-13 1997 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. Carbohydrates 32-44 serpin family C member 1 Homo sapiens 67-79 9169007-13 1997 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. Carbohydrates 32-44 serpin family C member 1 Homo sapiens 221-233 9169007-13 1997 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. Heparin 97-104 serpin family C member 1 Homo sapiens 67-79 9169007-13 1997 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. Heparin 97-104 serpin family C member 1 Homo sapiens 221-233 9169007-13 1997 These results indicate that all carbohydrate chains of recombinant antithrombin adversely affect heparin-binding affinity to an extent that correlates with their relative proximity to the putative heparin-binding site in antithrombin. Heparin 197-204 serpin family C member 1 Homo sapiens 221-233 9115268-2 1997 Mutations that decreased the susceptibility of thrombin to inhibition by antithrombin III in the presence and absence of heparin (W50A, E229A, and R233A) also decreased hydrolysis of a small tripeptidyl substrate. Heparin 121-128 serpin family C member 1 Homo sapiens 73-89 9158859-0 1997 Covalent linkage of recombinant hirudin to poly(ethylene terephthalate) (Dacron): creation of a novel antithrombin surface. Polyethylene Terephthalates 73-79 serpin family C member 1 Homo sapiens 102-114 9158859-3 1997 The purpose of this study was to covalently immobilize the potent, specific antithrombin agent recombinant hirudin (rHir) to a modified Dacron surface and characterize the in vitro efficacy of thrombin inhibition by this novel biomaterial surface. Polyethylene Terephthalates 136-142 serpin family C member 1 Homo sapiens 76-88 9065421-0 1997 Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation. Lysine 0-6 serpin family C member 1 Homo sapiens 28-44 9213829-9 1997 Heparansulphate and sulodexide were able to reduce signs and symptoms with similar degree and to significantly modify t-PA, alpha 2-antiplasmin and ATIII levels without any difference between treatments. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 148-153 9213829-9 1997 Heparansulphate and sulodexide were able to reduce signs and symptoms with similar degree and to significantly modify t-PA, alpha 2-antiplasmin and ATIII levels without any difference between treatments. glucuronyl glucosamine glycan sulfate 20-30 serpin family C member 1 Homo sapiens 148-153 9251237-4 1997 The diverse functions of heparan sulphate, which range from the control of blood coagulation to the regulation of cell growth and adhesion, depend on the capacity of the chains to activate protein ligands, such as antithrombin III and members of the fibroblast growth factor family. Heparitin Sulfate 25-41 serpin family C member 1 Homo sapiens 214-230 9147040-0 1997 A unique trisaccharide sequence in heparin mediates the early step of antithrombin III activation. Trisaccharides 9-22 serpin family C member 1 Homo sapiens 70-86 9147040-0 1997 A unique trisaccharide sequence in heparin mediates the early step of antithrombin III activation. Heparin 35-42 serpin family C member 1 Homo sapiens 70-86 9147040-1 1997 Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation. Trisaccharides 47-61 serpin family C member 1 Homo sapiens 115-131 9147040-1 1997 Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation. Trisaccharides 47-61 serpin family C member 1 Homo sapiens 133-139 9147040-1 1997 Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation. Trisaccharides 47-61 serpin family C member 1 Homo sapiens 241-247 9147040-1 1997 Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation. Trisaccharides 47-60 serpin family C member 1 Homo sapiens 115-131 9147040-1 1997 Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation. Trisaccharides 47-60 serpin family C member 1 Homo sapiens 133-139 9147040-1 1997 Spectrofluorimetry experiments using synthetic trisaccharides indicate that in compounds that display affinity for antithrombin III (AT-III), a unique trisaccharide sequence plays the key role in the early recognition, and the first step of AT-III activation. Trisaccharides 47-60 serpin family C member 1 Homo sapiens 241-247 9065421-0 1997 Lysine residue 114 in human antithrombin III is required for heparin pentasaccharide-mediated activation. IC 831423 61-84 serpin family C member 1 Homo sapiens 28-44 9065421-2 1997 The purified proteins were used to evaluate the potential role(s) of these residues in the pentasaccharide-mediated activation of ATIII. pentasaccharide 91-106 serpin family C member 1 Homo sapiens 130-135 9065421-5 1997 In contrast, lysine 114 was found to be critical in the activation of ATIII toward factor Xa. Lysine 13-19 serpin family C member 1 Homo sapiens 70-75 9065421-6 1997 No activation was observed, even at a pentasaccharide concentration 10 times higher than that required to activate recombinant native ATIII. pentasaccharide 38-53 serpin family C member 1 Homo sapiens 134-139 9065421-7 1997 These data are the first to demonstrate a pivotal role for lysine 114 in the pentasaccharide-mediated activation of ATIII. Lysine 59-65 serpin family C member 1 Homo sapiens 116-121 9065421-7 1997 These data are the first to demonstrate a pivotal role for lysine 114 in the pentasaccharide-mediated activation of ATIII. pentasaccharide 77-92 serpin family C member 1 Homo sapiens 116-121 9140889-1 1997 Heparan sulfate proteoglycans produced by vascular endothelium may function physiologically to restrain the migration, multiplication, and phenotypic transition of vascular smooth-muscle cells, and to maintain an anticoagulant luminal surface by bonding and activating antithrombin III. heparan 0-7 serpin family C member 1 Homo sapiens 269-285 9130607-2 1997 Our results confirmed the predictions: under very strict conditions of pH (6.3), CaCl2 concentration (2 mM), ionic strength (25 mM) and protein/heparin ratio (1/1), the first component of the complement recognizes the high antithrombin III affinity fraction of heparin, and allows a concentration of the biological activity of the original low molecular weight-heparin. Calcium Chloride 81-86 serpin family C member 1 Homo sapiens 223-239 9130607-2 1997 Our results confirmed the predictions: under very strict conditions of pH (6.3), CaCl2 concentration (2 mM), ionic strength (25 mM) and protein/heparin ratio (1/1), the first component of the complement recognizes the high antithrombin III affinity fraction of heparin, and allows a concentration of the biological activity of the original low molecular weight-heparin. Heparin 261-268 serpin family C member 1 Homo sapiens 223-239 9130607-2 1997 Our results confirmed the predictions: under very strict conditions of pH (6.3), CaCl2 concentration (2 mM), ionic strength (25 mM) and protein/heparin ratio (1/1), the first component of the complement recognizes the high antithrombin III affinity fraction of heparin, and allows a concentration of the biological activity of the original low molecular weight-heparin. Heparin 261-268 serpin family C member 1 Homo sapiens 223-239 9076381-3 1997 The effects of heparin may be partly counteracted by a decrease in antithrombin (III). Heparin 15-22 serpin family C member 1 Homo sapiens 67-79 9076381-7 1997 Treatment targeted to an antithrombin level of 120% was started with a 2h intravenous infusion before the percutaneous transluminal coronary angioplasty and was repeated, if there were further subnormal values, every 12th hour for 48 h. RESULTS: Angiographic success was 20/25 in the antithrombin group and 21/25 in the placebo group (ns). Deuterium 71-73 serpin family C member 1 Homo sapiens 25-37 9050848-3 1997 Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity. Heparin 35-42 serpin family C member 1 Homo sapiens 141-157 9050848-3 1997 Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity. Heparin 35-42 serpin family C member 1 Homo sapiens 159-165 9050848-3 1997 Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity. Heparin 192-199 serpin family C member 1 Homo sapiens 141-157 9050848-3 1997 Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin"s anticoagulant activity. Heparin 192-199 serpin family C member 1 Homo sapiens 159-165 9050848-4 1997 The HIP peptide was shown to compete with AT-III for binding to heparin and to neutralize the anticoagulant activity of heparin in blood plasma assays. Heparin 64-71 serpin family C member 1 Homo sapiens 42-48 9147313-3 1997 The results obtained strongly suggest that the procoagulant activity of SV-IV/A is due, like SV-IV, to a selective inhibition of the antithrombin III (AT III) activation process induced by heparin, an essential cofactor of AT III. Heparin 189-196 serpin family C member 1 Homo sapiens 133-149 15622771-0 1997 [The antithrombin action of stichopus japonicus acid mucopolysaccharide (Sjamp) is mediated by heparin cofactor II]. sjamp 73-78 serpin family C member 1 Homo sapiens 5-17 15622771-4 1997 CONCLUSION: Sjamp was similar to dermatan sulfate both in the efficiency and in the mechanism of antithrombin. Dermatan Sulfate 33-49 serpin family C member 1 Homo sapiens 97-109 9067613-0 1997 The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site. Heparin 77-84 serpin family C member 1 Homo sapiens 23-35 9067613-8 1997 In particular, the observed hydrogen bonding of these residues to the body of the molecule in the latent form explains the mechanism for the release of newly formed antithrombin-protease complexes into the circulation for catabolic removal. Hydrogen 28-36 serpin family C member 1 Homo sapiens 165-177 9211051-1 1997 Heparin, the most widely used antithrombin, suffers several limitations, including high inter-individual variability of anticoagulant response, a nonlinear dose-response curve, inability to inactivate clot-bound thrombin, a requirement for endogenous cofactors and inactivation by platelet factor 4 and heparinase. Heparin 0-7 serpin family C member 1 Homo sapiens 30-42 9147313-3 1997 The results obtained strongly suggest that the procoagulant activity of SV-IV/A is due, like SV-IV, to a selective inhibition of the antithrombin III (AT III) activation process induced by heparin, an essential cofactor of AT III. Heparin 189-196 serpin family C member 1 Homo sapiens 151-157 9147313-3 1997 The results obtained strongly suggest that the procoagulant activity of SV-IV/A is due, like SV-IV, to a selective inhibition of the antithrombin III (AT III) activation process induced by heparin, an essential cofactor of AT III. Heparin 189-196 serpin family C member 1 Homo sapiens 223-229 9013799-8 1997 These results suggest that the fibrinolytic factor release and the antithrombin binding of vascular endothelial cells are impaired by the attack of 15-HPETE, and that the presence of antioxidants prevents the injurious action of lipid hydroperoxide. Lipid Peroxides 229-248 serpin family C member 1 Homo sapiens 67-79 9018048-7 1997 The cofactor heparin compensated partially for the loss of interactions with Ser195; it increased the affinity of S195A for protease nexin-1 and antithrombin by 140-fold and 1000-fold, respectively. Heparin 13-20 serpin family C member 1 Homo sapiens 145-157 8994426-0 1997 Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate. Heparin 98-105 serpin family C member 1 Homo sapiens 56-68 8994426-0 1997 Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate. Heparin 128-135 serpin family C member 1 Homo sapiens 56-68 8994426-0 1997 Effect of nonspecific binding to plasma proteins on the antithrombin activities of unfractionated heparin, low-molecular-weight heparin, and dermatan sulfate. Dermatan Sulfate 141-157 serpin family C member 1 Homo sapiens 56-68 8994426-6 1997 The addition of a chemically modified heparin with low affinity for antithrombin III to plasma containing UFH increased the anti-IIa activity in a concentration-dependent fashion by displacing UFH from plasma proteins. Heparin 38-45 serpin family C member 1 Homo sapiens 68-84 9017120-3 1997 The thrombin-like enzyme with Gly-Pro-Arg-pNA amidolytic activity was inhibited by human seminal plasma trypsin-like enzyme inhibitor (HSP-TI) and antithrombin III. gly-pro-arg-pna 30-45 serpin family C member 1 Homo sapiens 147-163 9195333-3 1997 In this study, to recognize the mechanism of anticoagulant activity of poly(GEMA)-sulfate, we estimated the binding capacity of antithrombin III to thrombin and some in vitro clotting tests in the presence of poly(GEMA)-sulfate. poly(glucosyloxyethyl methacrylate) sulfate 71-89 serpin family C member 1 Homo sapiens 128-144 9868079-4 1997 Low molecular weight heparin (LMWH) prolonged significantly PT and APTT, and this effect ws weakened by an antibody against human AT III. Heparin 21-28 serpin family C member 1 Homo sapiens 130-136 9868079-4 1997 Low molecular weight heparin (LMWH) prolonged significantly PT and APTT, and this effect ws weakened by an antibody against human AT III. Heparin, Low-Molecular-Weight 30-34 serpin family C member 1 Homo sapiens 130-136 9476567-3 1997 Aspirin and heparin have been used as therapeutic mainstays for acute coronary syndromes, acting as antiplatelet and antithrombin agents, respectively. Aspirin 0-7 serpin family C member 1 Homo sapiens 117-129 9476567-3 1997 Aspirin and heparin have been used as therapeutic mainstays for acute coronary syndromes, acting as antiplatelet and antithrombin agents, respectively. Heparin 12-19 serpin family C member 1 Homo sapiens 117-129 9195333-3 1997 In this study, to recognize the mechanism of anticoagulant activity of poly(GEMA)-sulfate, we estimated the binding capacity of antithrombin III to thrombin and some in vitro clotting tests in the presence of poly(GEMA)-sulfate. poly(glucosyloxyethyl methacrylate) sulfate 209-227 serpin family C member 1 Homo sapiens 128-144 10214462-3 1997 Significantly higher levels of F VIIC and AT III were found only in the MI-NLP group. NORLEUCINE PHOSPHONATE 75-78 serpin family C member 1 Homo sapiens 42-48 9031474-0 1997 A 5-nucleotide insertion in the antithrombin gene causing a quantitative antithrombin deficiency. 5-nucleotide 2-14 serpin family C member 1 Homo sapiens 32-44 9469623-6 1997 For coronary artery disease in patients with deficiency of antithrombin activities attributable to either antithrombin III or heparin cofactor II deficiency, argatroban is effective as an anticoagulant. argatroban 158-168 serpin family C member 1 Homo sapiens 59-71 9469623-6 1997 For coronary artery disease in patients with deficiency of antithrombin activities attributable to either antithrombin III or heparin cofactor II deficiency, argatroban is effective as an anticoagulant. argatroban 158-168 serpin family C member 1 Homo sapiens 106-122 9469625-1 1997 Argatroban is a direct antithrombin agent developed for the first time by Okamoto et al in 1978. argatroban 0-10 serpin family C member 1 Homo sapiens 23-35 8983127-4 1997 The dissociation constants of the ATIII-pentasaccharide complex formed by SR 90107A/ORG 31540 and by two close analogues: SR 80327A and SR 80027A in the presence of purified human ATIII were found to be 41 +/- 8, 96 +/- 1 and 3 +/- 1.4 nM (mean +/- sem, n = 3) respectively. SR 80327A 122-131 serpin family C member 1 Homo sapiens 34-39 9031474-0 1997 A 5-nucleotide insertion in the antithrombin gene causing a quantitative antithrombin deficiency. 5-nucleotide 2-14 serpin family C member 1 Homo sapiens 73-85 9092408-2 1996 Recently, molecules have been developed which either catalyse the inactivation of factor Xa by the antithrombin (pentasaccharide) or directly inhibit factor Xa (synthetic inhibitor or peptides extracted from the saliva of tics or leeches). pentasaccharide 113-128 serpin family C member 1 Homo sapiens 99-111 8943254-0 1996 Enzymatic preparation of heparin oligosaccharides containing antithrombin III binding sites. heparin oligosaccharides 25-49 serpin family C member 1 Homo sapiens 61-73 8943254-1 1996 Two new oligosaccharides were prepared from heparin by its partial depolymerization using heparin lyase I (EC 4.2.2.7) in an attempt to prepare oligosaccharides having intact antithrombin III binding sites. Oligosaccharides 8-24 serpin family C member 1 Homo sapiens 175-187 8943254-1 1996 Two new oligosaccharides were prepared from heparin by its partial depolymerization using heparin lyase I (EC 4.2.2.7) in an attempt to prepare oligosaccharides having intact antithrombin III binding sites. Heparin 44-51 serpin family C member 1 Homo sapiens 175-187 8943254-1 1996 Two new oligosaccharides were prepared from heparin by its partial depolymerization using heparin lyase I (EC 4.2.2.7) in an attempt to prepare oligosaccharides having intact antithrombin III binding sites. Oligosaccharides 144-160 serpin family C member 1 Homo sapiens 175-187 8943254-5 1996 A hexasaccharide containing a similar structural motif to that found in the antithrombin III binding site and having greatly reduced anticoagulant activity was also isolated. hexasaccharide 2-16 serpin family C member 1 Homo sapiens 76-92 8943254-8 1996 Sufficient quantities of the decasaccharide were obtained to examine its interaction with antithrombin III using microtitration calorimetry. decasaccharide 29-43 serpin family C member 1 Homo sapiens 90-106 8943254-9 1996 This decasaccharide bound to antithrombin III with similar avidity as heparin and showed comparable anticoagulant activity, as determined using an antithrombin III dependent anti-factor Xa assay. decasaccharide 5-19 serpin family C member 1 Homo sapiens 29-45 8943254-9 1996 This decasaccharide bound to antithrombin III with similar avidity as heparin and showed comparable anticoagulant activity, as determined using an antithrombin III dependent anti-factor Xa assay. decasaccharide 5-19 serpin family C member 1 Homo sapiens 147-163 8943254-10 1996 Interestingly, while both decasaccharide and heparin bound to antithrombin with nanomolar affinity, very little heat of binding was observed. decasaccharide 26-40 serpin family C member 1 Homo sapiens 62-74 8943254-10 1996 Interestingly, while both decasaccharide and heparin bound to antithrombin with nanomolar affinity, very little heat of binding was observed. Heparin 45-52 serpin family C member 1 Homo sapiens 62-74 9013237-4 1996 Following the debridement under control of diabetes mellitus, antimicrobial agents and argatroban, a newly synthesized antithrombin medicine, were administered. argatroban 87-97 serpin family C member 1 Homo sapiens 119-131 8910598-0 1996 Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. Arginine 8-16 serpin family C member 1 Homo sapiens 76-88 8910598-0 1996 Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. Lysine 25-31 serpin family C member 1 Homo sapiens 76-88 8910598-0 1996 Role of arginine 132 and lysine 133 in heparin binding to and activation of antithrombin. Heparin 39-46 serpin family C member 1 Homo sapiens 76-88 8910598-1 1996 The binding of heparin to antithrombin greatly accelerates the rate of inhibition of the target proteinases thrombin and factor Xa. Heparin 15-22 serpin family C member 1 Homo sapiens 26-38 8910598-2 1996 Acceleration of the rate of inhibition of factor Xa involves a conformational change in antithrombin that is translated from the heparin binding site to the reactive center loop. Heparin 129-136 serpin family C member 1 Homo sapiens 88-100 8910598-3 1996 A mechanism has been proposed for generation and propagation of the conformational change in which the binding of the negatively charged heparin reduces ionic repulsions between positively charged residues on and adjacent to the D-helix in the heparin binding site of antithrombin (van Boeckel, C. A. Heparin 137-144 serpin family C member 1 Homo sapiens 268-280 8910598-3 1996 A mechanism has been proposed for generation and propagation of the conformational change in which the binding of the negatively charged heparin reduces ionic repulsions between positively charged residues on and adjacent to the D-helix in the heparin binding site of antithrombin (van Boeckel, C. A. Heparin 244-251 serpin family C member 1 Homo sapiens 268-280 9141800-12 1996 Steroid therapy significantly increased the levels of proteins C, protein S. AT-III and fibrinogen as compared to controls. Steroids 0-7 serpin family C member 1 Homo sapiens 77-83 8958394-0 1996 Homozygous variant of antithrombin with lack of affinity for heparin: management of severe thrombotic complications associated with intrauterine fetal demise. Heparin 61-68 serpin family C member 1 Homo sapiens 22-34 8900197-1 1996 LTA cells synthesize a minor population of heparan sulfate proteoglycans (HSPGact) bearing anticoagulant heparan sulfate (HSact) with a specific monosaccharide sequence that accelerates the action of antithrombin (AT). Heparitin Sulfate 43-58 serpin family C member 1 Homo sapiens 200-212 8900197-1 1996 LTA cells synthesize a minor population of heparan sulfate proteoglycans (HSPGact) bearing anticoagulant heparan sulfate (HSact) with a specific monosaccharide sequence that accelerates the action of antithrombin (AT). Monosaccharides 145-159 serpin family C member 1 Homo sapiens 200-212 8951806-6 1996 Numerous studies indicate that in the case of thinning of the anionic glycosaminoglycan film on the endothelial surface, the lipoprotein-lipase and antithrombin III activity induced by heparin is reduced, as result of which hyperlipoproteinaemia and increased tendency to thrombosis can only by compensated for to an inadequate extent. Glycosaminoglycans 70-87 serpin family C member 1 Homo sapiens 148-164 8951806-6 1996 Numerous studies indicate that in the case of thinning of the anionic glycosaminoglycan film on the endothelial surface, the lipoprotein-lipase and antithrombin III activity induced by heparin is reduced, as result of which hyperlipoproteinaemia and increased tendency to thrombosis can only by compensated for to an inadequate extent. Heparin 185-192 serpin family C member 1 Homo sapiens 148-164 8898593-8 1996 Regular alcohol intake predicted multiple changes in vascular risk factors over a five year period including increased concentrations of high density lipoprotein cholesterol and apolipoprotein A I; higher blood pressure; and decreased concentration of antithrombin III. Alcohols 8-15 serpin family C member 1 Homo sapiens 252-268 8900394-0 1996 Structure-function relations of antithrombin III-heparin interactions as assessed by biophysical and biological assays and molecular modeling of peptide-pentasaccharide-docked complexes. Heparin 49-56 serpin family C member 1 Homo sapiens 32-48 8900394-0 1996 Structure-function relations of antithrombin III-heparin interactions as assessed by biophysical and biological assays and molecular modeling of peptide-pentasaccharide-docked complexes. pentasaccharide 153-168 serpin family C member 1 Homo sapiens 32-48 8900394-2 1996 ATIII attains its full biological activity only upon binding polysulfated glycosaminoglycans, such as heparin. A73025 61-92 serpin family C member 1 Homo sapiens 0-5 8900394-2 1996 ATIII attains its full biological activity only upon binding polysulfated glycosaminoglycans, such as heparin. Heparin 102-109 serpin family C member 1 Homo sapiens 0-5 8900394-4 1996 3, 620-627, 1994) to encompass part (or all) of the purported high-affinity heparin binding region of ATIII. Heparin 76-83 serpin family C member 1 Homo sapiens 102-107 8900394-6 1996 In one case, the Arg residue of the reference peptide corresponding to R129 of ATIII has been replaced by Gln (R129deltaQ peptide), thus mimicking the naturally occurring mutant protein, ATIII Geneva. Arginine 17-20 serpin family C member 1 Homo sapiens 79-84 8900394-6 1996 In one case, the Arg residue of the reference peptide corresponding to R129 of ATIII has been replaced by Gln (R129deltaQ peptide), thus mimicking the naturally occurring mutant protein, ATIII Geneva. Glutamine 106-109 serpin family C member 1 Homo sapiens 187-192 8900394-10 1996 Furthermore, each of the Ala-replacement peptides was a less-effective inhibitor of ATIII-heparin complex formation than the reference peptide. Heparin 90-97 serpin family C member 1 Homo sapiens 84-89 8900394-17 1996 The observations from molecular modeling allow us to suggest that ATIII Geneva displays decreased heparin binding affinity due to its inability to form a productive binding complex in which essential electrostatic contacts are made between suitably juxtaposed saccharide anionic functional groups and cationic amino acid side chains. Heparin 98-105 serpin family C member 1 Homo sapiens 66-71 8958394-1 1996 Patients with homozygous heparin-binding-site (HBS) qualitative antithrombin deficiencies are at significant risk of venous and arterial thrombosis. Heparin 25-32 serpin family C member 1 Homo sapiens 64-76 8902986-4 1996 The corresponding region of antithrombin III gene is affected by a cluster of frameshift mutations suggesting that heparin cofactor II and antithrombin III could share similar mutational patterns. Heparin 115-122 serpin family C member 1 Homo sapiens 28-44 8915986-3 1996 The anticoagulant action of heparin is mediated by antithrombin III. Heparin 28-35 serpin family C member 1 Homo sapiens 51-67 8915986-8 1996 The magnitude of the inhibitory action of antithrombin III was equal to that of equimolar concentrations of heparin and that observed with the combination of the two. Heparin 108-115 serpin family C member 1 Homo sapiens 42-58 8905024-9 1996 Significant reductions of plasma fibrinogen by 14% and AT III by 8% were seen in women who received tamoxifen. Tamoxifen 100-109 serpin family C member 1 Homo sapiens 55-61 8885144-3 1996 Unlike heparin, DS does not act through Antithrombin III (ATIII) but primarily through thrombin on Heparin Cofactor II (HCII). Dermatan Sulfate 16-18 serpin family C member 1 Homo sapiens 58-63 8798631-9 1996 Assays with purified reagents show that the fucosylated chondroitin sulfate can potentiate the thrombin inhibition activity of both antithrombin and heparin cofactor II. Chondroitin Sulfates 56-75 serpin family C member 1 Homo sapiens 132-144 8790074-8 1996 Naturally occurring anticoagulant proteins such as antithrombin and protein C fell slightly in women treated with tamoxifen. Tamoxifen 114-123 serpin family C member 1 Homo sapiens 51-63 8702852-0 1996 Requirement of lysine residues outside of the proposed pentasaccharide binding region for high affinity heparin binding and activation of human antithrombin III. Lysine 15-21 serpin family C member 1 Homo sapiens 144-160 8781492-3 1996 It is analogue of the "synthetic pentasaccharide" (SR 90107/ORG 31540), which represents the antithrombin III (AT-III) binding site of heparin. pentasaccharide 33-48 serpin family C member 1 Homo sapiens 111-117 8781492-3 1996 It is analogue of the "synthetic pentasaccharide" (SR 90107/ORG 31540), which represents the antithrombin III (AT-III) binding site of heparin. Heparin 135-142 serpin family C member 1 Homo sapiens 111-117 8781492-4 1996 Like SR 90107, it shows high affinity for human AT-III (Kd = 3.7 +/- 0.7 nmol/L) and is a potent catalyst of its inhibitory effect with regard to factor Xa (1100 +/- 31 versus 850 +/- 27 anti-Xa U/mg for SR 90107). PENTA 5-13 serpin family C member 1 Homo sapiens 48-54 8883279-3 1996 Alcohol use was associated with increased levels of factor X and decreased levels of antithrombin III. Alcohols 0-7 serpin family C member 1 Homo sapiens 85-101 8896339-1 1996 Antithrombin III was purified to homogeneity from hamster plasma by affinity chromatography on heparin-agrose, ion-exchange chromatography on Mono Q and size-exclusion chromatography on TSK G3000SWG column with 50% yield. Heparin 95-102 serpin family C member 1 Homo sapiens 0-16 8896339-1 1996 Antithrombin III was purified to homogeneity from hamster plasma by affinity chromatography on heparin-agrose, ion-exchange chromatography on Mono Q and size-exclusion chromatography on TSK G3000SWG column with 50% yield. agrose 103-109 serpin family C member 1 Homo sapiens 0-16 8896339-2 1996 The molecular mass of hamster antithrombin III was estimated at 62.5 kDa and the absorption coefficient (A280 nm 1%, 1 cm) at 6.48 (in 0.1 M sodium phosphate pH 7.0). sodium phosphate 141-157 serpin family C member 1 Homo sapiens 30-46 8702852-0 1996 Requirement of lysine residues outside of the proposed pentasaccharide binding region for high affinity heparin binding and activation of human antithrombin III. pentasaccharide 55-70 serpin family C member 1 Homo sapiens 144-160 8702852-1 1996 Variant forms of human antithrombin III with glutamine or threonine substitutions at Lys114, Lys125, Lys133, Lys136, and Lys139 were expressed in insect cells to evaluate their roles in heparin binding and activation. Glutamine 45-54 serpin family C member 1 Homo sapiens 23-39 8702852-1 1996 Variant forms of human antithrombin III with glutamine or threonine substitutions at Lys114, Lys125, Lys133, Lys136, and Lys139 were expressed in insect cells to evaluate their roles in heparin binding and activation. Heparin 186-193 serpin family C member 1 Homo sapiens 23-39 8702852-2 1996 Recombinant native ATIII and all of the variants had very similar second order rate constants for thrombin inhibition in the absence of heparin, ranging from 1.13 x 10(5) M-1min-1 to 1.66 x 10(5) M-1min-1. Heparin 136-143 serpin family C member 1 Homo sapiens 19-24 8702852-3 1996 Direct binding studies using 125I-flouresceinamine-heparin yielded a Kd of 6 nM for the recombinant native ATIII and K136T, whereas K114Q and K139Q bound heparin so poorly that a Kd could not be determined. 125i-flouresceinamine-heparin 29-58 serpin family C member 1 Homo sapiens 107-112 8702852-3 1996 Direct binding studies using 125I-flouresceinamine-heparin yielded a Kd of 6 nM for the recombinant native ATIII and K136T, whereas K114Q and K139Q bound heparin so poorly that a Kd could not be determined. Heparin 51-58 serpin family C member 1 Homo sapiens 107-112 8702852-8 1996 Based on these data, Lys114 and Lys139, which are outside of the putative pentasaccharide binding site, play pivotal roles in the high affinity binding of heparin to ATIII and the activation of thrombin inhibitory activity. pentasaccharide 74-89 serpin family C member 1 Homo sapiens 166-171 8702852-8 1996 Based on these data, Lys114 and Lys139, which are outside of the putative pentasaccharide binding site, play pivotal roles in the high affinity binding of heparin to ATIII and the activation of thrombin inhibitory activity. Heparin 155-162 serpin family C member 1 Homo sapiens 166-171 8756699-6 1996 The Phe residue of this epitope is highly conserved in members of the serpin superfamily and appears to stabilize the region of the epitope in antithrombin and other serpins by interacting with the protein core. Phenylalanine 4-7 serpin family C member 1 Homo sapiens 143-155 8761481-4 1996 Stimulation of the hepatoma cell line HepG2 with the receptor ligands L-3,5,3"-tri-iodothyronine, all-trans retinoic acid, or their combination, increased production of antithrombin into the culture medium by 1.3-, 1.6-, and 2.0-fold, respectively. Triiodothyronine 70-96 serpin family C member 1 Homo sapiens 169-181 8761481-4 1996 Stimulation of the hepatoma cell line HepG2 with the receptor ligands L-3,5,3"-tri-iodothyronine, all-trans retinoic acid, or their combination, increased production of antithrombin into the culture medium by 1.3-, 1.6-, and 2.0-fold, respectively. all-trans 98-107 serpin family C member 1 Homo sapiens 169-181 8761481-4 1996 Stimulation of the hepatoma cell line HepG2 with the receptor ligands L-3,5,3"-tri-iodothyronine, all-trans retinoic acid, or their combination, increased production of antithrombin into the culture medium by 1.3-, 1.6-, and 2.0-fold, respectively. Tretinoin 108-121 serpin family C member 1 Homo sapiens 169-181 9528269-0 1996 Clinical evaluation of the efficacy of an antithrombin agent "Argatroban" combined with exercise therapy on increase of the skeletal muscle blood flow. argatroban 62-72 serpin family C member 1 Homo sapiens 42-54 8679610-2 1996 A heparin-induced conformational change is required to convert antithrombin from a slow to a fast inhibitor of factor Xa. Heparin 2-9 serpin family C member 1 Homo sapiens 63-75 8679610-7 1996 1, 423-425] that the reactive center residue P14 is inserted into beta-sheet A in native antithrombin and is displaced from the beta-sheet by heparin binding, thereby altering the conformation of the reactive center and making it a better target for factor Xa binding. Heparin 142-149 serpin family C member 1 Homo sapiens 89-101 8679610-8 1996 To test this hypothesis, we have characterized a P14 serine --> tryptophan antithrombin variant. Serine 53-59 serpin family C member 1 Homo sapiens 78-90 8679610-8 1996 To test this hypothesis, we have characterized a P14 serine --> tryptophan antithrombin variant. Tryptophan 67-77 serpin family C member 1 Homo sapiens 78-90 8679610-9 1996 From changes in tryptophan fluorescence upon heparin binding, increased affinity for heparin, and partial activation of the variant against factor Xa, we conclude that the proposed mechanism of heparin activation is correct with respect to loop expulsion and that it may consequently be possible to create more highly activated antithrombin variants through suitable hinge region substitutions. Tryptophan 16-26 serpin family C member 1 Homo sapiens 328-340 8874869-0 1996 A novel nonsense mutation in the antithrombin III gene (Cys-4-->stop) causing recurrent venous thrombosis. Cysteine 56-59 serpin family C member 1 Homo sapiens 33-49 8874869-1 1996 We describe a novel mutation identified in the antithrombin III (AT-III) propeptide responsible for AT-III deficiency. propeptide 73-83 serpin family C member 1 Homo sapiens 47-63 8874869-1 1996 We describe a novel mutation identified in the antithrombin III (AT-III) propeptide responsible for AT-III deficiency. propeptide 73-83 serpin family C member 1 Homo sapiens 65-71 8908527-3 1996 The use of the 20 micrograms ethinylestradiol formulation was associated with the same pattern of changes, but with lower magnitude (F1+2 + 61.1%, D-dimer +36.0%, antithrombin III -5.3%, protein C +4.6% and protein S-16.0%). Ethinyl Estradiol 29-45 serpin family C member 1 Homo sapiens 163-179 8908527-4 1996 The changes from baseline were significantly smaller in the 20 micrograms ethinylestradiol group for D-dimer, antithrombin III and protein S than in the 30 micrograms ethinylestradiol group (p = 0.019, p = 0.038 and p = 0.001, respectively). Ethinyl Estradiol 74-90 serpin family C member 1 Homo sapiens 110-126 8840467-5 1996 The profile of protein binding to the UFH column was almost the same as that of the DHG column except that ATIII showed affinity for UFH. Heparin 133-136 serpin family C member 1 Homo sapiens 107-112 8840467-6 1996 One of the reasons why DHG caused much less bleeding than UFH is thus suggested to be the differences in their affinity for ATIII in plasma. dhg 23-26 serpin family C member 1 Homo sapiens 124-129 8688424-0 1996 Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155. Carbohydrates 57-69 serpin family C member 1 Homo sapiens 0-12 8688424-0 1996 Antithrombin-heparin affinity reduced by fucosylation of carbohydrate at asparagine 155. Asparagine 73-83 serpin family C member 1 Homo sapiens 0-12 8688424-1 1996 The two human plasma antithrombin isoforms, alpha and beta, differ in glycosylation at asparagine 135. Asparagine 87-97 serpin family C member 1 Homo sapiens 21-33 8688424-3 1996 We previously found additional heterogeneity in a recombinant N135Q antithrombin variant, evidenced by two isoforms with a 2-fold difference in heparin affinity [Turko, I. V., Fan, B., & Gettins, P. G. W. (1993) FEBS Lett. Heparin 144-151 serpin family C member 1 Homo sapiens 68-80 8688424-3 1996 We previously found additional heterogeneity in a recombinant N135Q antithrombin variant, evidenced by two isoforms with a 2-fold difference in heparin affinity [Turko, I. V., Fan, B., & Gettins, P. G. W. (1993) FEBS Lett. Adenosine Monophosphate 186-189 serpin family C member 1 Homo sapiens 68-80 8688424-9 1996 We conclude that formation of the two heparin-affinity isoforms of N135Q antithrombin results from the specific difference in fucosylation at residue 155, which may result in different structural properties of the carbohydrate. Heparin 38-45 serpin family C member 1 Homo sapiens 73-85 8688424-9 1996 We conclude that formation of the two heparin-affinity isoforms of N135Q antithrombin results from the specific difference in fucosylation at residue 155, which may result in different structural properties of the carbohydrate. Carbohydrates 214-226 serpin family C member 1 Homo sapiens 73-85 8688424-10 1996 Consistent with these findings was the elimination of heparin-affinity heterogeneity in a double N135Q-N155Q variant antithrombin. Heparin 54-61 serpin family C member 1 Homo sapiens 117-129 8741550-9 1996 Left heart bypass with the Bio-Pump without heparin or with an antithrombin agent, argatroban, was used in recent 6 patients. argatroban 83-93 serpin family C member 1 Homo sapiens 63-75 8813337-2 1996 Antithrombin has two functional domains, a heparin binding site and a reactive centre (that complexes and inactivates the proteinase). Heparin 43-50 serpin family C member 1 Homo sapiens 0-12 8819242-0 1996 Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin. pentasaccharide 87-102 serpin family C member 1 Homo sapiens 0-12 8819242-0 1996 Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin. pentasaccharide 87-102 serpin family C member 1 Homo sapiens 144-156 8819242-0 1996 Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin. Heparin 120-127 serpin family C member 1 Homo sapiens 0-12 8819242-0 1996 Antithrombin-mediated inhibition of factor VIIa-tissue factor complex by the synthetic pentasaccharide representing the heparin binding site to antithrombin. Heparin 120-127 serpin family C member 1 Homo sapiens 144-156 8819242-1 1996 We examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor VIIa bound to tissue factor. pentasaccharide 40-55 serpin family C member 1 Homo sapiens 108-120 8819242-1 1996 We examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor VIIa bound to tissue factor. pentasaccharide 40-55 serpin family C member 1 Homo sapiens 128-140 8819242-1 1996 We examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor VIIa bound to tissue factor. Heparin 97-104 serpin family C member 1 Homo sapiens 128-140 8819242-3 1996 Using purified recombinant human coagulation factors and either a clotting or an amidolytic assay for the determination of the residual activity of factor VIIa, we showed that the pentasaccharide was an efficient antithrombin-dependent inhibitor of the coagulant activity of tissue factor-factor VIIa complex. pentasaccharide 180-195 serpin family C member 1 Homo sapiens 213-225 8819242-4 1996 In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3). Heparin 65-72 serpin family C member 1 Homo sapiens 122-127 8819242-4 1996 In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3). Heparin 65-72 serpin family C member 1 Homo sapiens 157-162 8819242-4 1996 In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3). Heparin 171-178 serpin family C member 1 Homo sapiens 122-127 8819242-4 1996 In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3). Heparin 171-178 serpin family C member 1 Homo sapiens 157-162 8819242-4 1996 In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 +/- 10,500 min-1 and 112,000 +/- 12,000 min-1 (mean +/- s.e.m., n = 3). pentasaccharide 200-215 serpin family C member 1 Homo sapiens 122-127 8776531-4 1996 We report successful coronary stent implantation in a HITTS patient using the antithrombin agent argatroban. argatroban 97-107 serpin family C member 1 Homo sapiens 78-90 8813337-5 1996 The structure of antithrombin is now considered in terms of the models derived from X-ray crystallography, which have provided explanations for the function of its heparin interaction site and of its reactive loop. Heparin 164-171 serpin family C member 1 Homo sapiens 17-29 8813337-6 1996 The structural organization of the antithrombin gene has been defined and numerous mutations have been identified that are responsible for antithrombin deficiency: these may reduce the level of the protein (Type I deficiency), alter the function of the protein (Type II deficiency, altering heparin binding or reactive sites), or even have multiple or "pleiotropic effects" (Type II deficiency, altering both functional domains and the level of protein). Heparin 291-298 serpin family C member 1 Homo sapiens 35-47 8611699-7 1996 Antithrombin in the presence or absence of heparin prevented this basal activation, whereas TF pathway inhibitor (TFPI/factor Xa complexes had only a limited inhibitory effect. Heparin 43-50 serpin family C member 1 Homo sapiens 0-12 8662679-4 1996 The rate constants of the inactivation of FXIa by C1 inhibitor and by antithrombin III increased up to 117-fold in the presence of glycosaminoglycans. Glycosaminoglycans 131-149 serpin family C member 1 Homo sapiens 70-86 9389029-1 1996 The genetic polymorphisms of antithrombin III (AT III) in 5 Chinese populations were studied by isoelectric focusing on polyacrylamide gels followed by immunoblotting. polyacrylamide 120-134 serpin family C member 1 Homo sapiens 29-45 9389029-1 1996 The genetic polymorphisms of antithrombin III (AT III) in 5 Chinese populations were studied by isoelectric focusing on polyacrylamide gels followed by immunoblotting. polyacrylamide 120-134 serpin family C member 1 Homo sapiens 47-53 9594175-6 1996 The early administration of heparin and aprotinin after the supplement of fibrinogen has shown a great potential benifit to stop the cascade of hypercoagulation and hyperplasminogenemia by enhancing the level of AT-III and fibrinogen in plasma. Heparin 28-35 serpin family C member 1 Homo sapiens 212-218 8626560-9 1996 Polymer formation was prevented by the addition of synthetic peptides with sequences corresponding to residues P2 to P14 in the reactive center loop of PAI-2 and antithrombin. Polymers 0-7 serpin family C member 1 Homo sapiens 162-174 8718936-3 1996 In addition to their capacity to adsorb thrombin, such surfaces were shown to be able to catalyse its inhibition by antithrombin III (AT), i.e. they are endowed with heparin-like activity. Heparin 166-173 serpin family C member 1 Homo sapiens 116-132 8718936-3 1996 In addition to their capacity to adsorb thrombin, such surfaces were shown to be able to catalyse its inhibition by antithrombin III (AT), i.e. they are endowed with heparin-like activity. Heparin 166-173 serpin family C member 1 Homo sapiens 134-136 8718936-8 1996 The relevant calculations, carried out with the help of a computer program, lead to determination of relative second order rate constants of thrombin adsorption and inhibitions by AT and HC in the presence of the polymers. Polymers 213-221 serpin family C member 1 Homo sapiens 180-182 8718936-9 1996 In addition to thrombin adsorption, polystyrene surfaces bearing only sulphonate groups catalyse inhibition by AT, whereas polystyrene surfaces bearing either aspartate, glycinate or isophthalate sulphonamide groups catalyse both inhibitions by AT and HC. Polystyrenes 36-47 serpin family C member 1 Homo sapiens 111-113 8718936-9 1996 In addition to thrombin adsorption, polystyrene surfaces bearing only sulphonate groups catalyse inhibition by AT, whereas polystyrene surfaces bearing either aspartate, glycinate or isophthalate sulphonamide groups catalyse both inhibitions by AT and HC. sulphonate 70-80 serpin family C member 1 Homo sapiens 111-113 8707354-6 1996 Preincubation with anti-thrombin compounds such as hirudin and antithrombin-III-heparin almost completely suppressed the action of thrombin without affecting the actions of other stimuli including IL-1 beta, phorbol 12-myristate 13-acetate (PMA) and TRAP. Tetradecanoylphorbol Acetate 208-239 serpin family C member 1 Homo sapiens 63-79 8707354-6 1996 Preincubation with anti-thrombin compounds such as hirudin and antithrombin-III-heparin almost completely suppressed the action of thrombin without affecting the actions of other stimuli including IL-1 beta, phorbol 12-myristate 13-acetate (PMA) and TRAP. Tetradecanoylphorbol Acetate 241-244 serpin family C member 1 Homo sapiens 63-79 8847350-1 1996 The ability of heparin to interact with plasma proteins, in particular antithrombin III (ATIII) and thrombin, is its primary mechanism as an anticoagulant drug. Heparin 15-22 serpin family C member 1 Homo sapiens 71-87 8847350-1 1996 The ability of heparin to interact with plasma proteins, in particular antithrombin III (ATIII) and thrombin, is its primary mechanism as an anticoagulant drug. Heparin 15-22 serpin family C member 1 Homo sapiens 89-94 8847350-4 1996 In this report, insights into binding interaction of direct versus polyethylene oxide space immobilized heparin with ATIII, thrombin, and the generation of the thrombin-antithrombin complex will be presented. Polyethylene Glycols 67-85 serpin family C member 1 Homo sapiens 117-122 8847350-4 1996 In this report, insights into binding interaction of direct versus polyethylene oxide space immobilized heparin with ATIII, thrombin, and the generation of the thrombin-antithrombin complex will be presented. Heparin 104-111 serpin family C member 1 Homo sapiens 117-122 8735800-8 1996 Partially carbohydrate-deficient isoforms were demonstrated in antithrombin, protein C, protein S and in alpha 2-antiplasmin, but not in factors II, X and fibrinogen. Carbohydrates 10-22 serpin family C member 1 Homo sapiens 63-75 8642472-5 1996 Homocysteine inhibits the antithrombin III binding activity of endothelial heparan sulfate proteoglycan, thereby suppressing the anticoagulant effect of antithrombin III. Homocysteine 0-12 serpin family C member 1 Homo sapiens 26-42 8642472-5 1996 Homocysteine inhibits the antithrombin III binding activity of endothelial heparan sulfate proteoglycan, thereby suppressing the anticoagulant effect of antithrombin III. Homocysteine 0-12 serpin family C member 1 Homo sapiens 153-169 8630391-2 1996 At near-plasma concentrations of TFPI, ATIII, and factor X, factor X activation that occurs in response to TF:VII is essentially abolished in the presence of heparin (0.5 micromol/L). Heparin 158-165 serpin family C member 1 Homo sapiens 39-44 8630391-3 1996 This effect requires both inhibitors, acting on different targets: (1) ATIII, which in the presence of heparin blocks the activation of TF:VII, and (2) TFPI, which inhibits the TF:VIIa that is generated. Heparin 103-110 serpin family C member 1 Homo sapiens 71-76 8630391-6 1996 These results indicated that when the unactivated TF:VII complex is the initiating stimulus, heparin-dependent reduction in the rate and extent of factor X activation requires both ATIII and TFPI. Heparin 93-100 serpin family C member 1 Homo sapiens 181-186 8857192-0 1996 Binding of antithrombin III and thrombin to immobilized heparin under flow conditions. Heparin 56-63 serpin family C member 1 Homo sapiens 11-27 9119287-0 1996 Anticoagulant effect of unfractionated heparin in antithrombin-depleted plasma in vitro. Heparin 39-46 serpin family C member 1 Homo sapiens 50-62 8857192-3 1996 However, few studies have been performed to investigate the binding kinetics of spacer-immobilized heparin under flow (shear stress) with antithrombin III (ATIII) and thrombin. Heparin 99-106 serpin family C member 1 Homo sapiens 138-154 8857192-3 1996 However, few studies have been performed to investigate the binding kinetics of spacer-immobilized heparin under flow (shear stress) with antithrombin III (ATIII) and thrombin. Heparin 99-106 serpin family C member 1 Homo sapiens 156-161 8857192-5 1996 Heparinized tubing was prepared by chemically immobilizing a high-ATIII-affinity fraction of heparin onto the surface of poly(ethylene)-oxide grafted, poly(styrene-co-p-aminostyrene)-coated polyethylene tubing. Heparin 93-100 serpin family C member 1 Homo sapiens 66-71 8857192-6 1996 ATIII was first bound onto the immobilized heparin, followed by the introduction of thrombin to interact with ATIII. Heparin 43-50 serpin family C member 1 Homo sapiens 0-5 8857192-9 1996 As the TAT complex dissociates from immobilized heparin, this "recovered" heparin is available for subsequent binding of more ATIII and thrombin. Heparin 48-55 serpin family C member 1 Homo sapiens 126-131 8857192-9 1996 As the TAT complex dissociates from immobilized heparin, this "recovered" heparin is available for subsequent binding of more ATIII and thrombin. Heparin 74-81 serpin family C member 1 Homo sapiens 126-131 9119287-1 1996 The aim of the study was to determine the effect of the antithrombin concentration on the anticoagulant response to heparin in vitro. Heparin 116-123 serpin family C member 1 Homo sapiens 56-68 9119287-4 1996 Plasma with an antithrombin concentration over 0.27 U/ml shows a similar response to heparin as normal plasma; at lower levels the response is diminished. Heparin 85-92 serpin family C member 1 Homo sapiens 15-27 9119287-5 1996 Even in plasma fully depleted of antithrombin, the APTT can be prolonged to a therapeutic level, although the amount of heparin needed is twice as high. Heparin 120-127 serpin family C member 1 Homo sapiens 33-45 9119287-6 1996 At antithrombin concentrations over 0.27 U/ml, heparin is the major determinant of the anticoagulant effect. Heparin 47-54 serpin family C member 1 Homo sapiens 3-15 8752690-10 1996 Treatment with antithrombin (argatroban 20mg i.v. argatroban 29-39 serpin family C member 1 Homo sapiens 15-27 8907299-4 1996 Heparins exert their anticoagulant effect by enhancing ATIII inhibitory action on factor Xa and thrombin, which results in decreased factor X activation, prothrombinase formation, prothrombin activation and thrombin generation. Heparin 0-8 serpin family C member 1 Homo sapiens 55-60 8907301-4 1996 Although it is well established that the in vitro and in vivo anticoagulant activities of heparin is mediated via the potentiation of the major coagulation inhibitor, antithrombin III (ATIII), some in vivo antithrombotic mechanisms are not fully understood. Heparin 90-97 serpin family C member 1 Homo sapiens 167-183 8907301-4 1996 Although it is well established that the in vitro and in vivo anticoagulant activities of heparin is mediated via the potentiation of the major coagulation inhibitor, antithrombin III (ATIII), some in vivo antithrombotic mechanisms are not fully understood. Heparin 90-97 serpin family C member 1 Homo sapiens 185-190 8689765-12 1996 Heparan sulphate binds antithrombin III (ATIII), thereby accelerating inactivation of intrinsic coagulation enzymes. Heparitin Sulfate 0-16 serpin family C member 1 Homo sapiens 23-39 8928095-5 1996 The bioactivity of HyalSx in terms of FXa and thrombin inactivation increases increasing with sulphation degree but the FXa inactivation seems to be mediated by ATIII, while the aspecific electrostatic interaction seems to play an important role in the inactivation of thrombin. hyalsx 19-25 serpin family C member 1 Homo sapiens 161-166 8734279-6 1996 Immediately postoperatively the patient received therapeutic doses of heparin with AT-III concentrates to increase AT-III levels; no recurrent thrombotic episode was observed. Heparin 70-77 serpin family C member 1 Homo sapiens 115-121 8739928-0 1996 The effect of dextran infusion on antithrombin III concentrations and on platelet function during minor surgery. Dextrans 14-21 serpin family C member 1 Homo sapiens 34-50 8739928-1 1996 The effects of dextran on the antithrombin (AT) III activity and blood coagulation, evaluated with thromboelastography, were investigated in 26 patients (anaesthesia risk class I or II) scheduled for minor surgery under general anaesthesia. Dextrans 15-22 serpin family C member 1 Homo sapiens 30-51 8739928-8 1996 In the recovery room, the median AT III value was lower in the Dextran than in the Ringer group, 78% and 92%, respectively (P < 0.05). Dextrans 63-70 serpin family C member 1 Homo sapiens 33-39 8766399-6 1996 AT III is of special importance for the treatment of DIC, where as different opinions exist regarding the application of heparin. Heparin 121-128 serpin family C member 1 Homo sapiens 0-6 8689765-12 1996 Heparan sulphate binds antithrombin III (ATIII), thereby accelerating inactivation of intrinsic coagulation enzymes. Heparitin Sulfate 0-16 serpin family C member 1 Homo sapiens 41-46 8707164-2 1996 The anticoagulant activity of unfractionated heparin is mainly accounted for by its fractions with a sequence with binding affinity for antithrombin III. Heparin 45-52 serpin family C member 1 Homo sapiens 136-152 14650442-9 1996 The pentasaccharide did not bind as strongly as the other heparin-derived oligosaccharides, indicating an AT III-independent mechanism. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 106-112 8713577-10 1996 Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species. Heparin 74-81 serpin family C member 1 Homo sapiens 36-52 8664906-1 1996 Human antithrombin is the major plasma inhibitor of thrombin both in the presence and absence of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 6-18 8713577-10 1996 Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species. Heparin 74-81 serpin family C member 1 Homo sapiens 168-184 8713577-10 1996 Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species. Heparin 107-114 serpin family C member 1 Homo sapiens 36-52 8713577-10 1996 Our collective finding suggest that antithrombin III and factor X bind to heparin at distinct sites on the heparin molecule resulting in a transient ternary complex of antithrombin III-heparin-factor X that represents the anticoagulant species. Heparin 107-114 serpin family C member 1 Homo sapiens 168-184 8788110-0 1996 Effect of fibronectin on the binding of antithrombin III to immobilized heparin. Heparin 72-79 serpin family C member 1 Homo sapiens 40-56 8788110-8 1996 The extent of ATIII binding to heparin in each experiment was assayed using a chromogenic substrate for ATIII, S-2238. Heparin 31-38 serpin family C member 1 Homo sapiens 14-19 8788110-2 1996 The competition and binding interaction between immobilized heparin and antithrombin III (ATIII)/thrombin have been described in vitro. Heparin 60-67 serpin family C member 1 Homo sapiens 72-88 8788110-8 1996 The extent of ATIII binding to heparin in each experiment was assayed using a chromogenic substrate for ATIII, S-2238. Heparin 31-38 serpin family C member 1 Homo sapiens 104-109 8788110-2 1996 The competition and binding interaction between immobilized heparin and antithrombin III (ATIII)/thrombin have been described in vitro. Heparin 60-67 serpin family C member 1 Homo sapiens 90-95 8788110-9 1996 The results of this study demonstrate that the displacement of ATIII from immobilized heparin was proportional to the fibronectin concentration, and was reversible. Heparin 86-93 serpin family C member 1 Homo sapiens 63-68 8858487-0 1996 The interactions between antithrombin III, thrombin and surface immobilized heparin. Heparin 76-83 serpin family C member 1 Homo sapiens 25-41 8858487-2 1996 Carboxylated polystyrene modified with covalently immobilized albumin-heparin conjugate contain sites which can bind ATIII from buffer and plasma solutions. Polystyrenes 13-24 serpin family C member 1 Homo sapiens 117-122 8858487-2 1996 Carboxylated polystyrene modified with covalently immobilized albumin-heparin conjugate contain sites which can bind ATIII from buffer and plasma solutions. Heparin 70-77 serpin family C member 1 Homo sapiens 117-122 8788110-6 1996 The binding interaction of immobilized heparin with ATIII was then determined in the presence of different fibronectin concentrations. Heparin 39-46 serpin family C member 1 Homo sapiens 52-57 8907177-1 1996 Our previous study has shown that depolymerized holothurian glycosaminoglycan (DHG) has two different inhibitory activities in the blood coagulation cascade: heparin cofactor II-dependent thrombin inhibition; and antithrombin III- and heparin cofactor II-independent inhibition of the intrinsic factor Xase complex [Nagase et al. holothurian glycosaminoglycan 48-77 serpin family C member 1 Homo sapiens 213-229 8683171-6 1996 The decline of AT-III may be due to bonding of coated heparin to AT-III, leading to effective anticoagulation. Heparin 54-61 serpin family C member 1 Homo sapiens 15-21 8907177-1 1996 Our previous study has shown that depolymerized holothurian glycosaminoglycan (DHG) has two different inhibitory activities in the blood coagulation cascade: heparin cofactor II-dependent thrombin inhibition; and antithrombin III- and heparin cofactor II-independent inhibition of the intrinsic factor Xase complex [Nagase et al. dhg 79-82 serpin family C member 1 Homo sapiens 213-229 8858487-7 1996 It was observed that heparin binding proteins were able to compete with ATIII for binding to the immobilized heparin. Heparin 21-28 serpin family C member 1 Homo sapiens 72-77 8858487-15 1996 In general it was concluded that only the surface immobilized heparin molecules that can bind ATIII in a reversible way determine the anticoagulant properties of the surface. Heparin 62-69 serpin family C member 1 Homo sapiens 94-99 8858487-16 1996 The mechanism of inactivation of a protease on a heparinized surface depends either on the catalytic effect of heparin on the inactivation rate of proteases by ATIII or on an increased uncatalytic inactivation due to increased concentrations of ATIII near the surface as compared to the concentration of ATIII in the bulk phase. Heparin 49-56 serpin family C member 1 Homo sapiens 160-165 8858487-16 1996 The mechanism of inactivation of a protease on a heparinized surface depends either on the catalytic effect of heparin on the inactivation rate of proteases by ATIII or on an increased uncatalytic inactivation due to increased concentrations of ATIII near the surface as compared to the concentration of ATIII in the bulk phase. Heparin 49-56 serpin family C member 1 Homo sapiens 245-250 8858487-16 1996 The mechanism of inactivation of a protease on a heparinized surface depends either on the catalytic effect of heparin on the inactivation rate of proteases by ATIII or on an increased uncatalytic inactivation due to increased concentrations of ATIII near the surface as compared to the concentration of ATIII in the bulk phase. Heparin 49-56 serpin family C member 1 Homo sapiens 245-250 8558740-4 1996 One or more NAC deficiencies were found in 15 (30%) patients and included antithrombin III (n = 5), protein C (n = 8), protein S (n = 4), and heparin cofactor II (n = 2). nac 12-15 serpin family C member 1 Homo sapiens 74-90 8683171-6 1996 The decline of AT-III may be due to bonding of coated heparin to AT-III, leading to effective anticoagulation. Heparin 54-61 serpin family C member 1 Homo sapiens 65-71 8772222-0 1995 Pharmacokinetics and tolerance of the natural pentasaccharide (SR90107/Org31540) with high affinity to antithrombin III in man. pentasaccharide 46-61 serpin family C member 1 Homo sapiens 103-119 8822125-3 1996 LMWH contains both high and low affinity fragments to antithrombin-III. Heparin, Low-Molecular-Weight 0-4 serpin family C member 1 Homo sapiens 54-70 8713781-6 1996 K86E in PCI*B causes a charge alteration in helix D which is likely involved in heparin binding in antithrombin III but not likely involved in glycosaminoglycan binding in PCI. Heparin 80-87 serpin family C member 1 Homo sapiens 99-115 8772222-0 1995 Pharmacokinetics and tolerance of the natural pentasaccharide (SR90107/Org31540) with high affinity to antithrombin III in man. PENTA 63-70 serpin family C member 1 Homo sapiens 103-119 8772222-1 1995 This paper reports the results of the first administration of the synthetic natural pentasaccharide with high affinity to antithrombin III (NP) in man. pentasaccharide 84-99 serpin family C member 1 Homo sapiens 122-138 8772223-0 1995 The effect of the synthetic pentasaccharide SR 90107/ORG 31540 on thrombin generation ex vivo is uniquely due to ATIII-mediated neutralization of factor Xa. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 113-118 8772223-5 1995 The plotting of TG inhibition versus SP concentration could be fitted with a good correlation (r = 0.94) to the graphical representation linking [ATIII-SP] to [SP]. TFF2 protein, human 37-39 serpin family C member 1 Homo sapiens 146-151 8772223-5 1995 The plotting of TG inhibition versus SP concentration could be fitted with a good correlation (r = 0.94) to the graphical representation linking [ATIII-SP] to [SP]. TFF2 protein, human 152-154 serpin family C member 1 Homo sapiens 146-151 8772223-6 1995 These results demonstrate that following subcutaneous administration to man, SP inhibits TG ex vivo and likely in vivo exclusively through the same selective ATIII-mediated inhibition of factor Xa as the one elicited in vitro. TFF2 protein, human 77-79 serpin family C member 1 Homo sapiens 158-163 7586247-0 1995 Prolonged antithrombin activity of low-molecular-weight heparins. Heparin 56-64 serpin family C member 1 Homo sapiens 10-22 8573397-2 1995 The major anticoagulant activity of heparin results from binding to the plasma protein antithrombin (AT). Heparin 36-43 serpin family C member 1 Homo sapiens 87-99 8578545-1 1995 Antithrombin from bony fish (Teleostei), represented by an ancient salmonid, Atlantic salmon (Salmo salar L.), and a more evolved species from the same family, rainbow trout (Oncorhynchus mykiss Walbaum), functions in vitro as does its human counterpart: it inactivates thrombin almost instantaneously in the presence of heparin and only slowly when heparin is absent. Heparin 321-328 serpin family C member 1 Homo sapiens 0-12 8582900-0 1995 Interaction of antithrombin III with surface-immobilized albumin-heparin conjugates. Heparin 65-72 serpin family C member 1 Homo sapiens 15-31 8582900-1 1995 The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII. Polystyrenes 117-128 serpin family C member 1 Homo sapiens 24-40 8582900-1 1995 The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII. Polystyrenes 117-128 serpin family C member 1 Homo sapiens 42-47 8582900-1 1995 The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII. Carbon-14 202-205 serpin family C member 1 Homo sapiens 24-40 8582900-1 1995 The interaction between antithrombin III (ATIII) and albumin-heparin conjugates covalently coupled onto carboxylated polystyrene beads either in buffer containing albumin or in plasma was studied using 14C-labeled ATIII. Carbon-14 202-205 serpin family C member 1 Homo sapiens 42-47 8582900-4 1995 The binding of ATIII to surface binding sites with a high affinity for ATIII was correlated with the presence of specific ATIII binding sites in the immobilized heparin. Heparin 161-168 serpin family C member 1 Homo sapiens 15-20 8582900-4 1995 The binding of ATIII to surface binding sites with a high affinity for ATIII was correlated with the presence of specific ATIII binding sites in the immobilized heparin. Heparin 161-168 serpin family C member 1 Homo sapiens 71-76 8582900-4 1995 The binding of ATIII to surface binding sites with a high affinity for ATIII was correlated with the presence of specific ATIII binding sites in the immobilized heparin. Heparin 161-168 serpin family C member 1 Homo sapiens 71-76 8582900-5 1995 Binding of ATIII from albumin solutions to binding sites with a low affinity for ATIII was dominated by nonspecific binding of ATIII to the immobilized heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 11-16 8582900-5 1995 Binding of ATIII from albumin solutions to binding sites with a low affinity for ATIII was dominated by nonspecific binding of ATIII to the immobilized heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 81-86 8582900-5 1995 Binding of ATIII from albumin solutions to binding sites with a low affinity for ATIII was dominated by nonspecific binding of ATIII to the immobilized heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 81-86 8582900-7 1995 ATIII is probably adsorbed to sites on the surface not covered with heparin. Heparin 68-75 serpin family C member 1 Homo sapiens 0-5 8582900-11 1995 The amount of ATIII bound to immobilized heparin via specific ATIII binding sites was 30% lower in plasma solutions as compared to the specific binding of ATIII using albumin solutions. Heparin 41-48 serpin family C member 1 Homo sapiens 14-19 8582900-11 1995 The amount of ATIII bound to immobilized heparin via specific ATIII binding sites was 30% lower in plasma solutions as compared to the specific binding of ATIII using albumin solutions. Heparin 41-48 serpin family C member 1 Homo sapiens 62-67 8582900-11 1995 The amount of ATIII bound to immobilized heparin via specific ATIII binding sites was 30% lower in plasma solutions as compared to the specific binding of ATIII using albumin solutions. Heparin 41-48 serpin family C member 1 Homo sapiens 62-67 8582900-12 1995 It is concluded that the accessibility of immobilized heparin for ATIII in plasma decreases by binding of heparin-binding proteins onto the immobilized heparin and/or adsorption of other plasma proteins on the heparinized surface. Heparin 54-61 serpin family C member 1 Homo sapiens 66-71 8582900-12 1995 It is concluded that the accessibility of immobilized heparin for ATIII in plasma decreases by binding of heparin-binding proteins onto the immobilized heparin and/or adsorption of other plasma proteins on the heparinized surface. Heparin 106-113 serpin family C member 1 Homo sapiens 66-71 8582900-12 1995 It is concluded that the accessibility of immobilized heparin for ATIII in plasma decreases by binding of heparin-binding proteins onto the immobilized heparin and/or adsorption of other plasma proteins on the heparinized surface. Heparin 106-113 serpin family C member 1 Homo sapiens 66-71 8733245-0 1995 [Antithrombin III dosage using the chromogenic substrate Tos-Gly-Pro-Arg-NAN, in several pathological situations]. N(alpha)-4-tosyl-glycyl-prolyl-arginine-4-nitroanilide 57-76 serpin family C member 1 Homo sapiens 1-17 8733245-3 1995 METHOD: ATIII levels were measured, using the chromogenic substrate Tos-Gly-Pro-Arg-NAN, which is specific for thrombin, and which has been sinthesized at the Biophysical Department of the Escola Paulista de Medicina of the Federal University of Sao Paulo, Brazil. N(alpha)-4-tosyl-glycyl-prolyl-arginine-4-nitroanilide 68-87 serpin family C member 1 Homo sapiens 8-13 8733245-10 1995 There was a significant correlation between ATIII levels measured using the chromogenic substrate Tos-Gly-Pro-Arg-NAN and those measured using S-2238, produced by Kabi Laboratories. N(alpha)-4-tosyl-glycyl-prolyl-arginine-4-nitroanilide 98-117 serpin family C member 1 Homo sapiens 44-49 8578545-1 1995 Antithrombin from bony fish (Teleostei), represented by an ancient salmonid, Atlantic salmon (Salmo salar L.), and a more evolved species from the same family, rainbow trout (Oncorhynchus mykiss Walbaum), functions in vitro as does its human counterpart: it inactivates thrombin almost instantaneously in the presence of heparin and only slowly when heparin is absent. Heparin 350-357 serpin family C member 1 Homo sapiens 0-12 8578545-6 1995 And the thrombin inactivating capacity of purified antithrombin and diluted plasma in the presence of heparin was indeed present at temperatures down to 3 degrees C, a capacity that human antithrombin also has retained. Heparin 102-109 serpin family C member 1 Homo sapiens 51-63 8578545-6 1995 And the thrombin inactivating capacity of purified antithrombin and diluted plasma in the presence of heparin was indeed present at temperatures down to 3 degrees C, a capacity that human antithrombin also has retained. Heparin 102-109 serpin family C member 1 Homo sapiens 188-200 8619306-4 1995 alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B. Urea 128-132 serpin family C member 1 Homo sapiens 21-67 8562839-0 1995 Thrombocytopenia, antithrombin deficiency and extensive thromboembolism in pregnancy: treatment with low-molecular-weight heparin. Heparin 122-129 serpin family C member 1 Homo sapiens 18-30 8619306-4 1995 alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B. Sodium Dodecyl Sulfate 134-155 serpin family C member 1 Homo sapiens 21-67 8619306-4 1995 alpha 2-Antiplasmin, proteinase alpha 1-inhibitor, antithrombin III and ITI with collagen yield complexes that are resistant to urea, sodium dodecylsulfate, and Trilon B. Edetic Acid 161-169 serpin family C member 1 Homo sapiens 21-67 8607111-12 1995 The antithrombotic effects of both heparins were correlated with their plasma activities as measured by the antifactor Xa or the antithrombin assays. Heparin 35-43 serpin family C member 1 Homo sapiens 129-141 8588189-0 1995 Heparan-dependent endothelial antithrombin binding is increased by butyrate. heparan 0-7 serpin family C member 1 Homo sapiens 30-42 8588189-0 1995 Heparan-dependent endothelial antithrombin binding is increased by butyrate. Butyrates 67-75 serpin family C member 1 Homo sapiens 30-42 8588189-2 1995 Such inhibition causes mast cells to produce heparins with high affinity for antithrombin (AT). Heparin 45-53 serpin family C member 1 Homo sapiens 77-89 8562839-2 1995 We describe a case of extensive thromboembolism associated with antithrombin (AT) deficiency complicated by thrombocytopenia which resolved when low-molecular-weight heparin was instituted. Heparin 166-173 serpin family C member 1 Homo sapiens 64-76 7582773-0 1995 [Significance of heparin elimination from plasma in the assessment of coagulogram and antithrombin III activity]. Heparin 17-24 serpin family C member 1 Homo sapiens 86-102 8557728-0 1995 Antithrombin activity of surface-bound heparin studied under flow conditions. Heparin 39-46 serpin family C member 1 Homo sapiens 0-12 8557728-5 1995 It is demonstrated that the rate of thrombin inactivation at the antithrombin-heparin surface equals the maximal rate of transport of thrombin toward the surface when the surface coverage of antithrombin exceeds 10 pmol/cm2. Heparin 78-85 serpin family C member 1 Homo sapiens 65-77 8557728-5 1995 It is demonstrated that the rate of thrombin inactivation at the antithrombin-heparin surface equals the maximal rate of transport of thrombin toward the surface when the surface coverage of antithrombin exceeds 10 pmol/cm2. Heparin 78-85 serpin family C member 1 Homo sapiens 191-203 8557728-8 1995 The uptake of antithrombin increased with the heparin content of the surface, but the stoichiometry decreased from 2 to 0.5 pmol antithrombin/micrograms heparin. Heparin 46-53 serpin family C member 1 Homo sapiens 14-26 8557728-8 1995 The uptake of antithrombin increased with the heparin content of the surface, but the stoichiometry decreased from 2 to 0.5 pmol antithrombin/micrograms heparin. Heparin 153-160 serpin family C member 1 Homo sapiens 14-26 7547966-6 1995 Heparin increased markedly the kon values for antithrombin III and protease nexin-1 with all thrombin variants tested, but a more dramatic effect was observed with a thrombin mutant (des-ETW) lacking residues Glu146, Thr147, and Trp148 (on the opposite side of the catalytic site relative to the 60-loop insertion). Heparin 0-7 serpin family C member 1 Homo sapiens 46-62 7547966-7 1995 At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin. Heparin 30-37 serpin family C member 1 Homo sapiens 78-94 7547966-7 1995 At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin. Heparin 193-200 serpin family C member 1 Homo sapiens 78-94 7547966-7 1995 At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin. Diethylstilbestrol 69-72 serpin family C member 1 Homo sapiens 78-94 7668220-2 1995 Recombinant hirudin is potentially effective as an antithrombotic treatment in the management of heparin-induced thrombocytopenia, given its potent antithrombin effects without known interaction with platelets. Heparin 97-104 serpin family C member 1 Homo sapiens 148-160 7547966-7 1995 At the optimum concentration, heparin increased the kon value of the des-ETW--antithrombin III interaction by nearly 5 orders of magnitude, considerably more than for thrombin, suggesting that heparin is able to compensate in part for the adverse effects of the des-ETW mutation on the structure of thrombin. ETW 73-76 serpin family C member 1 Homo sapiens 78-94 7673182-7 1995 Mutation of two Asp residues flanking Arg221a (D221A/D222K) almost abolishes the allosteric properties of thrombin and shows that the Na+ binding loop is also involved in direct recognition of protein C and antithrombin. Aspartic Acid 16-19 serpin family C member 1 Homo sapiens 207-219 7673182-7 1995 Mutation of two Asp residues flanking Arg221a (D221A/D222K) almost abolishes the allosteric properties of thrombin and shows that the Na+ binding loop is also involved in direct recognition of protein C and antithrombin. arg221a 38-45 serpin family C member 1 Homo sapiens 207-219 8551493-4 1995 On the other hand, the therapeutic dose of celiprolol was shown to reduce total platelet aggregation, without any harmful effects on fibrinolytic activity and coagulation inhibitors such as protein C and antithrombin III. Celiprolol 43-53 serpin family C member 1 Homo sapiens 204-220 7646463-0 1995 Elimination of glycosylation heterogeneity affecting heparin affinity of recombinant human antithrombin III by expression of a beta-like variant in baculovirus-infected insect cells. Heparin 53-60 serpin family C member 1 Homo sapiens 91-107 7641350-11 1995 The results of TIMI 7 lend support to the use of an antithrombin agent with aspirin in patients with unstable angina. timi 7 15-21 serpin family C member 1 Homo sapiens 52-64 7641350-11 1995 The results of TIMI 7 lend support to the use of an antithrombin agent with aspirin in patients with unstable angina. Aspirin 76-83 serpin family C member 1 Homo sapiens 52-64 7646463-1 1995 In order to promote homogeneity of recombinant antithrombin III interactions with heparin, an asparagine-135 to alanine substitution mutant was expressed in baculovirus-infected insect cells. Heparin 82-89 serpin family C member 1 Homo sapiens 47-63 7646463-4 1995 Second-order rate constants for thrombin and factor Xa inhibition determined in the absence and presence of heparin are in good agreement with values established for plasma antithrombin and these enzymes. Heparin 108-115 serpin family C member 1 Homo sapiens 173-185 7646463-5 1995 Based on far- and near-UV CD, bv.hat3.N135A has a high degree of conformational similarity to plasma antithrombin. Cadmium 26-28 serpin family C member 1 Homo sapiens 101-113 7646463-7 1995 The Kds of bv.hat3.N135A for high-affinity heparin and pentasaccharide were determined and are in good agreement with those of the plasma beta-antithrombin isoform. Heparin 43-50 serpin family C member 1 Homo sapiens 143-155 7482443-0 1995 Functional assay of plasma antithrombin using polyethylene glycol (PEG) defibrinated plasma. Polyethylene Glycols 46-65 serpin family C member 1 Homo sapiens 27-39 17607884-1 1995 Antithrombin, the main inhibitor of thrombosis in blood, is bound and activated by the heparin-like side-chains that line the small vasculature. Heparin 87-94 serpin family C member 1 Homo sapiens 0-12 7482443-0 1995 Functional assay of plasma antithrombin using polyethylene glycol (PEG) defibrinated plasma. Polyethylene Glycols 67-70 serpin family C member 1 Homo sapiens 27-39 7482443-1 1995 Polyethylene glycol(PEG) was used to precipitate fibrinogen to prepare defibrinated plasma in the two stage clotting assay of antithrombin activity. Polyethylene Glycols 0-19 serpin family C member 1 Homo sapiens 126-138 7482443-1 1995 Polyethylene glycol(PEG) was used to precipitate fibrinogen to prepare defibrinated plasma in the two stage clotting assay of antithrombin activity. Polyethylene Glycols 20-23 serpin family C member 1 Homo sapiens 126-138 7500917-3 1995 We have previously shown that a region of this protein shows structural similarities to the high-affinity heparin-binding site of the serum protease-inhibitor antithrombin III (ATII). Heparin 106-113 serpin family C member 1 Homo sapiens 159-175 7500917-5 1995 ATIII bound specifically to heparan sulfate residues on the surface of herpesvirus-permissive RK13 cells. Heparitin Sulfate 28-43 serpin family C member 1 Homo sapiens 0-5 7500917-9 1995 Since amino acids 130-137 of the high affinity heparin-binding site of ATIII show structural similarities to amino acids 134-141 of PrV-gC, both sequences were synthesized as synthetic peptides. Heparin 47-54 serpin family C member 1 Homo sapiens 71-76 7500917-9 1995 Since amino acids 130-137 of the high affinity heparin-binding site of ATIII show structural similarities to amino acids 134-141 of PrV-gC, both sequences were synthesized as synthetic peptides. Peptides 185-193 serpin family C member 1 Homo sapiens 71-76 7500917-10 1995 Although interaction of the peptide derived from ATIII with heparin was significantly stronger, both peptides interacted specifically with heparin in assays in vitro. Heparin 60-67 serpin family C member 1 Homo sapiens 49-54 17607884-2 1995 We now have good depictions of the heparin-binding site on antithrombin, and of the way in which mutations at this site cause thrombotic disease. Heparin 35-42 serpin family C member 1 Homo sapiens 59-71 17607884-3 1995 The interaction of heparin with antithrombin is, however, a kinetic one, with binding being followed by formation of a complex with thrombin and then release from the heparin. Heparin 19-26 serpin family C member 1 Homo sapiens 32-44 17607884-3 1995 The interaction of heparin with antithrombin is, however, a kinetic one, with binding being followed by formation of a complex with thrombin and then release from the heparin. Heparin 167-174 serpin family C member 1 Homo sapiens 32-44 7606009-0 1995 Iodine-mediated inactivation of lipid- and nonlipid-enveloped viruses in human antithrombin III concentrate. Iodine 0-6 serpin family C member 1 Homo sapiens 79-95 7606009-3 1995 Iodine at levels of 0.01% to 0.02% caused between 43% and 94% loss of AT-III activity, as well as degradation of AT-III as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis. Iodine 0-6 serpin family C member 1 Homo sapiens 70-76 7606009-3 1995 Iodine at levels of 0.01% to 0.02% caused between 43% and 94% loss of AT-III activity, as well as degradation of AT-III as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis. Sodium Dodecyl Sulfate 132-154 serpin family C member 1 Homo sapiens 113-119 7676404-0 1995 Antithrombin binding by human umbilical vein endothelial cells: effects of exogenous heparin. Heparin 85-92 serpin family C member 1 Homo sapiens 0-12 7647008-2 1995 The predominant species of factor Xa-ATIII detected after plasma and plasma to which factor Xa had been added were gel filtered on Sephadex G-200 and Sepharose 4B had apparent M(r) > 200,000, in which factor Xa-ATIII was associated with vitronectin. Sepharose 150-159 serpin family C member 1 Homo sapiens 37-42 7647008-1 1995 The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 132-135 serpin family C member 1 Homo sapiens 60-76 7647008-1 1995 The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 132-135 serpin family C member 1 Homo sapiens 78-83 7647008-1 1995 The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis. polyacrylamide 136-150 serpin family C member 1 Homo sapiens 60-76 7647008-1 1995 The M(r) of the complexes formed when factor Xa reacts with antithrombin III (ATIII) in plasma were estimated by gel filtration and SDS-polyacrylamide electrophoresis. polyacrylamide 136-150 serpin family C member 1 Homo sapiens 78-83 7647008-2 1995 The predominant species of factor Xa-ATIII detected after plasma and plasma to which factor Xa had been added were gel filtered on Sephadex G-200 and Sepharose 4B had apparent M(r) > 200,000, in which factor Xa-ATIII was associated with vitronectin. sephadex 131-145 serpin family C member 1 Homo sapiens 37-42 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Asparagine 42-52 serpin family C member 1 Homo sapiens 25-41 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Asparagine 42-52 serpin family C member 1 Homo sapiens 191-207 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Serine 74-80 serpin family C member 1 Homo sapiens 25-41 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Nitrogen 110-111 serpin family C member 1 Homo sapiens 25-41 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Nitrogen 110-111 serpin family C member 1 Homo sapiens 191-207 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Heparin 230-237 serpin family C member 1 Homo sapiens 25-41 7599134-0 1995 Partial glycosylation of antithrombin III asparagine-135 is caused by the serine in the third position of its N-glycosylation consensus sequence and is responsible for production of the beta-antithrombin III isoform with enhanced heparin affinity. Heparin 230-237 serpin family C member 1 Homo sapiens 191-207 7599134-2 1995 The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192. n-linked oligosaccharides 33-58 serpin family C member 1 Homo sapiens 10-15 7599134-2 1995 The alpha-ATIII isoform has four N-linked oligosaccharides attached to asparagines 96, 135, 155, and 192. Asparagine 71-82 serpin family C member 1 Homo sapiens 10-15 7599134-3 1995 The beta-ATIII isoform lacks carbohydrate on asparagine-135 (N135), which is near the heparin binding site, and binds heparin with higher affinity than does alpha-ATIII. Asparagine 45-55 serpin family C member 1 Homo sapiens 9-14 7599134-3 1995 The beta-ATIII isoform lacks carbohydrate on asparagine-135 (N135), which is near the heparin binding site, and binds heparin with higher affinity than does alpha-ATIII. Heparin 86-93 serpin family C member 1 Homo sapiens 9-14 7599134-3 1995 The beta-ATIII isoform lacks carbohydrate on asparagine-135 (N135), which is near the heparin binding site, and binds heparin with higher affinity than does alpha-ATIII. Heparin 118-125 serpin family C member 1 Homo sapiens 9-14 7599134-4 1995 Two isoforms are also produced when the normal human ATIII cDNA sequence is expressed in baculovirus-infected insect cells, and the recombinant beta" isoform similarly binds heparin with higher affinity than the recombinant alpha" isoform. Heparin 174-181 serpin family C member 1 Homo sapiens 53-58 7599134-5 1995 Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192. Nitrogen 39-40 serpin family C member 1 Homo sapiens 33-38 7599134-5 1995 Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192. n-x-s 65-70 serpin family C member 1 Homo sapiens 33-38 7599134-5 1995 Consensus sequences (CSs) of the ATIII N-glycosylation sites are N-X-S for 135 and N-X-T for 96, 155, and 192. n-x-t 83-88 serpin family C member 1 Homo sapiens 33-38 7599134-6 1995 On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position. n-x-s css 76-85 serpin family C member 1 Homo sapiens 162-167 7599134-6 1995 On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position. n-x-t 121-126 serpin family C member 1 Homo sapiens 162-167 7599134-6 1995 On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position. (2-benzoylethyl)trimethylammonium 157-161 serpin family C member 1 Homo sapiens 162-167 7599134-6 1995 On the basis of database and in vitro glycosylation studies suggesting that N-X-S CSs are utilized less efficiently than N-X-T CSs, we hypothesized that the beta-ATIII isoform might result from inefficient core glycosylation of the N135 N-X-S CS due to the presence of a serine, rather than a threonine, in the third position. n-x-s cs 76-84 serpin family C member 1 Homo sapiens 162-167 7599134-9 1995 Thus, serine in the third position of the N135 CS is responsible for its "partial" glycosylation and leads to production of beta-ATIII. Serine 6-12 serpin family C member 1 Homo sapiens 129-134 7599134-9 1995 Thus, serine in the third position of the N135 CS is responsible for its "partial" glycosylation and leads to production of beta-ATIII. N-[3-(Trimethoxysilyl)propyl]aniline 42-46 serpin family C member 1 Homo sapiens 129-134 7557658-6 1995 In addition, AT III was characterized by crossed immunoelectrophoresis in the presence of heparin and by gel filtration. Heparin 90-97 serpin family C member 1 Homo sapiens 13-19 8589216-0 1995 Activation of antithrombin III isoforms by heparan sulphate glycosaminoglycans and other sulphated polysaccharides. heparan sulphate glycosaminoglycans 43-78 serpin family C member 1 Homo sapiens 14-30 8589216-0 1995 Activation of antithrombin III isoforms by heparan sulphate glycosaminoglycans and other sulphated polysaccharides. Polysaccharides 99-114 serpin family C member 1 Homo sapiens 14-30 8589216-4 1995 High-molecular-weight dextran sulphate was the most effective of those studied, increasing thrombin inhibition by the higher-affinity antithrombin III isoform up to five-fold more efficiently than did heparin fractions with low-affinity for antithrombin III. Dextran Sulfate 22-38 serpin family C member 1 Homo sapiens 134-150 8589216-4 1995 High-molecular-weight dextran sulphate was the most effective of those studied, increasing thrombin inhibition by the higher-affinity antithrombin III isoform up to five-fold more efficiently than did heparin fractions with low-affinity for antithrombin III. Dextran Sulfate 22-38 serpin family C member 1 Homo sapiens 241-257 8589216-9 1995 The observed effects of the heparan sulphates on this anticoagulant pathway, although of low potency, are consistent with the hypotheses that these substances naturally regulate blood homeostasis in vascular tissues and that much of this function may be mediated by the higher-affinity antithrombin III isoform. Heparitin Sulfate 28-45 serpin family C member 1 Homo sapiens 286-302 7615164-10 1995 The chondroitin sulfate enhances the affinity of thrombin for thrombomodulin approximately 10- to 20-fold, making thrombomodulin a more potent inhibitor of coagulation, altering thrombin"s conformation and specificity, and accelerating thrombin inhibition by the serpin, antithrombin. Chondroitin Sulfates 4-23 serpin family C member 1 Homo sapiens 271-283 7614042-2 1995 AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation. Heparin 21-28 serpin family C member 1 Homo sapiens 0-6 7614042-2 1995 AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation. Heparin 76-83 serpin family C member 1 Homo sapiens 0-6 7614042-2 1995 AT III-high affinity heparin is a more potent inhibitor than unfractionated heparin and mollusc heparin in the intrinsic and extrinsic pathways of thrombin and factor Xa generation. Heparin 76-83 serpin family C member 1 Homo sapiens 0-6 7614042-3 1995 Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin. Heparin 9-16 serpin family C member 1 Homo sapiens 144-160 7614042-3 1995 Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin. Heparin 73-80 serpin family C member 1 Homo sapiens 52-58 7614042-3 1995 Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin. Heparin 73-80 serpin family C member 1 Homo sapiens 144-160 7614042-3 1995 Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin. Heparin 73-80 serpin family C member 1 Homo sapiens 52-58 7614042-3 1995 Mollusan heparin has about the same activity as the AT III high affinity-heparin on the inhibition of factor Xa and thrombin in the presence of antithrombin III and four times more inhibitory activity than unfractionated heparin on the heparin cofactor II mediated inhibition of thrombin. Heparin 73-80 serpin family C member 1 Homo sapiens 144-160 7647223-1 1995 It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs). Heparin 202-210 serpin family C member 1 Homo sapiens 45-50 7647222-7 1995 This proposed heparin recognition region in TFPI is similar to the recognition region in antithrombin III and other proteins. Heparin 14-21 serpin family C member 1 Homo sapiens 89-105 7730349-2 1995 To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated. Serine 150-153 serpin family C member 1 Homo sapiens 56-68 7647222-9 1995 A comparison of a helical wheel diagram of antithrombin III and tissue factor pathway inhibitor support also the proposal of this form of a heparin recognition region in TFPI. Heparin 140-147 serpin family C member 1 Homo sapiens 43-59 7647223-1 1995 It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs). Heparin 163-170 serpin family C member 1 Homo sapiens 27-43 7647223-1 1995 It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs). Heparin 163-170 serpin family C member 1 Homo sapiens 45-50 7647223-1 1995 It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs). Heparin 172-175 serpin family C member 1 Homo sapiens 27-43 7647223-1 1995 It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs). Heparin 172-175 serpin family C member 1 Homo sapiens 45-50 7647223-1 1995 It is widely accepted that antithrombin III (ATIII) mediated anti-Xa and anti-IIa effects are the sole determinant of the antithrombotic actions of unfractionated heparin (UFH) and low-molecular-weight heparins (LMWHs). Heparin 202-210 serpin family C member 1 Homo sapiens 27-43 7641602-10 1995 In addition to natural and recombinant human antithrombin III, direct antithrombin III-independent thrombin inhibitors have been developed as recombinant hirudin, hirulog, argatroban, boroarginine derivatives and single stranded DNA oligonucleotides (aptanes). boroarginine 184-196 serpin family C member 1 Homo sapiens 70-86 7641602-10 1995 In addition to natural and recombinant human antithrombin III, direct antithrombin III-independent thrombin inhibitors have been developed as recombinant hirudin, hirulog, argatroban, boroarginine derivatives and single stranded DNA oligonucleotides (aptanes). Oligonucleotides 233-249 serpin family C member 1 Homo sapiens 70-86 7641602-10 1995 In addition to natural and recombinant human antithrombin III, direct antithrombin III-independent thrombin inhibitors have been developed as recombinant hirudin, hirulog, argatroban, boroarginine derivatives and single stranded DNA oligonucleotides (aptanes). aptanes 251-258 serpin family C member 1 Homo sapiens 70-86 7607583-3 1995 Based on reports of increases in the endogenous anticoagulants (protein C, protein S, antithrombin III and plasminogen) with synthetic androgen therapy, the patient was treated with danazol for 8 weeks. Danazol 182-189 serpin family C member 1 Homo sapiens 86-102 7622551-8 1995 After depletion of antithrombin, but not complement C1 esterase inhibitor, the recalcified plasma clotted in contact with the unfractionated heparin surface as well. Heparin 141-148 serpin family C member 1 Homo sapiens 19-31 7622551-9 1995 We conclude that antithrombin and the antithrombin-binding sequence in the surface-immobilized heparin are essential for the prevention of surface activation of FXII and triggering of the intrinsic coagulation system. Heparin 95-102 serpin family C member 1 Homo sapiens 17-29 7622551-9 1995 We conclude that antithrombin and the antithrombin-binding sequence in the surface-immobilized heparin are essential for the prevention of surface activation of FXII and triggering of the intrinsic coagulation system. Heparin 95-102 serpin family C member 1 Homo sapiens 38-50 7730349-2 1995 To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated. Serine 150-153 serpin family C member 1 Homo sapiens 70-72 7730349-2 1995 To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated. Leucine 163-166 serpin family C member 1 Homo sapiens 56-68 7730349-2 1995 To elucidate the role of the P1" residue of the serpin, antithrombin (AT), in proteinase inhibition, the source of the functional defect in a natural Ser-394-->Leu variant, AT-Denver, was investigated. Leucine 163-166 serpin family C member 1 Homo sapiens 70-72 7730349-4 1995 AT-Denver inhibited thrombin and Factor Xa with nearly equimolar stoichiometries and formed SDS-stable complexes with these proteinases, indicating that the diminished inhibitor activity was not due to an enhanced turnover of the inhibitor as a substrate. Sodium Dodecyl Sulfate 92-95 serpin family C member 1 Homo sapiens 0-2 7736468-0 1995 Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements. pentasaccharide 37-52 serpin family C member 1 Homo sapiens 102-118 7721817-0 1995 Mechanism of acceleration of antithrombin-proteinase reactions by low affinity heparin. Heparin 79-86 serpin family C member 1 Homo sapiens 29-41 7721817-1 1995 Role of the antithrombin binding pentasaccharide in heparin rate enhancement. pentasaccharide 33-48 serpin family C member 1 Homo sapiens 12-24 7721817-1 1995 Role of the antithrombin binding pentasaccharide in heparin rate enhancement. Heparin 52-59 serpin family C member 1 Homo sapiens 12-24 7721817-2 1995 The role of the sequence-specific pentasaccharide region of high affinity heparin (HAH) in heparin acceleration of antithrombin-proteinase reactions was elucidated by determining the accelerating mechanism of low affinity heparin (LAH) lacking this sequence. pentasaccharide 34-49 serpin family C member 1 Homo sapiens 115-127 7721817-2 1995 The role of the sequence-specific pentasaccharide region of high affinity heparin (HAH) in heparin acceleration of antithrombin-proteinase reactions was elucidated by determining the accelerating mechanism of low affinity heparin (LAH) lacking this sequence. Heparin 74-81 serpin family C member 1 Homo sapiens 115-127 7721817-2 1995 The role of the sequence-specific pentasaccharide region of high affinity heparin (HAH) in heparin acceleration of antithrombin-proteinase reactions was elucidated by determining the accelerating mechanism of low affinity heparin (LAH) lacking this sequence. Heparin 91-98 serpin family C member 1 Homo sapiens 115-127 7721817-3 1995 LAH was shown to be free of HAH (< 0.001%) from the lack of exchange of added fluorescein-labeled HAH into LAH after separating the polysaccharides by antithrombin-agarose chromatography. lithium aluminium hydride 0-3 serpin family C member 1 Homo sapiens 154-166 7721817-7 1995 By contrast, LAH and HAH both accelerated the antithrombin-factor Xa reaction with a simple saturable dependence on heparin or inhibitor concentrations which paralleled the formation of an antithrombin-heparin binary complex. Heparin 116-123 serpin family C member 1 Homo sapiens 46-58 7721817-8 1995 The maximal accelerations of the two heparins in this case correlated with the inhibitor fluorescence enhancements induced by the polysaccharides, consistent with the accelerations arising from conformational activation of antithrombin. Heparin 37-45 serpin family C member 1 Homo sapiens 223-235 7721817-8 1995 The maximal accelerations of the two heparins in this case correlated with the inhibitor fluorescence enhancements induced by the polysaccharides, consistent with the accelerations arising from conformational activation of antithrombin. Polysaccharides 130-145 serpin family C member 1 Homo sapiens 223-235 7721817-9 1995 1H NMR difference spectroscopy of antithrombin complexes with LAH and HAH and competitive binding studies were consistent with LAH accelerating activity being mediated by binding to the same site on the inhibitor as HAH. Hydrogen 0-2 serpin family C member 1 Homo sapiens 34-46 7495073-0 1995 Inhibition of prothrombinase by antithrombin-heparin at a macroscopic surface. Heparin 45-52 serpin family C member 1 Homo sapiens 32-44 7495073-1 1995 The antithrombin-dependent inhibition of prothrombinase, assembled at a macroscopic surface, was studied under flow conditions utilizing a tubular flow reactor that consists of a phospholipid-coated glass capillary. Phospholipids 179-191 serpin family C member 1 Homo sapiens 4-16 7495073-6 1995 Inhibition was much faster when antithrombin was complexed with heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 32-44 7495073-9 1995 The heparin-independent inhibition of prothrombinase by antithrombin (4 microM) in the presence of prothrombin (0.2 microM) was virtually negligible. Heparin 4-11 serpin family C member 1 Homo sapiens 56-68 7736468-0 1995 Dynamics in aqueous solutions of the pentasaccharide corresponding to the binding site of heparin for antithrombin III studied by NMR relaxation measurements. Heparin 90-97 serpin family C member 1 Homo sapiens 102-118 7736468-1 1995 1H NMR and 13C NMR relaxation measurements at different magnetic field strengths were used to study the nature of overall and internal motions, in aqueous solution, of the synthetic pentasaccharide (A-G-A*-I-AM) corresponding to the binding site of heparin for antithrombin III. pentasaccharide 182-197 serpin family C member 1 Homo sapiens 261-277 7534133-6 1995 However, in the presence of heparin (1 or 50 U/mL), C1Inh appeared to be the major inhibitor of FXIa, followed by ATIII. Heparin 28-35 serpin family C member 1 Homo sapiens 114-119 7540495-3 1995 This inhibition can be reversed by antithrombin III (ATIII), an inhibitor of thrombin, in combination with heparin, a cofactor of ATIII and a glycosaminoglycan. Heparin 107-114 serpin family C member 1 Homo sapiens 130-135 7888673-0 1995 Depolymerized holothurian glycosaminoglycan with novel anticoagulant actions: antithrombin III- and heparin cofactor II-independent inhibition of factor X activation by factor IXa-factor VIIIa complex and heparin cofactor II-dependent inhibition of thrombin. holothurian glycosaminoglycan 14-43 serpin family C member 1 Homo sapiens 78-94 7888673-1 1995 The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors. Polysaccharides 30-44 serpin family C member 1 Homo sapiens 198-214 7888673-1 1995 The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors. Polysaccharides 30-44 serpin family C member 1 Homo sapiens 216-221 7888673-1 1995 The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors. holothurian glycosaminoglycan 74-103 serpin family C member 1 Homo sapiens 198-214 7888673-1 1995 The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors. holothurian glycosaminoglycan 74-103 serpin family C member 1 Homo sapiens 216-221 7888673-1 1995 The inhibition mechanism of a polysaccharide anticoagulant, depolymerized holothurian glycosaminoglycan (DHG), was examined by analyzing its effects on the clotting time of human plasma depleted of antithrombin III (ATIII), of heparin cofactor II (HCII), or of both heparin cofactors. dhg 105-108 serpin family C member 1 Homo sapiens 216-221 7888673-5 1995 These results indicated that DHG has two different inhibitory activities, one being an HCII-dependent thrombin inhibition and the other an ATIII- and HCII-independent inhibition of the coagulation cascade. dhg 29-32 serpin family C member 1 Homo sapiens 139-144 7893664-2 1995 The serpins antithrombin, protease nexin 1, and alpha 1-antitrypsin with a reactive-center arginine (Arg-alpha 1-antitrypsin) were found to inhibit the sperm protease acrosin with varying efficiency. Arginine 91-99 serpin family C member 1 Homo sapiens 12-24 7893664-10 1995 Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively. Heparin 0-7 serpin family C member 1 Homo sapiens 58-70 7893664-10 1995 Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively. Heparin 0-7 serpin family C member 1 Homo sapiens 207-219 7893664-10 1995 Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively. Heparin 137-144 serpin family C member 1 Homo sapiens 58-70 7893664-10 1995 Heparin markedly accelerated the inhibition of acrosin by antithrombin and protease nexin 1; at the optimal concentration, the degree of heparin acceleration of the inhibition rate was 250- and 500-fold for antithrombin and protease nexin 1, respectively. Heparin 137-144 serpin family C member 1 Homo sapiens 207-219 7734360-0 1995 Antithrombins Southport (Leu 99 to Val) and Vienna (Gln 118 to Pro): two novel antithrombin variants with abnormal heparin binding. Heparin 115-122 serpin family C member 1 Homo sapiens 79-91 7545318-2 1995 Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical uses of heparin. Heparin 96-103 serpin family C member 1 Homo sapiens 0-16 10155375-2 1995 However, the anticoagulation activity of heparin is based on its binding to antithrombin, and if the specific structure involved in this interaction is compromised by the coating procedure, then the activity is lost. Heparin 41-48 serpin family C member 1 Homo sapiens 76-88 7545318-2 1995 Antithrombin III is a major inhibitor of thrombin and augmentation of its inhibitory actions by heparin is the basis for the clinical uses of heparin. Heparin 142-149 serpin family C member 1 Homo sapiens 0-16 7540878-1 1995 The purpose of this pilot study was to determine the effect of recombinant hirudin (r-hirudin) on coagulopathy and the relationship between concentrations of thrombin-antithrombin III (ATIII) complex (TAT) and thrombin-hirudin complex (THC) in patients with disseminated intravascular coagulation (DIC). Dronabinol 236-239 serpin family C member 1 Homo sapiens 158-183 7873519-2 1995 Heparin is best known as an anticoagulant, an activity that results largely from a specific pentasaccharide sequence in heparin that interacts with a unique site in antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 165-181 7873519-2 1995 Heparin is best known as an anticoagulant, an activity that results largely from a specific pentasaccharide sequence in heparin that interacts with a unique site in antithrombin III. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 165-181 7873519-2 1995 Heparin is best known as an anticoagulant, an activity that results largely from a specific pentasaccharide sequence in heparin that interacts with a unique site in antithrombin III. Heparin 120-127 serpin family C member 1 Homo sapiens 165-181 7873519-4 1995 Unfractionated glycosaminoglycan heparin that had been prepared from porcine intestinal mucosa was examined for its capacity to bind antithrombin III using a new technique developed to quantitate that interaction. glycosaminoglycan heparin 15-40 serpin family C member 1 Homo sapiens 133-149 7873519-7 1995 Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides. Heparin 34-41 serpin family C member 1 Homo sapiens 54-70 7873519-7 1995 Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides. Heparin 34-41 serpin family C member 1 Homo sapiens 196-212 7873519-7 1995 Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides. Oligosaccharides 151-167 serpin family C member 1 Homo sapiens 54-70 7873519-7 1995 Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides. Oligosaccharides 151-167 serpin family C member 1 Homo sapiens 196-212 7873519-7 1995 Furthermore, the affinity of each heparin species for antithrombin III appears to vary inversely with the size of the heparin chain, with some smaller oligosaccharides having greater affinity for antithrombin III than larger oligosaccharides. Oligosaccharides 225-241 serpin family C member 1 Homo sapiens 54-70 7749832-7 1995 During the long-term follow-up of three patients with congenital antithrombin III or protein C deficiency, the factor VIIa level was more responsive to changes in the warfarin dose than the INR, and there were generally no corresponding changes of the thrombin-antithrombin III complex (TAT) level. Warfarin 167-175 serpin family C member 1 Homo sapiens 65-81 7540878-1 1995 The purpose of this pilot study was to determine the effect of recombinant hirudin (r-hirudin) on coagulopathy and the relationship between concentrations of thrombin-antithrombin III (ATIII) complex (TAT) and thrombin-hirudin complex (THC) in patients with disseminated intravascular coagulation (DIC). Dronabinol 236-239 serpin family C member 1 Homo sapiens 185-190 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Heparin 141-148 serpin family C member 1 Homo sapiens 38-44 7833476-0 1995 Fibrinogen inhibits the heparin cofactor II-mediated antithrombin activity of dermatan sulfate. Dermatan Sulfate 78-94 serpin family C member 1 Homo sapiens 53-65 7833476-2 1995 The antithrombin activity of several dermatan sulfate preparations has been measured in whole human plasma and found to be -55% of that in purified systems. Dermatan Sulfate 37-53 serpin family C member 1 Homo sapiens 4-16 7833476-3 1995 Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate. Dermatan Sulfate 109-125 serpin family C member 1 Homo sapiens 84-96 7833476-3 1995 Kinetic studies under pseudo-first-order conditions indicated that the reduction in antithrombin activity of dermatan sulfate in plasma compared with that in buffer was due to noncompetitive inhibition with respect to dermatan sulfate. Dermatan Sulfate 218-234 serpin family C member 1 Homo sapiens 84-96 7833476-5 1995 Addition of these proteins to the purified system showed that only fibrinogen inhibited the antithrombin activity of dermatan sulfate and that it did so in a concentration-dependent manner over the physiologic range of plasma fibrinogen levels. Dermatan Sulfate 117-133 serpin family C member 1 Homo sapiens 92-104 7789600-0 1995 Administration of heparin inhalations for correction of blood antithrombin activity in pregnant women with IDDM. Heparin 18-25 serpin family C member 1 Homo sapiens 62-74 7795154-0 1995 Two novel antithrombin variants, Asn187Asp and Asn187Lys, indicate a functional role for asparagine 187. Asparagine 89-99 serpin family C member 1 Homo sapiens 10-22 7795154-3 1995 In two families the mutation (6460 AAC-->GAC) results in an asparagine to aspartate substitution and is associated with normal immunological levels of antithrombin but a reduction in functional activity. Asparagine 63-73 serpin family C member 1 Homo sapiens 154-166 7795154-3 1995 In two families the mutation (6460 AAC-->GAC) results in an asparagine to aspartate substitution and is associated with normal immunological levels of antithrombin but a reduction in functional activity. Aspartic Acid 77-86 serpin family C member 1 Homo sapiens 154-166 7795154-5 1995 Asparagine 187 is located in the middle of the F helix of antithrombin and forms the major link between the F helix and strand 3 of the A sheet. Asparagine 0-10 serpin family C member 1 Homo sapiens 58-70 7832187-0 1995 Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin. Heparin 109-116 serpin family C member 1 Homo sapiens 0-12 7832187-0 1995 Antithrombin III Kumamoto II; a single mutation at Arg393-His increased the affinity of antithrombin III for heparin. Heparin 109-116 serpin family C member 1 Homo sapiens 88-104 7832187-6 1995 Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin. Heparin 98-105 serpin family C member 1 Homo sapiens 188-194 7832187-6 1995 Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin. Heparin 140-147 serpin family C member 1 Homo sapiens 188-194 7832187-6 1995 Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin. Sepharose 148-157 serpin family C member 1 Homo sapiens 188-194 7832187-6 1995 Analysis of the proposita"s plasma by crossed immunoelectrophoresis in the presence or absence of heparin and by affinity chromatography on heparin-Sepharose revealed that the proposita"s AT III had apparently normal affinity for heparin. Heparin 140-147 serpin family C member 1 Homo sapiens 188-194 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Heparin 0-7 serpin family C member 1 Homo sapiens 38-44 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Heparin 141-148 serpin family C member 1 Homo sapiens 249-265 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Heparin 0-7 serpin family C member 1 Homo sapiens 249-265 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Sepharose 149-158 serpin family C member 1 Homo sapiens 38-44 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Sepharose 149-158 serpin family C member 1 Homo sapiens 249-265 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Heparin 270-277 serpin family C member 1 Homo sapiens 38-44 7832187-10 1995 Heparin affinity of purified abnormal AT III from the proposita"s plasma was demonstrated to be increased upon affinity chromatography using heparin-Sepharose, suggesting that the mutation (Arg393-His) per se could possibly increase the affinity of antithrombin III for heparin. Heparin 270-277 serpin family C member 1 Homo sapiens 249-265 7588997-0 1995 Effect of sulfated xylans during the interaction of [125I]-thrombin with antithrombin III or heparin cofactor II of human plasma. Xylans 19-25 serpin family C member 1 Homo sapiens 73-89 7863710-5 1995 The AT III activity dropped significantly (p < 0.0001) after a heparin loading dose of 15,000 IU during stenting. Heparin 66-73 serpin family C member 1 Homo sapiens 4-10 7762756-5 1995 Its pI and molecular weight were the same as those of a physiological variant of antithrombin III (beta fraction), which is known to lack the asparagine-N-linked oligosaccharide chain at asparagine-135. asparagine-n-linked oligosaccharide 142-177 serpin family C member 1 Homo sapiens 81-97 7762756-5 1995 Its pI and molecular weight were the same as those of a physiological variant of antithrombin III (beta fraction), which is known to lack the asparagine-N-linked oligosaccharide chain at asparagine-135. Asparagine 142-152 serpin family C member 1 Homo sapiens 81-97 7660142-0 1995 Antithrombin III affinity dependence on the anticoagulant, antiprotease, and tissue factor pathway inhibitor actions of heparins. Heparin 120-128 serpin family C member 1 Homo sapiens 0-16 7660142-1 1995 To investigate AT-III affinity dependence on heparin"s actions, heparin (UH) was fractionated on an AT-III-Sepharose column into a high (HAH) and a low affinity (LAH) fraction. Heparin 45-52 serpin family C member 1 Homo sapiens 15-21 7660143-3 1995 The fractionated heparin retains many of its biological properties such as AT III affinity and sulfate content gamma-irradiation (60Co) has been used to depolymerize GAGs (De Ambrosi et al. Heparin 17-24 serpin family C member 1 Homo sapiens 75-81 7660143-8 1995 In standard clotting and amidolytic antiprotease assays (PT, APTT, AXa, Alla), gamma-irradiated depolymerized heparin produced equal or stronger activity when compared to a LMWH produced by nitrous acid depolymerization and retained the ability to active AT III and HCHII. Heparin 110-117 serpin family C member 1 Homo sapiens 255-261 7588997-2 1995 Addition of OSXS or SP-54 enhanced the complexation of thrombin with HC-II or with both AT-III and HC-II depending upon the concentration and the duration of the interactions of the sulfated compounds with plasma. osxs 12-16 serpin family C member 1 Homo sapiens 88-94 7588997-2 1995 Addition of OSXS or SP-54 enhanced the complexation of thrombin with HC-II or with both AT-III and HC-II depending upon the concentration and the duration of the interactions of the sulfated compounds with plasma. Pentosan Sulfuric Polyester 20-25 serpin family C member 1 Homo sapiens 88-94 7588997-3 1995 During the 30 s interaction, OSXS and SP-54 enhanced both AT-III-thrombin and HC-II-thrombin interaction while heparin was more selective and enhanced only the AT-III-thrombin interaction. osxs 29-33 serpin family C member 1 Homo sapiens 58-64 7588997-3 1995 During the 30 s interaction, OSXS and SP-54 enhanced both AT-III-thrombin and HC-II-thrombin interaction while heparin was more selective and enhanced only the AT-III-thrombin interaction. Pentosan Sulfuric Polyester 38-43 serpin family C member 1 Homo sapiens 58-64 7588997-3 1995 During the 30 s interaction, OSXS and SP-54 enhanced both AT-III-thrombin and HC-II-thrombin interaction while heparin was more selective and enhanced only the AT-III-thrombin interaction. Heparin 111-118 serpin family C member 1 Homo sapiens 160-166 7588997-5 1995 The complexations of AT-III-thrombin and HC-II-thrombin were reversed in the presence of 200 micrograms/ml of SP-54 during a 30 s interaction or in presence of 100 micrograms/ml of OSXS during a 2 min interaction. Pentosan Sulfuric Polyester 110-115 serpin family C member 1 Homo sapiens 21-27 7588997-5 1995 The complexations of AT-III-thrombin and HC-II-thrombin were reversed in the presence of 200 micrograms/ml of SP-54 during a 30 s interaction or in presence of 100 micrograms/ml of OSXS during a 2 min interaction. osxs 181-185 serpin family C member 1 Homo sapiens 21-27 7588997-6 1995 The Western blotting method of detecting thrombin showed that during the 10 s interaction, heparin enhanced the thrombin-AT-III complex formation while OSXS enhanced the thrombin-HC-II complex formation. Heparin 91-98 serpin family C member 1 Homo sapiens 121-127 7716890-2 1995 In a group of patients with medium and severe cardiac failure the administration of sulodexide led to an increased activation of the fibrinolytic potential--a drop of PAI-1 and fibrinogen, to an increased activation of anticoagulatory potential--an increase of AT III and reduced plasma viscosity. glucuronyl glucosamine glycan sulfate 84-94 serpin family C member 1 Homo sapiens 261-267 7863710-6 1995 As the heparin dose was reduced on the following days, AT III levels increased significantly (p < 0.0001) during the observation time. Heparin 7-14 serpin family C member 1 Homo sapiens 55-61 7863710-7 1995 There was a highly significant (p < 0.001) negative correlation between AT III and heparin levels. Heparin 86-93 serpin family C member 1 Homo sapiens 75-81 7893924-12 1994 Direct inhibition of the activity of AT-III and coagulation factor VIII and other factors by homocysteine was attempted in vitro but could not be shown at HC concentrations known to occur in the plasma of HOCY patients. Homocysteine 93-105 serpin family C member 1 Homo sapiens 37-43 7806495-3 1994 Thrombin is inhibited by the serpins antithrombin and heparin cofactor II (HCiI) in reactions that are accelerated markedly by specific glycosaminoglycans. Glycosaminoglycans 136-154 serpin family C member 1 Homo sapiens 37-49 7806495-12 1994 Antithrombin employs a template mechanism that requires heparin to interact with thrombin exosite II, whereas HCII employs an allosteric mechanism that requires thrombin exosite I but is largely independent of exosite II. Heparin 56-63 serpin family C member 1 Homo sapiens 0-12 7981186-1 1994 We have identified three novel mutations of the antithrombin (AT) gene in patients with thrombotic complications: a Cys 128 --> Tyr mutations, a G --> A mutation in the intervening sequence 4 (IVS4) 14 nucleotide 5" to exon 5, and a 9 bp deletion in the 3" end of exon 6 resulting in a short aberrant sequence after Arg 425. Arginine 316-319 serpin family C member 1 Homo sapiens 48-60 7981186-1 1994 We have identified three novel mutations of the antithrombin (AT) gene in patients with thrombotic complications: a Cys 128 --> Tyr mutations, a G --> A mutation in the intervening sequence 4 (IVS4) 14 nucleotide 5" to exon 5, and a 9 bp deletion in the 3" end of exon 6 resulting in a short aberrant sequence after Arg 425. Arginine 316-319 serpin family C member 1 Homo sapiens 62-64 7961924-0 1994 Role of N- and C-terminal amino acids in antithrombin binding to pentasaccharide. pentasaccharide 65-80 serpin family C member 1 Homo sapiens 41-53 7740457-12 1994 The same dose of naroparcil enhanced the formation of thrombin/heparin cofactor II complexes at the expense of thrombin/antithrombin III complexes in plasma incubated with (125I)-human alpha-thrombin and induced the appearance of dermatan sulfate-like material in the plasma of treated rabbits, as measured by a heparin cofactor II-mediated thrombin inhibition assay. naroparcil 17-27 serpin family C member 1 Homo sapiens 120-136 7947827-0 1994 Lysine-heparin interactions in antithrombin. Lysine 0-6 serpin family C member 1 Homo sapiens 31-43 7947827-2 1994 Lysine residues in two different regions of antithrombin have been proposed to be involved in heparin binding and heparin-mediated acceleration of proteinase inhibition. Lysine 0-6 serpin family C member 1 Homo sapiens 44-56 7947827-2 1994 Lysine residues in two different regions of antithrombin have been proposed to be involved in heparin binding and heparin-mediated acceleration of proteinase inhibition. Heparin 94-101 serpin family C member 1 Homo sapiens 44-56 7947827-2 1994 Lysine residues in two different regions of antithrombin have been proposed to be involved in heparin binding and heparin-mediated acceleration of proteinase inhibition. Heparin 114-121 serpin family C member 1 Homo sapiens 44-56 7947827-10 1994 The K290M,K294M,K297M variant had properties very similar to those of wild-type recombinant antithrombin in affinity for heparin, and in rates of inhibition of thrombin and factor Xa. Heparin 121-128 serpin family C member 1 Homo sapiens 92-104 7947827-11 1994 In contrast, K125M antithrombin had reduced affinity for both heparin pentasaccharide and full-length heparin, corresponding to delta delta Gs of 3.1 and 2.0 kcal mol-1, respectively. IC 831423 62-85 serpin family C member 1 Homo sapiens 19-31 7634317-4 1994 Heparin is the principal antithrombin drug currently used in acute syndromes; it acts mainly by binding to antithrombin III and increasing its inhibitory effect on thrombin and other coagulation factors. Heparin 0-7 serpin family C member 1 Homo sapiens 25-37 7634317-4 1994 Heparin is the principal antithrombin drug currently used in acute syndromes; it acts mainly by binding to antithrombin III and increasing its inhibitory effect on thrombin and other coagulation factors. Heparin 0-7 serpin family C member 1 Homo sapiens 107-123 7634317-5 1994 The heparin-antithrombin III complex, however, does not inhibit thrombus-bound thrombin; moreover, iv heparin requires frequent laboratory monitoring and dose adjustments. Heparin 4-11 serpin family C member 1 Homo sapiens 12-24 7634317-7 1994 heparin has been found to be effective in unstable angina and in myocardial infarction, especially when treated with accelerated rt-PA. New antithrombin drugs that selectively and directly inhibit thrombin are hirudin, its synthetic derivate hirulog, and argatroban. Heparin 0-7 serpin family C member 1 Homo sapiens 140-152 7947827-11 1994 In contrast, K125M antithrombin had reduced affinity for both heparin pentasaccharide and full-length heparin, corresponding to delta delta Gs of 3.1 and 2.0 kcal mol-1, respectively. Heparin 62-69 serpin family C member 1 Homo sapiens 19-31 7961924-1 1994 We have used a monoclonal antibody-based binding procedure to determine the dissociation constants of the interactions between the essential antithrombin-binding pentasaccharide and a series of 13 distinct N- and C-terminal antithrombin substitution mutation variants with defective binding interaction with heparin. pentasaccharide 162-177 serpin family C member 1 Homo sapiens 141-153 7961924-1 1994 We have used a monoclonal antibody-based binding procedure to determine the dissociation constants of the interactions between the essential antithrombin-binding pentasaccharide and a series of 13 distinct N- and C-terminal antithrombin substitution mutation variants with defective binding interaction with heparin. pentasaccharide 162-177 serpin family C member 1 Homo sapiens 224-236 7961924-1 1994 We have used a monoclonal antibody-based binding procedure to determine the dissociation constants of the interactions between the essential antithrombin-binding pentasaccharide and a series of 13 distinct N- and C-terminal antithrombin substitution mutation variants with defective binding interaction with heparin. Heparin 308-315 serpin family C member 1 Homo sapiens 141-153 7961924-2 1994 The reduction in binding affinity of the pentasaccharide with the N-terminal variants (with substitution mutations Pro-41-->Leu, Arg-47-->Cys and His, Leu-99-->Val and Phe, Gln-118-->Pro, Arg-129-->Gln) compared to normal antithrombin, Kd 200 nM, ranged from 15-984-fold and was generally less than 150-fold. pentasaccharide 41-56 serpin family C member 1 Homo sapiens 237-249 7961924-3 1994 Reduced binding affinity is assumed to arise mostly by perturbation, direct or indirect, of the initial contact of pentasaccharide with basic residues of antithrombin. pentasaccharide 115-130 serpin family C member 1 Homo sapiens 154-166 7959685-3 1994 The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin. Heparin 159-166 serpin family C member 1 Homo sapiens 74-79 7979371-4 1994 Heparin fractions differing in size and in antithrombin III affinity were prepared. Heparin 0-7 serpin family C member 1 Homo sapiens 43-59 7955182-2 1994 BACKGROUND: Heparin needs the plasma protein antithrombin III to function as an inhibitor of thrombin, and local antithrombin III deficiency might therefore limit the antithrombotic effectiveness of heparin during percutaneous transluminal coronary angioplasty. Heparin 12-19 serpin family C member 1 Homo sapiens 45-61 7955182-2 1994 BACKGROUND: Heparin needs the plasma protein antithrombin III to function as an inhibitor of thrombin, and local antithrombin III deficiency might therefore limit the antithrombotic effectiveness of heparin during percutaneous transluminal coronary angioplasty. Heparin 199-206 serpin family C member 1 Homo sapiens 45-61 7757423-0 1994 Feasible synthesis and biological properties of six "non-glycosamino" glycan analogues of the antithrombin III binding heparin pentasaccharide. glycosamino" 57-69 serpin family C member 1 Homo sapiens 94-110 7757423-0 1994 Feasible synthesis and biological properties of six "non-glycosamino" glycan analogues of the antithrombin III binding heparin pentasaccharide. Polysaccharides 70-76 serpin family C member 1 Homo sapiens 94-110 7757423-0 1994 Feasible synthesis and biological properties of six "non-glycosamino" glycan analogues of the antithrombin III binding heparin pentasaccharide. IC 831423 119-142 serpin family C member 1 Homo sapiens 94-110 7757423-1 1994 In this paper, we report the synthesis of "non-glycosamino" glycan analogues 5-10 of the antithrombin III binding pentasaccharide 1. Glycosaminoglycans 47-66 serpin family C member 1 Homo sapiens 89-105 7757423-1 1994 In this paper, we report the synthesis of "non-glycosamino" glycan analogues 5-10 of the antithrombin III binding pentasaccharide 1. pentasaccharide 114-129 serpin family C member 1 Homo sapiens 89-105 7959685-3 1994 The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin. Heparin 159-166 serpin family C member 1 Homo sapiens 97-102 7959685-3 1994 The other novel lesion (Met251-->Ile) was associated with a dysfunctional ATIII protein (type II ATIII deficiency) and is predicted to interfere either with a heparin-induced conformational change in the ATIII molecule or with docking to thrombin. Heparin 159-166 serpin family C member 1 Homo sapiens 97-102 7863468-7 1994 These minor AT III molecules were considered to lack an oligosaccharide sidechain. Oligosaccharides 56-71 serpin family C member 1 Homo sapiens 12-18 7863481-3 1994 In both cases, the expression of the mutation is pleiotropic, i.e. results in a reduction in the circulating concentration of antithrombin and impairs both its anti-thrombin activity and its ability to bind heparin. Heparin 207-214 serpin family C member 1 Homo sapiens 126-138 7929416-4 1994 The inhibition constant of heparin with low affinity for antithrombin was indistinguishable from heparin with high affinity for antithrombin (Ki = 20 nM). Heparin 27-34 serpin family C member 1 Homo sapiens 57-69 7929416-4 1994 The inhibition constant of heparin with low affinity for antithrombin was indistinguishable from heparin with high affinity for antithrombin (Ki = 20 nM). Heparin 97-104 serpin family C member 1 Homo sapiens 128-140 7929416-9 1994 We propose that part of the antithrombotic action of heparin and low molecular weight heparin is due to anti-thrombin-independent inhibition of intrinsic fXase and that heparin with low affinity for antithrombin may be useful as an antithrombotic agent. Heparin 53-60 serpin family C member 1 Homo sapiens 199-211 7896748-2 1994 As a step towards a better understanding of the heparin-binding mechanism of mammalian ATIIIs, the amino acid sequence of porcine ATIII was established by sequence analysis of the peptides derived from cyanogen bromide cleavage and enzymatic digestion with lysyl endopeptidase, V8 protease, and trypsin. Heparin 48-55 serpin family C member 1 Homo sapiens 87-92 7896748-3 1994 Porcine ATIII was found to consist of 431 amino acid residues, with a calculated molecular weight of 48,930 without carbohydrate. Carbohydrates 116-128 serpin family C member 1 Homo sapiens 8-13 7896748-5 1994 Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds. Heparin 102-109 serpin family C member 1 Homo sapiens 8-13 7896748-5 1994 Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds. Amino Acids, Basic 118-134 serpin family C member 1 Homo sapiens 8-13 7896748-5 1994 Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds. Disulfides 149-158 serpin family C member 1 Homo sapiens 8-13 7896748-6 1994 The most notable feature of porcine ATIII was that it possesses only three carbohydrate chains, at Asn136, 156, and 193, whereas other mammalian ATIIIs have four, additional chain being at Asn97; this is replaced by Asp in porcine ATIII. Carbohydrates 75-87 serpin family C member 1 Homo sapiens 36-41 7896748-6 1994 The most notable feature of porcine ATIII was that it possesses only three carbohydrate chains, at Asn136, 156, and 193, whereas other mammalian ATIIIs have four, additional chain being at Asn97; this is replaced by Asp in porcine ATIII. ASN 136 99-105 serpin family C member 1 Homo sapiens 36-41 7896748-6 1994 The most notable feature of porcine ATIII was that it possesses only three carbohydrate chains, at Asn136, 156, and 193, whereas other mammalian ATIIIs have four, additional chain being at Asn97; this is replaced by Asp in porcine ATIII. Aspartic Acid 216-219 serpin family C member 1 Homo sapiens 36-41 7896748-9 1994 Porcine ATIII eluted from the column with a peak at an NaCl concentration of 924 mM while human ATIII eluted at 838 mM NaCl. Sodium Chloride 55-59 serpin family C member 1 Homo sapiens 8-13 7896748-9 1994 Porcine ATIII eluted from the column with a peak at an NaCl concentration of 924 mM while human ATIII eluted at 838 mM NaCl. Sodium Chloride 119-123 serpin family C member 1 Homo sapiens 96-101 7896748-10 1994 Neuraminidase treatment of each ATIII enhanced the heparin-affinity to the same extent. Heparin 51-58 serpin family C member 1 Homo sapiens 32-37 7863481-4 1994 The effect of a denaturing agent (sodium dodecyl sulfate) on the recognition of the plasma antithrombin by a polyclonal antibody was studied in an immuno-enzymatic assay. Sodium Dodecyl Sulfate 34-56 serpin family C member 1 Homo sapiens 91-103 7957907-0 1994 Antithrombin histidine variants 1H NMR resonance assignments and functional properties. Histidine 13-22 serpin family C member 1 Homo sapiens 0-12 7957907-0 1994 Antithrombin histidine variants 1H NMR resonance assignments and functional properties. Hydrogen 32-34 serpin family C member 1 Homo sapiens 0-12 7966143-2 1994 Several antithrombin agents are being developed by chemical and structural optimization of these "hirupeptides". hirupeptides 98-110 serpin family C member 1 Homo sapiens 8-20 7841305-5 1994 DS500 inhibited both the PtdInsP and the sulphatide-mediated autoactivation in an antithrombin III independent manner. Phosphatidylinositol Phosphates 25-32 serpin family C member 1 Homo sapiens 82-98 7929178-1 1994 We have investigated the characteristics of clonal L cell mutant VI-7 that has previously been demonstrated to exhibit reduced levels of cell surface proteoglycans containing heparan sulfate (HS) with regions of defined monosaccharide sequence that interact with antithrombin (HSact) (de Agostini, A. L., Lau, H. K., Leone, C., Youssoufian, H., and Rosenberg, R. D. (1990) Proc. Monosaccharides 220-234 serpin family C member 1 Homo sapiens 263-275 7532447-1 1994 Protein C inhibitor (PCI), antithrombin, and heparin cofactor II are members of the serine proteinase inhibitor (serpin) superfamily that inhibit proteinases at rates which increase in the presence of the glycosaminoglycan heparin. glycosaminoglycan heparin 205-230 serpin family C member 1 Homo sapiens 27-39 7532447-4 1994 Antithrombin, which does not inhibit APC but which does bind to heparin/heparan sulphate with higher affinity than PCI, caused only a small decrease in the inhibition rate of PCI-APC in the presence of unfractionated heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 0-12 7532447-4 1994 Antithrombin, which does not inhibit APC but which does bind to heparin/heparan sulphate with higher affinity than PCI, caused only a small decrease in the inhibition rate of PCI-APC in the presence of unfractionated heparin. Heparitin Sulfate 72-88 serpin family C member 1 Homo sapiens 0-12 7532447-4 1994 Antithrombin, which does not inhibit APC but which does bind to heparin/heparan sulphate with higher affinity than PCI, caused only a small decrease in the inhibition rate of PCI-APC in the presence of unfractionated heparin. Heparin 217-224 serpin family C member 1 Homo sapiens 0-12 7523096-11 1994 Synthetic peptides, that contained the active sites of AT-III and alpha 1-antichymotrypsin, were also inhibitory. Peptides 10-18 serpin family C member 1 Homo sapiens 55-61 7523554-9 1994 Furthermore, this material inhibits the clotting of nonanticoagulated whole human blood (for > 16 hours at room temperature), perhaps by virtue of binding and activation of antithrombin III by the sulfonic acid residues on the surface-immobilized Cibacron blue. Sulfonic Acids 200-213 serpin family C member 1 Homo sapiens 176-192 7523554-9 1994 Furthermore, this material inhibits the clotting of nonanticoagulated whole human blood (for > 16 hours at room temperature), perhaps by virtue of binding and activation of antithrombin III by the sulfonic acid residues on the surface-immobilized Cibacron blue. Cibacron Blue 250-263 serpin family C member 1 Homo sapiens 176-192 7899138-3 1994 A defined pentasaccharide motif was found responsible for the enhancement of the rate of inactivation of factor Xa by antithrombin III. pentasaccharide 10-25 serpin family C member 1 Homo sapiens 118-134 7878631-6 1994 In age- and race-adjusted analyses, AT III was positively associated with smoking, HDL-cholesterol, triglycerides (men only), and in women, with diabetes and lipoprotein(a). Cholesterol 87-98 serpin family C member 1 Homo sapiens 36-42 7878631-6 1994 In age- and race-adjusted analyses, AT III was positively associated with smoking, HDL-cholesterol, triglycerides (men only), and in women, with diabetes and lipoprotein(a). Triglycerides 100-113 serpin family C member 1 Homo sapiens 36-42 7944706-1 1994 The anticoagulant effect of heparin in the milieu of altered antithrombin III levels was investigated in adult (n = 7) and pediatric (n = 14) patients undergoing open heart operations. Heparin 28-35 serpin family C member 1 Homo sapiens 61-77 7944706-7 1994 This result may be related to the different actions of heparin when antithrombin III levels are reduced. Heparin 55-62 serpin family C member 1 Homo sapiens 68-84 7841596-18 1994 Whether AT-III in the presence of glycosaminoglycans on cell surfaces expressing TF can function as an auxiliary second physiological regulator is not known. Glycosaminoglycans 34-52 serpin family C member 1 Homo sapiens 8-14 7841305-5 1994 DS500 inhibited both the PtdInsP and the sulphatide-mediated autoactivation in an antithrombin III independent manner. Sulfoglycosphingolipids 41-51 serpin family C member 1 Homo sapiens 82-98 7971256-1 1994 A male patient of 24 years who had experienced thrombotic episodes since the age of 15 displayed an unusually low antithrombin III (AT III) activity measured as heparin cofactor (13% of the normal), while a similarly decreased value (16% of normal) was found in a 26 year old brother who had suffered from thrombotic events since the age of 12 years. Heparin 161-168 serpin family C member 1 Homo sapiens 114-130 7971256-1 1994 A male patient of 24 years who had experienced thrombotic episodes since the age of 15 displayed an unusually low antithrombin III (AT III) activity measured as heparin cofactor (13% of the normal), while a similarly decreased value (16% of normal) was found in a 26 year old brother who had suffered from thrombotic events since the age of 12 years. Heparin 161-168 serpin family C member 1 Homo sapiens 132-138 7971256-2 1994 AT III heparin cofactor activities were close to 50% of normal in the father, mother, another brother and a sister, none of whom had experienced thrombotic episodes. Heparin 7-14 serpin family C member 1 Homo sapiens 0-6 8025278-1 1994 The ability of heparin to dramatically enhance the inactivation of thrombin (IIa) by antithrombin III (ATIII) in buffer is negated through formation of a IIa-fibrin-heparin ternary complex (Hogg and Jackson, Proc Natl Acad Sci USA 86:3619, 1989; Hogg and Jackson, J Biol Chem 265:241, 1990). Heparin 15-22 serpin family C member 1 Homo sapiens 85-101 7932105-3 1994 The procedures were based on the photometric determination of the inactivation of FXa and FIIa after incubation with LMWH in the presence of antithrombin III (AT III). Heparin, Low-Molecular-Weight 117-121 serpin family C member 1 Homo sapiens 159-165 8054362-6 1994 Intracellular forms of alpha 2-PI or ATIII synthesized by cells treated with 1 mM MdN were sensitive to endoglycosidase H (Endo H), whereas almost all the secreted forms were resistant, suggesting the presence of complex-type oligosaccharides. N-methyldeoxynojirimycin 82-85 serpin family C member 1 Homo sapiens 37-42 8054362-6 1994 Intracellular forms of alpha 2-PI or ATIII synthesized by cells treated with 1 mM MdN were sensitive to endoglycosidase H (Endo H), whereas almost all the secreted forms were resistant, suggesting the presence of complex-type oligosaccharides. Oligosaccharides 226-242 serpin family C member 1 Homo sapiens 37-42 8054362-7 1994 In the presence of 1 mM dMM, cells synthesized Endo H-sensitive alpha 2-PI and ATIII with similar secretion rates. 1-Deoxynojirimycin 24-27 serpin family C member 1 Homo sapiens 79-84 8054362-8 1994 These results suggest that retention of glucose on N-linked oligosaccharides not only retards the exit of alpha 2-PI and ATIII, but also changes the catabolic rate of alpha 2-PI in the endoplasmic reticulum. Glucose 40-47 serpin family C member 1 Homo sapiens 121-126 8054362-8 1994 These results suggest that retention of glucose on N-linked oligosaccharides not only retards the exit of alpha 2-PI and ATIII, but also changes the catabolic rate of alpha 2-PI in the endoplasmic reticulum. n-linked oligosaccharides 51-76 serpin family C member 1 Homo sapiens 121-126 8025278-1 1994 The ability of heparin to dramatically enhance the inactivation of thrombin (IIa) by antithrombin III (ATIII) in buffer is negated through formation of a IIa-fibrin-heparin ternary complex (Hogg and Jackson, Proc Natl Acad Sci USA 86:3619, 1989; Hogg and Jackson, J Biol Chem 265:241, 1990). Heparin 15-22 serpin family C member 1 Homo sapiens 103-108 8025278-7 1994 Fibrin was found to inhibit the heparin-catalyzed inactivation of IIa by ATIII with half-maximal effect at 97 +/- 19 nmol/L fibrin. Heparin 32-39 serpin family C member 1 Homo sapiens 73-78 8025278-9 1994 These findings imply that fibrin is a potent modulator of heparin activity in vivo by inhibiting heparin-catalyzed IIa-ATIII complex formation through formation of ternary IIa-fibrin-heparin complexes. Heparin 58-65 serpin family C member 1 Homo sapiens 119-124 7974394-1 1994 Congenital deficiency of antithrombin (AT) is associated with thrombotic events and AT consumption occurs in some severe disorders and after treatment with heparin. Heparin 156-163 serpin family C member 1 Homo sapiens 25-37 8026575-5 1994 We have measured the stability to denaturation of one of these non-inhibitor substrate mutants, antithrombin-Hamilton, which has an Ala-->Thr change at position P12 in strand s4A. Alanine 132-135 serpin family C member 1 Homo sapiens 96-108 8026575-5 1994 We have measured the stability to denaturation of one of these non-inhibitor substrate mutants, antithrombin-Hamilton, which has an Ala-->Thr change at position P12 in strand s4A. Threonine 141-144 serpin family C member 1 Homo sapiens 96-108 8026575-6 1994 We find that it undergoes the transformation to the more stable form which is observed for inhibitor serpins, from which we conclude that the Ala-->Thr change in antithrombin-Hamilton does not prevent insertion of s4A into beta-sheet A in the cleaved form. Alanine 142-145 serpin family C member 1 Homo sapiens 165-177 8027055-7 1994 The mutant and wild type thrombin are inhibited at comparable rates by antithrombin +/- the pentasaccharide capable of inducing the "active" antithrombin conformation, but heparin acceleration of antithrombin inhibition of the mutant is reduced by more than 95%. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 71-83 8026575-6 1994 We find that it undergoes the transformation to the more stable form which is observed for inhibitor serpins, from which we conclude that the Ala-->Thr change in antithrombin-Hamilton does not prevent insertion of s4A into beta-sheet A in the cleaved form. Threonine 151-154 serpin family C member 1 Homo sapiens 165-177 8037658-0 1994 Interaction of heparin with synthetic antithrombin III peptide analogues. Heparin 15-22 serpin family C member 1 Homo sapiens 38-54 8027055-7 1994 The mutant and wild type thrombin are inhibited at comparable rates by antithrombin +/- the pentasaccharide capable of inducing the "active" antithrombin conformation, but heparin acceleration of antithrombin inhibition of the mutant is reduced by more than 95%. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 141-153 8027055-7 1994 The mutant and wild type thrombin are inhibited at comparable rates by antithrombin +/- the pentasaccharide capable of inducing the "active" antithrombin conformation, but heparin acceleration of antithrombin inhibition of the mutant is reduced by more than 95%. pentasaccharide 92-107 serpin family C member 1 Homo sapiens 141-153 8037658-8 1994 Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. Leucine 81-88 serpin family C member 1 Homo sapiens 200-216 8037658-8 1994 Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. Tyrosine 93-101 serpin family C member 1 Homo sapiens 200-216 8037658-8 1994 Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. Nitrogen 141-142 serpin family C member 1 Homo sapiens 200-216 8037658-8 1994 Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. Cysteine 143-149 serpin family C member 1 Homo sapiens 200-216 8037658-8 1994 Proton nuclear Overhauser enhancement spectroscopy demonstrated the proximity of leucine and tyrosine (within the consensus sequence) to the N-acetyl moiety found primarily within the pentasaccharide antithrombin III-binding site of heparin. Heparin 233-240 serpin family C member 1 Homo sapiens 200-216 7664058-0 1994 A mechanism for heparin-induced potentiation of antithrombin III. Heparin 16-23 serpin family C member 1 Homo sapiens 48-64 7952425-5 1994 This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream. Heparin 60-67 serpin family C member 1 Homo sapiens 78-94 7952425-5 1994 This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream. Heparin 60-67 serpin family C member 1 Homo sapiens 96-102 7952425-5 1994 This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream. Heparin 133-140 serpin family C member 1 Homo sapiens 78-94 7952425-5 1994 This study was designed to determine whether consumption of heparin cofactor, antithrombin-III (AT-III), compromises the efficacy of heparin in the setting of pharmacologic fibrinolysis and, if so, whether this degradation or inactivation is directly attributable to the effects of tissue-type plasminogen activator (t-PA) or plasmin in the blood stream. Heparin 133-140 serpin family C member 1 Homo sapiens 96-102 7965660-4 1994 Substituents introduced at this position had a minimal effect on the antithrombin III binding sites found in heparin"s interior. Heparin 109-116 serpin family C member 1 Homo sapiens 69-85 7987496-2 1994 Heparin immobilized in this way proved to be useful as an affinity carrier for the isolation of antithrombin III and heparin-binding proteins from boar seminal plasma. Heparin 0-7 serpin family C member 1 Homo sapiens 96-112 8172176-0 1994 Genetic linkage studies in antithrombin-deficient kindreds using a highly polymorphic trinucleotide short tandem repeat (STR) within the human antithrombin gene. trinucleotide 86-99 serpin family C member 1 Homo sapiens 27-39 8206990-10 1994 Changing the P2 residue Phe353-->Gly generated a mutant with a reactive site like antithrombin which was better at inhibiting thrombin or urokinase, but was much less active with APC or trypsin. Glycine 36-39 serpin family C member 1 Homo sapiens 85-97 8202520-5 1994 Heparin affinity was assessed by NaCl gradient elution from heparin-agarose, and second-order rate constants for inhibition by antithrombin III were determined in the absence and presence of heparin. Heparin 191-198 serpin family C member 1 Homo sapiens 127-143 8202520-8 1994 However, affinity for heparin-agarose correlated directly with the rate of inhibition by antithrombin III with heparin. Heparin 22-29 serpin family C member 1 Homo sapiens 89-105 8202520-8 1994 However, affinity for heparin-agarose correlated directly with the rate of inhibition by antithrombin III with heparin. Sepharose 30-37 serpin family C member 1 Homo sapiens 89-105 8202520-8 1994 However, affinity for heparin-agarose correlated directly with the rate of inhibition by antithrombin III with heparin. Heparin 111-118 serpin family C member 1 Homo sapiens 89-105 8172176-0 1994 Genetic linkage studies in antithrombin-deficient kindreds using a highly polymorphic trinucleotide short tandem repeat (STR) within the human antithrombin gene. trinucleotide 86-99 serpin family C member 1 Homo sapiens 143-155 7522311-8 1994 The thrombogenicity of APA may result from their interference with endothelial phospholipids required for antithrombin III and protein C and S anticoagulant activity and prostacyclin synthesis and/or increased endothelial expression of the procoagulants: tissue factor, von Willebrand factor, platelet-activating factor, and plasminogen activator inhibitor type-1. Phospholipids 79-92 serpin family C member 1 Homo sapiens 106-122 8042197-0 1994 Characterization of a highly polymorphic trinucleotide short tandem repeat within the human antithrombin gene. trinucleotide 41-54 serpin family C member 1 Homo sapiens 92-104 8167338-0 1994 Autoantibodies to heparin from patients with antiphospholipid antibody syndrome inhibit formation of antithrombin III-thrombin complexes. Heparin 18-25 serpin family C member 1 Homo sapiens 101-117 8167338-2 1994 Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 158-174 8167338-2 1994 Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan. Heparitin Sulfate 17-19 serpin family C member 1 Homo sapiens 158-174 8167338-2 1994 Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan. Oligosaccharides 122-137 serpin family C member 1 Homo sapiens 158-174 8167338-2 1994 Heparan sulfate (HS) is a physiologic endothelial cell surface modulator of normal anticoagulation, containing a specific oligosaccharide sequence that binds antithrombin III with high affinity and also is present in heparin, a related glycosaminoglycan. Glycosaminoglycans 236-253 serpin family C member 1 Homo sapiens 158-174 8167338-6 1994 Specificity studies showed that low-affinity electrostatic interactions clearly did not account for the observed reactivity with heparin, and that APS IgG antiheparin antibodies were specifically reactive with a disaccharide present in the heparin pentasaccharide that binds antithrombin III. IC 831423 240-263 serpin family C member 1 Homo sapiens 275-291 8167338-7 1994 Furthermore, APS IgG antiheparin antibodies inhibited heparin-accelerated formation of antithrombin III-thrombin complexes. Heparin 25-32 serpin family C member 1 Homo sapiens 87-103 7518511-7 1994 The aggregation induced by neuroblastomas and the pheochromocytoma was also suppressed by pretreatment with an antithrombin agent, argatroban, whereas the aggregation induced by Wilms" tumors was not suppressed by this agent. argatroban 131-141 serpin family C member 1 Homo sapiens 111-123 7512382-0 1994 Conformational change in antithrombin induced by heparin probed with a monoclonal antibody against the 1C/4B region. Heparin 49-56 serpin family C member 1 Homo sapiens 25-37 7512382-1 1994 A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin. Heparin 74-81 serpin family C member 1 Homo sapiens 61-73 7512382-1 1994 A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin. Heparin 74-81 serpin family C member 1 Homo sapiens 160-172 7512382-1 1994 A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin. Heparin 182-189 serpin family C member 1 Homo sapiens 61-73 8087553-1 1994 BACKGROUND: Antithrombin, a member of the serpin family of inhibitors, controls coagulation in human plasma by forming complexes with thrombin and other coagulation proteases in a process greatly accelerated by heparin. Heparin 211-218 serpin family C member 1 Homo sapiens 12-24 7512382-1 1994 A murine monoclonal antibody (MAb) raised against a covalent antithrombin-heparin complex was used to probe the conformational change resulting when the serpin antithrombin binds to heparin. Heparin 182-189 serpin family C member 1 Homo sapiens 160-172 8087553-3 1994 We have determined the structure of intact antithrombin in order to study its mechanism of activation, particularly with respect to heparin, and the dysfunctions of this mechanism that predispose individuals to thrombotic disease. Heparin 132-139 serpin family C member 1 Homo sapiens 43-55 8087553-9 1994 The conformation of the two forms of antithrombin demonstrates the extraordinary mobility of the reactive loop in the serpins and provides insights into the folding of the loop required for inhibitory activity together with the potential modification of this by heparin. Heparin 262-269 serpin family C member 1 Homo sapiens 37-49 7512382-3 1994 However, although the MAb remained bound to antithrombin in the presence of heparin, it did not significantly inhibit heparin cofactor activity against thrombin, and increasing concentrations of the antithrombin-binding pentasaccharide progressively unblocked the inhibitory action of the MAb. pentasaccharide 220-235 serpin family C member 1 Homo sapiens 199-211 7512382-7 1994 However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B. Cysteine 109-112 serpin family C member 1 Homo sapiens 37-49 7512382-7 1994 However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B. Serine 126-129 serpin family C member 1 Homo sapiens 37-49 7512382-7 1994 However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B. Leucine 143-146 serpin family C member 1 Homo sapiens 37-49 7512382-7 1994 However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B. Threonine 160-163 serpin family C member 1 Homo sapiens 37-49 7512382-7 1994 However, interaction of the MAb with antithrombin was reduced by several substitution mutations (Phe402-->Cys, Phe402-->Ser, Phe402-->Leu, Ala404-->Thr, Pro407-->Thr) in the 402-407 sequence which codes for amino acid residues of strand 1C and the polypeptide leading to strand 4B. Threonine 177-180 serpin family C member 1 Homo sapiens 37-49 8054465-0 1994 Prolonged oral contraceptive therapy in a woman with an antithrombin III abnormality involving heparin binding (type IIc) without thromboembolic complications. Heparin 95-102 serpin family C member 1 Homo sapiens 56-72 8003980-2 1994 ATIII attains its full biological activity only upon binding polysulfated oligosaccharides, such as heparin. polysulfated oligosaccharides 61-90 serpin family C member 1 Homo sapiens 0-5 7935513-0 1994 Trinucleotide repeat polymorphism within the human antithrombin gene (AT3): allele frequency data for three population groups. trinucleotide 0-13 serpin family C member 1 Homo sapiens 51-63 7935513-0 1994 Trinucleotide repeat polymorphism within the human antithrombin gene (AT3): allele frequency data for three population groups. trinucleotide 0-13 serpin family C member 1 Homo sapiens 70-73 8003980-2 1994 ATIII attains its full biological activity only upon binding polysulfated oligosaccharides, such as heparin. Heparin 100-107 serpin family C member 1 Homo sapiens 0-5 8003980-3 1994 A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay. Heparin 72-79 serpin family C member 1 Homo sapiens 99-104 8003980-3 1994 A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay. Heparin 131-138 serpin family C member 1 Homo sapiens 99-104 8003980-3 1994 A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay. Heparin 131-138 serpin family C member 1 Homo sapiens 265-270 8003980-3 1994 A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay. Heparin 131-138 serpin family C member 1 Homo sapiens 99-104 8003980-3 1994 A series of synthetic peptides have been prepared based on the proposed heparin binding regions of ATIII and their ability to bind heparin has been assessed by CD spectrometry, by isothermal titration calorimetry, and by the ability of the peptides to compete with ATIII for binding heparin in a factor Xa procoagulant enzyme assay. Heparin 131-138 serpin family C member 1 Homo sapiens 265-270 8003980-4 1994 Peptide F123-G148, which encompasses both the purported high-affinity pentasaccharide binding region and an adjacent, C-terminally directed segment of ATIII, was found to bind heparin with good affinity, but amino-terminal truncations of this sequence, including L130-G148 and K136-G148 displayed attenuated heparin binding activities. Heparin 176-183 serpin family C member 1 Homo sapiens 151-156 8003980-8 1994 K121-A134 also effectively competes with ATIII for binding heparin. Heparin 59-66 serpin family C member 1 Homo sapiens 41-46 8003980-9 1994 Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions. Heparin 84-91 serpin family C member 1 Homo sapiens 115-120 8003980-9 1994 Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions. Heparin 84-91 serpin family C member 1 Homo sapiens 193-198 8003980-9 1994 Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions. Heparin 185-192 serpin family C member 1 Homo sapiens 115-120 8003980-9 1994 Thus, through the use of synthetic peptides that encompass part, if not all, of the heparin binding site(s) within ATIII, we have further elucidated the structure-function relations of heparin-ATIII interactions. Heparin 185-192 serpin family C member 1 Homo sapiens 193-198 8176841-7 1994 Although neither net negative charge nor proportion in total glycosaminoglycans of cell surface heparan sulfate was altered by homocysteine treatment, a substantial reduction in antithrombin III binding capacity of heparan sulfate isolated from homocysteine-treated endothelial cells was found using both affinity chromatography and dot blot assay techniques. Heparitin Sulfate 215-230 serpin family C member 1 Homo sapiens 178-194 8176841-5 1994 Incubations of cultured endothelial cells with homocysteine reduced the amount of antithrombin III bound to the cell surface in a dose- and time-dependent fashion. Homocysteine 47-59 serpin family C member 1 Homo sapiens 82-98 8176841-8 1994 The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine. Homocysteine 94-106 serpin family C member 1 Homo sapiens 4-20 8176841-8 1994 The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine. Cysteine 98-106 serpin family C member 1 Homo sapiens 4-20 8176841-8 1994 The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine. Mercaptoethanol 121-138 serpin family C member 1 Homo sapiens 4-20 8176841-8 1994 The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine. Methionine 242-252 serpin family C member 1 Homo sapiens 4-20 8176841-8 1994 The antithrombin III binding activity of endothelial cells decreased after preincubation with homocysteine, cysteine, or 2-mercaptoethanol, containing a sulfhydryl group; no reduction in binding activity was observed after preincubation with methionine, alanine. Alanine 254-261 serpin family C member 1 Homo sapiens 4-20 8052972-0 1994 Platelet deposition induced by severely damaged vessel wall is inhibited by a boroarginine synthetic peptide with antithrombin activity. boroarginine 78-90 serpin family C member 1 Homo sapiens 114-126 7517074-3 1994 At 0.5-1.0 units/mL antithrombin activity with heparin or hirudin, the ACT was lowered progressively by the addition of increasing concentrations of lysed platelets to as much as 20 seconds below the baseline clotting time obtained with unanticoagulated blood samples. Heparin 47-54 serpin family C member 1 Homo sapiens 20-32 8052962-2 1994 In the present work, we investigated the effects of decreased plasma antithrombin III (ATIII) levels on anticoagulant effects of rhs-TM, as compared to findings with heparin, of which effect is lowered by the decreased plasma ATIII levels in patients with DIC. Heparin 166-173 serpin family C member 1 Homo sapiens 226-231 7935513-1 1994 The fifth intron of the human antithrombin gene (AT3) of chromosome 1q23 contains a highly polymorphic short tandem repeat based on the trinucleotide repeat [ATT]. trinucleotide 136-149 serpin family C member 1 Homo sapiens 30-42 7935513-1 1994 The fifth intron of the human antithrombin gene (AT3) of chromosome 1q23 contains a highly polymorphic short tandem repeat based on the trinucleotide repeat [ATT]. trinucleotide 136-149 serpin family C member 1 Homo sapiens 49-52 8205009-3 1994 Two functional domains in antithrombin are recognised, the reactive site domain which interacts with the active site serine residue of the protease and the heparin binding domain. Serine 117-123 serpin family C member 1 Homo sapiens 26-38 8205009-3 1994 Two functional domains in antithrombin are recognised, the reactive site domain which interacts with the active site serine residue of the protease and the heparin binding domain. Heparin 156-163 serpin family C member 1 Homo sapiens 26-38 8208096-6 1994 Based on experimental evidence, a scheme was proposed, which describes the impact of protein adsorption processes on the anticoagulative activity of surface-bound heparin, It is concluded that AT-III plays a particular role as the major component of the adsorption layer that is responsible for the nature of interactions of polymer materials with blood at the protein and cellular levels. Heparin 163-170 serpin family C member 1 Homo sapiens 193-199 8208096-6 1994 Based on experimental evidence, a scheme was proposed, which describes the impact of protein adsorption processes on the anticoagulative activity of surface-bound heparin, It is concluded that AT-III plays a particular role as the major component of the adsorption layer that is responsible for the nature of interactions of polymer materials with blood at the protein and cellular levels. Polymers 325-332 serpin family C member 1 Homo sapiens 193-199 8180343-2 1994 Antithrombin is also the major plasma cofactor of heparin which exerts its therapeutic effect primarily through its ability to substantially increase the rate of inactivation by antithrombin of the procoagulant serine proteases. Heparin 50-57 serpin family C member 1 Homo sapiens 0-12 8305417-6 1994 The inhibitory activity of antithrombin III was enhanced in the presence of heparin, which on its own had no inhibitory effect on thrombin-induced DNA synthesis. Heparin 76-83 serpin family C member 1 Homo sapiens 27-43 8305417-8 1994 This inhibition was dependent on the presence of antithrombin III in serum, since heparin lacked effect if antithrombin III was depleted from serum by immunoaffinity chromatography. Heparin 82-89 serpin family C member 1 Homo sapiens 49-65 8016817-3 1994 Furthermore, the assay was modified by supplementation with either purified antithrombin III or factor V. The synthetic peptide Ac-(D)Phe-Pro-boroArg-OH (DuP 714) was shown to be the most effective inhibitor of thrombin and also had strong inhibitor actions against factor Xa generation. acetylphenylalanyl-prolyl-boroarginine 128-152 serpin family C member 1 Homo sapiens 76-92 8016817-3 1994 Furthermore, the assay was modified by supplementation with either purified antithrombin III or factor V. The synthetic peptide Ac-(D)Phe-Pro-boroArg-OH (DuP 714) was shown to be the most effective inhibitor of thrombin and also had strong inhibitor actions against factor Xa generation. acetylphenylalanyl-prolyl-boroarginine 154-161 serpin family C member 1 Homo sapiens 76-92 8016817-6 1994 The addition of AT-III to the system did not influence the action of DuP 714 or rH, but it strongly increased the inhibitory effects of unfractionated heparin (PMH) as well as of a low molecular weight heparin (LMWH) on both thrombin and factor Xa generation. Heparin 151-158 serpin family C member 1 Homo sapiens 16-22 8016817-6 1994 The addition of AT-III to the system did not influence the action of DuP 714 or rH, but it strongly increased the inhibitory effects of unfractionated heparin (PMH) as well as of a low molecular weight heparin (LMWH) on both thrombin and factor Xa generation. Heparin 202-209 serpin family C member 1 Homo sapiens 16-22 8029789-0 1994 Thrombin-based antithrombin assays show overestimation of antithrombin III activity in patients on heparin therapy due to heparin cofactor II influence. Heparin 99-106 serpin family C member 1 Homo sapiens 15-27 8029789-0 1994 Thrombin-based antithrombin assays show overestimation of antithrombin III activity in patients on heparin therapy due to heparin cofactor II influence. Heparin 99-106 serpin family C member 1 Homo sapiens 58-74 8029789-6 1994 The results thus suggest that the Factor Xa-based antithrombin III activity method provides more valid results in patients on heparin therapy. Heparin 126-133 serpin family C member 1 Homo sapiens 50-66 8313964-6 1994 Hydrophobic (Val) or negatively charged (Asp or Glu) substitutions were particularly disruptive, in that these variants exhibited less than 10% wild-type antithrombin or antitrypsin activity. Aspartic Acid 41-44 serpin family C member 1 Homo sapiens 154-166 8313964-6 1994 Hydrophobic (Val) or negatively charged (Asp or Glu) substitutions were particularly disruptive, in that these variants exhibited less than 10% wild-type antithrombin or antitrypsin activity. Glutamic Acid 48-51 serpin family C member 1 Homo sapiens 154-166 8180343-2 1994 Antithrombin is also the major plasma cofactor of heparin which exerts its therapeutic effect primarily through its ability to substantially increase the rate of inactivation by antithrombin of the procoagulant serine proteases. Heparin 50-57 serpin family C member 1 Homo sapiens 178-190 8180343-3 1994 Binding of heparin to antithrombin is thus believed to be a prerequisite for this rate enhancement effect. Heparin 11-18 serpin family C member 1 Homo sapiens 22-34 8180343-4 1994 Heparin binding to antithrombin is mediated by a well-defined unique heparin pentasaccharide sequence. Heparin 69-76 serpin family C member 1 Homo sapiens 19-31 8180343-4 1994 Heparin binding to antithrombin is mediated by a well-defined unique heparin pentasaccharide sequence. pentasaccharide 77-92 serpin family C member 1 Homo sapiens 19-31 8180343-5 1994 Interaction between this pentasaccharide sequence and antithrombin induces a conformational change in antithrombin, an alteration that appears to be sufficient to explain the enhanced ability of antithrombin to inhibit factor Xa and related serine proteases, but not thrombin. pentasaccharide 25-40 serpin family C member 1 Homo sapiens 54-66 8180343-5 1994 Interaction between this pentasaccharide sequence and antithrombin induces a conformational change in antithrombin, an alteration that appears to be sufficient to explain the enhanced ability of antithrombin to inhibit factor Xa and related serine proteases, but not thrombin. pentasaccharide 25-40 serpin family C member 1 Homo sapiens 102-114 8180343-5 1994 Interaction between this pentasaccharide sequence and antithrombin induces a conformational change in antithrombin, an alteration that appears to be sufficient to explain the enhanced ability of antithrombin to inhibit factor Xa and related serine proteases, but not thrombin. pentasaccharide 25-40 serpin family C member 1 Homo sapiens 102-114 8299226-17 1994 SLE IgG anti-HS antibodies recognize a sulfated uronic acid epitope containing 2-O-sulfate which is important in certain functions of HS, including antithrombin III binding. Uronic Acids 48-59 serpin family C member 1 Homo sapiens 148-164 8180343-6 1994 Heparin species with longer polysaccharide chains appear to be required in order to enhance the inhibition of thrombin by antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 122-134 8180343-6 1994 Heparin species with longer polysaccharide chains appear to be required in order to enhance the inhibition of thrombin by antithrombin. Polysaccharides 28-42 serpin family C member 1 Homo sapiens 122-134 8180343-7 1994 This may be because the enhancement of this reaction requires that heparin interacts simultaneously with both the antithrombin and the thrombin molecules. Heparin 67-74 serpin family C member 1 Homo sapiens 114-126 8299226-17 1994 SLE IgG anti-HS antibodies recognize a sulfated uronic acid epitope containing 2-O-sulfate which is important in certain functions of HS, including antithrombin III binding. 2-o-sulfate 79-90 serpin family C member 1 Homo sapiens 148-164 8180343-8 1994 This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin. Heparin 47-54 serpin family C member 1 Homo sapiens 59-71 8180343-8 1994 This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin. Heparin 47-54 serpin family C member 1 Homo sapiens 89-101 8180343-8 1994 This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin. Heparin 148-155 serpin family C member 1 Homo sapiens 59-71 8180343-8 1994 This review describes the interactions between heparin and antithrombin, focusing on the antithrombin residues which are involved in the binding of heparin. Heparin 148-155 serpin family C member 1 Homo sapiens 89-101 8180343-9 1994 The role of the heparin-induced conformational change in enhancing serine protease inhibition by antithrombin is also explored. Heparin 16-23 serpin family C member 1 Homo sapiens 97-109 8180343-10 1994 Then, based on available data, an hypothesis is proposed to explain the mechanisms by which heparin accelerates the rate of inactivation by antithrombin of the various serine proteases. Heparin 92-99 serpin family C member 1 Homo sapiens 140-152 8186356-2 1994 Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus. Heparin 36-43 serpin family C member 1 Homo sapiens 92-104 8288594-0 1994 Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III. Amino Acids, Basic 18-34 serpin family C member 1 Homo sapiens 104-120 8288594-0 1994 Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III. Heparin 70-77 serpin family C member 1 Homo sapiens 104-120 8288594-1 1994 The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin. Heparin 44-51 serpin family C member 1 Homo sapiens 90-106 8288594-1 1994 The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin. Heparin 44-51 serpin family C member 1 Homo sapiens 90-102 8288594-1 1994 The therapeutically important anticoagulant heparin catalyzes inactivation of thrombin by antithrombin III via formation of an intermediary ternary thrombin-heparin-antithrombin III complex that is subsequently converted to a stable thrombin-antithrombin III complex with the release of heparin. Heparin 44-51 serpin family C member 1 Homo sapiens 165-177 8288594-2 1994 Point mutations at Arg-180, Arg-245, Lys-248, and Lys-252 in thrombin markedly reduced the efficiency of heparin catalysis by decreasing the stability of the ternary intermediate, whereas the inactivation of thrombin by antithrombin alone was not affected by these mutations. Lysine 50-53 serpin family C member 1 Homo sapiens 220-232 8288594-2 1994 Point mutations at Arg-180, Arg-245, Lys-248, and Lys-252 in thrombin markedly reduced the efficiency of heparin catalysis by decreasing the stability of the ternary intermediate, whereas the inactivation of thrombin by antithrombin alone was not affected by these mutations. Heparin 105-112 serpin family C member 1 Homo sapiens 220-232 8186357-2 1994 In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans. Heparin 91-98 serpin family C member 1 Homo sapiens 40-52 8186357-2 1994 In vitro, the inhibition of thrombin by antithrombin is very slow; but greatly enhanced by heparin and related glycosaminoglycans. Glycosaminoglycans 111-129 serpin family C member 1 Homo sapiens 40-52 8186357-5 1994 This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule. Esters 40-45 serpin family C member 1 Homo sapiens 153-165 8186357-5 1994 This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule. Serine 78-84 serpin family C member 1 Homo sapiens 153-165 8186357-5 1994 This is followed by the formation of an ester linkage between the active site serine residue of the protease and the arginine 393 residue of the cleaved antithrombin molecule. Arginine 117-125 serpin family C member 1 Homo sapiens 153-165 8280781-0 1994 Arg-129 plays a specific role in the conformation of antithrombin and in the enhancement of factor Xa inhibition by the pentasaccharide sequence of heparin. Arginine 0-3 serpin family C member 1 Homo sapiens 53-65 8280781-0 1994 Arg-129 plays a specific role in the conformation of antithrombin and in the enhancement of factor Xa inhibition by the pentasaccharide sequence of heparin. pentasaccharide 120-135 serpin family C member 1 Homo sapiens 53-65 8280781-1 1994 Small amounts of a variant antithrombin (AT) bearing an Arg-129 to Gln mutation were purified from plasma by means of affinity chromatography on insolubilized heparin at very low ionic strength. Heparin 159-166 serpin family C member 1 Homo sapiens 27-39 8186356-2 1994 Inactivation of soluble thrombin by heparin involves the complexing of thrombin with plasma antithrombin, and heparin with heparin, plasma antithrombin and thrombin via binding domains shared by fibrin, thereby explaining the heparin resistance for thrombin bound to thrombus. Heparin 36-43 serpin family C member 1 Homo sapiens 139-151 7947469-0 1994 Heparin surface immobilization through hydrophilic spacers: thrombin and antithrombin III binding kinetics. Heparin 0-7 serpin family C member 1 Homo sapiens 73-89 7951256-0 1994 (ATT) trinucleotide repeats in the antithrombin gene and their use in determining the origin of repeated mutations. trinucleotide 6-19 serpin family C member 1 Homo sapiens 35-47 7951256-1 1994 Two (ATT) trinucleotide repeat polymorphisms have been identified in the tails of Alu repeat elements in intron 5 of the antithrombin gene. trinucleotide 10-23 serpin family C member 1 Homo sapiens 121-133 7947469-2 1994 In this study, the effect of hydrophilic spacers (PEO) on the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin was investigated. Heparin 94-101 serpin family C member 1 Homo sapiens 107-123 7947469-2 1994 In this study, the effect of hydrophilic spacers (PEO) on the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin was investigated. Heparin 94-101 serpin family C member 1 Homo sapiens 125-130 7947469-3 1994 Monodispersed, low molecular weight heparin was fractionated on an ATIII affinity column to isolate high-ATIII affinity heparin. Heparin 36-43 serpin family C member 1 Homo sapiens 67-72 7947469-3 1994 Monodispersed, low molecular weight heparin was fractionated on an ATIII affinity column to isolate high-ATIII affinity heparin. Heparin 120-127 serpin family C member 1 Homo sapiens 105-110 7947469-4 1994 This high-ATIII affinity fraction was immobilized onto a styrene/p-amino styrene random copolymer surface using hydrophilic poly(ethylene oxide) (PEO) spacer groups. Styrene 57-64 serpin family C member 1 Homo sapiens 10-15 7947469-4 1994 This high-ATIII affinity fraction was immobilized onto a styrene/p-amino styrene random copolymer surface using hydrophilic poly(ethylene oxide) (PEO) spacer groups. p-amino styrene random copolymer 65-97 serpin family C member 1 Homo sapiens 10-15 7947469-4 1994 This high-ATIII affinity fraction was immobilized onto a styrene/p-amino styrene random copolymer surface using hydrophilic poly(ethylene oxide) (PEO) spacer groups. Polyethylene Glycols 124-144 serpin family C member 1 Homo sapiens 10-15 7947469-9 1994 Soluble heparin bound both thrombin and ATIII, while heparin immobilized directly onto the surface bound only thrombin. Heparin 8-15 serpin family C member 1 Homo sapiens 40-45 7947469-10 1994 Spacer-immobilized heparin bound both ATIII and thrombin, although to a lesser extent than soluble heparin. Heparin 19-26 serpin family C member 1 Homo sapiens 38-43 7947469-11 1994 Thus, the enhanced bioactivity of spacer-immobilized heparin, compared to direct-immobilization, may be attributed to the retention of ATIII binding. Heparin 53-60 serpin family C member 1 Homo sapiens 135-140 8241508-6 1993 This was confirmed in a heparin cofactor II-dependent antithrombin assay for DS that showed anticoagulant equivalent to 2.2 +/- 0.3 micrograms/mL (mean +/- SD) of porcine mucosal DS. Dermatan Sulfate 77-79 serpin family C member 1 Homo sapiens 54-66 8165617-2 1993 In molar terms, antithrombin III was the most abundant protein bound to therapeutic doses of unfractionated heparin (M(r) = 12,000), whereas heparin cofactor II constituted < 1% of the protein bound. Heparin 108-115 serpin family C member 1 Homo sapiens 16-32 8165617-5 1993 Binding of both antithrombin III and histidine-rich glycoprotein varied with the ratio of heparin to plasma. Heparin 90-97 serpin family C member 1 Homo sapiens 16-32 8165617-6 1993 Clexane (M(r) = 4,500) also bound antithrombin III, but both histidine-rich glycoprotein and vitronectin were quantitatively significant neutralising proteins. Enoxaparin 0-7 serpin family C member 1 Homo sapiens 34-50 8148487-6 1993 We conclude that long-term treatment with tamoxifen for 2 or more years tends to reduce both AT-III and PC, a situation possibly predisposing towards thrombosis. Tamoxifen 42-51 serpin family C member 1 Homo sapiens 93-99 8028997-3 1994 The anticoagulant effect is particularly dependent upon the presence of a specific pentasaccharide sequence, which binds to the proteinase inhibitor, antithrombin. pentasaccharide 83-98 serpin family C member 1 Homo sapiens 150-162 8152901-1 1994 Some commercially available chronometric assays are influenced by the residual antithrombin activity of low molecular weight heparins (LMWH) and they underestimate the ex vivo anti Xa activity. Heparin 125-133 serpin family C member 1 Homo sapiens 79-91 8152901-1 1994 Some commercially available chronometric assays are influenced by the residual antithrombin activity of low molecular weight heparins (LMWH) and they underestimate the ex vivo anti Xa activity. Heparin, Low-Molecular-Weight 135-139 serpin family C member 1 Homo sapiens 79-91 7801599-1 1994 We describe an improved method for large-scale purification of antithrombin III (AT-III) from human plasma involving heparin affinity chromatography of redissolved fraction IV-1 paste, viral inactivation by heating, followed by a second heparin affinity column. Heparin 117-124 serpin family C member 1 Homo sapiens 63-79 7801599-1 1994 We describe an improved method for large-scale purification of antithrombin III (AT-III) from human plasma involving heparin affinity chromatography of redissolved fraction IV-1 paste, viral inactivation by heating, followed by a second heparin affinity column. Heparin 117-124 serpin family C member 1 Homo sapiens 81-87 8262929-10 1993 The enhancing effect of heparin on the inhibitory process is concentration dependent and exhibits an optimum, reminiscent of the "template" model for heparin"s acceleration of thrombin and factor IXa inhibition by antithrombin III. Heparin 24-31 serpin family C member 1 Homo sapiens 214-230 8263926-1 1993 Human antithrombin has been crystallized by microdialysis at pH 6.7 using 18% (w/v) polyethylene glycol-4000 as precipitant. polyethylene glycol 4000 84-108 serpin family C member 1 Homo sapiens 6-18 8263926-7 1993 This latter form also had a low affinity for heparin and in these ways resembles latent antithrombin. Heparin 45-52 serpin family C member 1 Homo sapiens 88-100 7693706-3 1993 Vitronectin complexed to thrombin-antithrombin or C5b-9 is conformationally altered as evidenced by enhanced reactivity with monoclonal antibody 8E6 and binding to heparin; these same alterations also occur when vitronectin is treated with urea (Tomasini, B. R., and Mosher, D.F. Urea 240-244 serpin family C member 1 Homo sapiens 34-46 8243674-0 1993 Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinities. Carbohydrates 0-12 serpin family C member 1 Homo sapiens 25-37 8243674-0 1993 Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinities. Heparin 67-74 serpin family C member 1 Homo sapiens 25-37 8137606-3 1993 All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin. Heparin, Low-Molecular-Weight 4-16 serpin family C member 1 Homo sapiens 29-45 8137606-3 1993 All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin. pentasaccharide 55-70 serpin family C member 1 Homo sapiens 29-45 8137606-3 1993 All LMW heparins contain the antithrombin III-specific pentasaccharide unit found on unfractionated heparin. Heparin 8-15 serpin family C member 1 Homo sapiens 29-45 8175200-3 1993 Binding of antibodies against factor XII, antithrombin III (ATIII) and platelet receptor GpIb were significantly higher (p < 0.01) on the Duraflo II treated surface. duraflo ii 141-151 serpin family C member 1 Homo sapiens 42-58 8175200-3 1993 Binding of antibodies against factor XII, antithrombin III (ATIII) and platelet receptor GpIb were significantly higher (p < 0.01) on the Duraflo II treated surface. duraflo ii 141-151 serpin family C member 1 Homo sapiens 60-65 8243674-1 1993 We have changed one of the carbohydrate-bearing asparagine residues of human antithrombin to glutamine by site-directed mutagenesis and expressed the variant antithrombin, N135Q, in baby hamster kidney cells. Carbohydrates 27-39 serpin family C member 1 Homo sapiens 77-89 7692967-5 1993 Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present. Sodium Dodecyl Sulfate 31-34 serpin family C member 1 Homo sapiens 212-224 8243674-1 1993 We have changed one of the carbohydrate-bearing asparagine residues of human antithrombin to glutamine by site-directed mutagenesis and expressed the variant antithrombin, N135Q, in baby hamster kidney cells. Asparagine 48-58 serpin family C member 1 Homo sapiens 77-89 7692967-5 1993 Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present. Iodine-125 62-66 serpin family C member 1 Homo sapiens 212-224 7692967-0 1993 High molecular weight kininogen potentiates the heparin-accelerated inhibition of plasma kallikrein by antithrombin: role for antithrombin in the regulation of kallikrein. Heparin 48-55 serpin family C member 1 Homo sapiens 103-115 7692967-5 1993 Consistent with these results, SDS gel electrophoresis of the 125I-labeled kallikrein-inhibitor complexes formed in a mixture of these kallikrein inhibitors at their relative plasma concentrations indicated that antithrombin effectively competed with C1-inhibitor and alpha 2-macroglobulin for kallikrein, accounting for 54% of the total kallikrein complexes, only when both heparin and H-kininogen were present. Heparin 375-382 serpin family C member 1 Homo sapiens 212-224 7692967-2 1993 H-kininogen, at levels sufficient to fully complex kallikrein, greatly potentiated the acceleration of antithrombin inhibition of kallikrein produced by heparin with high affinity for antithrombin. Heparin 153-160 serpin family C member 1 Homo sapiens 103-115 7692967-2 1993 H-kininogen, at levels sufficient to fully complex kallikrein, greatly potentiated the acceleration of antithrombin inhibition of kallikrein produced by heparin with high affinity for antithrombin. Heparin 153-160 serpin family C member 1 Homo sapiens 184-196 7692967-6 1993 Similarly, the presence of therapeutic levels of heparin (approximately 1 unit/mL) in normal, factor XII-deficient, and prekallikrein-deficient plasmas enhanced the rate of inactivation of added kallikrein by 2.3-fold and significantly altered the partitioning of radiolabeled kallikrein from predominantly C1-inhibitor and alpha 2-macroglobulin complexes (86-92%) to mostly antithrombin complexes (50-53%). Heparin 49-56 serpin family C member 1 Homo sapiens 375-387 7692967-3 1993 At I = 0.15, pH 7.4, 25 degrees C, kininogen thus maximally increased the heparin enhancement of the second-order rate constant for the antithrombin-kallikrein reaction from 13-fold (1.6 x 10(2) M-1 s-1 to 2.1 x 10(3) M-1 s-1) to 1200-fold (1.9 x 10(5) M-1 s-1). Heparin 74-81 serpin family C member 1 Homo sapiens 136-148 7692967-8 1993 The contribution of antithrombin to kallikrein inhibition in plasma remained significant (approximately 40-70%) at optimal concentrations of unfractionated or size- and antithrombin affinity-fractionated heparin, in the presence of plasma levels of calcium and zinc ions, at 37 degrees C, and with minimal plasma dilution. Heparin 204-211 serpin family C member 1 Homo sapiens 20-32 8218292-3 1993 Both H-kininogen-stimulated and unstimulated heparin rate enhancements initially increased with increasing heparin concentration in a manner corresponding to the saturation of antithrombin with heparin (KD = 10-30 nM). Heparin 45-52 serpin family C member 1 Homo sapiens 176-188 7692967-9 1993 These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans. Heparin 141-148 serpin family C member 1 Homo sapiens 27-39 7692967-9 1993 These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans. Heparin 152-159 serpin family C member 1 Homo sapiens 27-39 8218292-3 1993 Both H-kininogen-stimulated and unstimulated heparin rate enhancements initially increased with increasing heparin concentration in a manner corresponding to the saturation of antithrombin with heparin (KD = 10-30 nM). Heparin 107-114 serpin family C member 1 Homo sapiens 176-188 7692967-9 1993 These results suggest that antithrombin and H-kininogen may play important roles in the regulation of kallikrein activity in the presence of heparin or heparin-like glycosaminoglycans. Glycosaminoglycans 165-183 serpin family C member 1 Homo sapiens 27-39 8218292-3 1993 Both H-kininogen-stimulated and unstimulated heparin rate enhancements initially increased with increasing heparin concentration in a manner corresponding to the saturation of antithrombin with heparin (KD = 10-30 nM). Heparin 107-114 serpin family C member 1 Homo sapiens 176-188 8227367-7 1993 When the second-order rate constant of PN-2/A beta PP"s inhibition of Factor IXa (2.7 x 10(8) M-1min-1) was compared to that of antithrombin III (3.8 x 10(6) M-1min-1), PN-2/A beta PP was at least a 71-fold more potent inhibitor of Factor IXa than antithrombin III. beta pp 46-53 serpin family C member 1 Homo sapiens 248-264 8218292-5 1993 These results implied that H-kininogen stimulation required the formation of a quaternary complex in which antithrombin and H-kininogen-kallikrein complex were bound to the same heparin chain. Heparin 178-185 serpin family C member 1 Homo sapiens 107-119 8218292-6 1993 In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen. IC 831423 49-72 serpin family C member 1 Homo sapiens 90-102 8218292-6 1993 In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen. IC 831423 49-72 serpin family C member 1 Homo sapiens 136-148 8218292-6 1993 In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen. pentasaccharide 57-72 serpin family C member 1 Homo sapiens 90-102 8218292-6 1993 In keeping with this interpretation, a synthetic heparin pentasaccharide representing the antithrombin binding sequence accelerated the antithrombin-kallikrein reaction to an extent similar to that of full-length heparin chains containing this sequence, but the pentasaccharide acceleration was not stimulated by H-kininogen. pentasaccharide 57-72 serpin family C member 1 Homo sapiens 136-148 8218292-7 1993 The importance of H-kininogen-kallikrein complex binding to heparin for kininogen stimulation was further indicated from the marked salt dependence of the second-order rate constant for the association of H-kininogen-kallikrein complex but not free kallikrein with antithrombin-heparin complex, under conditions where saturation of the two binary complexes was maintained. Heparin 60-67 serpin family C member 1 Homo sapiens 265-277 8128425-3 1993 As an alternative we define a unit of heparin in terms of anti-factor Xa- and antithrombin-activity that is independent of the heparin standard and of the assay method, but that is based upon a quantitative description of the catalytic effect of heparin on AT III mediated thrombin- and factor Xa breakdown. Heparin 38-45 serpin family C member 1 Homo sapiens 78-90 8128425-3 1993 As an alternative we define a unit of heparin in terms of anti-factor Xa- and antithrombin-activity that is independent of the heparin standard and of the assay method, but that is based upon a quantitative description of the catalytic effect of heparin on AT III mediated thrombin- and factor Xa breakdown. Heparin 38-45 serpin family C member 1 Homo sapiens 257-263 8128425-4 1993 Expression of the results of existing anti-factor Xa- and antithrombin tests in terms of these units will allow to express heparin levels in plasma in terms of concentrations of active anticoagulant material. Heparin 123-130 serpin family C member 1 Homo sapiens 58-70 8246447-0 1993 Ultrastructural localization of heparin to human mast cells of the MCTC and MCT types by labeling with antithrombin III-gold. Heparin 32-39 serpin family C member 1 Homo sapiens 103-119 8246447-9 1993 CONCLUSIONS: The data with rodent mast cells indicate that antithrombin III-gold labels cells that contain heparin, but not those that contain only over-sulfated chondroitin sulfates. Heparin 107-114 serpin family C member 1 Homo sapiens 59-75 8309935-2 1993 A general procedure for arriving at 3-D models of disulphide-rich polypeptide systems based on the covalent cross-link constraints has been developed. disulphide 50-60 serpin family C member 1 Homo sapiens 33-39 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 90-102 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. ps 21-23 serpin family C member 1 Homo sapiens 90-106 8115989-0 1993 Antithrombotic effects of synthetic pentasaccharide with high affinity for plasma antithrombin III in non-human primates. pentasaccharide 36-51 serpin family C member 1 Homo sapiens 82-98 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 90-106 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. ps 21-23 serpin family C member 1 Homo sapiens 108-113 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 108-113 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. ps 21-23 serpin family C member 1 Homo sapiens 90-102 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. Heparin 48-55 serpin family C member 1 Homo sapiens 90-106 8115989-1 1993 The pentasaccharide (PS) comprising the minimal heparin structure capable of binding with antithrombin III (ATIII) and exhibiting anti-factor Xa (anti-fXa) activity in plasma without producing detectable antithrombin activity, has been evaluated for its relative antithrombotic and antihemostatic effects in a baboon model combining both platelet-rich and fibrin-rich thrombosis. Heparin 48-55 serpin family C member 1 Homo sapiens 90-102 8122184-5 1993 Antithrombin-III activity returned to the control values 4 hours after the discontinuation of heparin. Heparin 94-101 serpin family C member 1 Homo sapiens 0-16 8408007-7 1993 The cytoplasmic antithrombin activity was purified to apparent homogeneity from the cytosol of BSC-1 cells previously pulsed with [35S]methionine by a combination of heparin-agarose chromatography, Mono Q fast protein liquid chromatography, and anhydrotrypsin-Affi-Gel 10 affinity chromatography. Sulfur-35 131-134 serpin family C member 1 Homo sapiens 16-28 8408007-7 1993 The cytoplasmic antithrombin activity was purified to apparent homogeneity from the cytosol of BSC-1 cells previously pulsed with [35S]methionine by a combination of heparin-agarose chromatography, Mono Q fast protein liquid chromatography, and anhydrotrypsin-Affi-Gel 10 affinity chromatography. Methionine 135-145 serpin family C member 1 Homo sapiens 16-28 8408007-7 1993 The cytoplasmic antithrombin activity was purified to apparent homogeneity from the cytosol of BSC-1 cells previously pulsed with [35S]methionine by a combination of heparin-agarose chromatography, Mono Q fast protein liquid chromatography, and anhydrotrypsin-Affi-Gel 10 affinity chromatography. Heparin 166-173 serpin family C member 1 Homo sapiens 16-28 8408007-7 1993 The cytoplasmic antithrombin activity was purified to apparent homogeneity from the cytosol of BSC-1 cells previously pulsed with [35S]methionine by a combination of heparin-agarose chromatography, Mono Q fast protein liquid chromatography, and anhydrotrypsin-Affi-Gel 10 affinity chromatography. Sepharose 174-181 serpin family C member 1 Homo sapiens 16-28 8122184-0 1993 Antithrombin-III plasma activity during and after prolonged use of heparin in unstable angina. Heparin 67-74 serpin family C member 1 Homo sapiens 0-16 8122184-4 1993 Plasma antithrombin-III activity decreased rapidly from 1.05 +/- 0.03 to 1.0 +/- 0.03 U/ml (p < 0.03) following heparin initiation with no further significant subsequent decrease. Heparin 115-122 serpin family C member 1 Homo sapiens 7-23 8216224-11 1993 for protease nexin I, protein C inhibitor and antithrombin III showed a bell-shaped dependence on heparin concentration. Heparin 98-105 serpin family C member 1 Homo sapiens 46-62 8216224-12 1993 At optimal concentrations, heparin accelerated the rate of inhibition by protease nexin I, protein C inhibitor and antithrombin III by 44-, 18- and 13-fold respectively. Heparin 27-34 serpin family C member 1 Homo sapiens 115-131 8122184-6 1993 Thus, heparin treatment is associated with small, non-cumulative and rapidly reversible decrease in antithrombin-III activity. Heparin 6-13 serpin family C member 1 Homo sapiens 100-116 8350363-4 1993 Tamoxifen may also influence risk factors for cardiac and thromboembolic disease (e.g., serum cholesterol and antithrombin III). Tamoxifen 0-9 serpin family C member 1 Homo sapiens 110-126 8376590-3 1993 Incubations of porcine aortic endothelial cell cultures with homocysteine reduced the amount of antithrombin III bound to the cell surface in a dose- and time-dependent fashion. Homocysteine 61-73 serpin family C member 1 Homo sapiens 96-112 8376590-4 1993 The inhibitory effect was observed at a homocysteine concentration as low as 0.1 mM, and the maximal suppression occurred at 1 mM of homocysteine after 24 h. In contrast with a marked reduction in the maximal antithrombin III binding capacity (approximately 30% of control), the radioactivity of [35S]sulfate incorporated into heparan sulfate on the cell surface was minimally (< 15%) reduced. Homocysteine 133-145 serpin family C member 1 Homo sapiens 209-225 8376590-6 1993 Although neither net negative charge nor proportion in total glycosaminoglycans of cell surface heparan sulfate was altered by homocysteine treatment, a substantial reduction in antithrombin III binding capacity of heparan sulfate isolated from homocysteine-treated endothelial cells was found using both affinity chromatography and dot blot assay techniques. Heparitin Sulfate 215-230 serpin family C member 1 Homo sapiens 178-194 8376590-7 1993 The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine. Cysteine 103-111 serpin family C member 1 Homo sapiens 4-20 8376590-7 1993 The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine. Mercaptoethanol 126-143 serpin family C member 1 Homo sapiens 4-20 8376590-7 1993 The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine. Methionine 242-252 serpin family C member 1 Homo sapiens 4-20 8376590-7 1993 The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine. Alanine 254-261 serpin family C member 1 Homo sapiens 4-20 8259546-6 1993 DS addition selectively increases the formation of heparin cofactor II (HCII)-IIa complexes, whereas LMWH enhances ATIII-IIa complex generation. Heparin, Low-Molecular-Weight 101-105 serpin family C member 1 Homo sapiens 115-120 8376590-7 1993 The antithrombin III binding activity of endothelial cells decreased after preincubation with 1 mM homocysteine, cysteine, or 2-mercaptoethanol; no reduction in binding activity was observed after preincubation with the same concentration of methionine, alanine, or valine. Valine 266-272 serpin family C member 1 Homo sapiens 4-20 8259546-7 1993 Compared to plasma containing DS alone, the formation of ATIII-IIa complexes also is increased when the combination of DS and LMWH is added. Dermatan Sulfate 119-121 serpin family C member 1 Homo sapiens 57-62 8259546-7 1993 Compared to plasma containing DS alone, the formation of ATIII-IIa complexes also is increased when the combination of DS and LMWH is added. Heparin, Low-Molecular-Weight 126-130 serpin family C member 1 Homo sapiens 57-62 8259547-6 1993 However, when heparin was added ATIII was the major anticoagulant, but profound prolongation of the clotting time was only seen when TFPI was also added. Heparin 14-21 serpin family C member 1 Homo sapiens 32-37 8259547-7 1993 In an ATIII deficient plasma heparin did not augment the effect of TFPI, showing that the increased effect of TFPI in the presence of heparin is dependent on the anticoagulant activity of ATIII/heparin. Heparin 134-141 serpin family C member 1 Homo sapiens 188-193 8343518-2 1993 We have determined the dissociation constants, Kd, of 48.8 nM for the heparin-AT III interaction, of 175 nM for the specific pentasaccharide-AT III interaction, and of 13 microM for the low-affinity heparin-AT III interaction, using a binding assay based on a monoclonal antibody (MAb) that recognizes an epitope at or close to the heparin binding site of AT III. pentasaccharide 125-140 serpin family C member 1 Homo sapiens 141-147 8238864-5 1993 A hexasaccharide having a 3-O-sulfated glucosamine residue at the reducing end and arising from heparin"s antithrombin III binding site, migrated in an unusual fashion. hexasaccharide 2-16 serpin family C member 1 Homo sapiens 106-122 8357789-0 1993 Transmission of conformational change from the heparin binding site to the reactive center of antithrombin. Heparin 47-54 serpin family C member 1 Homo sapiens 94-106 8357789-1 1993 Heparin greatly increases the rates at which antithrombin inhibits target proteinases. Heparin 0-7 serpin family C member 1 Homo sapiens 45-57 8357789-2 1993 An important part of this rate acceleration is a heparin-induced conformational change in antithrombin. Heparin 49-56 serpin family C member 1 Homo sapiens 90-102 8357789-3 1993 To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide. Cysteine 169-177 serpin family C member 1 Homo sapiens 136-148 8357789-3 1993 To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide. 2-Nitrobenzofuran 183-198 serpin family C member 1 Homo sapiens 136-148 8357789-3 1993 To answer the question of whether or not this change is transmitted to the reactive center, we have prepared a recombinant P1 mutant of antithrombin, R393C, labeled the cysteine with nitrobenzofuran (NBD) fluorophore, and examined the perturbation of NBD fluorescence intensity as a function of bound sulfated oligosaccharide. Oligosaccharides 310-325 serpin family C member 1 Homo sapiens 136-148 8357789-5 1993 We found (i) that binding to antithrombin of all these oligosaccharides resulted in transmission of conformational change to P1 in the reactive center, (ii) that these oligosaccharides all gave enhancements of the rate of inhibition of factor Xa beyond any contribution from surface approximation, and (iii) that the degree of perturbation of P1 correlated with the enhancement of the rate of factor Xa inhibition that was not due to surface approximation. Oligosaccharides 55-71 serpin family C member 1 Homo sapiens 29-41 8357789-5 1993 We found (i) that binding to antithrombin of all these oligosaccharides resulted in transmission of conformational change to P1 in the reactive center, (ii) that these oligosaccharides all gave enhancements of the rate of inhibition of factor Xa beyond any contribution from surface approximation, and (iii) that the degree of perturbation of P1 correlated with the enhancement of the rate of factor Xa inhibition that was not due to surface approximation. Oligosaccharides 168-184 serpin family C member 1 Homo sapiens 29-41 8236137-2 1993 The present report describes the antithrombin mediated inhibition of thrombin and factor Xa by surfaces modified with end point immobilized heparin. Heparin 140-147 serpin family C member 1 Homo sapiens 33-45 8236137-4 1993 Both enzymes were rapidly inactivated by heparin surfaces after selective presaturation with antithrombin on the immobilized high affinity heparin molecules. Heparin 41-48 serpin family C member 1 Homo sapiens 93-105 8236137-4 1993 Both enzymes were rapidly inactivated by heparin surfaces after selective presaturation with antithrombin on the immobilized high affinity heparin molecules. Heparin 139-146 serpin family C member 1 Homo sapiens 93-105 8215954-3 1993 The other surface consisted of a fraction of heparin molecules with low affinity for antithrombin (LA heparin surface) and essentially devoid of antithrombin-binding as well as anticoagulant activity. Heparin 45-52 serpin family C member 1 Homo sapiens 85-97 8343518-2 1993 We have determined the dissociation constants, Kd, of 48.8 nM for the heparin-AT III interaction, of 175 nM for the specific pentasaccharide-AT III interaction, and of 13 microM for the low-affinity heparin-AT III interaction, using a binding assay based on a monoclonal antibody (MAb) that recognizes an epitope at or close to the heparin binding site of AT III. Heparin 70-77 serpin family C member 1 Homo sapiens 78-84 8343518-0 1993 Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 60-76 8343518-0 1993 Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 145-161 8343518-0 1993 Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III. Heparin 121-128 serpin family C member 1 Homo sapiens 60-76 8343518-0 1993 Heparin binding affinity of normal and genetically modified antithrombin III measured using a monoclonal antibody to the heparin binding site of antithrombin III. Heparin 121-128 serpin family C member 1 Homo sapiens 145-161 8343518-1 1993 The inhibitory activity of the plasma serine proteinase inhibitor antithrombin III (AT III) is enhanced about 1000-fold upon binding to heparin. Heparin 136-143 serpin family C member 1 Homo sapiens 66-82 8343518-1 1993 The inhibitory activity of the plasma serine proteinase inhibitor antithrombin III (AT III) is enhanced about 1000-fold upon binding to heparin. Heparin 136-143 serpin family C member 1 Homo sapiens 84-90 8343518-2 1993 We have determined the dissociation constants, Kd, of 48.8 nM for the heparin-AT III interaction, of 175 nM for the specific pentasaccharide-AT III interaction, and of 13 microM for the low-affinity heparin-AT III interaction, using a binding assay based on a monoclonal antibody (MAb) that recognizes an epitope at or close to the heparin binding site of AT III. pentasaccharide 125-140 serpin family C member 1 Homo sapiens 141-147 8343518-2 1993 We have determined the dissociation constants, Kd, of 48.8 nM for the heparin-AT III interaction, of 175 nM for the specific pentasaccharide-AT III interaction, and of 13 microM for the low-affinity heparin-AT III interaction, using a binding assay based on a monoclonal antibody (MAb) that recognizes an epitope at or close to the heparin binding site of AT III. pentasaccharide 125-140 serpin family C member 1 Homo sapiens 141-147 8343518-3 1993 The heparin binding affinities and proportions of normal and variant AT III in plasma from patients with mutations of AT III have been quantitated for the first time using the binding assay. Heparin 4-11 serpin family C member 1 Homo sapiens 118-124 7687144-1 1993 Identical or highly similar antigenic determinants, not present in the intact inhibitor, were induced in antithrombin on cleavage of the reactive bond, on formation of a complex between antithrombin and a synthetic reactive-loop tetradecapeptide, and on partial denaturation of antithrombin at low concentrations of guanidinium chloride. Guanidine 316-336 serpin family C member 1 Homo sapiens 105-117 8362374-3 1993 One of these antibodies was studied in detail and was found to inhibit the heparin dependent activation of antithrombin III by up to 80%. Heparin 75-82 serpin family C member 1 Homo sapiens 107-123 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Polysaccharides 16-31 serpin family C member 1 Homo sapiens 125-141 8331659-6 1993 The most significant difference between ATIII and alpha 1-antitrypsin lies in the 45 residue N-terminal extension in ATIII which contribute to the definition of the heparin binding site. Heparin 165-172 serpin family C member 1 Homo sapiens 40-45 8331659-6 1993 The most significant difference between ATIII and alpha 1-antitrypsin lies in the 45 residue N-terminal extension in ATIII which contribute to the definition of the heparin binding site. Heparin 165-172 serpin family C member 1 Homo sapiens 117-122 8331659-9 1993 Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein. pentasaccharide 15-30 serpin family C member 1 Homo sapiens 101-106 8331659-9 1993 Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein. Heparin 77-84 serpin family C member 1 Homo sapiens 101-106 8331659-9 1993 Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein. Arginine 137-145 serpin family C member 1 Homo sapiens 101-106 8331659-9 1993 Docking of the pentasaccharide unit which represents the minimum fragment of heparin able to bind to ATIII indicates a possible role for arginine 14 in the interaction of heparin and the protein. Heparin 171-178 serpin family C member 1 Homo sapiens 101-106 8331144-6 1993 The ATIII binding capacities of the membranes were found to be 91 micrograms/cm2 for the amine-modified and 39 micrograms/cm2 for the epoxy-activated membrane, achieving purities of 75%. Amines 89-94 serpin family C member 1 Homo sapiens 4-9 8331144-5 1993 The second approach consisted of using heparin, a mucopolysaccharide with a strong affinity towards ATIII, coupled to amine-modified or epoxy-activated membranes by reductive amination, for the purification of rATIII. Heparin 39-46 serpin family C member 1 Homo sapiens 100-105 8331144-5 1993 The second approach consisted of using heparin, a mucopolysaccharide with a strong affinity towards ATIII, coupled to amine-modified or epoxy-activated membranes by reductive amination, for the purification of rATIII. Glycosaminoglycans 50-68 serpin family C member 1 Homo sapiens 100-105 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Polysaccharides 16-31 serpin family C member 1 Homo sapiens 143-148 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Dermatan Sulfate 33-50 serpin family C member 1 Homo sapiens 125-141 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Dermatan Sulfate 33-50 serpin family C member 1 Homo sapiens 143-148 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. fucan 52-57 serpin family C member 1 Homo sapiens 125-141 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. fucan 52-57 serpin family C member 1 Homo sapiens 143-148 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Heparin 62-69 serpin family C member 1 Homo sapiens 125-141 8335699-1 1993 Three sulphated polysaccharides, dermatan sulphate, fucan and heparin, were fractionated according to their affinity towards antithrombin III (ATIII) and heparin cofactor II (HCII), the two main physiological thrombin (IIa) inhibitors. Heparin 62-69 serpin family C member 1 Homo sapiens 143-148 8335699-5 1993 The possible presence of a unique binding site for ATIII and HCII, on each sulphated polysaccharide, was also studied. Polysaccharides 85-99 serpin family C member 1 Homo sapiens 51-56 8392392-4 1993 Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser). Arginine 156-159 serpin family C member 1 Homo sapiens 111-123 8392392-4 1993 Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser). Serine 160-163 serpin family C member 1 Homo sapiens 111-123 8392392-4 1993 Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser). Leucine 200-203 serpin family C member 1 Homo sapiens 111-123 8392392-4 1993 Proteinases recognize a specific peptide, termed the reactive site, near the carboxyl-terminus of serpins (for antithrombin and protein C inhibitor this is Arg-Ser and for heparin cofactor II this is Leu-Ser). Serine 204-207 serpin family C member 1 Homo sapiens 111-123 8392392-6 1993 The therapeutic anticoagulant action of the glycosaminoglycan heparin is believed to depend partially on heparin-accelerated inhibition of proteinases by antithrombin. glycosaminoglycan heparin 44-69 serpin family C member 1 Homo sapiens 154-166 8358152-2 1993 The mode of binding of PF4 to heparin was investigated in a comparative study also involving antithrombin (AT; previously shown to selectively bind a specific oligosaccharide sequence) and fibronectin (FN; non-specific electrostatic interaction). Oligosaccharides 159-174 serpin family C member 1 Homo sapiens 93-105 8388351-8 1993 The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin. Chondroitin Sulfates 4-23 serpin family C member 1 Homo sapiens 100-116 8408111-1 1993 Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE). Oligosaccharides 0-16 serpin family C member 1 Homo sapiens 51-67 8408111-1 1993 Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE). Oligosaccharides 0-16 serpin family C member 1 Homo sapiens 69-74 8408111-1 1993 Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE). Heparin 20-27 serpin family C member 1 Homo sapiens 51-67 8408111-1 1993 Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE). Heparin 20-27 serpin family C member 1 Homo sapiens 69-74 8408111-1 1993 Oligosaccharides of heparin with high affinity for antithrombin III (ATIII) have been immobilized onto surface-modified NHLBI Primary Reference low density polyethylene (PE). Polyethylene 144-168 serpin family C member 1 Homo sapiens 69-74 8408111-6 1993 Visual confirmation of ATIII binding to immobilized HA-heparin was demonstrated by a gold-labeled double antibody method with imaging by SEM. ha-heparin 52-62 serpin family C member 1 Homo sapiens 23-28 8350512-8 1993 The authors developed an antithrombin III assay method to be able to estimate real activity without the influence of heparin cofactor II activity11), and to apply the low molecular weight heparin to prevent relapse of thrombosis, and finally to find an anticoagulant substance in an interesting case of hepatocellular carcinoma (Edmondson type 1) producing normal antithrombin III30). Heparin 117-124 serpin family C member 1 Homo sapiens 25-41 8491059-12 1993 A highly significant correlation (p < 0.001) was found between phenazone clearance and the prothrombin time, albumin, gamma-globulin, factor V, antithrombin III, fibrinogen and total bilirubin. Antipyrine 66-75 serpin family C member 1 Homo sapiens 147-163 8443391-0 1993 Antithrombin III Nagasaki (Ser116-Pro): a heterozygous variant with defective heparin binding associated with thrombosis. Heparin 78-85 serpin family C member 1 Homo sapiens 0-16 8443391-1 1993 A novel variant of antithrombin III (AT III) that lacks affinity for heparin was found in a 33-year-old man who suffered from recurrent cerebral infarction. Heparin 69-76 serpin family C member 1 Homo sapiens 19-35 8443391-1 1993 A novel variant of antithrombin III (AT III) that lacks affinity for heparin was found in a 33-year-old man who suffered from recurrent cerebral infarction. Heparin 69-76 serpin family C member 1 Homo sapiens 37-43 8443391-7 1993 Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally. Heparin 100-107 serpin family C member 1 Homo sapiens 152-158 8443391-7 1993 Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally. Sepharose 108-117 serpin family C member 1 Homo sapiens 152-158 8443391-7 1993 Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally. Heparin 100-107 serpin family C member 1 Homo sapiens 152-158 8443391-7 1993 Analysis by crossed immunoelectrophoresis in the presence of heparin and affinity chromatography on heparin-Sepharose demonstrated that the propositus" AT III was composed of two populations, one having no affinity for heparin and the other binding heparin normally. Heparin 100-107 serpin family C member 1 Homo sapiens 152-158 8443391-8 1993 Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion. Thymine 137-144 serpin family C member 1 Homo sapiens 52-58 8443391-8 1993 Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion. Thymine 137-144 serpin family C member 1 Homo sapiens 187-193 8443391-8 1993 Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion. Cytosine 148-156 serpin family C member 1 Homo sapiens 52-58 8443391-8 1993 Nucleotide sequencing of 7 exons of the propositus" AT III gene using polymerase chain reaction and subcloning disclosed a transition of thymine to cytosine in exon 3a (codon 116) of the AT III gene leading to a Ser116-Pro conversion. Cytosine 148-156 serpin family C member 1 Homo sapiens 187-193 8495867-6 1993 The development of ATIII-reactive capillaries was associated with a survival advantage, and such reactivity seemed to be promoted by heparin. Heparin 133-140 serpin family C member 1 Homo sapiens 19-24 8490170-2 1993 However, in the present study, we present evidence that factor VIIa bound to tissue factor, unlike free factor VIIa, is readily inactivated by AT III in the presence of heparin. Heparin 169-176 serpin family C member 1 Homo sapiens 143-149 8490170-4 1993 AT III/heparin was also shown to inhibit the catalytic activity towards factor X of factor VIIa/tissue factor complexes formed on monolayers of an ovarian carcinoma cell line (OC-2008) that constitutively expresses surface membrane tissue factor. Heparin 7-14 serpin family C member 1 Homo sapiens 0-6 8518817-0 1993 Trinucleotide repeat polymorphism in the human antithrombin III (AT3) gene. trinucleotide 0-13 serpin family C member 1 Homo sapiens 47-63 8518817-0 1993 Trinucleotide repeat polymorphism in the human antithrombin III (AT3) gene. trinucleotide 0-13 serpin family C member 1 Homo sapiens 65-68 8515556-3 1993 Although antithrombin-III activity was not measured in this case, the heparin resistance might have been caused by the decrease in the activity of antithrombin-III which might have resulted from the preoperative malnutrition, infection of urinary tract and/or institution of intraaortic balloon pumping (IABP). Heparin 70-77 serpin family C member 1 Homo sapiens 147-163 8473344-4 1993 In fact, point mutation of the P1" site from Ser (present in AT-III) to Ile (present in prothrombin) is sufficient to dissociate heparin-dependent thrombin and Factor Xa inhibitory activities. Serine 45-48 serpin family C member 1 Homo sapiens 61-67 8473344-4 1993 In fact, point mutation of the P1" site from Ser (present in AT-III) to Ile (present in prothrombin) is sufficient to dissociate heparin-dependent thrombin and Factor Xa inhibitory activities. Isoleucine 72-75 serpin family C member 1 Homo sapiens 61-67 8463348-9 1993 Albumin, IgG, and antithrombin III were mainly present in the cuprophane eluates. cuprammonium cellulose 62-72 serpin family C member 1 Homo sapiens 18-34 8388351-8 1993 The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin. Heparin 145-152 serpin family C member 1 Homo sapiens 100-116 8388351-8 1993 The chondroitin sulfate moiety of thrombomodulin also can affect the rate of thrombin inhibition by antithrombin III, possibly by competing with heparin for the heparin binding site on thrombin. Heparin 161-168 serpin family C member 1 Homo sapiens 100-116 8388354-7 1993 In whole plasma in the absence of platelet release, antithrombin III was the most abundant protein bound to therapeutic doses of unfractionated heparin, and histidine-rich glycoprotein its only effective competitor, while both histidine-rich glycoprotein and vitronectin were potentially important modulators of LMW heparin activity. Heparin 144-151 serpin family C member 1 Homo sapiens 52-68 8384381-0 1993 Comparative inhibition of extrinsic and intrinsic thrombin generation by standard heparin, a low molecular weight heparin and the synthetic ATIII-binding pentasaccharide. pentasaccharide 154-169 serpin family C member 1 Homo sapiens 140-145 8429040-3 1993 Thrombin is inhibited by the serpins antithrombin III and heparin cofactor II in a reaction that is dramatically accelerated by glycosaminoglycans. Glycosaminoglycans 128-146 serpin family C member 1 Homo sapiens 37-53 8429040-6 1993 The second order rate constant (k2) for inhibition by antithrombin III without heparin was 3.7 x 10(5) M-1 min-1 for wild-type thrombin; rates for the mutant thrombins varied less than 2-fold. Heparin 79-86 serpin family C member 1 Homo sapiens 54-70 8429040-7 1993 For inhibition by antithrombin III with heparin, the rate constant was 4.5 x 10(8) M-1 min-1 for wild-type thrombin with no significant differences between any of the recombinant thrombins. Heparin 40-47 serpin family C member 1 Homo sapiens 18-34 8429008-1 1993 Heparin cofactor II and antithrombin are plasma serine proteinase inhibitors whose ability to inhibit alpha-thrombin is accelerated by glycosaminoglycans. Glycosaminoglycans 135-153 serpin family C member 1 Homo sapiens 24-36 8429008-8 1993 A three-dimensional molecular model of the Quick II active site compared to alpha-thrombin suggested that the heparin cofactor II Leu-Ser-reactive site sequence (P1-P1") is a compatible "pseudosubstrate" in contrast to the Arg-Ser sequence found in antithrombin. Leucine 130-133 serpin family C member 1 Homo sapiens 249-261 8470059-5 1993 Small amounts of heparin were consistently detected in AT-III concentrates and post-infusion plasma samples. Heparin 17-24 serpin family C member 1 Homo sapiens 55-61 8470059-6 1993 The short-lived quenching of thrombin generation after AT-III concentrate could be partially explained by the infusion of heparin, rather than by supranormal AT-III levels. Heparin 122-129 serpin family C member 1 Homo sapiens 55-61 8384381-1 1993 The inhibiting effect of standard heparin, CY216 and the ATIII-binding synthetic pentasaccharide on extrinsic and intrinsic thrombin generation were quantified by evaluating the decrease of the total amount of active thrombin appearing in plasma after triggering coagulation. pentasaccharide 81-96 serpin family C member 1 Homo sapiens 57-62 8154338-6 1993 Impairment by fibrin of thrombin inhibition by antithrombin III may account in part for the inability of unfractionated heparin to prevent post-operative deep vein thrombosis in up to 20% of patients who undergo major elective orthopaedic surgery, and may also explain the need for oral anticoagulants after unfractionated and low molecular weight heparins are used to initiate the treatment of established deep vein thrombi. Heparin 348-356 serpin family C member 1 Homo sapiens 47-63 8456425-0 1993 The effect of antithrombin III-independent thrombin inhibitors and heparin on fibrin accretion onto fibrin-coated polyethylene. Polyethylene 114-126 serpin family C member 1 Homo sapiens 14-30 8456425-8 1993 These studies show that the antithrombin III-independent inhibitors, r-hirudin and PPACK, are more effective inhibitors of fibrin accretion onto fibrin-coated polyethylene than heparin or Hirulog-1. fibrin-coated polyethylene 145-171 serpin family C member 1 Homo sapiens 28-44 8419351-4 1993 Our data show that the activity of recombinant human factor VIIa is inhibited by antithrombin III in the presence of heparin at a rate of 1.7 x 10(2) M-1 s-1. Heparin 117-124 serpin family C member 1 Homo sapiens 81-97 8419351-6 1993 A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 133-155 serpin family C member 1 Homo sapiens 44-69 8419351-6 1993 A 1:1 stoichiometric complex between factor VIIa and antithrombin III, with an apparent molecular weight of 110,000, was detected by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. polyacrylamide 156-170 serpin family C member 1 Homo sapiens 44-69 8291376-3 1993 After discovery of acquired antithrombin III deficiency superimposed on the protein S deficiency, he was given antithrombin III concentrates with the intravenous heparin. Heparin 162-169 serpin family C member 1 Homo sapiens 28-44 7678252-3 1993 Incorporation of radiolabeled ATIII was detected using polyacrylamide gel electrophoresis (PAGE) and autoradiography. polyacrylamide 55-69 serpin family C member 1 Homo sapiens 30-35 8421307-1 1993 Human antithrombin III has been crystallized from 18 to 21% (w/v) polyethylene glycol 4000 at pH 7.15. Polyethylene Glycols 66-85 serpin family C member 1 Homo sapiens 6-22 8465268-11 1993 On the other hand, antithrombin III makes little use of the recognition exosite; instead, its interactions are tightened with the help of heparin, which binds to a second basic site (the heparin binding site). Heparin 138-145 serpin family C member 1 Homo sapiens 19-35 8412815-0 1993 Kinetic characterization of heparin-catalyzed and uncatalyzed inhibition of blood coagulation proteinases by antithrombin. Heparin 28-35 serpin family C member 1 Homo sapiens 109-121 8362268-4 1993 In the AT III supplemented systems, heparin was able to inhibit strongly both Factor Xa and thrombin, while pentasaccharide could only inhibit Factor Xa. Heparin 36-43 serpin family C member 1 Homo sapiens 7-13 8121125-7 1993 A decrease in antithrombin III observed in heparin group (from 115 +/- 3.2% to 98 +/- 3.4%, p < 0.001) reflected specific action of the drug. Heparin 43-50 serpin family C member 1 Homo sapiens 14-30 8362268-9 1993 These studies suggest that specific synthetic analogues of heparin such as the pentasaccharide and lactobionic acid can be used to study the relative contributions of AT III and HC II in the control of protease activation during thrombogenesis. Heparin 59-66 serpin family C member 1 Homo sapiens 167-173 8362268-9 1993 These studies suggest that specific synthetic analogues of heparin such as the pentasaccharide and lactobionic acid can be used to study the relative contributions of AT III and HC II in the control of protease activation during thrombogenesis. pentasaccharide 79-94 serpin family C member 1 Homo sapiens 167-173 8362268-9 1993 These studies suggest that specific synthetic analogues of heparin such as the pentasaccharide and lactobionic acid can be used to study the relative contributions of AT III and HC II in the control of protease activation during thrombogenesis. lactobionic acid 99-115 serpin family C member 1 Homo sapiens 167-173 8465268-11 1993 On the other hand, antithrombin III makes little use of the recognition exosite; instead, its interactions are tightened with the help of heparin, which binds to a second basic site (the heparin binding site). Heparin 187-194 serpin family C member 1 Homo sapiens 19-35 1448834-7 1992 CONCLUSIONS: We conclude that abnormal antithrombin III with defective heparin binding, even though heterozygous, may cause ischemic stroke in young adults. Heparin 71-78 serpin family C member 1 Homo sapiens 39-55 1469094-2 1992 In all seven families, variant antithrombins with heparin-binding abnormalities were detected by crossed immunoelectrophoresis, and in six of the kindreds there was a reduced antigen concentration of plasma antithrombin. Heparin 50-57 serpin family C member 1 Homo sapiens 31-43 1469094-5 1992 In contrast, s1C is spatially distant to the positively charged surface which forms the heparin binding site of antithrombin; altered heparin binding properties of s1C variants may therefore reflect conformational linkage between the reactive site and heparin binding regions of the molecule. Heparin 88-95 serpin family C member 1 Homo sapiens 112-124 1469094-5 1992 In contrast, s1C is spatially distant to the positively charged surface which forms the heparin binding site of antithrombin; altered heparin binding properties of s1C variants may therefore reflect conformational linkage between the reactive site and heparin binding regions of the molecule. Heparin 134-141 serpin family C member 1 Homo sapiens 112-124 1469094-5 1992 In contrast, s1C is spatially distant to the positively charged surface which forms the heparin binding site of antithrombin; altered heparin binding properties of s1C variants may therefore reflect conformational linkage between the reactive site and heparin binding regions of the molecule. Heparin 134-141 serpin family C member 1 Homo sapiens 112-124 1366018-2 1992 Studies of the complexing of antithrombin and its variants with heparin fractions and with reactive center loop peptides including intermolecular loop-sheet polymers all support a 3-fold mechanism for the heparin activation of antithrombin. Polymers 157-165 serpin family C member 1 Homo sapiens 29-41 1366018-2 1992 Studies of the complexing of antithrombin and its variants with heparin fractions and with reactive center loop peptides including intermolecular loop-sheet polymers all support a 3-fold mechanism for the heparin activation of antithrombin. Polymers 157-165 serpin family C member 1 Homo sapiens 227-239 1366018-6 1992 Full activation requires longer heparin chains in order to stabilize the ternary complex between antithrombin and thrombin. Heparin 32-39 serpin family C member 1 Homo sapiens 97-109 1390700-6 1992 An analog with an 18-membered lactam ring showed higher antithrombin activity (IC50 = 0.57 microM) than the corresponding analogs with 17- or 16-membered rings and was 2-fold more potent than its linear counterpart. Lactams 30-36 serpin family C member 1 Homo sapiens 56-68 1442974-8 1992 There was a significant increase in antithrombin III activity with norethindrone plus ethinyl estradiol at 12 months. Norethindrone 67-80 serpin family C member 1 Homo sapiens 36-52 1442974-8 1992 There was a significant increase in antithrombin III activity with norethindrone plus ethinyl estradiol at 12 months. Ethinyl Estradiol 86-103 serpin family C member 1 Homo sapiens 36-52 1333106-4 1992 High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS. Dermatan Sulfate 14-30 serpin family C member 1 Homo sapiens 50-62 1333106-4 1992 High affinity dermatan sulfate (DS) increased the antithrombin inhibition activity of HC II about 1000-fold in contrast to about 100-fold in the case of low affinity DS. Dermatan Sulfate 32-34 serpin family C member 1 Homo sapiens 50-62 1331047-6 1992 The two peptides, particularly IIFMGRVANP, directly enhanced the amidolytic activity of thrombin and Factor Xa on the synthetic substrate Boc-Ala-Gly-Arg-MCA (where Boc is t-butoxycarbonyl and MCA is 4-methylcoumarin), which corresponds to residues P3-P1 of the reactive site of antithrombin III, and also on other substrates due to increased Vmax. (S)-2-(2-((tert-Butoxycarbonyl)amino)propanamido)acetic acid 138-149 serpin family C member 1 Homo sapiens 279-295 1331047-6 1992 The two peptides, particularly IIFMGRVANP, directly enhanced the amidolytic activity of thrombin and Factor Xa on the synthetic substrate Boc-Ala-Gly-Arg-MCA (where Boc is t-butoxycarbonyl and MCA is 4-methylcoumarin), which corresponds to residues P3-P1 of the reactive site of antithrombin III, and also on other substrates due to increased Vmax. Arginine 150-153 serpin family C member 1 Homo sapiens 279-295 1428206-2 1992 Heparin-assisted dialysis resulted in a significant rise of VIII:C and AT III; with defibrotide, instead, there was evidence of thrombin activation (increased FPA and TAT). Heparin 0-7 serpin family C member 1 Homo sapiens 71-77 1326550-0 1992 Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. Structural link between the autolysis loop and the Tyr-Pro-Pro-Trp insertion of thrombin. des-etw 24-31 serpin family C member 1 Homo sapiens 37-53 1326550-3 1992 Whereas des-ETW resists antithrombin III inactivation with a rate constant (Kon) approximately 350-fold slower than for thrombin, des-ETW is remarkably sensitive to the Kunitz inhibitors, with inhibition constants (Ki) decreased from 2.6 microM to 34 nM for the soybean trypsin inhibitor and from 52 microM to 1.8 microM for the bovine pancreatic trypsin inhibitor. des-etw 8-15 serpin family C member 1 Homo sapiens 24-40 1390919-0 1992 Thermodynamic analysis of heparin binding to human antithrombin. Heparin 26-33 serpin family C member 1 Homo sapiens 51-63 1390919-1 1992 The binding of heparin to human antithrombin III (ATIII) was investigated by titration calorimetry (TC) and differential scanning calorimetry (DSC). Heparin 15-22 serpin family C member 1 Homo sapiens 32-48 1390919-1 1992 The binding of heparin to human antithrombin III (ATIII) was investigated by titration calorimetry (TC) and differential scanning calorimetry (DSC). Heparin 15-22 serpin family C member 1 Homo sapiens 50-55 1390919-5 1992 The 3-fold lower binding enthalpy in Tris can be attributed to the transfer of a proton from the buffer to the heparin-ATIII complex. Tromethamine 37-41 serpin family C member 1 Homo sapiens 119-124 1390919-8 1992 This supports a two domain model of ATIII folding in which the lower stability domain (329 K) binds and is stabilized by heparin. Heparin 121-128 serpin family C member 1 Homo sapiens 36-41 1492385-3 1992 The ester, similarly to heparin, inhibited blood coagulation mainly via accelerated thrombin inactivation by means of blood plasma antithrombin III. Esters 4-9 serpin family C member 1 Homo sapiens 131-147 1433937-1 1992 A pregnant woman with congenital antithrombin III (AT III) deficiency was given AT III concentrate and warfarin at the first and after 36th week of gestation periods and at the other gestation period, respectively. Warfarin 103-111 serpin family C member 1 Homo sapiens 33-49 1412223-4 1992 The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III. Heparin 62-69 serpin family C member 1 Homo sapiens 13-29 1433937-1 1992 A pregnant woman with congenital antithrombin III (AT III) deficiency was given AT III concentrate and warfarin at the first and after 36th week of gestation periods and at the other gestation period, respectively. Warfarin 103-111 serpin family C member 1 Homo sapiens 51-57 1412157-1 1992 The decay rate of thrombin in plasma is shown to be linearly proportional to the concentration of antithrombin III (AT III), not only in the absence but also in the presence of heparin. Heparin 177-184 serpin family C member 1 Homo sapiens 98-114 1412157-1 1992 The decay rate of thrombin in plasma is shown to be linearly proportional to the concentration of antithrombin III (AT III), not only in the absence but also in the presence of heparin. Heparin 177-184 serpin family C member 1 Homo sapiens 116-122 1412157-2 1992 This is a consequence of partitioning of heparin between AT III and other plasma proteins. Heparin 41-48 serpin family C member 1 Homo sapiens 57-63 1412157-7 1992 From the results presented it is evident that characteristic parameters of heparin action have to be normalised to the AT III concentration. Heparin 75-82 serpin family C member 1 Homo sapiens 119-125 1412157-8 1992 On this basis we define a Standard Independent Unit of the antithrombin activity of heparin. Heparin 84-91 serpin family C member 1 Homo sapiens 59-71 1440655-6 1992 In SDS-PAGE inactivation of human antithrombin III was correlated with the occurrence of two cleavage products. Sodium Dodecyl Sulfate 3-6 serpin family C member 1 Homo sapiens 34-50 1412223-4 1992 The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III. Sepharose 105-112 serpin family C member 1 Homo sapiens 13-29 1412223-4 1992 The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III. Sodium Chloride 87-91 serpin family C member 1 Homo sapiens 13-29 1418069-12 1992 Therefore, the anticoagulant activity of the synthesized laminarin sulfates is due to the interaction at an early stage of the coagulation cascade and neither to a direct inhibition of Factor Xa and IIa nor to an indirect effect mediated by antithrombin III. laminarin sulfate 57-75 serpin family C member 1 Homo sapiens 241-257 1412223-4 1992 The modified antithrombin III retained a reduced affinity for heparin (eluting at 0.3M NaCl from heparin Agarose) and was observed to be a competitive inhibitor of the heparin-dependent rate of inhibition of thrombin by native antithrombin III. Heparin 97-104 serpin family C member 1 Homo sapiens 13-29 1412223-7 1992 These findings, together with our previous report upon tryptophan modification of antithrombin III [1] suggest that the nature of the molecule is such that considerable care must be taken in interpretation of results when investigating the structure/function relationships of this protein by chemical modification. Tryptophan 55-65 serpin family C member 1 Homo sapiens 82-98 1418078-0 1992 Fibrinogen and antithrombin III blood levels fluctuations during isoniazid or isoniazid plus rifampicin administration. Isoniazid 65-74 serpin family C member 1 Homo sapiens 15-31 1418078-0 1992 Fibrinogen and antithrombin III blood levels fluctuations during isoniazid or isoniazid plus rifampicin administration. Isoniazid 78-87 serpin family C member 1 Homo sapiens 15-31 1418078-0 1992 Fibrinogen and antithrombin III blood levels fluctuations during isoniazid or isoniazid plus rifampicin administration. Rifampin 93-103 serpin family C member 1 Homo sapiens 15-31 1457941-0 1992 Binding kinetics of thrombin and antithrombin III with immobilized heparin using a spacer. Heparin 67-74 serpin family C member 1 Homo sapiens 33-49 1440521-1 1992 Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively. sodium carbonate 61-77 serpin family C member 1 Homo sapiens 116-132 1440521-1 1992 Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively. Sodium Chloride 95-99 serpin family C member 1 Homo sapiens 116-132 1440521-1 1992 Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively. Pyruvaldehyde 191-204 serpin family C member 1 Homo sapiens 116-132 1440521-1 1992 Under conditions closely approximating those in vivo (100 mM sodium carbonate pH 7.3 with 0.9% NaCl, 37 degrees C), antithrombin III (AT III) and the C1 inhibitor (C1-INH) are inactivated by methylglyoxal (MG) with pseudofirst-order kinetics and second-order rate constants of 25.2 and 7.8 M-1 min-1, respectively. Pyruvaldehyde 191-204 serpin family C member 1 Homo sapiens 134-140 1457941-2 1992 In this study, the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin were investigated. Heparin 51-58 serpin family C member 1 Homo sapiens 64-80 1457941-2 1992 In this study, the binding kinetics of immobilized heparin with antithrombin III (ATIII) and thrombin were investigated. Heparin 51-58 serpin family C member 1 Homo sapiens 82-87 1457941-3 1992 Low molecular weight heparin (molecular weight, 6,000 daltons) was fractionated on an ATIII affinity column, and it was immobilized onto a styrene/p-amino styrene random co-polymer surface via hydrophilic spacer groups. Heparin 21-28 serpin family C member 1 Homo sapiens 86-91 1457941-7 1992 The binding constants of immobilized heparin and ATIII, and immobilized heparin and thrombin, were 0.958 x 10(7) M-1 and 1.76 x 10(8) M-1, respectively. Heparin 37-44 serpin family C member 1 Homo sapiens 49-54 1457941-8 1992 The immobilized heparin bound with both ATIII and thrombin, and the binding mechanism was similar to that of free heparin. Heparin 16-23 serpin family C member 1 Homo sapiens 40-45 1377216-5 1992 We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP. Heparin 162-169 serpin family C member 1 Homo sapiens 142-158 1377216-3 1992 SAP neutralized the catalytic effect of heparin on the thrombin-antithrombin III reaction more effectively than vitronectin, histidine-rich glycoprotein, fibronectin, and high-molecular-weight kininogen and almost as effectively as platelet factor 4. Heparin 40-47 serpin family C member 1 Homo sapiens 64-80 1447499-5 1992 If AT-III levels were above 0.30 U/ml, SF levels remained low, whereas SF levels were increased in patients with AT-III levels below 0.30 U/ml. sf 39-41 serpin family C member 1 Homo sapiens 3-9 1377216-5 1992 We found evidence for the formation of a high-affinity 1:1 complex between SAP and heparin and for inhibition of binding of both thrombin and antithrombin III to heparin-Sepharose by SAP. Sepharose 170-179 serpin family C member 1 Homo sapiens 142-158 1643210-9 1992 Mutations causing amino acid substitutions solely affecting the heparin binding site have thus far been located primarily at the N-terminal region of the molecule, residues 7-129; this region has been postulated to align as a positive groove in the molecule that forms the primary contact region for the essential antithrombin binding pentasaccharide of heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 314-326 1447499-5 1992 If AT-III levels were above 0.30 U/ml, SF levels remained low, whereas SF levels were increased in patients with AT-III levels below 0.30 U/ml. sf 71-73 serpin family C member 1 Homo sapiens 113-119 1618758-0 1992 Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. pentasaccharide 33-48 serpin family C member 1 Homo sapiens 12-24 1618758-0 1992 Role of the antithrombin-binding pentasaccharide in heparin acceleration of antithrombin-proteinase reactions. pentasaccharide 33-48 serpin family C member 1 Homo sapiens 76-88 1618758-1 1992 Resolution of the antithrombin conformational change contribution to heparin rate enhancement. Heparin 69-76 serpin family C member 1 Homo sapiens 18-30 1425930-6 1992 This inhibitory effect was not related to the anticoagulant property of the compounds, since a heparin preparation with an inactivated active for antithrombin III was also effective. Heparin 95-102 serpin family C member 1 Homo sapiens 146-162 1618758-2 1992 The synthetic antithrombin-binding heparin pentasaccharide and a full-length heparin of approximately 26 saccharides containing this specific sequence have been compared with respect to their interactions with antithrombin and their ability to promote inhibition and substrate reactions of antithrombin with thrombin and factor Xa. IC 831423 35-58 serpin family C member 1 Homo sapiens 14-26 1618758-2 1992 The synthetic antithrombin-binding heparin pentasaccharide and a full-length heparin of approximately 26 saccharides containing this specific sequence have been compared with respect to their interactions with antithrombin and their ability to promote inhibition and substrate reactions of antithrombin with thrombin and factor Xa. Heparin 35-42 serpin family C member 1 Homo sapiens 14-26 1618758-3 1992 The aim of these studies was to elucidate the pentasaccharide contribution to heparin"s accelerating effect on antithrombin-proteinase reactions. pentasaccharide 46-61 serpin family C member 1 Homo sapiens 111-123 1618758-4 1992 Pentasaccharide and full-length heparins bound antithrombin with comparable high affinities (KD values of 36 +/- 11 and 10 +/- 3 nM, respectively, at I 0.15) and induced highly similar protein fluorescence, ultraviolet and circular dichroism changes in the inhibitor. pentasaccharide 0-15 serpin family C member 1 Homo sapiens 47-59 1618758-6 1992 Second order rate constants for antithrombin reactions with thrombin and factor Xa were maximally enhanced by the pentasaccharide only 1.7-fold for thrombin, but a substantial 270-fold for factor Xa, in an ionic strength-independent manner at saturating oligosaccharide. pentasaccharide 114-129 serpin family C member 1 Homo sapiens 32-44 1618758-6 1992 Second order rate constants for antithrombin reactions with thrombin and factor Xa were maximally enhanced by the pentasaccharide only 1.7-fold for thrombin, but a substantial 270-fold for factor Xa, in an ionic strength-independent manner at saturating oligosaccharide. Oligosaccharides 254-269 serpin family C member 1 Homo sapiens 32-44 1618758-7 1992 In contrast, the full-length heparin produced large ionic strength-dependent enhancements in second order rate constants for both antithrombin reactions of 4,300-fold for thrombin and 580-fold for factor Xa at I 0.15. Heparin 29-36 serpin family C member 1 Homo sapiens 130-142 1322691-0 1992 Ratios of anti-factor Xa to antithrombin activities of heparins as determined in recalcified human plasma. Heparin 55-63 serpin family C member 1 Homo sapiens 28-40 1322691-8 1992 Calcium reduced the anti-thrombin activities of all the heparin preparations studied about 1.5 times when purified ATIII was used, although in plasma this effect was less clear. Calcium 0-7 serpin family C member 1 Homo sapiens 115-120 1322691-8 1992 Calcium reduced the anti-thrombin activities of all the heparin preparations studied about 1.5 times when purified ATIII was used, although in plasma this effect was less clear. Heparin 56-63 serpin family C member 1 Homo sapiens 115-120 1315738-4 1992 This differs from the putative heparin-binding site in the related proteins antithrombin and heparin cofactor. Heparin 31-38 serpin family C member 1 Homo sapiens 76-88 1394292-5 1992 The heparin cofactor II-mediated antithrombin activity of the oversulfated fucans also increased significantly with increase in sulfate content. Sulfates 66-73 serpin family C member 1 Homo sapiens 33-45 1394292-7 1992 However, the increment of the anticoagulant and the antithrombin effects gradually decreased with increase in the sulfate content of the fucans. Sulfates 114-121 serpin family C member 1 Homo sapiens 52-64 1394292-7 1992 However, the increment of the anticoagulant and the antithrombin effects gradually decreased with increase in the sulfate content of the fucans. fucans 137-143 serpin family C member 1 Homo sapiens 52-64 1329257-0 1992 Study of low molecular weight heparin effect on the relation between anticoagulant activity and antithrombin III affinity. Heparin 30-37 serpin family C member 1 Homo sapiens 96-112 1315739-3 1992 Synthetic peptides corresponding to the putative heparin binding regions of antithrombin, heparin cofactor, and protein C inhibitor bound to heparin directly and interfered in heparin-enhanced proteinase inhibition assays. Heparin 49-56 serpin family C member 1 Homo sapiens 76-88 1315739-6 1992 In assays with heparin oligosaccharides of known size, only the antithrombin-thrombin reaction exhibited a sharp threshold for rate enhancement at 14-16 saccharide units. heparin oligosaccharides 15-39 serpin family C member 1 Homo sapiens 64-76 1519214-6 1992 These findings suggest that untreated antithrombin III deficient subjects generate more thrombin than their non-deficient family members and that warfarin inhibits this thrombin formation. Warfarin 146-154 serpin family C member 1 Homo sapiens 38-54 1505142-5 1992 Heparin produces its antithrombotic effect by binding to antithrombin III and this complex then binds to thrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 57-73 1519763-0 1992 Enzyme-linked immunosorbent assay for proteolytically inactivated antithrombin-III: use of sodium dodecyl sulfate to eliminate signal due to intact antithrombin-III. Sodium Dodecyl Sulfate 91-113 serpin family C member 1 Homo sapiens 66-82 1519763-4 1992 Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III. Sodium Dodecyl Sulfate 6-28 serpin family C member 1 Homo sapiens 133-139 1519763-4 1992 Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III. Sodium Dodecyl Sulfate 30-33 serpin family C member 1 Homo sapiens 133-139 1519763-4 1992 Using sodium dodecyl sulfate (SDS), we were able to devise an enzyme-linked immunosorbent assay (ELISA) capable of detecting cleaved AT-III in the presence of intact AT-III. Sodium Dodecyl Sulfate 30-33 serpin family C member 1 Homo sapiens 166-172 1519763-5 1992 It seems likely that the SDS alters the intact AT-III so that it is not detected in the ELISA. Sodium Dodecyl Sulfate 25-28 serpin family C member 1 Homo sapiens 47-53 1519763-8 1992 The generation of cleaved AT-III in human plasma by HNE in the presence of heparin could be monitored as well. Heparin 75-82 serpin family C member 1 Homo sapiens 26-32 1505142-6 1992 In order to accomplish this a total of 18 to 22 monosaccharide units is necessary including a specific pentasaccharide binding site for antithrombin III. Monosaccharides 48-62 serpin family C member 1 Homo sapiens 136-152 1505142-6 1992 In order to accomplish this a total of 18 to 22 monosaccharide units is necessary including a specific pentasaccharide binding site for antithrombin III. pentasaccharide 103-118 serpin family C member 1 Homo sapiens 136-152 1311598-0 1992 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments. Hydrogen 0-2 serpin family C member 1 Homo sapiens 70-86 1569192-4 1992 A G to T transition at nucleotide 10038 results in the substitution of Met to an Arg, converting alpha 1-AT into an Arg-Ser protease inhibitor (serpin) that inhibited thrombin and Factor Xa more effectively than antithrombin III. Arginine 81-84 serpin family C member 1 Homo sapiens 212-228 1566349-1 1992 This is the first study of the antithrombin III-heparan sulfate natural anticoagulant pathway in human kidneys. Heparitin Sulfate 48-63 serpin family C member 1 Homo sapiens 31-47 1566349-3 1992 Enzymatic studies were done to show that the antithrombin III was anchored to endothelium by molecules of heparan sulfate. Heparitin Sulfate 106-121 serpin family C member 1 Homo sapiens 45-61 1566349-4 1992 Displacement studies were done with glycosaminoglycans to show that the antithrombin III was bound to its glycosaminoglycan anchor via a heparinlike binding site, and replacement studies showed that antithrombin III could be returned to the same endothelial cells from which it was displaced. Glycosaminoglycans 36-54 serpin family C member 1 Homo sapiens 72-88 1566349-4 1992 Displacement studies were done with glycosaminoglycans to show that the antithrombin III was bound to its glycosaminoglycan anchor via a heparinlike binding site, and replacement studies showed that antithrombin III could be returned to the same endothelial cells from which it was displaced. Glycosaminoglycans 36-53 serpin family C member 1 Homo sapiens 72-88 1566349-5 1992 Immunocytochemical studies of biopsies showed that normally functioning renal allografts manifested the endothelial antithrombin III-heparan sulfate anticoagulant pathway. Heparitin Sulfate 133-148 serpin family C member 1 Homo sapiens 116-132 1566349-7 1992 It is concluded that compromise of the antithrombin III-heparan sulfate natural anticoagulant pathway results in compromised renal function in transplanted kidneys. Heparitin Sulfate 56-71 serpin family C member 1 Homo sapiens 39-55 1554734-4 1992 Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII. Heparin 109-116 serpin family C member 1 Homo sapiens 93-98 1554734-4 1992 Slightly greater differences were observed for the effect of these fractions on the thrombin-ATIII reaction; heparin that did not bind to the GDN affinity column was about 60% more effective than heparin with a high affinity for GDN in accelerating the inhibition of thrombin by ATIII. Heparin 196-203 serpin family C member 1 Homo sapiens 93-98 1554734-7 1992 Fragment 63-144 was less effective in decreasing the heparin-accelerated rate of inhibition of thrombin by ATIII. Heparin 53-60 serpin family C member 1 Homo sapiens 107-112 1554734-8 1992 The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII. Heparin 42-49 serpin family C member 1 Homo sapiens 116-121 1554734-8 1992 The results are discussed in terms of the heparin species that are responsible for the acceleration of the GDN- and ATIII-thrombin reactions and the heparin-binding sites of GDN and ATIII. Heparin 149-156 serpin family C member 1 Homo sapiens 182-187 1555650-1 1992 An antithrombin variant with reduced heparin affinity resulting from the substitution L99F. Heparin 37-44 serpin family C member 1 Homo sapiens 3-15 1547341-0 1992 Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity. Glycine 41-44 serpin family C member 1 Homo sapiens 0-16 1547341-0 1992 Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity. Aspartic Acid 48-51 serpin family C member 1 Homo sapiens 0-16 1547341-0 1992 Antithrombin-III-Stockholm: a codon 392 (Gly----Asp) mutation with normal heparin binding and impaired serine protease reactivity. Heparin 74-81 serpin family C member 1 Homo sapiens 0-16 1547341-1 1992 Antithrombin-III-Stockholm is a new structural variant of antithrombin-III (AT-III) with normal heparin affinity but defective serine protease inhibitory activity. Heparin 96-103 serpin family C member 1 Homo sapiens 0-16 1547341-1 1992 Antithrombin-III-Stockholm is a new structural variant of antithrombin-III (AT-III) with normal heparin affinity but defective serine protease inhibitory activity. Heparin 96-103 serpin family C member 1 Homo sapiens 58-74 1547341-1 1992 Antithrombin-III-Stockholm is a new structural variant of antithrombin-III (AT-III) with normal heparin affinity but defective serine protease inhibitory activity. Heparin 96-103 serpin family C member 1 Homo sapiens 76-82 1547341-11 1992 The minimal thrombin-complexing ability of the mutant AT-III protein that was observed was accelerated by heparin, but to subnormal levels. Heparin 106-113 serpin family C member 1 Homo sapiens 54-60 1321995-1 1992 The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses. Heparin 44-51 serpin family C member 1 Homo sapiens 149-155 1321995-1 1992 The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses. Heparin 94-101 serpin family C member 1 Homo sapiens 149-155 1321995-1 1992 The binding ability of low molecular weight heparin (FR-860), and conventional unfractionated heparin (UF-heparin) to factor Xa (F.Xa), thrombin and AT III was investigated using FR-860- and UF-heparin-Sepharoses. Heparin 94-101 serpin family C member 1 Homo sapiens 149-155 1321995-4 1992 On the other hand, UF-heparin bound to F.Xa, thrombin and AT III with the strongest affinity to AT III followed by thrombin and F.Xa. Heparin 22-29 serpin family C member 1 Homo sapiens 58-64 1321995-4 1992 On the other hand, UF-heparin bound to F.Xa, thrombin and AT III with the strongest affinity to AT III followed by thrombin and F.Xa. Heparin 22-29 serpin family C member 1 Homo sapiens 96-102 1321995-5 1992 AT III mediated the binding between F.Xa and FR-860 and accelerated the reaction between F.Xa and UF-heparin. Heparin 101-108 serpin family C member 1 Homo sapiens 0-6 1321995-7 1992 Diisopropyl fluorophosphate-treated thrombin inhibited the binding between AT III and FR-860, but not that between AT III and UF-heparin. Isoflurophate 0-27 serpin family C member 1 Homo sapiens 75-81 1311598-0 1992 1H NMR spectroscopic studies on the interactions between human plasma antithrombin III and defined low molecular weight heparin fragments. Heparin 120-127 serpin family C member 1 Homo sapiens 70-86 1311598-4 1992 Perturbations to the 1H resonances in the NMR spectrum of antithrombin upon binding of the two series of heparin fragments are compared to those generated by intact heparin binding, as well as to the effects of binding of a synthetic high-affinity pentasaccharide. Hydrogen 21-23 serpin family C member 1 Homo sapiens 58-70 1311598-4 1992 Perturbations to the 1H resonances in the NMR spectrum of antithrombin upon binding of the two series of heparin fragments are compared to those generated by intact heparin binding, as well as to the effects of binding of a synthetic high-affinity pentasaccharide. Heparin 105-112 serpin family C member 1 Homo sapiens 58-70 1540583-0 1992 A peptide model for the heparin binding site of antithrombin III. Heparin 24-31 serpin family C member 1 Homo sapiens 48-64 1540583-1 1992 A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding. Heparin 24-31 serpin family C member 1 Homo sapiens 48-64 1540583-1 1992 A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding. Heparin 24-31 serpin family C member 1 Homo sapiens 66-71 1540583-1 1992 A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding. Heparin 133-140 serpin family C member 1 Homo sapiens 48-64 1311598-4 1992 Perturbations to the 1H resonances in the NMR spectrum of antithrombin upon binding of the two series of heparin fragments are compared to those generated by intact heparin binding, as well as to the effects of binding of a synthetic high-affinity pentasaccharide. pentasaccharide 248-263 serpin family C member 1 Homo sapiens 58-70 1311598-5 1992 All of the heparin fragments examined appear to bind to antithrombin at the same site. Heparin 11-18 serpin family C member 1 Homo sapiens 56-68 1311598-6 1992 Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49. Heparin 13-20 serpin family C member 1 Homo sapiens 136-148 1311598-6 1992 Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49. hexasaccharide-2 32-48 serpin family C member 1 Homo sapiens 136-148 1540583-1 1992 A peptide model for the heparin binding site of antithrombin III (ATIII) was synthesized to elucidate the structural consequences of heparin binding. Heparin 133-140 serpin family C member 1 Homo sapiens 66-71 1540583-3 1992 In the presence of heparin, however, the peptide ATIII(123-139) assumed a stable conformation, whereas peptide ATIII random did not. Heparin 19-26 serpin family C member 1 Homo sapiens 49-54 1540583-5 1992 The ATIII(123-139)-heparin complex contained beta-structure, rather than helical structure. Heparin 19-26 serpin family C member 1 Homo sapiens 4-9 1540583-6 1992 This finding is incompatible with current models of heparin binding and suggests that heparin binding may induce nonnative structures at the binding site which could, in turn, lead to activation of ATIII. Heparin 52-59 serpin family C member 1 Homo sapiens 198-203 1311598-6 1992 Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49. octasaccharide-2 50-66 serpin family C member 1 Homo sapiens 136-148 1540583-6 1992 This finding is incompatible with current models of heparin binding and suggests that heparin binding may induce nonnative structures at the binding site which could, in turn, lead to activation of ATIII. Heparin 86-93 serpin family C member 1 Homo sapiens 198-203 1311598-6 1992 Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49. octasaccharide-1 72-88 serpin family C member 1 Homo sapiens 136-148 1540583-7 1992 The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site. Heparin 71-78 serpin family C member 1 Homo sapiens 12-17 1540583-7 1992 The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site. Heparin 71-78 serpin family C member 1 Homo sapiens 62-67 1311598-6 1992 Three of the heparin fragments (hexasaccharide-2, octasaccharide-2, and octasaccharide-1) produce almost identical perturbations in the antithrombin 1H NMR spectrum compared to binding of intact heparin, including perturbations of resonances from tryptophan 49. Hydrogen 149-151 serpin family C member 1 Homo sapiens 136-148 1540583-7 1992 The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site. Heparin 148-155 serpin family C member 1 Homo sapiens 12-17 1546950-0 1992 The N-terminal domain of antithrombin-III is essential for heparin binding and complex-formation with, but not cleavage by, alpha-thrombin. Heparin 59-66 serpin family C member 1 Homo sapiens 25-41 1540583-7 1992 The peptide ATIII(123-139) was able to inhibit the binding of ATIII by heparin, consistent with the notion that this peptide may be a model for the heparin binding site. Heparin 148-155 serpin family C member 1 Homo sapiens 62-67 1546950-3 1992 70% of cell-free-derived normal AT-III-(1-432)-polypeptide as a peak between 0.2 M- and 0.7 M-NaCl. Sodium Chloride 94-98 serpin family C member 1 Homo sapiens 32-38 1546950-11 1992 The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained. disulphide 21-31 serpin family C member 1 Homo sapiens 68-74 1546950-11 1992 The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained. Cysteine 45-48 serpin family C member 1 Homo sapiens 68-74 1546950-11 1992 The formation of the disulphide bond between Cys-247 and Cys-430 in AT-III-(219-432)-polypeptide had no effect on the results obtained. Cysteine 57-60 serpin family C member 1 Homo sapiens 68-74 1546950-12 1992 Mutations in full-length AT-III at Cys-430 had no effect on the ability of AT-III to bind heparin. Cysteine 35-38 serpin family C member 1 Homo sapiens 25-31 1546950-14 1992 A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide. Heparin 87-94 serpin family C member 1 Homo sapiens 20-26 1546950-14 1992 A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide. Heparin 87-94 serpin family C member 1 Homo sapiens 115-121 1546950-14 1992 A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide. Heparin 87-94 serpin family C member 1 Homo sapiens 115-121 1546950-14 1992 A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide. Heparin 146-153 serpin family C member 1 Homo sapiens 20-26 1546950-14 1992 A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide. Heparin 146-153 serpin family C member 1 Homo sapiens 115-121 1546950-14 1992 A cell-free-derived AT-III mutant, devoid of amino acid residues 41-49, which comprise heparin-binding region 1 of AT-III, had slightly decreased heparin binding compared with cell-free-derived normal AT-III-(1-432)-polypeptide. Heparin 146-153 serpin family C member 1 Homo sapiens 115-121 1546950-16 1992 We conclude therefore that the N-terminal domain of AT-III is essential for both heparin binding and complex-formation with alpha-thrombin, but not for the cleavage of AT-III at its reactive centre by alpha-thrombin. Heparin 81-88 serpin family C member 1 Homo sapiens 52-58 1542853-7 1992 Fibrinogen concentration and antithrombin-III level were lowest in the CS group but were not decreased critically during the entire investigation period. Cesium 71-73 serpin family C member 1 Homo sapiens 29-45 1315572-13 1992 It is possible that heparin could interact with endothelium and bind ATIII to maintain a state of thromboresistance. Heparin 20-27 serpin family C member 1 Homo sapiens 69-74 1346414-2 1992 While heparin functions as an anticoagulant primarily by its ability to accelerate the action of the plasma protein inhibitor antithrombin III, dermatan sulphate acts selectively through a structurally related inhibitor, heparin co-factor II, to inhibit thrombin. Heparin 6-13 serpin family C member 1 Homo sapiens 126-142 1739360-0 1992 Antithrombin III level, fibrinogen level, and platelet count changes with adjuvant tamoxifen therapy. Tamoxifen 83-92 serpin family C member 1 Homo sapiens 0-16 1731639-6 1992 Depolymerization products with 20 or more sugar units retain significant anticoagulant potencies as measured by their effect in accelerating the neutralization of factor Xa by antithrombin. Sugars 42-47 serpin family C member 1 Homo sapiens 176-188 1733939-1 1992 The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity. Heparin 17-24 serpin family C member 1 Homo sapiens 128-144 1733939-1 1992 The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity. Heparin 17-24 serpin family C member 1 Homo sapiens 146-151 1733939-1 1992 The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity. Heparin 179-186 serpin family C member 1 Homo sapiens 128-144 1733939-1 1992 The last step of heparin biosynthesis is thought to involve the action of 3-O-sulfotransferase resulting in the formation of an antithrombin III (ATIII) binding site required for heparin"s anticoagulant activity. Heparin 179-186 serpin family C member 1 Homo sapiens 146-151 1733939-2 1992 The isolation of a significant fraction of heparin chains without antithrombin III-binding sites and having low affinity for ATIII suggests the presence of a precursor site, lacking the 3-O-sulfate group. Heparin 43-50 serpin family C member 1 Homo sapiens 125-130 1733939-4 1992 One of these oligosaccharides was derived from heparin"s ATIII-binding site. Oligosaccharides 13-29 serpin family C member 1 Homo sapiens 57-62 1733939-5 1992 In an effort to find the ATIII-binding site precursor, the structures of several minor oligosaccharides were determined. Oligosaccharides 87-103 serpin family C member 1 Homo sapiens 25-30 1733939-7 1992 An oligosaccharide arising from the ATIII-binding site precursor was found that comprised only 0.8 mol % of the oligosaccharide product mixture. Oligosaccharides 3-18 serpin family C member 1 Homo sapiens 36-41 1733939-7 1992 An oligosaccharide arising from the ATIII-binding site precursor was found that comprised only 0.8 mol % of the oligosaccharide product mixture. Oligosaccharides 112-127 serpin family C member 1 Homo sapiens 36-41 1733939-8 1992 This oligosaccharide was only slightly enriched in heparin having a low affinity for ATIII and only slightly disenriched in high affinity heparin. Oligosaccharides 5-20 serpin family C member 1 Homo sapiens 85-90 1733939-8 1992 This oligosaccharide was only slightly enriched in heparin having a low affinity for ATIII and only slightly disenriched in high affinity heparin. Heparin 51-58 serpin family C member 1 Homo sapiens 85-90 1733939-9 1992 The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis. Heparin 98-106 serpin family C member 1 Homo sapiens 26-31 1733939-9 1992 The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis. Heparin 98-105 serpin family C member 1 Homo sapiens 26-31 1733939-9 1992 The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis. Heparin 155-162 serpin family C member 1 Homo sapiens 26-31 1733939-9 1992 The small number of these ATIII-binding site precursors, found in unfractionated and fractionated heparins, suggests the existence of a low ATIII affinity heparin may not simply be the result of the incomplete action of 3-O-sulfotransferase in the final step in heparin biosynthesis. Heparin 155-162 serpin family C member 1 Homo sapiens 140-145 1739360-4 1992 Antithrombin III levels, elevated at baseline evaluation, decreased in tamoxifen-treated subjects at 6 months, but no subject exhibited a drop to clinically significant levels. Tamoxifen 71-80 serpin family C member 1 Homo sapiens 0-16 1319616-2 1992 From CY222 (MMW 3,770) as well as from CY216 and its three fractions the material with high affinity to antithrombin III (AT III) was obtained by chromatography on immobilised AT III. Nadroparin 39-44 serpin family C member 1 Homo sapiens 104-120 1733939-10 1992 Rather these data suggest that some earlier step, involved in the formation of placement of these precursor sites, may be primarily responsible for high and low ATIII affinity heparins. Heparin 176-184 serpin family C member 1 Homo sapiens 161-166 1585693-2 1992 The activity of AT III is decreased in metabolic acidosis, hyperlipoproteinemias and by lipid peroxides. Lipid Peroxides 88-103 serpin family C member 1 Homo sapiens 16-22 1730729-0 1992 Conversion of antithrombin from an inhibitor of thrombin to a substrate with reduced heparin affinity and enhanced conformational stability by binding of a tetradecapeptide corresponding to the P1 to P14 region of the putative reactive bond loop of the inhibitor. Heparin 85-92 serpin family C member 1 Homo sapiens 14-26 1730729-6 1992 The antithrombin-peptide complex had a conformation similar to that of reactive bond-cleaved antithrombin and, like the cleaved inhibitor, also had a higher conformational stability and lower heparin affinity than intact antithrombin. Heparin 192-199 serpin family C member 1 Homo sapiens 4-16 1730729-8 1992 The extent of complex formation was reduced in the presence of heparin with high affinity for antithrombin, which is consistent with heparin binding and peptide incorporation being linked. Heparin 63-70 serpin family C member 1 Homo sapiens 94-106 1319616-2 1992 From CY222 (MMW 3,770) as well as from CY216 and its three fractions the material with high affinity to antithrombin III (AT III) was obtained by chromatography on immobilised AT III. Nadroparin 39-44 serpin family C member 1 Homo sapiens 122-128 1730729-8 1992 The extent of complex formation was reduced in the presence of heparin with high affinity for antithrombin, which is consistent with heparin binding and peptide incorporation being linked. Heparin 133-140 serpin family C member 1 Homo sapiens 94-106 1319616-7 1992 The specific antithrombin activity of all heparins, when expressed in terms of material with high affinity to antithrombin III (HAM) with a MW greater than 5,400 is 13.0 min-1/(microgram/ml) (range 10.5-15.9). Heparin 42-50 serpin family C member 1 Homo sapiens 110-126 1579895-8 1992 Based on the good results in these two patients, and a review of previously reported cases, we propose that heparin alone, in a dose to maintain the APTT in a therapeutic range, provides adequate prophylaxis and treatment for VTE during pregnancy and delivery in many AT III deficient subjects. Heparin 108-115 serpin family C member 1 Homo sapiens 268-274 1579900-5 1992 The absence of any interference due to AT III-heparin complexes was verified in a kinetic HC II assay of some human plasma pools. Heparin 46-53 serpin family C member 1 Homo sapiens 39-45 1579900-7 1992 Progressive increase of heparin concentration in the assay was effective only starting from 30 U/ml (the assay was carried out in the presence of polybrene to prevent any AT III activation). Heparin 24-31 serpin family C member 1 Homo sapiens 171-177 1730217-4 1992 The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III. Heparin 25-32 serpin family C member 1 Homo sapiens 73-89 1730217-4 1992 The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III. Heparin 25-32 serpin family C member 1 Homo sapiens 138-154 1730217-4 1992 The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III. octadecasaccharide 96-114 serpin family C member 1 Homo sapiens 73-89 1730217-4 1992 The smallest fragment of heparin able to catalyze thrombin inhibition by antithrombin III is an octadecasaccharide with high affinity for antithrombin III. octadecasaccharide 96-114 serpin family C member 1 Homo sapiens 138-154 1579900-2 1992 Nevertheless functional assays can be biased by the antithrombin III (AT III)-heparin complex activity; in fact trace amounts of heparin generally contaminate dermatan sulfate (DS) commercial preparations used as HC II reaction activators. Heparin 78-85 serpin family C member 1 Homo sapiens 52-68 1579900-2 1992 Nevertheless functional assays can be biased by the antithrombin III (AT III)-heparin complex activity; in fact trace amounts of heparin generally contaminate dermatan sulfate (DS) commercial preparations used as HC II reaction activators. Heparin 78-85 serpin family C member 1 Homo sapiens 70-76 1332442-10 1992 Further studies show that the GlcA residue in the antithrombin III binding pentasaccharide is oxidized much more rapidly than the bulk of the GlcA residues in heparin. Glucuronic Acid 30-34 serpin family C member 1 Homo sapiens 50-66 1576105-0 1992 In vivo inactivation of antithrombin III is promoted by heparin during cardiopulmonary bypass. Heparin 56-63 serpin family C member 1 Homo sapiens 24-40 1332442-10 1992 Further studies show that the GlcA residue in the antithrombin III binding pentasaccharide is oxidized much more rapidly than the bulk of the GlcA residues in heparin. pentasaccharide 75-90 serpin family C member 1 Homo sapiens 50-66 1332442-10 1992 Further studies show that the GlcA residue in the antithrombin III binding pentasaccharide is oxidized much more rapidly than the bulk of the GlcA residues in heparin. Glucuronic Acid 142-146 serpin family C member 1 Homo sapiens 50-66 1332442-10 1992 Further studies show that the GlcA residue in the antithrombin III binding pentasaccharide is oxidized much more rapidly than the bulk of the GlcA residues in heparin. Heparin 159-166 serpin family C member 1 Homo sapiens 50-66 1379965-2 1992 It consists of heparan, dermatan and chondroitin sulfate; a small proportion of heparan sulfate (4%) has high affinity for antithrombin III (AT III). Heparitin Sulfate 80-95 serpin family C member 1 Homo sapiens 123-139 1379965-2 1992 It consists of heparan, dermatan and chondroitin sulfate; a small proportion of heparan sulfate (4%) has high affinity for antithrombin III (AT III). Heparitin Sulfate 80-95 serpin family C member 1 Homo sapiens 141-147 1466276-1 1992 High molecular weight kininogen (HK) or its procoagulant light-chain but not the heavy chain potentiated the heparin enhancement of antithrombin III inactivation of plasma kallikrein and factor XIa from 10-50-fold to approximately 1000-fold at I 0.15, pH 7.4, 25 degrees C. This potentiation resulted in antithrombin becoming a predominant inhibitor of kallikrein and factor XIa in heparinized normal but not HK-deficient plasmas. Heparin 109-116 serpin family C member 1 Homo sapiens 132-148 1466276-1 1992 High molecular weight kininogen (HK) or its procoagulant light-chain but not the heavy chain potentiated the heparin enhancement of antithrombin III inactivation of plasma kallikrein and factor XIa from 10-50-fold to approximately 1000-fold at I 0.15, pH 7.4, 25 degrees C. This potentiation resulted in antithrombin becoming a predominant inhibitor of kallikrein and factor XIa in heparinized normal but not HK-deficient plasmas. Heparin 109-116 serpin family C member 1 Homo sapiens 132-144 1637525-8 1992 The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III). Glucose 70-77 serpin family C member 1 Homo sapiens 180-197 1637525-8 1992 The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III). Glucose 70-77 serpin family C member 1 Homo sapiens 199-205 1637525-8 1992 The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III). Lactic Acid 82-89 serpin family C member 1 Homo sapiens 180-197 1637525-8 1992 The system has been successfully applied to the on-line monitoring of glucose and lactate concentrations of an animal cell culture designed for the production of recombinant human antithrombine III (AT-III). Lactic Acid 82-89 serpin family C member 1 Homo sapiens 199-205 1576105-1 1992 To study the in vivo effect of heparin on antithrombin III (AT3) when elastase is elevated, the blood of 20 patients undergoing cardiopulmonary bypass (CPB) was assayed for elastase and AT3. Heparin 31-38 serpin family C member 1 Homo sapiens 42-58 1576105-1 1992 To study the in vivo effect of heparin on antithrombin III (AT3) when elastase is elevated, the blood of 20 patients undergoing cardiopulmonary bypass (CPB) was assayed for elastase and AT3. Heparin 31-38 serpin family C member 1 Homo sapiens 60-63 1576105-7 1992 These data indicate that (1) CPB is associated with an increase in plasma elastase, (2) elevated plasma elastase is associated with a reduction in AT3, and (3) heparin promotes the inactivation of AT3 when serum elastase is increased. Heparin 160-167 serpin family C member 1 Homo sapiens 197-200 1576105-8 1992 These data confirm the in vitro observation that heparin accelerates the inactivation of AT3 in the presence of elastase. Heparin 49-56 serpin family C member 1 Homo sapiens 89-92 1326098-3 1992 It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM). Heparin 62-69 serpin family C member 1 Homo sapiens 103-119 1326098-3 1992 It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM). Heparin 62-69 serpin family C member 1 Homo sapiens 103-115 1326098-3 1992 It is taken into account that the fraction of a low molecular heparin that binds with high affinity to antithrombin III contains two fundamentally different components: the material above the critical chain-length of 17 sugar units that has both anti-factor Xa activity and antithrombin activity (ACLM) and the material below that length with anti-factor Xa activity only (BCLM). Sugars 220-225 serpin family C member 1 Homo sapiens 103-119 1604438-0 1992 A useful restriction analysis for the determination of human antithrombin III variants with mutations from Ala 382 to Ala 384. Alanine 107-110 serpin family C member 1 Homo sapiens 61-77 1604438-0 1992 A useful restriction analysis for the determination of human antithrombin III variants with mutations from Ala 382 to Ala 384. Alanine 118-121 serpin family C member 1 Homo sapiens 61-77 1763970-0 1991 Binding of antithrombin to immobilized heparin under varying flow conditions. Heparin 39-46 serpin family C member 1 Homo sapiens 11-23 1660219-2 1991 The plasma levels of thrombin-antithrombin III complex (TAT) and alpha 2 plasmin inhibitor complex (PIC) were significantly elevated after TAE, concurrently with a decrease in antithrombin III and antiplasmin (alpha 2-plasmin inhibitor) levels. tae 139-142 serpin family C member 1 Homo sapiens 30-46 1746447-7 1991 Although antiplatelet and antithrombin agents such as aspirin and heparin help to decrease rethrombosis, these agents are far from ideal. Aspirin 54-61 serpin family C member 1 Homo sapiens 26-38 1746447-7 1991 Although antiplatelet and antithrombin agents such as aspirin and heparin help to decrease rethrombosis, these agents are far from ideal. Heparin 66-73 serpin family C member 1 Homo sapiens 26-38 1763970-2 1991 In this study, the effects of flow-velocity/wall shear stress on the interaction of antithrombin (AT) with surface-immobilized heparin were investigated. Heparin 127-134 serpin family C member 1 Homo sapiens 84-96 1763970-2 1991 In this study, the effects of flow-velocity/wall shear stress on the interaction of antithrombin (AT) with surface-immobilized heparin were investigated. Heparin 127-134 serpin family C member 1 Homo sapiens 98-100 1763970-3 1991 The binding of AT to low-affinity and high-affinity heparin could be discriminated by measurements at physiological of elevated ionic strength. Heparin 52-59 serpin family C member 1 Homo sapiens 15-17 1763970-4 1991 Under low shear stress conditions, substantial binding of AT to both high- and low-affinity heparin was observed, in relative quantities largely reflecting the proportion of these polysaccharide populations on the surface. Heparin 92-99 serpin family C member 1 Homo sapiens 58-60 1763970-4 1991 Under low shear stress conditions, substantial binding of AT to both high- and low-affinity heparin was observed, in relative quantities largely reflecting the proportion of these polysaccharide populations on the surface. Polysaccharides 180-194 serpin family C member 1 Homo sapiens 58-60 1763970-6 1991 Furthermore, under the highest shear stress (greater than 1,000 N/m2), the binding of AT to low-affinity heparin completely disappeared while binding to the high-affinity fraction persisted. Heparin 105-112 serpin family C member 1 Homo sapiens 86-88 1804603-7 1991 The mechanism of aspirin may be the inhibition of TXA2 and Fn synthesis and decreased consumption of AT-III. Aspirin 17-24 serpin family C member 1 Homo sapiens 101-107 1953677-7 1991 We also studied the affinity of the endothelial heparan sulphate chains towards two presumptive biological ligands, namely antithrombin III and lipoprotein lipase. Heparitin Sulfate 48-64 serpin family C member 1 Homo sapiens 123-139 1953677-8 1991 A major part of the endothelial heparan sulphate chains showed a weak affinity for antithrombin III and the affinity was essentially lost on heparinase digestion. Heparitin Sulfate 32-48 serpin family C member 1 Homo sapiens 83-99 1773617-9 1991 The decrease in apolipoprotein A1 and increase in antithrombin III may be related either to the decrease in estradiol levels induced by the treatment or to the effect of the progestogen itself. Estradiol 108-117 serpin family C member 1 Homo sapiens 50-66 1683643-2 1991 In this study multipoint linkage analysis of two Duffy-linked families given a combined LOD score of 8.65 to establish that the Duffy-linked CMT1B gene exists in the 18 centimorgan region between the antithrombin III gene and the Duffy/sodium-potassium ATPase loci. Sodium 236-242 serpin family C member 1 Homo sapiens 200-216 1683643-2 1991 In this study multipoint linkage analysis of two Duffy-linked families given a combined LOD score of 8.65 to establish that the Duffy-linked CMT1B gene exists in the 18 centimorgan region between the antithrombin III gene and the Duffy/sodium-potassium ATPase loci. Potassium 243-252 serpin family C member 1 Homo sapiens 200-216 1797807-2 1991 Poly(sodium vinyl sulfonate) is a water-soluble synthetic polymer and activates antithrombin III to exert nonthrombogenicity that was dependent on the molecular weight. lyapolate 0-27 serpin family C member 1 Homo sapiens 80-96 1837769-3 1991 Treatment with picotamide significantly reduced circulating platelet aggregates, beta-TG and TxB2 levels, without change of 6-keto-PGF-alpha values, with reduction of F VIII-C and slight increase of plasminogen and ATIII levels. picotamide 15-25 serpin family C member 1 Homo sapiens 215-220 1940573-3 1991 The IXa-AT III complex in the eluate was then measured by using polystyrene balls coated with immobilized rabbit anti-AT III antibody-binding fragments and anti-factor IX (anti-FIX) antibody-binding fragments labeled with beta-D-galactosidase. Polystyrenes 64-75 serpin family C member 1 Homo sapiens 8-14 1922367-3 1991 We show here that the reactive centre of the serpins can adopt varying conformations and that mobility of the reactive centre is necessary for the function of antithrombin and its binding and activation by heparin; the identification of a new locked conformation explains the latent inactive state of PAI-1. Heparin 206-213 serpin family C member 1 Homo sapiens 159-171 1741682-2 1991 The negative correlation between the degree of irreversibility of plasma protein adsorption and the amount of adsorbed AT-III for HEP, immobilized onto the polymer surface passivated with HSA, FG, and plasma was found. Polymers 156-163 serpin family C member 1 Homo sapiens 119-125 1663665-2 1991 With the help of a combined assay method heparin characterization is made possible using the TAT/XAT quotient under consideration of the simultaneous inhibition of the two serine proteases thrombin and factor Xa by antithrombin III. Heparin 41-48 serpin family C member 1 Homo sapiens 215-231 1833592-7 1991 Despite this increased heparin consumption, the patients who had received heparin before operation demonstrated increased activation of coagulation at the end of cardiopulmonary bypass (thrombin-antithrombin III complex, 19 +/- 4.1 ng/ml in group M and 61 +/- 7 ng/ml in group Hsc, p less than 0.05; cross-linked fibrin fragments, 257 +/- 92 ng/ml in group M and 875 +/- 152 ng/ml in group Hiv, p less than 0.05). Heparin 74-81 serpin family C member 1 Homo sapiens 195-211 1839430-3 1991 Patients treated with heparan sulphate also showed an increased fibrinolytic activity and a reduced antithrombin III consumption, both of which were statistically significant. Heparitin Sulfate 22-38 serpin family C member 1 Homo sapiens 100-116 1665594-0 1991 Low molecular weight heparin-catalyzed inactivation of factor Xa and thrombin by antithrombin III--effect of platelet factor 4. Heparin 21-28 serpin family C member 1 Homo sapiens 81-97 1744977-5 1991 In addition, thrombin inactivation by antithrombin III was accelerated on the endothelial surface, providing strong evidence that heparan sulfate on the surface of endothelial cells exerts a heparin-like activity. Heparitin Sulfate 130-145 serpin family C member 1 Homo sapiens 38-54 1780805-6 1991 Inhibition by heparin was restored by addition of increasing amounts of antithrombin (AT) to samples containing constant amounts of heparin, thrombin and 125I-r.hirudin and was not neutralized by protamine sulfate. Heparin 14-21 serpin family C member 1 Homo sapiens 72-84 1776135-3 1991 Arginine-406 is located at the 12th amino acid residue from the reactive site on the C-terminal side of AT-III in a core region of the molecule which has been highly conserved during evolution of serine protease inhibitor (serpin) family. Arginine 0-8 serpin family C member 1 Homo sapiens 104-110 1665594-3 1991 Pseudo-first order rate constants of inactivation of factor Xa and thrombin by antithrombin III were determined as function of heparin concentration, in the presence of 4.0 mM CaCl2. Heparin 127-134 serpin family C member 1 Homo sapiens 79-95 1665594-3 1991 Pseudo-first order rate constants of inactivation of factor Xa and thrombin by antithrombin III were determined as function of heparin concentration, in the presence of 4.0 mM CaCl2. Calcium Chloride 176-181 serpin family C member 1 Homo sapiens 79-95 1780805-6 1991 Inhibition by heparin was restored by addition of increasing amounts of antithrombin (AT) to samples containing constant amounts of heparin, thrombin and 125I-r.hirudin and was not neutralized by protamine sulfate. Heparin 132-139 serpin family C member 1 Homo sapiens 72-84 1911389-4 1991 To remove the normal component, the antithrombin was passed through a column of thrombin-Sepharose. Sepharose 89-98 serpin family C member 1 Homo sapiens 36-48 1897511-7 1991 Purified GAC possessed only 2% (W/W) of the antithrombin III cofactor activity of porcine heparin. Heparin 90-97 serpin family C member 1 Homo sapiens 44-60 1911389-3 1991 Accordingly, the antithrombin was isolated by heparin-Sepharose chromatography: this produced a mixture of normal and variant antithrombin, as the patient was heterozygous for the abnormality. Heparin 46-53 serpin family C member 1 Homo sapiens 17-29 1911389-3 1991 Accordingly, the antithrombin was isolated by heparin-Sepharose chromatography: this produced a mixture of normal and variant antithrombin, as the patient was heterozygous for the abnormality. Sepharose 54-63 serpin family C member 1 Homo sapiens 17-29 1911389-5 1991 On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin. Sodium Dodecyl Sulfate 3-26 serpin family C member 1 Homo sapiens 126-138 1911389-5 1991 On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin. polyacrylamide 27-41 serpin family C member 1 Homo sapiens 126-138 1911389-5 1991 On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin. Sodium Dodecyl Sulfate 63-66 serpin family C member 1 Homo sapiens 126-138 1911389-5 1991 On sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE), prior to its application to thrombin-Sepharose, the antithrombin migrated as a single band with identical mobility to that of normal antithrombin. Sepharose 111-120 serpin family C member 1 Homo sapiens 126-138 1911389-8 1991 One site of cleavage was unambiguously ascertained to be the Arg 393-Ser 394 reactive site bond, by NH2 terminal sequencing of the cleaved variant antithrombin: 10 steps beginning at the P1" position, Ser-Leu-Asn-Pro-Asn-Arg,..., were clearly identified. Ser-Leu-Asn-Pro-Asn-Arg 201-224 serpin family C member 1 Homo sapiens 147-159 1911389-13 1991 The present results with antithrombin Glasgow II suggest that all the alanine residues at the base of the reactive site loop in positions P12-10 may be important for the formation of a stabilized inhibitor-thrombin complex. Alanine 70-77 serpin family C member 1 Homo sapiens 25-37 1814829-2 1991 Our findings were: (1) CAAE could induce aggregation and alpha-granule release reaction in the washed human platelet suspension; thus it could activate the platelets; (2) the aggregation effect of CAAE was inhibited by albumin and affected by Ca2+, Mg2+ concentration; (3) heparin and/or AT III did not inhibit the aggregation activation of CAAE, but alpha 2MG markedly inhibited it; (4) the aggregation activity of CAAE was associated with the serine protease activity. caae 197-201 serpin family C member 1 Homo sapiens 288-294 1840095-2 1991 Since adequate thromboembolism protection requires a cofactor AT III for heparin to provide full antithrombotic coverage, the preoperative AT III and protein C levels in the plasma of 105 patients treated with marcumar are measured. Heparin 73-80 serpin family C member 1 Homo sapiens 62-68 1814829-2 1991 Our findings were: (1) CAAE could induce aggregation and alpha-granule release reaction in the washed human platelet suspension; thus it could activate the platelets; (2) the aggregation effect of CAAE was inhibited by albumin and affected by Ca2+, Mg2+ concentration; (3) heparin and/or AT III did not inhibit the aggregation activation of CAAE, but alpha 2MG markedly inhibited it; (4) the aggregation activity of CAAE was associated with the serine protease activity. caae 23-27 serpin family C member 1 Homo sapiens 288-294 1747261-3 1991 Plasma Antithrombin III (ATIII) is one of the most important coagulation inhibitors and the fundamental enzyme for the therapeutical action of heparin. Heparin 143-150 serpin family C member 1 Homo sapiens 7-23 1747261-3 1991 Plasma Antithrombin III (ATIII) is one of the most important coagulation inhibitors and the fundamental enzyme for the therapeutical action of heparin. Heparin 143-150 serpin family C member 1 Homo sapiens 25-30 1747261-4 1991 In the last years it was well established that ATIII deficiency accounts for a thrombotic state and inefficiency of heparin therapy. Heparin 116-123 serpin family C member 1 Homo sapiens 47-52 1837483-8 1991 These data suggest that danazol is potentially useful therapy that may increase levels of natural anticoagulants in patients with thrombotic illnesses in which ATIII, PC and PS are low or normal. Danazol 24-31 serpin family C member 1 Homo sapiens 160-165 1868237-2 1991 Frameshift mutations of one base and two bases, respectively, were found to have occurred in two unrelated patients at the same GAG codon (Glu 245) within exon 4 of the ATIII gene. Glutamic Acid 139-142 serpin family C member 1 Homo sapiens 169-174 1860682-0 1991 Antithrombin III supplementation reduces heparin requirement and platelet loss during hemodialysis of patients with fulminant hepatic failure. Heparin 41-48 serpin family C member 1 Homo sapiens 0-16 1860682-2 1991 In this study, we have performed a controlled, randomized trial of antithrombin III supplementation on heparin activity, occurrence of bleeding and the platelet count and activation during hemodialysis in 24 patients with fulminant hepatic failure. Heparin 103-110 serpin family C member 1 Homo sapiens 67-83 1860682-6 1991 Total heparin usage was significantly decreased by antithrombin III supplementation (median 5,200 U; range = 2,000 to 13,000) as compared with the control group (median 10,200 U; range = 5,000 to 16,500; p less than 0.005). Heparin 6-13 serpin family C member 1 Homo sapiens 51-67 1860682-7 1991 Blood heparin level (antifactor Xa activity) after the initial bolus was significantly greater in the antithrombin III-supplemented subjects (0.40 +/- 0.07 U/ml compared with 0.22 +/- 0.05 U/ml in the control group; p less than 0.05). Heparin 6-13 serpin family C member 1 Homo sapiens 102-118 1920862-6 1991 Management of high TAT began with the use of an anticoagulant such as heparin under the condition of sufficient ATIII level. Heparin 70-77 serpin family C member 1 Homo sapiens 112-117 2070046-9 1991 Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly. Heparin 15-22 serpin family C member 1 Homo sapiens 99-104 2070046-9 1991 Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly. Heparin 57-64 serpin family C member 1 Homo sapiens 99-104 2070046-9 1991 Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly. pentasaccharide 66-81 serpin family C member 1 Homo sapiens 99-104 2070046-9 1991 Unfractionated heparin and an ultra-low molecular weight heparin (pentasaccharide) did enhance the ATIII-dependent neutralization of prothrombinase, but to a much lesser extent than observed with small unilaminar phospholipid vesicles as the catalytic sites for prothrombinase assembly. Phospholipids 213-225 serpin family C member 1 Homo sapiens 99-104 1649042-8 1991 In HCC patients, AT III levels were related to the total cholesterol level (R2 = 0.317), whereas in the cirrhotic patients it correlated with the prothrombin level (R2 = 0.274). Cholesterol 57-68 serpin family C member 1 Homo sapiens 17-23 1940520-8 1991 In patients with familial ATIII deficiency, 50% of normal ATIII activity can be expected because they are heterozygotes, so the cardio-pulmonary bypass should be run with special caution to the heparin dosage. Heparin 194-201 serpin family C member 1 Homo sapiens 26-31 1873224-4 1991 However, in quantitative AT III deficiencies, only three mutations have been described: Pro 407 to Leu and A1a404 to Thr (both located in the C-terminal part of the AT III molecule) and also a frameshift in exon IIIa. Threonine 117-120 serpin family C member 1 Homo sapiens 25-31 1716644-2 1991 Chlorthalidone produced a slight decrease in clearance of anti-Xa activity from 7.1 +/- 1.0 to 6.6 +/- 0.8 mL/min and a decrease of the volume of distribution from 0.20 +/- 0.05 to 0.16 +/- 0.04 L/kg, whereas the volume of distribution of antithrombin activity increased from 0.14 +/- 0.05 to 0.26 +/- 0.10 L/kg (all differences P less than .05). Chlorthalidone 0-14 serpin family C member 1 Homo sapiens 239-251 1920862-9 1991 To reduce the high TAT under the deficient state of ATIII, MD805, a synthetic thrombin inhibitor, was introduced to avoid further consumption of ATIII. argatroban 59-64 serpin family C member 1 Homo sapiens 52-57 1920862-9 1991 To reduce the high TAT under the deficient state of ATIII, MD805, a synthetic thrombin inhibitor, was introduced to avoid further consumption of ATIII. argatroban 59-64 serpin family C member 1 Homo sapiens 145-150 1896523-0 1991 6-Pentadecylsalicylic acid: an antithrombin component isolated from the stem of Rhus semialata var. anacardic acid 0-26 serpin family C member 1 Homo sapiens 31-43 2033259-1 1991 Heparin, a polyion, exerts its main activity to inhibit coagulation through a serine protease inhibitor, antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 105-121 2048592-6 1991 Plasma levels of contraceptive steroids also were related to changes in the most extreme levels of antithrombin III. Steroids 31-39 serpin family C member 1 Homo sapiens 99-115 2066426-2 1991 The heparin concentration and the incubation time in the assay were optimised specifically to permit the detection of heparin binding defects of antithrombin. Heparin 4-11 serpin family C member 1 Homo sapiens 145-157 2066426-2 1991 The heparin concentration and the incubation time in the assay were optimised specifically to permit the detection of heparin binding defects of antithrombin. Heparin 118-125 serpin family C member 1 Homo sapiens 145-157 2066426-4 1991 Several commercially available assays recommend a longer incubation time than 30 seconds and therefore some patients with heparin binding defects of antithrombin may not be identified. Heparin 122-129 serpin family C member 1 Homo sapiens 149-161 2066426-5 1991 The assay described here allows heparin binding variants of antithrombin to be identified and distinguished from other types of antithrombin deficiency in a simple two stage procedure. Heparin 32-39 serpin family C member 1 Homo sapiens 60-72 2029579-8 1991 Approximately 50% of the AT-III from the propositus isolated by heparin-Sepharose chromatography, when incubated with either human alpha-thrombin or factor Xa, did not form complex but was cleaved, presumably at the reactive center Arg393-Ser394. Heparin 64-71 serpin family C member 1 Homo sapiens 25-31 1908914-8 1991 In patients with accelerated fibrinolysis, PAI-C values correlated with t-PA antigen (r = 0.838), PAI-1 antigen (r = 0.519), ATIII activity (r = -0.669) (p less than 0.01) and D dimer levels (r = 0.391, p less than 0.05). pai-c 43-48 serpin family C member 1 Homo sapiens 125-130 2029579-8 1991 Approximately 50% of the AT-III from the propositus isolated by heparin-Sepharose chromatography, when incubated with either human alpha-thrombin or factor Xa, did not form complex but was cleaved, presumably at the reactive center Arg393-Ser394. Sepharose 72-81 serpin family C member 1 Homo sapiens 25-31 2029579-1 1991 Antithrombin-III-Hamilton has been shown to be a structural variant of antithrombin-III (AT-III) with normal heparin affinity but impaired protease inhibitory activity. Heparin 109-116 serpin family C member 1 Homo sapiens 0-16 1833126-5 1991 Treatment with the low and high dose contraceptive increased the plasma levels of ethinyl estradiol (728 +/- 139 and 1438 +/- 212 vs. 0 fmol/l [low and high dose vs. control], means +/- SEM, P less than 0.001) and fibrinogen (2.3 +/- 0.1 and 2.6 +/- 0.1 vs. 2.0 +/- 0.1 g/l, P less than 0.05); and decreased antithrombin III activity (95 +/- 3 and 92 +/- 3 vs. 101 +/- 3 %, P less than 0.05). Ethinyl Estradiol 82-99 serpin family C member 1 Homo sapiens 308-324 2029579-1 1991 Antithrombin-III-Hamilton has been shown to be a structural variant of antithrombin-III (AT-III) with normal heparin affinity but impaired protease inhibitory activity. Heparin 109-116 serpin family C member 1 Homo sapiens 71-87 2029579-1 1991 Antithrombin-III-Hamilton has been shown to be a structural variant of antithrombin-III (AT-III) with normal heparin affinity but impaired protease inhibitory activity. Heparin 109-116 serpin family C member 1 Homo sapiens 89-95 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Heparin 62-69 serpin family C member 1 Homo sapiens 5-11 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sepharose 70-79 serpin family C member 1 Homo sapiens 5-11 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sodium Dodecyl Sulfate 125-147 serpin family C member 1 Homo sapiens 5-11 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. polyacrylamide 148-162 serpin family C member 1 Homo sapiens 5-11 2029579-4 1991 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sodium Dodecyl Sulfate 184-187 serpin family C member 1 Homo sapiens 5-11 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Heparin 103-110 serpin family C member 1 Homo sapiens 13-19 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sepharose 111-120 serpin family C member 1 Homo sapiens 13-19 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sepharose 134-143 serpin family C member 1 Homo sapiens 13-19 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate 196-199 serpin family C member 1 Homo sapiens 13-19 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate 196-199 serpin family C member 1 Homo sapiens 76-82 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate 196-199 serpin family C member 1 Homo sapiens 76-82 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Heparin 258-265 serpin family C member 1 Homo sapiens 13-19 2029579-5 1991 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sepharose 134-143 serpin family C member 1 Homo sapiens 13-19 2029579-6 1991 Under nonreducing conditions this AT-III-Hamilton species had decreased mobility compared with AT-III from the propositus (or normal AT-III) isolated only by heparin-Sepharose chromatography. Heparin 158-165 serpin family C member 1 Homo sapiens 34-40 2029579-6 1991 Under nonreducing conditions this AT-III-Hamilton species had decreased mobility compared with AT-III from the propositus (or normal AT-III) isolated only by heparin-Sepharose chromatography. Sepharose 166-175 serpin family C member 1 Homo sapiens 34-40 2027669-2 1991 Only AT-III molecules with a low heparin affinity were detected in her plasma and these pathological AT-III molecules could not increase the rate of the thrombin-inactivation at all. Heparin 33-40 serpin family C member 1 Homo sapiens 5-11 2022745-5 1991 The inhibitory potency of heparin was not dependent upon its affinity for antithrombin III, but was molecular weight dependent: homogeneous preparations of lower molecular weight were less inhibitory. Heparin 26-33 serpin family C member 1 Homo sapiens 74-90 2015284-1 1991 The technique of competitive chromogenic substrate hydrolysis is used to examine the inhibitory effects of sucrose and glycerol on the inactivation of thrombin by antithrombin III. Sucrose 107-114 serpin family C member 1 Homo sapiens 163-179 2019790-1 1991 Three recent studies have reported that fibrin in solution significantly inhibits the ability of heparin to catalyze the inhibition of thrombin by antithrombin III. Heparin 97-104 serpin family C member 1 Homo sapiens 147-163 2019790-4 1991 Because the results of these studies suggest that fibrin inhibits the reactivity of thrombin with antithrombin III-heparin but not with heparin cofactor II-dermatan sulfate, we compared the relative catalytic effects of heparin and dermatan sulfate on thrombin inhibition in plasma, both in the presence and absence of fibrin. Heparin 115-122 serpin family C member 1 Homo sapiens 98-114 1870264-5 1991 Nucleotide sequencing of exon 6 of AT III gene showed a G to T transitional mutation resulting in the conversion of arginine-406 to methionine coexisted with normal allele which encodes arginine. Arginine 116-124 serpin family C member 1 Homo sapiens 35-41 2016290-7 1991 Chromatography on antithrombin III-Sepharose gel indicated that the structural change involved in ST heparin resulted in an obvious increase in the ability to bind antithrombin III. Sepharose 35-44 serpin family C member 1 Homo sapiens 18-34 2016290-7 1991 Chromatography on antithrombin III-Sepharose gel indicated that the structural change involved in ST heparin resulted in an obvious increase in the ability to bind antithrombin III. Sepharose 35-44 serpin family C member 1 Homo sapiens 164-180 2016290-7 1991 Chromatography on antithrombin III-Sepharose gel indicated that the structural change involved in ST heparin resulted in an obvious increase in the ability to bind antithrombin III. Heparin 101-108 serpin family C member 1 Homo sapiens 18-34 2016290-7 1991 Chromatography on antithrombin III-Sepharose gel indicated that the structural change involved in ST heparin resulted in an obvious increase in the ability to bind antithrombin III. Heparin 101-108 serpin family C member 1 Homo sapiens 164-180 2015284-1 1991 The technique of competitive chromogenic substrate hydrolysis is used to examine the inhibitory effects of sucrose and glycerol on the inactivation of thrombin by antithrombin III. Glycerol 119-127 serpin family C member 1 Homo sapiens 163-179 2007588-0 1991 Predominant contribution of surface approximation to the mechanism of heparin acceleration of the antithrombin-thrombin reaction. Heparin 70-77 serpin family C member 1 Homo sapiens 98-110 2057915-0 1991 Influence of tryptophan modification upon digestion of antithrombin III by elastase. Tryptophan 13-23 serpin family C member 1 Homo sapiens 55-71 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Tryptophan 25-35 serpin family C member 1 Homo sapiens 48-64 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium 68-120 serpin family C member 1 Homo sapiens 48-64 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. hnbsb 122-127 serpin family C member 1 Homo sapiens 48-64 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. hnbsb 122-127 serpin family C member 1 Homo sapiens 259-275 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. 2-hydroxy-5-nitrobenzyl 78-101 serpin family C member 1 Homo sapiens 48-64 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. (2S,5R)-5-pentyltetrahydrofuran-2-ol 122-125 serpin family C member 1 Homo sapiens 48-64 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. (2S,5R)-5-pentyltetrahydrofuran-2-ol 122-125 serpin family C member 1 Homo sapiens 259-275 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Heparin 311-318 serpin family C member 1 Homo sapiens 48-64 2057915-1 1991 Chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNBSB) generates products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl [HNB] incorporated/mole of antithrombin III) but with high or low affinity for heparin-Sepharose. Sepharose 319-328 serpin family C member 1 Homo sapiens 48-64 1893059-5 1991 If the XaI activity was corrected for the ATIII concentration, the heparin activities no longer differed significantly from zero. Heparin 67-74 serpin family C member 1 Homo sapiens 42-47 2007588-2 1991 Heparin has been shown to accelerate the inactivation of alpha-thrombin by antithrombin III (AT) by promoting the initial encounter of proteinase and inhibitor in a ternary thrombin-AT-heparin complex. Heparin 0-7 serpin family C member 1 Homo sapiens 75-91 2013315-2 1991 The heparin affinity of normal and two P1 variants of antithrombin-III (AT) was studied by gradient elution with NaCl in Tris buffer on heparin-Sepharose. Heparin 4-11 serpin family C member 1 Homo sapiens 54-70 1930634-4 1991 The primary structures of bovine and human ATIII were compared: all the residues required for the integrity of the heparin-binding domain are strictly conserved. Heparin 115-122 serpin family C member 1 Homo sapiens 43-48 1999418-7 1991 For example, interactions of the sulfate monoanion are important for the binding of heparin, a sulfated glycosaminoglycan, to antithrombin III. sulfate monoanion 33-50 serpin family C member 1 Homo sapiens 126-142 1831314-0 1991 [Antithrombin-III-control in Marcumar patients in oral surgery]. Phenprocoumon 29-37 serpin family C member 1 Homo sapiens 1-17 1872461-1 1991 The identification of a specific required carbohydrate structure for the antithrombin III binding site on heparin suggests that there may be specific structures in glycosaminoglycan chains which are necessary for other vascular functions of these carbohydrates. Carbohydrates 42-54 serpin family C member 1 Homo sapiens 73-89 1872461-1 1991 The identification of a specific required carbohydrate structure for the antithrombin III binding site on heparin suggests that there may be specific structures in glycosaminoglycan chains which are necessary for other vascular functions of these carbohydrates. Heparin 106-113 serpin family C member 1 Homo sapiens 73-89 1872461-1 1991 The identification of a specific required carbohydrate structure for the antithrombin III binding site on heparin suggests that there may be specific structures in glycosaminoglycan chains which are necessary for other vascular functions of these carbohydrates. Glycosaminoglycans 164-181 serpin family C member 1 Homo sapiens 73-89 1872461-1 1991 The identification of a specific required carbohydrate structure for the antithrombin III binding site on heparin suggests that there may be specific structures in glycosaminoglycan chains which are necessary for other vascular functions of these carbohydrates. Carbohydrates 247-260 serpin family C member 1 Homo sapiens 73-89 1999418-7 1991 For example, interactions of the sulfate monoanion are important for the binding of heparin, a sulfated glycosaminoglycan, to antithrombin III. Heparin 84-91 serpin family C member 1 Homo sapiens 126-142 1706595-1 1991 This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis. Heparin 116-123 serpin family C member 1 Homo sapiens 203-219 1706595-1 1991 This protein is known to be involved in processes that follow platelet stimulation, specifically, in the binding of heparin (interfering with the heparin-mediated inhibition of thrombin and Factor Xa by antithrombin III), in the growth of endothelial cells and in fibrinolysis. Heparin 146-153 serpin family C member 1 Homo sapiens 203-219 1995647-7 1991 This recombinant ATIII protein was immunologically reactive with antisera raised against native human ATIII, formed stable complexes with thrombin, and was heparin-accelerated at the same concentration as native human ATIII. Heparin 156-163 serpin family C member 1 Homo sapiens 17-22 2044614-11 1991 The fluctuations in ATIII levels in childhood nephrotic syndrome are determined by the response to steroids and not by the renal histology per se. Steroids 99-107 serpin family C member 1 Homo sapiens 20-25 1780907-1 1991 Affinity chromatography on heparin-Sepharose has been widely used for the purification of post-heparin plasma triglyceride lipases, but this procedure alone yields lipase fractions with a high content of antithrombin III (AT), which also binds to heparin and coelutes with the lipases. Heparin 27-34 serpin family C member 1 Homo sapiens 204-220 1780907-1 1991 Affinity chromatography on heparin-Sepharose has been widely used for the purification of post-heparin plasma triglyceride lipases, but this procedure alone yields lipase fractions with a high content of antithrombin III (AT), which also binds to heparin and coelutes with the lipases. Sepharose 35-44 serpin family C member 1 Homo sapiens 204-220 1995647-8 1991 In addition, the recombinant ATIII retained specificity for the same molecular species of heparin that activates authentic human ATIII. Heparin 90-97 serpin family C member 1 Homo sapiens 29-34 1995647-8 1991 In addition, the recombinant ATIII retained specificity for the same molecular species of heparin that activates authentic human ATIII. Heparin 90-97 serpin family C member 1 Homo sapiens 129-134 1703436-4 1991 Furthermore, it can be deduced that the amino acid residues, proposed to mediate heparin binding in the serpins antithrombin III and heparin cofactor II, are conserved in PAI-1. Heparin 81-88 serpin family C member 1 Homo sapiens 112-128 2035830-4 1991 The application of these new QAC developments is illustrated by the determination of binding constants for the interactions of high-affinity heparin (Mr 20,300) with antithrombin III at three temperatures. Benzethonium 29-32 serpin family C member 1 Homo sapiens 166-182 2035830-4 1991 The application of these new QAC developments is illustrated by the determination of binding constants for the interactions of high-affinity heparin (Mr 20,300) with antithrombin III at three temperatures. Heparin 141-148 serpin family C member 1 Homo sapiens 166-182 1848441-8 1991 The anti Xa activity peak seen after adding AT III to plasma was much higher with heparin than with enoxaparin. Heparin 82-89 serpin family C member 1 Homo sapiens 44-50 1848441-8 1991 The anti Xa activity peak seen after adding AT III to plasma was much higher with heparin than with enoxaparin. Enoxaparin 100-110 serpin family C member 1 Homo sapiens 44-50 1848441-9 1991 In urine, biological activities, measured with AT III supplementation, were higher with enoxaparin than with heparin. Enoxaparin 88-98 serpin family C member 1 Homo sapiens 47-53 1848441-9 1991 In urine, biological activities, measured with AT III supplementation, were higher with enoxaparin than with heparin. Heparin 109-116 serpin family C member 1 Homo sapiens 47-53 2033902-5 1991 Hematological examinations concerning coagulation and fibrinolysis remained within a normal range except for the serum concentration of antithrombin III (AT III) and its functional property with regard to the heparin cofactor, which were 8.8 mg/dl and 48%, respectively. Heparin 209-216 serpin family C member 1 Homo sapiens 136-152 1959799-3 1991 So, high plasma L-homocysteine concentration could play a role in the low antithrombin III activity level. Homocysteine 16-30 serpin family C member 1 Homo sapiens 74-90 2024235-4 1991 Administration of azathioprine (AZA), cyclosporine A (CSA) or both as immunosuppressive therapy did not affect HC II levels, but CSA seems to have raised plasma AT III. Azathioprine 18-30 serpin family C member 1 Homo sapiens 161-167 2062560-2 1991 Both the variant and normal antithrombin component were purified by affinity chromatography on heparin Sepharose. Sepharose 103-112 serpin family C member 1 Homo sapiens 28-40 1794749-4 1991 A pentasaccharide with high affinity for antithrombin III and the C-terminal dodecapeptide fragment of hirudin (hirugen) which occupy the anion-binding and fibrin(ogen) recognition exosites of alpha-thrombin, respectively, could not significantly inhibit factor VIII and factor V activation. pentasaccharide 2-17 serpin family C member 1 Homo sapiens 41-57 1794751-0 1991 Heparin requires both antithrombin and extrinsic pathway inhibitor for its anticoagulant effect in human blood. Heparin 0-7 serpin family C member 1 Homo sapiens 22-34 1650391-3 1991 The interest raised by low molecular weight heparins (LMWH), prepared as early as 1970, was based on a concept that is currently called into question: their anti-Xa activity, accounting for the antithrombotic activity, is high, while the anti-IIa (antithrombin) activity, producing the hemorrhagic risks, is lower. Heparin 44-52 serpin family C member 1 Homo sapiens 248-260 1650391-3 1991 The interest raised by low molecular weight heparins (LMWH), prepared as early as 1970, was based on a concept that is currently called into question: their anti-Xa activity, accounting for the antithrombotic activity, is high, while the anti-IIa (antithrombin) activity, producing the hemorrhagic risks, is lower. Heparin, Low-Molecular-Weight 54-58 serpin family C member 1 Homo sapiens 248-260 1664095-5 1991 The clearance of the antithrombin activity of a LMWH is higher than that of the antifactor Xa activity. Heparin, Low-Molecular-Weight 48-52 serpin family C member 1 Homo sapiens 21-33 2049431-6 1991 We conclude that the intraperitoneal administration of heparin at these doses is effective in preventing fibrin precipitation when intraperitoneal AT-III levels are expected to be relatively increased such as at the start of CAPD or in the presence of peritonitis. Heparin 55-62 serpin family C member 1 Homo sapiens 147-153 1665467-2 1991 We define a standard independent unit (SIU) of heparin as that amount that, in plasma containing 1 mumol of ATIII, raises the (pseudo-)first-order breakdown constant of factor Xa by 1 min-1. Heparin 47-54 serpin family C member 1 Homo sapiens 108-113 2019613-0 1991 Interaction of poly(sodium vinyl sulfonate) and its surface graft with antithrombin III. poly 15-19 serpin family C member 1 Homo sapiens 71-87 2019613-0 1991 Interaction of poly(sodium vinyl sulfonate) and its surface graft with antithrombin III. lyapolate 20-42 serpin family C member 1 Homo sapiens 71-87 2019613-1 1991 Poly(sodium vinyl sulfonate) (PVS) was found to be 1/14 times as active as heparin in inducing the conformational change and activation of antithrombin III. lyapolate 0-28 serpin family C member 1 Homo sapiens 139-155 2019613-1 1991 Poly(sodium vinyl sulfonate) (PVS) was found to be 1/14 times as active as heparin in inducing the conformational change and activation of antithrombin III. lyapolate 30-33 serpin family C member 1 Homo sapiens 139-155 2019613-1 1991 Poly(sodium vinyl sulfonate) (PVS) was found to be 1/14 times as active as heparin in inducing the conformational change and activation of antithrombin III. Heparin 75-82 serpin family C member 1 Homo sapiens 139-155 2019613-2 1991 The conformational change of antithrombin III was investigated in terms of the intrinsic fluorescence of tryptophan residue, the extrinsic fluorescence using 1,6-diphenyl-1,3,5-hexatriene as fluorescent probe, and Fourier-transform infrared spectroscopy. Tryptophan 105-115 serpin family C member 1 Homo sapiens 29-45 2019613-2 1991 The conformational change of antithrombin III was investigated in terms of the intrinsic fluorescence of tryptophan residue, the extrinsic fluorescence using 1,6-diphenyl-1,3,5-hexatriene as fluorescent probe, and Fourier-transform infrared spectroscopy. Diphenylhexatriene 158-187 serpin family C member 1 Homo sapiens 29-45 2019613-3 1991 It was evident in the experiment using 2,4,6-trinitrobenzene sulfonate that PVS elicited the activity of antithrombin III by interacting with amino groups of the protein as does heparin. Trinitrobenzenesulfonic Acid 39-70 serpin family C member 1 Homo sapiens 105-121 2019613-3 1991 It was evident in the experiment using 2,4,6-trinitrobenzene sulfonate that PVS elicited the activity of antithrombin III by interacting with amino groups of the protein as does heparin. lyapolate 76-79 serpin family C member 1 Homo sapiens 105-121 2019613-3 1991 It was evident in the experiment using 2,4,6-trinitrobenzene sulfonate that PVS elicited the activity of antithrombin III by interacting with amino groups of the protein as does heparin. Heparin 178-185 serpin family C member 1 Homo sapiens 105-121 1366314-4 1991 The index of biologic activity of Antithrombin III was significantly decreased after giving heparin to the patients with chronic renal failure on hemodialysis. Heparin 92-99 serpin family C member 1 Homo sapiens 34-50 2133241-4 1990 Two of the MAbs (11 and 16) inhibited heparin cofactor but not AT III progressive activity, and the binding of AT III to MAb 11, used for the IRMA, was blocked by heparin. Heparin 163-170 serpin family C member 1 Homo sapiens 111-117 1948084-0 1991 A new synthetic pentasaccharide with increased anti-factor Xa activity: possible role for anionic clusters in the interaction of heparin and antithrombin III. pentasaccharide 16-31 serpin family C member 1 Homo sapiens 141-157 2133241-5 1990 These results indicate that MAb 11 is directed at or near to the heparin binding site, and could therefore be useful in the study of structural aspects of this site in normal and genetically abnormal AT III. Heparin 65-72 serpin family C member 1 Homo sapiens 200-206 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Heparin 178-185 serpin family C member 1 Homo sapiens 212-217 2084825-0 1990 Pyridoxine reduces cholesterol and low-density lipoprotein and increases antithrombin III activity in 80-year-old men with low plasma pyridoxal 5-phosphate. Pyridoxine 0-10 serpin family C member 1 Homo sapiens 73-89 2084825-1 1990 We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels. Pyridoxine 33-43 serpin family C member 1 Homo sapiens 167-183 2084825-1 1990 We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels. Pyridoxine 33-43 serpin family C member 1 Homo sapiens 185-191 2084825-1 1990 We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels. Pyridoxal Phosphate 252-273 serpin family C member 1 Homo sapiens 185-191 2084825-1 1990 We have previously observed that pyridoxine treatment reduced plasma total cholesterol (TC) and low-density lipoprotein (LDL) cholesterol concentrations and increased antithrombin III (AT III) activity in atherosclerotic patients with subnormal plasma pyridoxal 5-phosphate (PLP) levels. Pyridoxal Phosphate 275-278 serpin family C member 1 Homo sapiens 185-191 2084825-5 1990 The mechanism by which pyridoxine acts is unclear but it is hypothesized that pyridoxine-derived PLP may enhance the catabolism of LDL and the activity of AT III by inhibiting their glycosylation. Pyridoxine 23-33 serpin family C member 1 Homo sapiens 155-161 2084825-5 1990 The mechanism by which pyridoxine acts is unclear but it is hypothesized that pyridoxine-derived PLP may enhance the catabolism of LDL and the activity of AT III by inhibiting their glycosylation. Pyridoxine 78-88 serpin family C member 1 Homo sapiens 155-161 2229057-0 1990 Important role of arginine 129 in heparin-binding site of antithrombin III. Arginine 18-26 serpin family C member 1 Homo sapiens 58-74 2292586-1 1990 The tributylammonium salt of a porcine heparin subfraction with low affinity for antithrombin III (Mr 7,500-18,000; anti-clotting activity, 7 USP units/mg), having degrees of sulfate substitution at D-glucosamine and L-iduronic acid residues of GlcNS 0.786, GlcN6s 0.628, and IdoA2s 0.682 mol, was reacted with 10 or 20 mol of pyridine-sulfur trioxide per mol equiv. tributylammonium salt 4-25 serpin family C member 1 Homo sapiens 81-97 2229057-0 1990 Important role of arginine 129 in heparin-binding site of antithrombin III. Heparin 34-41 serpin family C member 1 Homo sapiens 58-74 2229057-4 1990 This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding. Arginine 130-133 serpin family C member 1 Homo sapiens 31-36 2229057-4 1990 This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding. Lysine 137-140 serpin family C member 1 Homo sapiens 31-36 2229057-4 1990 This amino acid is part of the ATIII region comprising residues 114-154, which contains the highest proportion of basic residues (Arg or Lys), and is known from chemical modification studies to be involved in heparin binding. Heparin 209-216 serpin family C member 1 Homo sapiens 31-36 2229057-6 1990 High affinity (for ATIII) heparin had only a minimal effect on thrombin and activated factor X inhibition by the purified abnormal ATIII. Heparin 26-33 serpin family C member 1 Homo sapiens 19-24 2229057-7 1990 Taken together, these results demonstrate an important role for Arg-129 in the binding and interaction of ATIII with heparin of high affinity. Arginine 64-67 serpin family C member 1 Homo sapiens 106-111 2229057-7 1990 Taken together, these results demonstrate an important role for Arg-129 in the binding and interaction of ATIII with heparin of high affinity. Heparin 117-124 serpin family C member 1 Homo sapiens 106-111 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Lysine 38-41 serpin family C member 1 Homo sapiens 212-217 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Arginine 47-50 serpin family C member 1 Homo sapiens 212-217 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Lysine 56-59 serpin family C member 1 Homo sapiens 212-217 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. Arginine 69-72 serpin family C member 1 Homo sapiens 212-217 2229057-8 1990 We propose that a cooperation between Lys-125, Arg-129, Lys-136, and Arg-47 exposed at the surface of the inhibitor allows the binding of the essential pentasaccharide domain of heparin which is specific for the ATIII interaction. pentasaccharide 152-167 serpin family C member 1 Homo sapiens 212-217 2290238-6 1990 Then she was treated with AT III concentrate and urokinase and her asthmatic symptom was significantly improved and steroid hormone could be easily reduced. Steroids 116-131 serpin family C member 1 Homo sapiens 26-32 1977621-1 1990 Antithrombin Dublin is an electrophoretically fast variant of antithrombin which has normal heparin affinity. Heparin 92-99 serpin family C member 1 Homo sapiens 0-12 1977621-1 1990 Antithrombin Dublin is an electrophoretically fast variant of antithrombin which has normal heparin affinity. Heparin 92-99 serpin family C member 1 Homo sapiens 62-74 1977621-3 1990 N-terminal sequencing of antithrombin from two individuals, heterozygous for the Dublin mutation, showed the presence of a truncated antithrombin in which the N-terminal dipeptide is absent. Dipeptides 170-179 serpin family C member 1 Homo sapiens 25-37 1977621-3 1990 N-terminal sequencing of antithrombin from two individuals, heterozygous for the Dublin mutation, showed the presence of a truncated antithrombin in which the N-terminal dipeptide is absent. Dipeptides 170-179 serpin family C member 1 Homo sapiens 133-145 2248954-3 1990 The 10,000-fold rate enhancement elicited by the addition of heparin to the antithrombin III inhibition reaction, however, is the same. Heparin 61-68 serpin family C member 1 Homo sapiens 76-92 2226466-0 1990 Inhibition of factor X and factor V activation by dermatan sulfate and a pentasaccharide with high affinity for antithrombin III in human plasma. pentasaccharide 73-88 serpin family C member 1 Homo sapiens 112-128 2226466-4 1990 We determined the concentrations of each of heparin, dermatan sulfate and a pentasaccharide with high affinity for antithrombin III, to delay intrinsic prothrombin activation for at least 15s. Heparin 44-51 serpin family C member 1 Homo sapiens 115-131 2226466-4 1990 We determined the concentrations of each of heparin, dermatan sulfate and a pentasaccharide with high affinity for antithrombin III, to delay intrinsic prothrombin activation for at least 15s. pentasaccharide 76-91 serpin family C member 1 Homo sapiens 115-131 2207328-3 1990 AT-III messenger RNA (mRNA) transcripts derived from this construct were translated in an mRNA-dependent rabbit reticulocyte lysate (RRL) system containing (35S)methionine. Methionine 161-171 serpin family C member 1 Homo sapiens 0-6 2207328-4 1990 Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III. Sodium Dodecyl Sulfate 112-134 serpin family C member 1 Homo sapiens 94-100 2207328-4 1990 Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III. polyacrylamide 135-149 serpin family C member 1 Homo sapiens 94-100 2207328-4 1990 Immunoprecipitation of the cell-free translation mixture with rabbit polyclonal antibodies to AT-III showed, by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a 47-Kd polypeptide which is the non-glycosylated mature form of plasma AT-III. Sodium Dodecyl Sulfate 171-174 serpin family C member 1 Homo sapiens 94-100 2207328-6 1990 Heparin-Sepharose chromatography resulted in the elution of cell-free derived AT-III as a broad peak between 0.2 and 0.7 mol/L NaCl. Heparin 0-7 serpin family C member 1 Homo sapiens 78-84 2207328-6 1990 Heparin-Sepharose chromatography resulted in the elution of cell-free derived AT-III as a broad peak between 0.2 and 0.7 mol/L NaCl. Sepharose 8-17 serpin family C member 1 Homo sapiens 78-84 2207328-6 1990 Heparin-Sepharose chromatography resulted in the elution of cell-free derived AT-III as a broad peak between 0.2 and 0.7 mol/L NaCl. Sodium Chloride 127-131 serpin family C member 1 Homo sapiens 78-84 1964634-2 1990 Heparin is only effective as an anticoagulant in the presence of a plasma protein termed antithrombin III, with which it forms a complex. Heparin 0-7 serpin family C member 1 Homo sapiens 89-105 1964634-3 1990 High- and low-affinity heparin are 2 types that readily bind or do not bind, respectively, to antithrombin III. Heparin 23-30 serpin family C member 1 Homo sapiens 94-110 2292586-3 1990 Affinity chromatography of the sulfated products on antithrombin III-Sepharose gel indicated that the polysaccharide acquired some affinity for the protein following the sulfation, as shown by the increase in the proportion of the high-affinity heparin fraction (%) from 1.1 to 6.7. Sepharose 69-78 serpin family C member 1 Homo sapiens 52-68 2292586-3 1990 Affinity chromatography of the sulfated products on antithrombin III-Sepharose gel indicated that the polysaccharide acquired some affinity for the protein following the sulfation, as shown by the increase in the proportion of the high-affinity heparin fraction (%) from 1.1 to 6.7. Polysaccharides 102-116 serpin family C member 1 Homo sapiens 52-68 2292586-4 1990 Biological examination of these products indicated that sulfation at natural positions along with the polysaccharide chain resulted in significant increases in all the activities (blood anti-clotting, anti-Factor IIa, and anti-Factor Xa), and in the strength of intrinsic fluorescence of antithrombin III. Polysaccharides 102-116 serpin family C member 1 Homo sapiens 288-304 2271570-2 1990 The interaction between ATIII and thrombin is enhanced several thousandfold by the glycosaminoglycan, heparin. Heparin 102-109 serpin family C member 1 Homo sapiens 24-29 1962908-3 1990 The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction. Heparin 20-27 serpin family C member 1 Homo sapiens 231-237 1962908-3 1990 The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction. Heparin 103-110 serpin family C member 1 Homo sapiens 231-237 1962908-4 1990 Smaller molecules (18 or more monosaccharide units in length) are required to catalyze the thrombin-AT III reaction. Monosaccharides 30-44 serpin family C member 1 Homo sapiens 100-106 1962908-6 1990 The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II. pentasaccharide 28-43 serpin family C member 1 Homo sapiens 13-19 2271570-3 1990 We have previously proposed that the heparin binding site of ATIII resides within a region extending from amino acid residues 114-156 [Smith, J. W., & Knauer, D. J. Heparin 37-44 serpin family C member 1 Homo sapiens 61-66 2271570-9 1990 Affinity-purified IgG from these antisera, as well as monovalent Fab"s derived from them, specifically blocked the binding of heparin to ATIII. Heparin 126-133 serpin family C member 1 Homo sapiens 137-142 1962908-6 1990 The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II. 3-o 55-58 serpin family C member 1 Homo sapiens 13-19 2271570-10 1990 Additionally, occupancy of the heparin binding site by these same monovalent and bivalent IgG"s at least partially substituted for heparin, accelerating linkage formation between ATIII and thrombin. Heparin 31-38 serpin family C member 1 Homo sapiens 179-184 2271570-10 1990 Additionally, occupancy of the heparin binding site by these same monovalent and bivalent IgG"s at least partially substituted for heparin, accelerating linkage formation between ATIII and thrombin. Heparin 131-138 serpin family C member 1 Homo sapiens 179-184 2271570-11 1990 These results provide the first immunological evidence that region 124-145 is directly involved in the binding of heparin to ATIII and that an antibody-induced conformational change within this region can mediate ATIII activation. Heparin 114-121 serpin family C member 1 Homo sapiens 125-130 2271570-11 1990 These results provide the first immunological evidence that region 124-145 is directly involved in the binding of heparin to ATIII and that an antibody-induced conformational change within this region can mediate ATIII activation. Heparin 114-121 serpin family C member 1 Homo sapiens 213-218 1962908-6 1990 The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II. Glucosamine 68-79 serpin family C member 1 Homo sapiens 13-19 2264021-5 1990 By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII. Heparin 13-20 serpin family C member 1 Homo sapiens 112-117 1962909-0 1990 Comparative studies of heparin cofactor activity toward antithrombin III and heparin cofactor II, and antithrombin III affinity between low molecular weight heparin and unfractionated heparin. Heparin 23-30 serpin family C member 1 Homo sapiens 56-68 1962909-0 1990 Comparative studies of heparin cofactor activity toward antithrombin III and heparin cofactor II, and antithrombin III affinity between low molecular weight heparin and unfractionated heparin. Heparin 23-30 serpin family C member 1 Homo sapiens 56-72 1962909-1 1990 The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system. Heparin 61-69 serpin family C member 1 Homo sapiens 96-102 1962909-1 1990 The accelerating effects of an UF heparin (Novo) and two LMW heparins (Fragmin and PK 10169) on AT III and HC II were investigated in a purified system. Dalteparin 71-78 serpin family C member 1 Homo sapiens 96-102 2264021-5 1990 By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII. Heparin 13-20 serpin family C member 1 Homo sapiens 187-192 2264021-5 1990 By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII. Heparin 148-155 serpin family C member 1 Homo sapiens 112-117 2264021-5 1990 By contrast, heparin accelerated the time-dependent inactivation rate of thrombin and the formation of thrombin-ATIII complex, which indicates that heparin accelerates the consumption of ATIII. Heparin 148-155 serpin family C member 1 Homo sapiens 187-192 2264021-0 1990 Effect of a synthetic thrombin-inhibitor MD805 on the reaction between thrombin and plasma antithrombin-III. argatroban 41-46 serpin family C member 1 Homo sapiens 91-107 2402772-5 1990 Immediately after treatment of plasma with 2-percent TNBP, the recovery of factors VIII, IX, and V and antithrombin III was 80, 90, 40, and 100 percent, respectively. tributyl phosphate 53-57 serpin family C member 1 Homo sapiens 103-119 2264021-4 1990 As a result, MD805 would serve as a protective agent for ATIII from being consumed, in addition to its potent thrombin-inhibitory activity without the aid of ATIII. argatroban 13-18 serpin family C member 1 Homo sapiens 57-62 2394749-10 1990 The predicted reactive site (P1-P1") of this J6 protein is Arg-Ser, which is the same as that of antithrombin III. Arginine 59-62 serpin family C member 1 Homo sapiens 97-113 2394749-10 1990 The predicted reactive site (P1-P1") of this J6 protein is Arg-Ser, which is the same as that of antithrombin III. Serine 63-66 serpin family C member 1 Homo sapiens 97-113 2202741-9 1990 Furthermore, specific binding of 125I-labeled antithrombin III to the endothelial cell surface was reduced to 40-60% of control by cytokines. Iodine-125 33-37 serpin family C member 1 Homo sapiens 46-62 2175954-1 1990 Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min. Epoprostenol 54-66 serpin family C member 1 Homo sapiens 0-16 2175954-1 1990 Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min. Epoprostenol 54-66 serpin family C member 1 Homo sapiens 18-23 2175954-1 1990 Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min. Epoprostenol 68-72 serpin family C member 1 Homo sapiens 0-16 2175954-1 1990 Antithrombin III (ATIII) induced a marked increase in prostacyclin (PGI2) release from cultured human umbilical vein endothelial cells (HUVEC) after incubation for more than 2 hr and the induction continued for 8 hr, while thrombin induced the increase within 10 min. Epoprostenol 68-72 serpin family C member 1 Homo sapiens 18-23 2175954-2 1990 ATIII-dependent production of PGI2 was abolished by addition of heparin, but pretreatment of HUVEC with polyclonal antibody against thrombomodulin could not prevent the PGI2 productions by ATIII and thrombin. Epoprostenol 30-34 serpin family C member 1 Homo sapiens 0-5 2175954-2 1990 ATIII-dependent production of PGI2 was abolished by addition of heparin, but pretreatment of HUVEC with polyclonal antibody against thrombomodulin could not prevent the PGI2 productions by ATIII and thrombin. Heparin 64-71 serpin family C member 1 Homo sapiens 0-5 2175954-3 1990 ATIII-dependent PGI2 production was significantly inhibited by pretreatment of HUVEC with beta-D-xylosides or heparitinase, though neither pretreatment affected thrombin-induced PGI2 production. Epoprostenol 16-20 serpin family C member 1 Homo sapiens 0-5 2175954-3 1990 ATIII-dependent PGI2 production was significantly inhibited by pretreatment of HUVEC with beta-D-xylosides or heparitinase, though neither pretreatment affected thrombin-induced PGI2 production. xylosides 90-106 serpin family C member 1 Homo sapiens 0-5 2175954-3 1990 ATIII-dependent PGI2 production was significantly inhibited by pretreatment of HUVEC with beta-D-xylosides or heparitinase, though neither pretreatment affected thrombin-induced PGI2 production. Epoprostenol 178-182 serpin family C member 1 Homo sapiens 0-5 2175954-5 1990 ATIII-dependent PGI2 production was completely abolished. Epoprostenol 16-20 serpin family C member 1 Homo sapiens 0-5 2175954-6 1990 These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production. Epoprostenol 62-66 serpin family C member 1 Homo sapiens 81-86 2175954-6 1990 These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production. Glycosaminoglycans 109-127 serpin family C member 1 Homo sapiens 81-86 2175954-6 1990 These results indicate that the mechanism of the induction of PGI2 production by ATIII involves heparin-like glycosaminoglycans on HUVEC and the stimulation of synthesis of a protein related to PGI2 production. Epoprostenol 194-198 serpin family C member 1 Homo sapiens 81-86 2175954-7 1990 The ATIII-induced PGI2 production is very different from that induced by thrombin. Epoprostenol 18-22 serpin family C member 1 Homo sapiens 4-9 2147914-2 1990 Ticlopidine and aspirin/dipyridamole, but not xanthinol nicotinate, improved platelet aggregation, reduced beta-thromboglobulin, platelet factor IV and fibrinopeptide A concentrations, and increased antithrombin III concentrations and red blood cell filterability. Ticlopidine 0-11 serpin family C member 1 Homo sapiens 199-215 2147914-2 1990 Ticlopidine and aspirin/dipyridamole, but not xanthinol nicotinate, improved platelet aggregation, reduced beta-thromboglobulin, platelet factor IV and fibrinopeptide A concentrations, and increased antithrombin III concentrations and red blood cell filterability. Aspirin 16-23 serpin family C member 1 Homo sapiens 199-215 2147914-2 1990 Ticlopidine and aspirin/dipyridamole, but not xanthinol nicotinate, improved platelet aggregation, reduced beta-thromboglobulin, platelet factor IV and fibrinopeptide A concentrations, and increased antithrombin III concentrations and red blood cell filterability. Dipyridamole 24-36 serpin family C member 1 Homo sapiens 199-215 2246830-4 1990 In recent reports, pregnant women with hereditary AT-III deficiency had been treated with heparin or warfarin except for during abortion and delivery, in which time AT-III concentrate was widely utilized. Heparin 90-97 serpin family C member 1 Homo sapiens 50-56 2246830-4 1990 In recent reports, pregnant women with hereditary AT-III deficiency had been treated with heparin or warfarin except for during abortion and delivery, in which time AT-III concentrate was widely utilized. Warfarin 101-109 serpin family C member 1 Homo sapiens 50-56 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 76-79 serpin family C member 1 Homo sapiens 57-63 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 76-79 serpin family C member 1 Homo sapiens 57-63 2390061-0 1990 Re-formation of disulphide bonds in reduced antithrombin III. disulphide 16-26 serpin family C member 1 Homo sapiens 44-60 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Heparin 178-185 serpin family C member 1 Homo sapiens 57-63 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. disulphide 47-57 serpin family C member 1 Homo sapiens 6-22 2165828-9 1990 The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL). pentasaccharide heparin 14-37 serpin family C member 1 Homo sapiens 85-101 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. disulphide 47-57 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 68-71 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 68-71 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2126464-4 1990 The biological activity of antithrombin III is mediated by a polysaccharide, heparin. Polysaccharides 61-75 serpin family C member 1 Homo sapiens 27-43 2126464-4 1990 The biological activity of antithrombin III is mediated by a polysaccharide, heparin. Heparin 77-84 serpin family C member 1 Homo sapiens 27-43 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2165828-9 1990 The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL). Heparin 30-37 serpin family C member 1 Homo sapiens 85-101 2207233-3 1990 Amongst these antithrombogenic surfaces, this study demonstrates that some insoluble amino acid sulphamide derivatives of polystyrene strongly potentiate heparin cofactor II, in addition to antithrombin III. amino acid sulphamide 85-106 serpin family C member 1 Homo sapiens 190-206 2207233-3 1990 Amongst these antithrombogenic surfaces, this study demonstrates that some insoluble amino acid sulphamide derivatives of polystyrene strongly potentiate heparin cofactor II, in addition to antithrombin III. Polystyrenes 122-133 serpin family C member 1 Homo sapiens 190-206 2165828-9 1990 The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL). Heparin 52-59 serpin family C member 1 Homo sapiens 85-101 2165828-9 1990 The synthetic pentasaccharide heparin, the smallest heparin chain capable of binding antithrombin III, stimulated the inhibition of in situ generated factor IXa, but sevenfold less than unfractionated heparin (k = 0.76 min-1 per microgram pentasaccharide/mL). pentasaccharide 14-29 serpin family C member 1 Homo sapiens 85-101 1700488-2 1990 Heparin enhanced the reaction of antithrombin III (AT) with plasmin (up to 40-fold with 20 units/ml). Heparin 0-7 serpin family C member 1 Homo sapiens 33-49 2207233-4 1990 In contrast, an insoluble polystyrene sulphonate and, to a lesser extent, an insoluble heparin copolymer, are better catalysts of antithrombin III. polystyrene sulphonate 26-48 serpin family C member 1 Homo sapiens 130-146 2207233-4 1990 In contrast, an insoluble polystyrene sulphonate and, to a lesser extent, an insoluble heparin copolymer, are better catalysts of antithrombin III. heparin copolymer 87-104 serpin family C member 1 Homo sapiens 130-146 2384594-10 1990 These studies indicate that (a) clot-bound thrombin is relatively protected from inhibition by heparin, possibly because the heparin binding site on thrombin is inaccessible when the enzyme is bound to fibrin, and (b) clot-bound thrombin is susceptible to inactivation by antithrombin III-independent inhibitors because the sites of their interaction are not masked by thrombin binding to fibrin. Heparin 95-102 serpin family C member 1 Homo sapiens 272-288 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Cysteine 74-77 serpin family C member 1 Homo sapiens 24-30 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Heparin 191-198 serpin family C member 1 Homo sapiens 6-22 2390061-1 1990 Human antithrombin III (AT-III) contains three disulphide linkages (Cys-8-Cys-128, Cys-21-Cys-95 and Cys-247-Cys-430), and two of them (Cys-8-Cys-128 and Cys-21-Cys-95) are situated near the heparin-binding domain of the inhibitor. Heparin 191-198 serpin family C member 1 Homo sapiens 24-30 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 70-73 serpin family C member 1 Homo sapiens 57-63 2390061-2 1990 We demonstrate in this paper that: (i) partially reduced AT-III (with Cys-8-Cys-128 and Cys-21-Cys-95 quantitatively reduced) could be re-oxidized in air to regain 70-80% of its heparin cofactor activity and thrombin-inhibitory activity; (ii) completely reduced AT-III was re-oxidized under similar conditions and recovered 30-35% of it biological activities. Cysteine 76-79 serpin family C member 1 Homo sapiens 57-63 2394942-0 1990 The importance of anti-factor Xa and antithrombin activities of low molecular weight heparins. Heparin 85-93 serpin family C member 1 Homo sapiens 37-49 2237824-3 1990 This paper reports on the effect of a series of high-affinity heparin fractions with decreasing affinity for ATIII. Heparin 62-69 serpin family C member 1 Homo sapiens 109-114 2237824-4 1990 As affinity decreased, the ability of the heparin fractions to increase the rate of the ATIII-thrombin reactions decreased, and these fractions slightly more effectively increased the rate of thrombin inhibition by the higher-affinity ATIII isoform. Heparin 42-49 serpin family C member 1 Homo sapiens 88-93 2237824-4 1990 As affinity decreased, the ability of the heparin fractions to increase the rate of the ATIII-thrombin reactions decreased, and these fractions slightly more effectively increased the rate of thrombin inhibition by the higher-affinity ATIII isoform. Heparin 42-49 serpin family C member 1 Homo sapiens 235-240 2237824-5 1990 The effect of the heparin fractions on the ATIII-factor Xa reactions was also investigated. Heparin 18-25 serpin family C member 1 Homo sapiens 43-48 2237824-7 1990 Studies on the competition of isoforms for immobilized heparin showed that the isoform with higher affinity for ATIII effectively competes with its congener for binding to heparin. Heparin 55-62 serpin family C member 1 Homo sapiens 112-117 2173168-6 1990 Antithrombin III levels were significantly higher at the end of the observation period in the LMW heparin group (p less than 0.005). Heparin, Low-Molecular-Weight 94-105 serpin family C member 1 Homo sapiens 0-16 2237824-0 1990 Ability of high-affinity heparin fractions with decreasing affinity for antithrombin III to activate ATIII isoforms. Heparin 25-32 serpin family C member 1 Homo sapiens 72-88 2237824-0 1990 Ability of high-affinity heparin fractions with decreasing affinity for antithrombin III to activate ATIII isoforms. Heparin 25-32 serpin family C member 1 Homo sapiens 101-106 2237824-1 1990 Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin. Heparin 44-51 serpin family C member 1 Homo sapiens 121-137 2237824-1 1990 Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin. Heparin 44-51 serpin family C member 1 Homo sapiens 139-144 2237824-1 1990 Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin. Heparin 181-188 serpin family C member 1 Homo sapiens 121-137 2237824-1 1990 Previous studies investigated the effect of heparin fractions on the rates of thrombin inhibition by naturally occurring antithrombin III (ATIII) isoforms differing in affinity for heparin. Heparin 181-188 serpin family C member 1 Homo sapiens 139-144 2237824-2 1990 Heparin with low-affinity for ATIII increased the rate of thrombin inhibition by the higher affinity isoform about 10-fold more effectively than by the other isoform. Heparin 0-7 serpin family C member 1 Homo sapiens 30-35 1973278-0 1990 The confirmation of preclinical familial antithrombin deficiency using polymorphism and specific oligonucleotide probes . Oligonucleotides 97-112 serpin family C member 1 Homo sapiens 41-53 2237157-4 1990 However, pregnancy may be envisaged without risk since there has been an improvement in knowledge concerning the physiology of the AT III molecule, its exact role in coagulation, the application of accurate laboratory tests which measure the deficiency, and especially the programming of pregnancy under cover of preventive treatment consisting of the perfusion of AT III concentrate in association with heparin. Heparin 404-411 serpin family C member 1 Homo sapiens 131-137 2237824-7 1990 Studies on the competition of isoforms for immobilized heparin showed that the isoform with higher affinity for ATIII effectively competes with its congener for binding to heparin. Heparin 172-179 serpin family C member 1 Homo sapiens 112-117 2237824-8 1990 The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions. Heparin 57-64 serpin family C member 1 Homo sapiens 106-111 2237824-8 1990 The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions. Heparin 57-64 serpin family C member 1 Homo sapiens 191-196 2237824-8 1990 The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions. Heparin 169-176 serpin family C member 1 Homo sapiens 106-111 2237824-8 1990 The results indicate that heterogeneity in high-affinity heparin results in heterogeneity in affinity for ATIII that is significantly correlated with the ability of the heparin to potentiate ATIII-protease reactions. Heparin 169-176 serpin family C member 1 Homo sapiens 191-196 2237824-9 1990 In spite of about equal activation of the ATIII isoforms by high-affinity heparin, the importance of the higher-affinity isoform is indicated by its ability to compete effectively for these heparin species. Heparin 74-81 serpin family C member 1 Homo sapiens 42-47 2115298-9 1990 Antithrombin III decreased in the gestodene group but was unchanged in levonorgestrel-treated women. Gestodene 34-43 serpin family C member 1 Homo sapiens 0-16 2176902-3 1990 The mechanism by which such high affinity heparin acts when antithrombin III is the inhibitor is promotion of the formation of an intermediate proteinase-heparin-antithrombin complex. Heparin 42-49 serpin family C member 1 Homo sapiens 60-76 2176902-6 1990 Binding of heparin to both thrombin and antithrombin III interferes with thrombin inactivation. Heparin 11-18 serpin family C member 1 Homo sapiens 40-56 2176902-8 1990 Low ionic strength in in vitro reactions also results in cleavage of antithrombin III by thrombin in the presence of heparin and effectively converts antithrombin III from an inhibitor to a substrate. Heparin 117-124 serpin family C member 1 Homo sapiens 69-85 2121564-2 1990 Cyclandelate induced a reduction in euglobulin lysis time, an increase in tissue plasminogen activator concentration and a reduction in plasminogen activator inhibitor, alpha 2-antiplasmin and immunological fibrinogen concentrations, but no changes in antithrombin III and plasminogen concentrations were observed. Cyclandelate 0-12 serpin family C member 1 Homo sapiens 252-268 2365065-2 1990 A variant antithrombin with reduced heparin affinity was shown by mass spectrometry sequencing and DNA amplification to have a substitution of a cysteine for an arginine at residue 24. Heparin 36-43 serpin family C member 1 Homo sapiens 10-22 2169656-3 1990 In contrast, antithrombin III decreased progressively 25% during 5 days of heparin treatment. Heparin 75-82 serpin family C member 1 Homo sapiens 13-29 2142236-6 1990 These hormonal changes including the increase of SHBG at the dose levels of 220-680 mg and the decrease of antithrombin III (220-680 mg) may be attributed to a weak estrogen-like effect of toremifene. Toremifene 189-199 serpin family C member 1 Homo sapiens 107-123 2112878-0 1990 Intravenous nitroglycerin-induced heparin resistance: a qualitative antithrombin III abnormality. Nitroglycerin 12-25 serpin family C member 1 Homo sapiens 68-84 2112878-0 1990 Intravenous nitroglycerin-induced heparin resistance: a qualitative antithrombin III abnormality. Heparin 34-41 serpin family C member 1 Homo sapiens 68-84 2112878-10 1990 A nitroglycerin-induced qualitative ATIII abnormality may be the underlying mechanism. Nitroglycerin 2-15 serpin family C member 1 Homo sapiens 36-41 2372510-3 1990 The abnormal AT III was purified from the propositus" plasma, taking advantage of the difference in NaCl concentrations required to elute variant and normal AT III from heparin-Sepharose. Sodium Chloride 100-104 serpin family C member 1 Homo sapiens 13-19 2372510-3 1990 The abnormal AT III was purified from the propositus" plasma, taking advantage of the difference in NaCl concentrations required to elute variant and normal AT III from heparin-Sepharose. Heparin 169-176 serpin family C member 1 Homo sapiens 13-19 2372510-3 1990 The abnormal AT III was purified from the propositus" plasma, taking advantage of the difference in NaCl concentrations required to elute variant and normal AT III from heparin-Sepharose. Sepharose 177-186 serpin family C member 1 Homo sapiens 13-19 2372510-7 1990 The quantification of heparin AT III interaction with both normal and variant purified proteins in a double reciprocal plot yielded similar dissociation constants but a 9-fold decrease in the maximal pseudo-first order constant. Heparin 22-29 serpin family C member 1 Homo sapiens 30-36 2214165-2 1990 Commercially available AT III concentrates showed heterogeneity on agarose gel isoelectric focusing, however, they inhibited thrombin in the same manner. Sepharose 67-74 serpin family C member 1 Homo sapiens 23-29 2191783-14 1990 In a randomized, placebo-controlled double-blinded study, we will determine whether simultaneous administration of warfarin with heparin initiation provides more time to increase antithrombin III levels and prevent coronary reocclusion upon heparin discontinuance, compared to heparin without warfarin therapy. Warfarin 115-123 serpin family C member 1 Homo sapiens 179-195 2191783-14 1990 In a randomized, placebo-controlled double-blinded study, we will determine whether simultaneous administration of warfarin with heparin initiation provides more time to increase antithrombin III levels and prevent coronary reocclusion upon heparin discontinuance, compared to heparin without warfarin therapy. Heparin 129-136 serpin family C member 1 Homo sapiens 179-195 2353343-3 1990 The nonspecific interaction of thrombin with calcium ions prolonged fibrinogen-clotting and neutralization by antithrombin III (AT III) in the absence of heparin. Calcium 45-52 serpin family C member 1 Homo sapiens 110-126 2164263-3 1990 Using this assay we have estimated the relative potency of the following glycosaminoglycans: heparin; a fraction of heparin with high affinity for antithrombin III (high affinity heparin); the low molecular weight heparin Fragmin; the low molecular weight heparinoid Org 10172; a fraction of Org 10172 with high affinity for antithrombin III (high affinity Org 10172) and the O-methyl derivative of the pentasaccharide, representing the minimal structure required for binding to antithrombin III. Heparin 116-123 serpin family C member 1 Homo sapiens 147-163 2164263-7 1990 With the pentasaccharide a striking saturation of the inhibition is observed, due to saturation of the antithrombin III. pentasaccharide 9-24 serpin family C member 1 Homo sapiens 103-119 2353343-3 1990 The nonspecific interaction of thrombin with calcium ions prolonged fibrinogen-clotting and neutralization by antithrombin III (AT III) in the absence of heparin. Calcium 45-52 serpin family C member 1 Homo sapiens 128-134 2363123-4 1990 The abnormal AT III was characterized in plasma by the discrepancy between a normal progressive activity and a reduced heparin cofactor activity. Heparin 119-126 serpin family C member 1 Homo sapiens 13-19 2160076-7 1990 Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins. Serine 25-28 serpin family C member 1 Homo sapiens 135-151 2160076-7 1990 Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins. Serine 25-28 serpin family C member 1 Homo sapiens 153-159 2160076-7 1990 Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins. Tyrosine 77-80 serpin family C member 1 Homo sapiens 135-151 2160076-7 1990 Binding of peptide 105Y (Ser-Ile-Pro-Pro-Glu-Val-Lys-Phe-Asn-Lys-Pro-Phe-Val-Tyr-Leu-Ile) is blocked by alpha 1-AT-elastase complexes, antithrombin III (AT III)-thrombin complexes, alpha 1-antichymotrypsin (alpha 1-ACT)-cathepsin G complexes, and, to a lesser extent, complement component C1 inhibitor-C1s complexes, but not by the corresponding native proteins. Tyrosine 77-80 serpin family C member 1 Homo sapiens 153-159 2194315-2 1990 To define the molecular basis for the variant AT III, we used a combination of genomic amplification followed by cloning, sequencing, and hybridization with allele-specific oligonucleotide probes. Oligonucleotides 173-188 serpin family C member 1 Homo sapiens 46-52 2194315-3 1990 We obtained evidence for a cytosine to thymine transition in exon 2 (codon 47) of the AT III gene in the proband. Cytosine 27-35 serpin family C member 1 Homo sapiens 86-92 2194315-3 1990 We obtained evidence for a cytosine to thymine transition in exon 2 (codon 47) of the AT III gene in the proband. Thymine 39-46 serpin family C member 1 Homo sapiens 86-92 2363123-5 1990 This variant AT III was purified, separated from the normal protein by heparin-Sepharose chromatography and was eluted with increased NaCl concentrations. Heparin 71-78 serpin family C member 1 Homo sapiens 13-19 2363123-5 1990 This variant AT III was purified, separated from the normal protein by heparin-Sepharose chromatography and was eluted with increased NaCl concentrations. Sepharose 79-88 serpin family C member 1 Homo sapiens 13-19 2363123-5 1990 This variant AT III was purified, separated from the normal protein by heparin-Sepharose chromatography and was eluted with increased NaCl concentrations. Sodium Chloride 134-138 serpin family C member 1 Homo sapiens 13-19 2363123-6 1990 At pH 7.4, the variant AT III eluted at lower (0.3 to 0.5 M) NaCl concentrations than normal (1 to 1.5 M) AT III, thus demonstrating a decreased affinity for heparin. Sodium Chloride 61-65 serpin family C member 1 Homo sapiens 23-29 2363123-6 1990 At pH 7.4, the variant AT III eluted at lower (0.3 to 0.5 M) NaCl concentrations than normal (1 to 1.5 M) AT III, thus demonstrating a decreased affinity for heparin. Heparin 158-165 serpin family C member 1 Homo sapiens 23-29 2363123-7 1990 At pH 6.0, however, the abnormal molecule bound more avidly to heparin-Sepharose and was eluted like normal AT III at pH 7.4. Heparin 63-70 serpin family C member 1 Homo sapiens 108-114 2363123-8 1990 Similarly, the heparin enhancement of intrinsic fluorescence of the variant AT III, markedly reduced at pH 7.4, was normalized at pH 6.0. Heparin 15-22 serpin family C member 1 Homo sapiens 76-82 2363123-9 1990 The abnormal AT III showed a normal antiprotease activity, a normal molecular weight by SDS-PAGE, but displayed only a partial immunological identity with the normal protein. Sodium Dodecyl Sulfate 88-91 serpin family C member 1 Homo sapiens 13-19 2106684-6 1990 Both fractions of heparin effectively accelerate inactivation of thrombin by antithrombin III. Heparin 18-25 serpin family C member 1 Homo sapiens 77-93 2197226-7 1990 In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin dose required might cause an unacceptable bleeding risk, e.g. in simultaneous thrombocytopenia. Heparin 122-129 serpin family C member 1 Homo sapiens 46-62 2197226-7 1990 In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin dose required might cause an unacceptable bleeding risk, e.g. in simultaneous thrombocytopenia. Heparin 191-198 serpin family C member 1 Homo sapiens 21-33 2197226-7 1990 In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin dose required might cause an unacceptable bleeding risk, e.g. in simultaneous thrombocytopenia. Heparin 191-198 serpin family C member 1 Homo sapiens 46-62 2358716-3 1990 1) After chemotherapy, the levels of fibrinogen were increased, ATIII was decreased significantly in cases in the NC.PD group compared with the PR.CR group (p less than 0.05). Palladium 117-119 serpin family C member 1 Homo sapiens 64-69 2196192-0 1990 Low molecular weight heparin restores antithrombin III activity from hyperglycemia induced alterations. Heparin 21-28 serpin family C member 1 Homo sapiens 38-54 2196192-2 1990 In this study the ability of a low molecular weight heparin (LMWH) (Fluxum, Alfa-Wassermann S.p.A., Bologna, Italy), as well as unfractioned heparin, to preserve ATIII activity from glucose-induced alterations, both in vitro and in vivo, is reported. Heparin 52-59 serpin family C member 1 Homo sapiens 162-167 2196192-2 1990 In this study the ability of a low molecular weight heparin (LMWH) (Fluxum, Alfa-Wassermann S.p.A., Bologna, Italy), as well as unfractioned heparin, to preserve ATIII activity from glucose-induced alterations, both in vitro and in vivo, is reported. Heparin, Low-Molecular-Weight 61-65 serpin family C member 1 Homo sapiens 162-167 2196192-2 1990 In this study the ability of a low molecular weight heparin (LMWH) (Fluxum, Alfa-Wassermann S.p.A., Bologna, Italy), as well as unfractioned heparin, to preserve ATIII activity from glucose-induced alterations, both in vitro and in vivo, is reported. Heparin 141-148 serpin family C member 1 Homo sapiens 162-167 2196192-3 1990 The subcutaneous and intravenous LMWH and heparin administration increases basal depressed ATIII activity in diabetic patients. Heparin, Low-Molecular-Weight 33-37 serpin family C member 1 Homo sapiens 91-96 2196192-3 1990 The subcutaneous and intravenous LMWH and heparin administration increases basal depressed ATIII activity in diabetic patients. Heparin 42-49 serpin family C member 1 Homo sapiens 91-96 2196192-4 1990 Heparin shows an equivalent effect on both anti-IIa and anti-Xa activity of ATIII, while LMWH is more effective in preserving the anti-Xa activity. Heparin 0-7 serpin family C member 1 Homo sapiens 76-81 2191809-2 1990 The anticoagulant agent heparin inhibits thrombosis by interacting with antithrombin III. Heparin 24-31 serpin family C member 1 Homo sapiens 72-88 1690736-0 1990 Hydrophobic residues 382-386 of antithrombin III, Ala-Ala-Ala-Ser-Thr, serve as the epitope for an antibody which facilitates hydrolysis of the inhibitor by thrombin. Ala-Ala-Ala-Ser-Thr 50-69 serpin family C member 1 Homo sapiens 32-48 1690736-5 1990 By analyzing a CNBr fragment of the thrombin-antithrombin III complex that reacts with the antibody we localized the epitope for the antibody to a strongly hydrophobic residue 382-386 peptide segment, Ala-Ala-Ala-Ser-Thr, of the inhibitor, which is also contiguous with a hydrophobic amino acid Ala at its carboxyl terminus. Alanine 201-204 serpin family C member 1 Homo sapiens 45-61 2405068-0 1990 Novel sulfated polysaccharides: dissociation of anti-human immunodeficiency virus activity from antithrombin activity. Polysaccharides 15-30 serpin family C member 1 Homo sapiens 96-108 2339364-0 1990 Phosphotungstate as a useful eluent for antithrombin III purification by heparin-agarose affinity chromatography. phosphotungstate 0-16 serpin family C member 1 Homo sapiens 40-56 2339364-0 1990 Phosphotungstate as a useful eluent for antithrombin III purification by heparin-agarose affinity chromatography. Heparin 73-80 serpin family C member 1 Homo sapiens 40-56 2339364-0 1990 Phosphotungstate as a useful eluent for antithrombin III purification by heparin-agarose affinity chromatography. Sepharose 81-88 serpin family C member 1 Homo sapiens 40-56 2339364-2 1990 In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography. pta 41-44 serpin family C member 1 Homo sapiens 71-87 2339364-2 1990 In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography. pta 41-44 serpin family C member 1 Homo sapiens 89-94 2339364-2 1990 In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography. Heparin 99-106 serpin family C member 1 Homo sapiens 71-87 2339364-2 1990 In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography. Heparin 99-106 serpin family C member 1 Homo sapiens 89-94 2339364-2 1990 In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography. Sepharose 107-116 serpin family C member 1 Homo sapiens 71-87 2339364-2 1990 In the present paper, we studied whether PTA is useful as an eluent of antithrombin III (ATIII) on heparin-Sepharose affinity chromatography. Sepharose 107-116 serpin family C member 1 Homo sapiens 89-94 2339364-3 1990 Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M. Heparin 28-35 serpin family C member 1 Homo sapiens 6-11 2339364-3 1990 Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M. Sepharose 36-45 serpin family C member 1 Homo sapiens 6-11 2339364-3 1990 Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M. Sodium Chloride 66-70 serpin family C member 1 Homo sapiens 6-11 2339364-3 1990 Human ATIII adsorbed on the heparin-Sepharose gel was eluted with NaCl buffer at the NaCl level of 1M. Sodium Chloride 85-89 serpin family C member 1 Homo sapiens 6-11 2339367-3 1990 The AT-III deficient plasma is prepared by passage of plasma through a heparin-agarose column. Heparin 71-78 serpin family C member 1 Homo sapiens 4-10 2339367-3 1990 The AT-III deficient plasma is prepared by passage of plasma through a heparin-agarose column. Sepharose 79-86 serpin family C member 1 Homo sapiens 4-10 2339367-4 1990 In the presence of heparin, AT-III in the sample shows concentration dependent anticoagulant activity and calibration curve is linear on semi-logarithmic graph paper. Heparin 19-26 serpin family C member 1 Homo sapiens 28-34 2405068-5 1990 These results indicate that the anti-HIV activity of sulfated polysaccharides can be dissociated from their antithrombin activity. Polysaccharides 62-77 serpin family C member 1 Homo sapiens 108-120 2294104-9 1990 This effect of heparin is also independent of whether it has high or low affinity for antithrombin III. Heparin 15-22 serpin family C member 1 Homo sapiens 86-102 2315891-0 1990 Influence of chemical modification of tryptophan residues on the properties of human antithrombin III. Tryptophan 38-48 serpin family C member 1 Homo sapiens 85-101 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. Tryptophan 72-82 serpin family C member 1 Homo sapiens 95-111 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. Tryptophan 72-82 serpin family C member 1 Homo sapiens 306-322 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium 115-167 serpin family C member 1 Homo sapiens 95-111 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. 2-hydroxy-5-nitrobenzyl 255-278 serpin family C member 1 Homo sapiens 95-111 2315891-1 1990 According to the reaction conditions selected, chemical modification of tryptophan residues in antithrombin III by dimethyl (2-hydroxy-5 nitrobenzyl) sulfonium bromide (HNBSB) generated products with similar levels of modification (equivalent to 0.9 mole 2-hydroxy-5-nitrobenzyl (HNB) incorporated/mole of antithrombin III) but with high or low affinity for heparin. Heparin 358-365 serpin family C member 1 Homo sapiens 95-111 2315891-5 1990 A recovery of heparin cofactor activity towards coagulation factor Xa was observed upon prolonged storage of low affinity forms at -70 degrees C. It is considered that the loss of high affinity for heparin upon modification of antithrombin III arises from change or stabilization of conformation associated with tryptophan modification and is not a singular property of modification of Trp 49. Heparin 14-21 serpin family C member 1 Homo sapiens 227-243 2315891-5 1990 A recovery of heparin cofactor activity towards coagulation factor Xa was observed upon prolonged storage of low affinity forms at -70 degrees C. It is considered that the loss of high affinity for heparin upon modification of antithrombin III arises from change or stabilization of conformation associated with tryptophan modification and is not a singular property of modification of Trp 49. Tryptophan 312-322 serpin family C member 1 Homo sapiens 227-243 2315891-5 1990 A recovery of heparin cofactor activity towards coagulation factor Xa was observed upon prolonged storage of low affinity forms at -70 degrees C. It is considered that the loss of high affinity for heparin upon modification of antithrombin III arises from change or stabilization of conformation associated with tryptophan modification and is not a singular property of modification of Trp 49. Tryptophan 386-389 serpin family C member 1 Homo sapiens 227-243 2315894-1 1990 Heparin with low affinity for antithrombin III (ATIII) and devoid of anticoagulant activity was chemically oversulfated and fractionated by affinity for ATIII. Heparin 0-7 serpin family C member 1 Homo sapiens 30-46 2315894-1 1990 Heparin with low affinity for antithrombin III (ATIII) and devoid of anticoagulant activity was chemically oversulfated and fractionated by affinity for ATIII. Heparin 0-7 serpin family C member 1 Homo sapiens 48-53 2315894-1 1990 Heparin with low affinity for antithrombin III (ATIII) and devoid of anticoagulant activity was chemically oversulfated and fractionated by affinity for ATIII. Heparin 0-7 serpin family C member 1 Homo sapiens 153-158 2315894-3 1990 The fluorescence increase was comparable to that of the AT III high affinity fraction of native heparin. Heparin 96-103 serpin family C member 1 Homo sapiens 56-62 2315894-5 1990 The high affinity fractions of native heparin and the sulfated material were almost equally effective in enhancing the rate of thrombin neutralization by ATIII. Heparin 38-45 serpin family C member 1 Homo sapiens 154-159 2331700-0 1990 Conformation of the pentasaccharide corresponding to the binding site of heparin for antithrombin III. pentasaccharide 20-35 serpin family C member 1 Homo sapiens 85-101 2331700-1 1990 The conformation in solution of the pentasaccharide methyl glycoside (As-G-A*-Is-AM; 1), which represents the binding site of heparin for Antithrombin III, has been investigated using molecular mechanics and 1H-n.m.r. pentasaccharide 36-51 serpin family C member 1 Homo sapiens 138-154 2331700-1 1990 The conformation in solution of the pentasaccharide methyl glycoside (As-G-A*-Is-AM; 1), which represents the binding site of heparin for Antithrombin III, has been investigated using molecular mechanics and 1H-n.m.r. Methylglycosides 52-68 serpin family C member 1 Homo sapiens 138-154 2331700-1 1990 The conformation in solution of the pentasaccharide methyl glycoside (As-G-A*-Is-AM; 1), which represents the binding site of heparin for Antithrombin III, has been investigated using molecular mechanics and 1H-n.m.r. as-g-a 70-76 serpin family C member 1 Homo sapiens 138-154 2331700-1 1990 The conformation in solution of the pentasaccharide methyl glycoside (As-G-A*-Is-AM; 1), which represents the binding site of heparin for Antithrombin III, has been investigated using molecular mechanics and 1H-n.m.r. Heparin 126-133 serpin family C member 1 Homo sapiens 138-154 2154054-5 1990 Instead, we now use gabexate mesilate, which blocks the coagulation cascade without the aid of antithrombin III and works as an anticoagulant. Gabexate 20-37 serpin family C member 1 Homo sapiens 95-111 1963017-2 1990 In the intrinsic system, unfractionated heparin does have an indirect antiprothrombinase action because its antithrombin activity inhibits the feedback activation of Factor VIII. Heparin 40-47 serpin family C member 1 Homo sapiens 108-120 2322419-4 1990 Thus, the slow reactions in the case of bovine and pig HA-heparins were probably due to preferential binding of the two HA-heparins to thrombin rather than to ATIII, thus causing the HA-heparins to be inhibitory for the reaction by reducing the turnover rates of the polysaccharides as catalysts. Heparin 58-66 serpin family C member 1 Homo sapiens 159-164 1963018-1 1990 When measured in terms of biological activities (using only markers of molecules with affinity for antithrombin III), the pharmacokinetics of low molecular weight heparins are clearly different from those of unfractionated heparin after intravenous and subcutaneous injections. Heparin 163-171 serpin family C member 1 Homo sapiens 99-115 1963018-1 1990 When measured in terms of biological activities (using only markers of molecules with affinity for antithrombin III), the pharmacokinetics of low molecular weight heparins are clearly different from those of unfractionated heparin after intravenous and subcutaneous injections. Heparin 163-170 serpin family C member 1 Homo sapiens 99-115 1688695-7 1990 Third, based on the knowledge that tryptase stability is regulated by its interaction with heparin, antithrombin III was used as a model heparin-binding protein to demonstrate that a protein competitor for heparin-binding sites, presumably by displacement of tryptase, destabilizes this enzyme. Heparin 91-98 serpin family C member 1 Homo sapiens 100-116 1688695-7 1990 Third, based on the knowledge that tryptase stability is regulated by its interaction with heparin, antithrombin III was used as a model heparin-binding protein to demonstrate that a protein competitor for heparin-binding sites, presumably by displacement of tryptase, destabilizes this enzyme. Heparin 137-144 serpin family C member 1 Homo sapiens 100-116 1688695-8 1990 Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III. Heparin 76-83 serpin family C member 1 Homo sapiens 56-72 1688695-8 1990 Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III. Heparin 76-83 serpin family C member 1 Homo sapiens 152-168 1688695-8 1990 Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III. Heparin 109-116 serpin family C member 1 Homo sapiens 56-72 1688695-8 1990 Conversely, tryptase, in excess, blocked the binding of antithrombin III to heparin, thereby attenuating the heparin-mediated inhibition of thrombin by antithrombin III. Heparin 109-116 serpin family C member 1 Homo sapiens 152-168 2322419-6 1990 Since the strength of the interactions of these HA-heparins with thrombin was in the order, pig greater than or equal to bovine greater than whale, the faster reactions were probably due to higher associations of the enzyme with the essential HA-heparin-ATIII complex. Heparin 51-59 serpin family C member 1 Homo sapiens 254-259 1697824-9 1990 The present results indicate that low-dose heparin treatment modulates the plasmatic fluctuation of TAT complex as well as factor X, AT III and protein C levels in patients with acute myocardial infarction. Heparin 43-50 serpin family C member 1 Homo sapiens 133-139 2083865-8 1990 The activities of thrombin and other serine proteases are modulated by the serine protease inhibitors (serpins), including antithrombin III and heparin cofactor II which are important in regulating the physiological anticoagulant action of glycosaminoglycans at the endothelium and the pharmacological action of heparin. Glycosaminoglycans 240-258 serpin family C member 1 Homo sapiens 123-139 1697824-7 1990 Moreover, heparin administration was connected with significantly higher levels of AT III and protein C along with a lower concentration of factor X and FDP on the seventh day of the disease. Heparin 10-17 serpin family C member 1 Homo sapiens 83-89 2083874-4 1990 The active site for antithrombin is a specific pentasaccharide sequence containing 3-O-sulfated D-glucosamine. pentasaccharide 47-62 serpin family C member 1 Homo sapiens 20-32 2083874-4 1990 The active site for antithrombin is a specific pentasaccharide sequence containing 3-O-sulfated D-glucosamine. Glucosamine 96-109 serpin family C member 1 Homo sapiens 20-32 2275918-3 1990 Polymers substituted with aryl sulfonate and carboxyl groups specifically interact with antithrombin III and serine-proteases involved in the coagulation of blood. Polymers 0-8 serpin family C member 1 Homo sapiens 88-104 2275918-3 1990 Polymers substituted with aryl sulfonate and carboxyl groups specifically interact with antithrombin III and serine-proteases involved in the coagulation of blood. Arylsulfonates 26-40 serpin family C member 1 Homo sapiens 88-104 1705601-0 1990 [A photometric method of determining the activity of antithrombin III using a peptide coumarylamide substrate]. coumarylamide 86-99 serpin family C member 1 Homo sapiens 53-69 2313207-2 1990 Danazol (an attenuated synthetic androgen) already shown to be capable of compensating for a lack of certain antiproteases, was given in doses of 200 mg 3 times per day for 10 days, resulting in a rapid rise (mean 21.2%) in antithrombin III values. Danazol 0-7 serpin family C member 1 Homo sapiens 224-240 1710698-3 1990 Heparin content in U/ml is determined from the difference in the activities of heparin--AT-III complex and AT-III proper activity represented on the calibration curve. Heparin 79-86 serpin family C member 1 Homo sapiens 88-94 2298818-10 1990 The plasma thrombin inhibitor, antithrombin III, stimulated neurite outgrowth but only when its thrombin inhibitory activity was accelerated by heparin. Heparin 144-151 serpin family C member 1 Homo sapiens 31-47 1705601-1 1990 Toz-Gly-Pro-Arg-4-methylcoumaryl-7-amide is recommended for antithrombin-III (AT-III) photometry as a substrate. toz-gly-pro-arg-4-methylcoumaryl-7-amide 0-40 serpin family C member 1 Homo sapiens 60-76 1705601-1 1990 Toz-Gly-Pro-Arg-4-methylcoumaryl-7-amide is recommended for antithrombin-III (AT-III) photometry as a substrate. toz-gly-pro-arg-4-methylcoumaryl-7-amide 0-40 serpin family C member 1 Homo sapiens 78-84 1710698-0 1990 [A method of determining heparin in blood plasma based on its antithrombin activity]. Heparin 25-32 serpin family C member 1 Homo sapiens 62-74 1983502-1 1990 Heparin exerts its anticoagulant function by accelerating the inhibitory effect of antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 83-99 1710698-1 1990 The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor. Heparin 48-55 serpin family C member 1 Homo sapiens 95-107 1710698-1 1990 The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor. Heparin 48-55 serpin family C member 1 Homo sapiens 120-136 1710698-1 1990 The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor. Heparin 48-55 serpin family C member 1 Homo sapiens 138-144 1710698-1 1990 The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor. Heparin 68-75 serpin family C member 1 Homo sapiens 95-107 1710698-1 1990 The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor. Heparin 68-75 serpin family C member 1 Homo sapiens 120-136 1710698-1 1990 The suggested method for measuring blood plasma heparin is based on heparin ability to enhance antithrombin activity of antithrombin III (AT-III), the major Xa and thrombin inhibitor. Heparin 68-75 serpin family C member 1 Homo sapiens 138-144 1710698-2 1990 The method consists in measurement of blood plasma AT-III activity in the presence and absence of protamine sulfate that destroys the heparin--AT-III complex. Heparin 134-141 serpin family C member 1 Homo sapiens 51-57 1710698-2 1990 The method consists in measurement of blood plasma AT-III activity in the presence and absence of protamine sulfate that destroys the heparin--AT-III complex. Heparin 134-141 serpin family C member 1 Homo sapiens 143-149 1710698-3 1990 Heparin content in U/ml is determined from the difference in the activities of heparin--AT-III complex and AT-III proper activity represented on the calibration curve. Heparin 0-7 serpin family C member 1 Homo sapiens 88-94 1710698-3 1990 Heparin content in U/ml is determined from the difference in the activities of heparin--AT-III complex and AT-III proper activity represented on the calibration curve. Heparin 0-7 serpin family C member 1 Homo sapiens 107-113 15681940-0 2005 A phase III, double-blind, placebo-controlled, multicenter study on the efficacy of recombinant human antithrombin in heparin-resistant patients scheduled to undergo cardiac surgery necessitating cardiopulmonary bypass. Heparin 118-125 serpin family C member 1 Homo sapiens 102-114 2079995-6 1990 In contrast, ATIII and Plg correlated directly with serum albumin and inversely with cholesterol and urine protein excretion. Cholesterol 85-96 serpin family C member 1 Homo sapiens 13-18 2079997-6 1990 The inhibition of fibrin formation of intraperitoneal heparin was increased by addition of AT III without a systemic inhibitory effect on fibrin formation. Heparin 54-61 serpin family C member 1 Homo sapiens 91-97 2079997-7 1990 These data suggest that intraperitoneal administration of heparin without AT III would be sufficient for the purpose of preventing fibrin formation in CAPD patients without any trouble, and additional AT III might increase inhibitory effect of heparin. Heparin 244-251 serpin family C member 1 Homo sapiens 201-207 33794550-4 2021 Tissue factor pathway inhibitor and the strongest physiological anticoagulant antithrombin are attached to the endothelial cell surface by heparan sulfate. Heparitin Sulfate 139-154 serpin family C member 1 Homo sapiens 78-90 33234593-0 2021 A quantitative method to detect non-antithrombin-binding 3-O-sulfated units in heparan sulfate. 3-o 57-60 serpin family C member 1 Homo sapiens 36-48 33234593-0 2021 A quantitative method to detect non-antithrombin-binding 3-O-sulfated units in heparan sulfate. Heparitin Sulfate 79-94 serpin family C member 1 Homo sapiens 36-48 25855774-5 2015 Notably, in the puromycin aminonucleoside model, hyperfibrinogenemia and antithrombin deficiency were also correlated with proteinuria severity, consistent with reports in human nephrotic syndrome. Puromycin Aminonucleoside 16-41 serpin family C member 1 Homo sapiens 73-85 2154059-4 1990 The intensity of ATIII activity in the presence of heparin (0.01U/ml) was also diminished by the human TM. Heparin 51-58 serpin family C member 1 Homo sapiens 17-22 2154059-5 1990 However, this ATIII- heparin cofactor activity recovered with the addition of a 10-fold amount of heparin (0.1U/ml). Heparin 21-28 serpin family C member 1 Homo sapiens 14-19 2154059-6 1990 In SDS-polyacrylamide gel electrophoresis and immunoblotting analysis, we found a complex formation of ATIII with both human and rabbit TM (and further confirmed their presence with isoelectrofocusing electrophoresis- data not shown). Sodium Dodecyl Sulfate 3-6 serpin family C member 1 Homo sapiens 103-108 2154059-6 1990 In SDS-polyacrylamide gel electrophoresis and immunoblotting analysis, we found a complex formation of ATIII with both human and rabbit TM (and further confirmed their presence with isoelectrofocusing electrophoresis- data not shown). polyacrylamide 7-21 serpin family C member 1 Homo sapiens 103-108 33822598-0 2021 Paramount Importance of Core Conformational Changes for Heparin Allosteric Activation of Antithrombin. Heparin 56-63 serpin family C member 1 Homo sapiens 89-101 33822598-1 2021 Antithrombin is unique among serpin family protein protease inhibitors with respect to the major reactive center loop (RCL) and core conformational changes that mediate allosteric activation of its anticoagulant function by heparin. Heparin 224-231 serpin family C member 1 Homo sapiens 0-12 33822598-2 2021 A critical role for expulsion of the RCL hinge from a native stabilizing interaction with the hydrophobic core in the activation mechanism has been proposed from reports that antithrombin variants that block this change through engineered disulfide bonds block activation. Disulfides 239-248 serpin family C member 1 Homo sapiens 175-187 15681940-1 2005 BACKGROUND: The study evaluated the efficacy of recombinant human antithrombin (rhAT) for restoring heparin responsiveness in heparin resistant patients undergoing cardiac surgery. Heparin 100-107 serpin family C member 1 Homo sapiens 66-78 15681940-1 2005 BACKGROUND: The study evaluated the efficacy of recombinant human antithrombin (rhAT) for restoring heparin responsiveness in heparin resistant patients undergoing cardiac surgery. Heparin 126-133 serpin family C member 1 Homo sapiens 66-78 2088576-0 1990 Location of disulfide bonds in antithrombin III. Disulfides 12-21 serpin family C member 1 Homo sapiens 31-47 2088576-1 1990 Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII. Disulfides 201-210 serpin family C member 1 Homo sapiens 29-45 2088576-1 1990 Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII. Disulfides 201-210 serpin family C member 1 Homo sapiens 47-52 2088576-1 1990 Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII. Disulfides 201-210 serpin family C member 1 Homo sapiens 278-283 2088576-1 1990 Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII. Disulfides 256-265 serpin family C member 1 Homo sapiens 29-45 2088576-1 1990 Proteolytic digests of human antithrombin III (ATIII) have been analyzed by a combination of reversed-phase high-performance liquid chromatography and fast atom bombardment (FAB) mass spectrometry for disulfide-containing peptides which are diagnostic for disulfide linkages in ATIII. Disulfides 256-265 serpin family C member 1 Homo sapiens 47-52 34939461-9 2021 Patients receiving continuous AT-III infusions spent a significantly higher percentage of ECMO time within the therapeutic range, measured using anti-Factor Xa levels (64.9+-4.2% vs. 29.1+-8.57%, p = 0.008), and required fewer changes to the heparin infusion rate (6.48+-0.88 vs 2.38+-0.36 changes/day changes/day, p = 0.005). Heparin 242-249 serpin family C member 1 Homo sapiens 30-36 34529138-8 2022 Compared with before TACE, the maximum diameter of tumor was significantly decreased after TACE; ECOG was increased at 3d after TACE, while was decreased at 28d and 90d after TACE (P < 0.05); QOL and HAMA had no significant change at 3d after TACE, while increased significantly at 28d and 90d after TACE (all P < 0.05). Chlorotrianisene 21-25 serpin family C member 1 Homo sapiens 116-121 34529138-8 2022 Compared with before TACE, the maximum diameter of tumor was significantly decreased after TACE; ECOG was increased at 3d after TACE, while was decreased at 28d and 90d after TACE (P < 0.05); QOL and HAMA had no significant change at 3d after TACE, while increased significantly at 28d and 90d after TACE (all P < 0.05). Chlorotrianisene 128-132 serpin family C member 1 Homo sapiens 116-121 34529138-8 2022 Compared with before TACE, the maximum diameter of tumor was significantly decreased after TACE; ECOG was increased at 3d after TACE, while was decreased at 28d and 90d after TACE (P < 0.05); QOL and HAMA had no significant change at 3d after TACE, while increased significantly at 28d and 90d after TACE (all P < 0.05). Chlorotrianisene 300-304 serpin family C member 1 Homo sapiens 116-121 34939461-11 2021 CONCLUSION: AT-III as a continuous infusion in CDH neonates on ECMO provides a decreased need to modify heparin infusion and more consistent therapeutic anticoagulation without increasing the risk of life-threatening bleeding. Heparin 104-111 serpin family C member 1 Homo sapiens 12-18 34927362-8 2022 The introduced N-glycans exhibited position-specific effects on the interaction with two FXa inhibitors: tissue factor pathway inhibitor (TFPI) and antithrombin (ATIII). n-glycans 15-24 serpin family C member 1 Homo sapiens 148-160 34937572-13 2021 Genetic analyses showed the same mutation causing ATD in both son and mother: heterozygote missense mutation c.248 T > C, p.(Leu83Pro), within the heparin binding domain of antithrombin. Heparin 147-154 serpin family C member 1 Homo sapiens 173-185 34927362-8 2022 The introduced N-glycans exhibited position-specific effects on the interaction with two FXa inhibitors: tissue factor pathway inhibitor (TFPI) and antithrombin (ATIII). n-glycans 15-24 serpin family C member 1 Homo sapiens 162-167 34927362-9 2022 Ki for the inhibition by full-length TFPI of these FXa variants was increased by 7- to 1150-fold, while ATIII inhibition in the presence of the heparin-analogue Fondaparinux was modestly increased by 2- to 15-fold compared to wild type. Heparin 144-151 serpin family C member 1 Homo sapiens 104-109 34927362-9 2022 Ki for the inhibition by full-length TFPI of these FXa variants was increased by 7- to 1150-fold, while ATIII inhibition in the presence of the heparin-analogue Fondaparinux was modestly increased by 2- to 15-fold compared to wild type. Fondaparinux 161-173 serpin family C member 1 Homo sapiens 104-109 34091123-14 2021 010); AT III% was negatively predicted by the C-P classification (P = 0.000); copper levels, adjusted for C-P classification, were predicted by AT III% (P = 0.020) and fibrinogen concentrations, but not by PT% (P = 0.09). Copper 78-84 serpin family C member 1 Homo sapiens 144-150 34743814-4 2021 Herein, we found that the S protein can competitively inhibit the bindings of antithrombin and heparin cofactor II to heparin/HS, causing abnormal increase in thrombin activity. Heparin 118-125 serpin family C member 1 Homo sapiens 78-90 34743814-4 2021 Herein, we found that the S protein can competitively inhibit the bindings of antithrombin and heparin cofactor II to heparin/HS, causing abnormal increase in thrombin activity. Heparitin Sulfate 126-128 serpin family C member 1 Homo sapiens 78-90 34955853-2 2021 Low molecular weight heparin (LMWH) is one of the most widely used anticoagulants although LMWHs differ in their anti-Xa, antithrombin, and anticoagulant activities. Heparin, Low-Molecular-Weight 0-28 serpin family C member 1 Homo sapiens 122-134 34955853-2 2021 Low molecular weight heparin (LMWH) is one of the most widely used anticoagulants although LMWHs differ in their anti-Xa, antithrombin, and anticoagulant activities. Heparin, Low-Molecular-Weight 30-34 serpin family C member 1 Homo sapiens 122-134 34091123-16 2021 On the basis that oxidants may enhance the activity of the extrinsic coagulation cascade, ultimately leading to thrombin formation, via their combined effects on stimulation of tissue factor activity and inhibition of fibrinolytic pathways, the positive relationship of copper to coagulation/hypercoagulation parameters (mainly AT III) in our research could find a plausible interpretation. Copper 270-276 serpin family C member 1 Homo sapiens 328-334 34091123-0 2021 Copper concentrations are prevalently associated with antithrombin III, but also with prothrombin time and fibrinogen in patients with liver cirrhosis: A cross-sectional retrospective study. Copper 0-6 serpin family C member 1 Homo sapiens 54-70 34881176-1 2021 Serpinc1 is a serine protease inhibitor in the coagulation cascade, but its role in tumor biology remains obscure. Serine 14-20 serpin family C member 1 Homo sapiens 0-8 34091123-13 2021 Among the previous parameters, to which serum albumin was added, the unique predictor of copper levels was AT III%, at multiple regression (P = 0. Copper 89-95 serpin family C member 1 Homo sapiens 107-113 34881176-8 2021 Subsequent unbiased quantitative proteomic and ubiquitinome analyses identify that multiple poly-ubiquitination of proteins involved in signal pathways (such as autophagy, apoptosis, lactate metabolism, and VEGF signaling) are regulated by serpinc1. Lactic Acid 183-190 serpin family C member 1 Homo sapiens 240-248 34790076-3 2021 This case report describes a critically ill premature infant with a progressive, occlusive inferior vena cava thrombus who received supplemental ATIII during enoxaparin treatment. Enoxaparin 158-168 serpin family C member 1 Homo sapiens 145-150 34851773-0 2021 Management of heparin resistance due to antithrombin deficiency in a Chinese pregnant woman: a case report. Heparin 14-21 serpin family C member 1 Homo sapiens 40-52 34324733-5 2021 Notably, inhibition of neddylation with MLN4924 suppressed both ubiquitination and degradation of antithrombin, which is recapitulated by silencing of the neddylation enzymes, NAE1, UBA3, and UBE2M, with small interfering RNA (siRNA). pevonedistat 40-47 serpin family C member 1 Homo sapiens 98-110 34307597-16 2021 SAS and SDS scores were significantly lower in the observation group than in the control group at 3 d after operation (P < 0.05). sds 8-11 serpin family C member 1 Homo sapiens 95-101 34067120-2 2021 Antithrombin has different conformations: native, heparin-activated, prelatent, latent, and cleaved. Heparin 50-57 serpin family C member 1 Homo sapiens 0-12 34768285-1 2022 Plasmodium falciparum (Pf)-derived histidine-rich protein II (HRPII) has been shown to inhibit heparin-dependent anticoagulant activity of antithrombin (AT) and induce inflammation in vitro and in vivo. Heparin 95-102 serpin family C member 1 Homo sapiens 139-151 34754684-2 2021 Antithrombin III (ATIII) is the most potent endogenous anticoagulant and is required for the clinical efficacy of heparin. Heparin 114-121 serpin family C member 1 Homo sapiens 0-16 34754684-2 2021 Antithrombin III (ATIII) is the most potent endogenous anticoagulant and is required for the clinical efficacy of heparin. Heparin 114-121 serpin family C member 1 Homo sapiens 18-23 34513101-0 2021 Treatment of Homozygous Type II Antithrombin Heparin-Binding Site Deficiency in Pregnancy. Heparin 45-52 serpin family C member 1 Homo sapiens 32-44 34381261-13 2021 Conclusion: Argatroban may be more cost-effective during ECMO therapy in patients with low antithrombin III levels without increased risk of adverse events. argatroban 12-22 serpin family C member 1 Homo sapiens 91-107 34256393-0 2021 Antithrombin resistance rescues clotting defect of homozygous prothrombin-Tyr510N dysprothrombinemia. tyr510n 74-81 serpin family C member 1 Homo sapiens 0-12 34061194-7 2021 CONCLUSIONS: Risk factors for heparin resistance include antithrombin deficiency, elevation of factor VIII or fibrinogen level, elevation in heparin-binding proteins, increased heparin clearance, sepsis, trauma, and burns. Heparin 30-37 serpin family C member 1 Homo sapiens 57-69 35563651-2 2022 The action of plasmin is counteracted by alpha2-antiplasmin, alpha2-macroglobulin, TAFI, and other serine protease inhibitors (antithrombin and alpha2-antitrypsin) and PN-1 (protease nexin 1). Serine 99-105 serpin family C member 1 Homo sapiens 127-139 35605639-0 2022 Mixing study to diagnose heparin-resistance caused by functional antithrombin deficiency. Heparin 25-32 serpin family C member 1 Homo sapiens 65-77 35086148-10 2022 Plasma levels of fibrinogen, antithrombin, protein C and TFPI decreased, and free protein S increased in tamoxifen, but not in AI, users. Tamoxifen 105-114 serpin family C member 1 Homo sapiens 29-41 35013785-10 2022 Reduced CBL-48 h was shown to be most closely associated with the level of Antithrombin-III being decreased in females. Chlorambucil 8-11 serpin family C member 1 Homo sapiens 75-91 35592395-3 2022 A number of endogenous anticoagulant proteins, such as antithrombin and heparin cofactor II, are members of the serine protease inhibitor (SERPIN) family. Serine 112-118 serpin family C member 1 Homo sapiens 55-67 35124550-0 2022 Miniaturized antithrombin III affinity monolithic columns coupled to TOF-MS for the selective capture and release of fondaparinux a high affinity antithrombin III ligand. Fondaparinux 117-129 serpin family C member 1 Homo sapiens 13-29 35124550-0 2022 Miniaturized antithrombin III affinity monolithic columns coupled to TOF-MS for the selective capture and release of fondaparinux a high affinity antithrombin III ligand. Fondaparinux 117-129 serpin family C member 1 Homo sapiens 146-162 35124550-1 2022 This work explores the capability of antithrombin III-functionalized capillary monolithic columns (in-line coupled with MS detection) to selectively capture, release and detect high affinity binders of antithrombin III (AT III) from oligosaccharides mixtures. Oligosaccharides 233-249 serpin family C member 1 Homo sapiens 37-53 35124550-1 2022 This work explores the capability of antithrombin III-functionalized capillary monolithic columns (in-line coupled with MS detection) to selectively capture, release and detect high affinity binders of antithrombin III (AT III) from oligosaccharides mixtures. Oligosaccharides 233-249 serpin family C member 1 Homo sapiens 202-218 35124550-1 2022 This work explores the capability of antithrombin III-functionalized capillary monolithic columns (in-line coupled with MS detection) to selectively capture, release and detect high affinity binders of antithrombin III (AT III) from oligosaccharides mixtures. Oligosaccharides 233-249 serpin family C member 1 Homo sapiens 220-226 35124550-2 2022 The in-situ characterization of home-made AT III affinity columns was done by frontal affinity chromatography coupled to MS detection using fondaparinux as model ligand. Fondaparinux 140-152 serpin family C member 1 Homo sapiens 42-48 35124550-5 2022 The two other methods, direct grafting on aldehyde preactivated monoliths and immobilization of biotinylated antithrombin III to streptavidin-functionalized columns, require the presence of fondaparinux to protect the heparin binding site during the grafting process. Fondaparinux 190-202 serpin family C member 1 Homo sapiens 109-125 35124550-5 2022 The two other methods, direct grafting on aldehyde preactivated monoliths and immobilization of biotinylated antithrombin III to streptavidin-functionalized columns, require the presence of fondaparinux to protect the heparin binding site during the grafting process. Heparin 218-225 serpin family C member 1 Homo sapiens 109-125 35486842-0 2022 Two SERPINC1 variants affecting N-glycosylation of Asn224 cause severe thrombophilia not detected by functional assays. Nitrogen 32-33 serpin family C member 1 Homo sapiens 4-12 35486842-9 2022 Our study shows new elements involved in the regulation of N-glycosylation, a key post-translational modification that, according to our results affects folding, secretion and function, providing new evidence of the pathogenic consequence of an incorrect N-glycosylation of antithrombin. Nitrogen 59-60 serpin family C member 1 Homo sapiens 274-286 35410277-9 2022 At 3-d after the operation, the VAS (Visual analogue scale) was 4.64 +- 1.78 and 3.00 +- 1.71, and the ODI (Oswestry disability index) was 67.44 +- 11.37% and 56.73 +- 10.59% in TLF and NTLF group, respectively (P < 0.05). ntlf 186-190 serpin family C member 1 Homo sapiens 0-6 34626387-3 2022 Heparin polymers carrying rare 3-O-sulfated glucosamine units have been proven to be critical for binding to antithrombin and elicit an anticoagulant response. Heparin 0-7 serpin family C member 1 Homo sapiens 109-121 35387724-12 2022 Correlation analysis showed that there was a clear positive correlation between AT III and TBil in the dead patients of HBV liver failure group and the survival and death patients of non-HBV liver failure group (r values were 0.069, 0.341, 0.064, and P values were 0.723, 1.196 and 0.761, respectively); there was a significant inverse correlation between AT III and TBil in the HBV liver failure group (r = -0.105, P = 0.745). Bilirubin 91-95 serpin family C member 1 Homo sapiens 356-362 35387724-12 2022 Correlation analysis showed that there was a clear positive correlation between AT III and TBil in the dead patients of HBV liver failure group and the survival and death patients of non-HBV liver failure group (r values were 0.069, 0.341, 0.064, and P values were 0.723, 1.196 and 0.761, respectively); there was a significant inverse correlation between AT III and TBil in the HBV liver failure group (r = -0.105, P = 0.745). Bilirubin 367-371 serpin family C member 1 Homo sapiens 80-86 35062299-0 2022 Modulation of HIV Replication in Monocyte-Derived Macrophages (MDM) by Host Antiviral Factors Secretory Leukocyte Protease Inhibitor and Serpin Family C Member 1 Induced by Steroid Hormones. Steroids 173-180 serpin family C member 1 Homo sapiens 137-161 35062299-5 2022 Our in vitro results suggest that treatment with high doses of estrogen and progesterone promotes the expression of host antiviral factors Secretory leukocyte protease inhibitor (SLPI) and Serpin family C member 1 (SERPIN C1) among others produced in response to HIV-1 infection. Progesterone 76-88 serpin family C member 1 Homo sapiens 189-213 35062299-5 2022 Our in vitro results suggest that treatment with high doses of estrogen and progesterone promotes the expression of host antiviral factors Secretory leukocyte protease inhibitor (SLPI) and Serpin family C member 1 (SERPIN C1) among others produced in response to HIV-1 infection. Progesterone 76-88 serpin family C member 1 Homo sapiens 215-224 35062299-7 2022 SERPIN C1 is a plasma protease inhibitor that regulates the blood coagulation cascade by the inhibition of thrombin and other activated serine proteases of the coagulation system. Serine 136-142 serpin family C member 1 Homo sapiens 0-9 34626387-3 2022 Heparin polymers carrying rare 3-O-sulfated glucosamine units have been proven to be critical for binding to antithrombin and elicit an anticoagulant response. Glucosamine 44-55 serpin family C member 1 Homo sapiens 109-121 2482548-11 1989 Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups. Heparin 40-47 serpin family C member 1 Homo sapiens 101-106 35481431-6 2022 These assess the capacity of low-molecular-mass heparins to accelerate the inhibition of factor Xa and factor IIa by antithrombin. low-molecular-mass heparins 29-56 serpin family C member 1 Homo sapiens 117-129 2482548-11 1989 Upon addition of therapeutic amounts of heparin (0.4 U/ml), differences between the contributions of ATIII and alpha 2M to the inhibition of thrombin were no longer apparent, as over 90% of complexed thrombin was bound to ATIII in heparinized plasmas of all age groups. Heparin 40-47 serpin family C member 1 Homo sapiens 222-227 2483984-2 1989 It was showed: (1) Fn, alpha 2-MG. AT-III activity were considerably decreased in COPD, when compare with that of controls; (2) there is a negative correlation between the value of PaCO2, r = -0.719, P less than 0.01. paco2 181-186 serpin family C member 1 Homo sapiens 35-41 2592856-1 1989 Inhibition of thrombin by heparin is mediated by at least two plasma proteins, antithrombin III, and heparin cofactor II. Heparin 26-33 serpin family C member 1 Homo sapiens 79-95 2629459-3 1989 Perturbation of the endothelial proteoglycan metabolism by beta-D-xyloside resulted in a reduced biosynthesis of cell surface heparan sulfate, and impaired antithrombin III binding to endothelial cells in parallel with an inhibition of endothelial cell heparin-like activity. xylosides 59-74 serpin family C member 1 Homo sapiens 156-172 2614848-1 1989 Crystals of bovine antithrombin III were obtained in the presence of metal ions with ammonium sulphate as precipitating agent. Metals 69-74 serpin family C member 1 Homo sapiens 19-35 2614848-1 1989 Crystals of bovine antithrombin III were obtained in the presence of metal ions with ammonium sulphate as precipitating agent. Ammonium Sulfate 85-102 serpin family C member 1 Homo sapiens 19-35 2597694-0 1989 Phosphate promotes glycation of antithrombin III which interferes with heparin binding. Phosphates 0-9 serpin family C member 1 Homo sapiens 32-48 2597694-0 1989 Phosphate promotes glycation of antithrombin III which interferes with heparin binding. Heparin 71-78 serpin family C member 1 Homo sapiens 32-48 2597694-1 1989 Nonenzymatic glycation of antithrombin III has been reported to cause the reduction of heparin-catalyzed thrombin-inhibiting activity in diabetes. Heparin 87-94 serpin family C member 1 Homo sapiens 26-42 2597694-2 1989 The effect of in vitro nonenzymatic glycation of pure antithrombin III on heparin binding and heparin-potentiated activity under a variety of buffers and pH values was studied to further clarify the physiological significance of this reaction. Heparin 74-81 serpin family C member 1 Homo sapiens 54-70 2597694-2 1989 The effect of in vitro nonenzymatic glycation of pure antithrombin III on heparin binding and heparin-potentiated activity under a variety of buffers and pH values was studied to further clarify the physiological significance of this reaction. Heparin 94-101 serpin family C member 1 Homo sapiens 54-70 2597694-4 1989 Conversely, the heparin-catalyzed antithrombin activity decreased from 93.1% of controls for 0.01 M phosphate to 73.5% for 0.2 M phosphate as the extent of glycation increased. Heparin 16-23 serpin family C member 1 Homo sapiens 34-46 2597694-4 1989 Conversely, the heparin-catalyzed antithrombin activity decreased from 93.1% of controls for 0.01 M phosphate to 73.5% for 0.2 M phosphate as the extent of glycation increased. Phosphates 100-109 serpin family C member 1 Homo sapiens 34-46 2597694-4 1989 Conversely, the heparin-catalyzed antithrombin activity decreased from 93.1% of controls for 0.01 M phosphate to 73.5% for 0.2 M phosphate as the extent of glycation increased. Phosphates 129-138 serpin family C member 1 Homo sapiens 34-46 2597694-5 1989 The increase in intrinsic fluorescence induced by binding of heparin to antithrombin III was also moderated by glycation of antithrombin III in a dose-dependent manner with a negative correlation coefficient of -0.94. Heparin 61-68 serpin family C member 1 Homo sapiens 72-88 2597694-5 1989 The increase in intrinsic fluorescence induced by binding of heparin to antithrombin III was also moderated by glycation of antithrombin III in a dose-dependent manner with a negative correlation coefficient of -0.94. Heparin 61-68 serpin family C member 1 Homo sapiens 124-140 2611327-6 1989 Although heparin significantly accelerated thrombin inhibition by antithrombin lll, the remaining thrombin levels were still significantly above the minimum threshold required for irreversible platelet aggregation. Heparin 9-16 serpin family C member 1 Homo sapiens 66-78 2609289-0 1989 Identification and characterisation of an antithrombin III mutant (AT Dublin 2) with marginally decreased heparin reactivity. Heparin 106-113 serpin family C member 1 Homo sapiens 42-58 2609289-6 1989 Mutant plasma ATIII showed reduced thrombin reactivity at low concentrations of thrombin and demonstrated decreased reactivity with heparin over a range of heparin concentrations. Heparin 132-139 serpin family C member 1 Homo sapiens 14-19 2609289-6 1989 Mutant plasma ATIII showed reduced thrombin reactivity at low concentrations of thrombin and demonstrated decreased reactivity with heparin over a range of heparin concentrations. Heparin 156-163 serpin family C member 1 Homo sapiens 14-19 2609289-7 1989 This was confirmed using a modified ATIII heparin cofactor activity assay with varying heparin concentrations. Heparin 42-49 serpin family C member 1 Homo sapiens 36-41 2509458-5 1989 Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 32-48 2609289-8 1989 The abnormal ATIII was also found to elute from heparin agarose at a lower ionic strength than normal ATIII. Heparin 48-55 serpin family C member 1 Homo sapiens 13-18 2509458-5 1989 Heparin accelerated the rate of antithrombin III inhibition of alpha-thrombin, heparin-protected modified-alpha-thrombin, and gamma T-thrombin in a manner consistent with a template mechanism but was without effect on unprotected modified alpha-thrombin. Heparin 79-86 serpin family C member 1 Homo sapiens 32-48 2509458-6 1989 In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding. Heparin 5-12 serpin family C member 1 Homo sapiens 23-39 2509458-6 1989 In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding. phenylalanyl-prolyl-arginine-chloromethyl ketone 90-123 serpin family C member 1 Homo sapiens 23-39 2509458-6 1989 In a heparin-catalyzed antithrombin III inhibition assay of alpha-thrombin, we found that D-Phe-Pro-Arg chloromethyl ketone-active site-inactivated gamma T-thrombin competed for heparin binding. Heparin 178-185 serpin family C member 1 Homo sapiens 23-39 2609289-8 1989 The abnormal ATIII was also found to elute from heparin agarose at a lower ionic strength than normal ATIII. Sepharose 56-63 serpin family C member 1 Homo sapiens 13-18 2632043-1 1989 It is known that antithrombin III (ATIII) activity is inhibited by tissue thromboplastin (TP) in the presence of heparin. Heparin 113-120 serpin family C member 1 Homo sapiens 17-33 2627551-1 1989 Affinity chromatography on heparin-Sepharose was used to isolate two forms of antithrombin III(AT) from human, bovine, rabbit and rat blood plasma. Heparin 27-34 serpin family C member 1 Homo sapiens 78-94 2627551-1 1989 Affinity chromatography on heparin-Sepharose was used to isolate two forms of antithrombin III(AT) from human, bovine, rabbit and rat blood plasma. Sepharose 35-44 serpin family C member 1 Homo sapiens 78-94 2632043-9 1989 ATIII antigenicity was altered in the presence of both heparin and TP but not in the presence of TP alone. Heparin 55-62 serpin family C member 1 Homo sapiens 0-5 2632043-1 1989 It is known that antithrombin III (ATIII) activity is inhibited by tissue thromboplastin (TP) in the presence of heparin. Heparin 113-120 serpin family C member 1 Homo sapiens 35-40 2625740-3 1989 Moreover and ratio of AT-III-heparin complex formation was significantly reduced during two years, too (50.7 +/- 3.0% to 53.0 +/- 1.5%). Heparin 29-36 serpin family C member 1 Homo sapiens 22-28 2625740-5 1989 Therefore, it was interestingly suggested the possibility that prolonged hemodialysis treatment induced a functional loss of AT-III, especially in a capacity to form a AT-III-heparin complex due to partial loss of the affinity for heparin. Heparin 175-182 serpin family C member 1 Homo sapiens 125-131 2625740-5 1989 Therefore, it was interestingly suggested the possibility that prolonged hemodialysis treatment induced a functional loss of AT-III, especially in a capacity to form a AT-III-heparin complex due to partial loss of the affinity for heparin. Heparin 231-238 serpin family C member 1 Homo sapiens 125-131 2478015-3 1989 Patients receiving ATIII/heparin had significantly higher postoperative ATIII concentrations than dextran-treated patients and also had a low incidence of venous thromboembolic disease (7 percent). Heparin 25-32 serpin family C member 1 Homo sapiens 72-77 2688761-2 1989 The anticoagulant heparin greatly accelerates the rate of inactivation of proteinases by antithrombin, predominantly through its well defined, highly specific binding reaction with the inhibitor, but also through a less strictly defined interaction with some of the proteinases (such as thrombin). Heparin 18-25 serpin family C member 1 Homo sapiens 89-101 2688761-3 1989 There is evidence for an analogous acceleratory mechanism in vivo, that functions by the binding of antithrombin to a subpopulation of heparan sulphate proteoglycans intercalated in the surface of endothelial cells. Heparitin Sulfate 135-151 serpin family C member 1 Homo sapiens 100-112 2512688-2 1989 Although ATIII at 20 mInh.U/ml slightly but significantly inhibited thrombin-induced prostacyclin production, neither unfractionated heparin (UFH) nor low molecular weight heparin (LMWH) at 1 U/ml accelerated the inhibitory effect of ATIII. Epoprostenol 85-97 serpin family C member 1 Homo sapiens 9-14 2552799-8 1989 Since this ATIII is probably associated with heparin-like substances and exists in a high-affinity state, the inhibitor rapidly binds proteinases such as alpha-thrombin. Heparin 45-52 serpin family C member 1 Homo sapiens 11-16 2478364-0 1989 The heparin and pentosan polysulfate binding sites of human antithrombin overlap but are not identical. Heparin 4-11 serpin family C member 1 Homo sapiens 60-72 2478364-0 1989 The heparin and pentosan polysulfate binding sites of human antithrombin overlap but are not identical. Pentosan Sulfuric Polyester 16-36 serpin family C member 1 Homo sapiens 60-72 2478364-3 1989 This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding. Polysaccharides 48-62 serpin family C member 1 Homo sapiens 145-157 2478364-3 1989 This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding. Lysine 102-105 serpin family C member 1 Homo sapiens 145-157 2478364-3 1989 This was characterized by the extent to which a polysaccharide could protect chemical modification of Lys-125 and Lys-136, two lysyl residues of antithrombin which have been implicated in heparin binding. Lysine 114-117 serpin family C member 1 Homo sapiens 145-157 2478364-6 1989 Compared to the unfractionated heparin on an equal mass basis, the low-molecular-mass heparin (molecular mass 4-6 kDa) binds more strongly to antithrombin, induces a greater conformational change (about twofold), but is less potent in accelerating the inhibitory activity. Heparin 31-38 serpin family C member 1 Homo sapiens 142-154 2478364-6 1989 Compared to the unfractionated heparin on an equal mass basis, the low-molecular-mass heparin (molecular mass 4-6 kDa) binds more strongly to antithrombin, induces a greater conformational change (about twofold), but is less potent in accelerating the inhibitory activity. Heparin 86-93 serpin family C member 1 Homo sapiens 142-154 2478364-8 1989 On the other hand, pentosan polysulfate protects only Lys-125 and causes no appreciable conformational change, although it is also capable of enhancing the antithrombin-thrombin interaction. Pentosan Sulfuric Polyester 19-39 serpin family C member 1 Homo sapiens 156-168 2478364-9 1989 These data clearly demonstrate that the heparin and pentosan polysulfate binding sites of antithrombin overlap (at Lys-125) but are not identical. Heparin 40-47 serpin family C member 1 Homo sapiens 90-102 2478364-9 1989 These data clearly demonstrate that the heparin and pentosan polysulfate binding sites of antithrombin overlap (at Lys-125) but are not identical. Pentosan Sulfuric Polyester 52-72 serpin family C member 1 Homo sapiens 90-102 2478364-9 1989 These data clearly demonstrate that the heparin and pentosan polysulfate binding sites of antithrombin overlap (at Lys-125) but are not identical. Lysine 115-118 serpin family C member 1 Homo sapiens 90-102 2794060-2 1989 The genes of seven structural mutants of antithrombin III (ATIII), presenting either defective serine protease reactivity or abnormal heparin binding, were analyzed. Heparin 134-141 serpin family C member 1 Homo sapiens 41-57 2794060-2 1989 The genes of seven structural mutants of antithrombin III (ATIII), presenting either defective serine protease reactivity or abnormal heparin binding, were analyzed. Heparin 134-141 serpin family C member 1 Homo sapiens 59-64 2512688-0 1989 Interaction of thrombin with heparin cofactor II and antithrombin III on prostacyclin production by cultured endothelial cells. Epoprostenol 73-85 serpin family C member 1 Homo sapiens 53-69 2504719-5 1989 However, these preparations of heparin still efficiently accelerate the inhibition of thrombin by antithrombin III. Heparin 31-38 serpin family C member 1 Homo sapiens 98-114 2679069-7 1989 It is concluded that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-ATIII mechanism. Warfarin 35-43 serpin family C member 1 Homo sapiens 123-128 2679069-7 1989 It is concluded that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-ATIII mechanism. Heparitin Sulfate 107-122 serpin family C member 1 Homo sapiens 123-128 2529852-0 1989 Effect of a heparan sulphate with high affinity for antithrombin III upon inactivation of thrombin and coagulation factor Xa. Heparitin Sulfate 12-28 serpin family C member 1 Homo sapiens 52-68 2801726-6 1989 The final product has a specific activity of not less than 6.4 IU ATIII per mg protein, of which over 90 percent binds to heparin on crossed immunoelectrophoresis. Heparin 122-129 serpin family C member 1 Homo sapiens 66-71 2801725-0 1989 Antithrombin inactivation by neutrophil elastase requires heparin. Heparin 58-65 serpin family C member 1 Homo sapiens 0-12 2801725-2 1989 Alternatively, we have recently observed an unexpected and paradoxical in vitro functioning of heparin that could result in the inactivation of antithrombin in pathologic conditions. Heparin 95-102 serpin family C member 1 Homo sapiens 144-156 2801725-3 1989 Specifically, antithrombin was rendered nonfunctional as an inhibitor of clotting enzymes as a result of a limited, heparin-dependent cleavage by neutrophil elastase. Heparin 116-123 serpin family C member 1 Homo sapiens 14-26 2801725-7 1989 This affinity of both antithrombin and elastase for heparin suggests a novel mechanism of potential specificity. Heparin 52-59 serpin family C member 1 Homo sapiens 22-47 2801726-4 1989 After heating, a second heparin-affinity chromatography step is employed to isolate the active ATIII and to remove heat-denatured protein. Heparin 24-31 serpin family C member 1 Homo sapiens 95-100 2529852-1 1989 The kinetics of inhibition of human alpha-thrombin and coagulation Factor Xa by antithrombin III were examined under pseudo-first-order reaction conditions as a function of the concentration of heparan sulphate with high affinity for antithrombin III. Heparitin Sulfate 194-210 serpin family C member 1 Homo sapiens 80-96 2529852-1 1989 The kinetics of inhibition of human alpha-thrombin and coagulation Factor Xa by antithrombin III were examined under pseudo-first-order reaction conditions as a function of the concentration of heparan sulphate with high affinity for antithrombin III. Heparitin Sulfate 194-210 serpin family C member 1 Homo sapiens 234-250 2529852-2 1989 The maximum observed second-order rate constant was, for the antithrombin III-thrombin reaction, 1.2 x 10(9) M-1.min-1 compared with 2.4 x 10(9) M-1.min-1 in the presence of high-affinity heparin. Heparin 188-195 serpin family C member 1 Homo sapiens 61-77 2529852-4 1989 Differences were also observed in the maximal acceleration of the antithrombin III-Factor Xa interaction: 1.2 x 10(9) M-1.min-1 at 0.2 microM-heparin sulphate compared with 2.2 x 10(9) M-1.min-1 at 0.04 microM-heparin. heparin sulphate 142-158 serpin family C member 1 Homo sapiens 66-82 2529852-4 1989 Differences were also observed in the maximal acceleration of the antithrombin III-Factor Xa interaction: 1.2 x 10(9) M-1.min-1 at 0.2 microM-heparin sulphate compared with 2.2 x 10(9) M-1.min-1 at 0.04 microM-heparin. Heparin 142-149 serpin family C member 1 Homo sapiens 66-82 2529852-11 1989 The rate constant for transformation of the antithrombin III-Factor Xa complex into irreversible product differed between heparan sulphate (96 min-1) and heparin (429 min-1). Heparitin Sulfate 122-138 serpin family C member 1 Homo sapiens 44-60 2529852-11 1989 The rate constant for transformation of the antithrombin III-Factor Xa complex into irreversible product differed between heparan sulphate (96 min-1) and heparin (429 min-1). Heparin 154-161 serpin family C member 1 Homo sapiens 44-60 2544589-0 1989 Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages. Heparin 0-7 serpin family C member 1 Homo sapiens 32-48 2814937-2 1989 The abnormal antithrombin was isolated from plasma by chromatography on heparin-Sepharose at pH 6.0, and ion exchange on DEAE-Sephadex at pH 8.6 and 6.0. Heparin 72-79 serpin family C member 1 Homo sapiens 13-25 2814937-2 1989 The abnormal antithrombin was isolated from plasma by chromatography on heparin-Sepharose at pH 6.0, and ion exchange on DEAE-Sephadex at pH 8.6 and 6.0. Sepharose 80-89 serpin family C member 1 Homo sapiens 13-25 2814937-2 1989 The abnormal antithrombin was isolated from plasma by chromatography on heparin-Sepharose at pH 6.0, and ion exchange on DEAE-Sephadex at pH 8.6 and 6.0. DEAE-Dextran 121-134 serpin family C member 1 Homo sapiens 13-25 2598315-3 1989 The HA-heparin-catalyzed thrombin/AT III reaction was faster in the presence of 0.1 M NaCl at pH 6.05 than that in the absence of the salt. Heparin 7-14 serpin family C member 1 Homo sapiens 34-40 2598315-3 1989 The HA-heparin-catalyzed thrombin/AT III reaction was faster in the presence of 0.1 M NaCl at pH 6.05 than that in the absence of the salt. Sodium Chloride 86-90 serpin family C member 1 Homo sapiens 34-40 2598315-4 1989 LA-heparin and dextran sulfate (DS) were also found to accelerate the thrombin/AT III reaction rate, but neither substance catalyzed the formation of the complex in the presence of 0.1 M NaCl at pH 7.4. la-heparin 0-10 serpin family C member 1 Homo sapiens 79-85 2598315-4 1989 LA-heparin and dextran sulfate (DS) were also found to accelerate the thrombin/AT III reaction rate, but neither substance catalyzed the formation of the complex in the presence of 0.1 M NaCl at pH 7.4. Dextran Sulfate 15-30 serpin family C member 1 Homo sapiens 79-85 2598315-4 1989 LA-heparin and dextran sulfate (DS) were also found to accelerate the thrombin/AT III reaction rate, but neither substance catalyzed the formation of the complex in the presence of 0.1 M NaCl at pH 7.4. Dextran Sulfate 32-34 serpin family C member 1 Homo sapiens 79-85 2598315-5 1989 LA-heparin was also confirmed to compete with HA-heparin for enhancement of the thrombin/AT III reaction. la-heparin 0-10 serpin family C member 1 Homo sapiens 89-95 2598315-5 1989 LA-heparin was also confirmed to compete with HA-heparin for enhancement of the thrombin/AT III reaction. ha-heparin 46-56 serpin family C member 1 Homo sapiens 89-95 2598315-6 1989 Thus, it appears that AT III tends to form a ternary complex with the thrombin-DS or thrombin-LA-heparin complex, even in the presence of 0.1 M NaCl, whereas factor Xa reacts with the AT III-DS or AT III-LA-heparin complex. Heparin 97-104 serpin family C member 1 Homo sapiens 22-28 2598315-6 1989 Thus, it appears that AT III tends to form a ternary complex with the thrombin-DS or thrombin-LA-heparin complex, even in the presence of 0.1 M NaCl, whereas factor Xa reacts with the AT III-DS or AT III-LA-heparin complex. Sodium Chloride 144-148 serpin family C member 1 Homo sapiens 22-28 2598315-6 1989 Thus, it appears that AT III tends to form a ternary complex with the thrombin-DS or thrombin-LA-heparin complex, even in the presence of 0.1 M NaCl, whereas factor Xa reacts with the AT III-DS or AT III-LA-heparin complex. Heparin 207-214 serpin family C member 1 Homo sapiens 22-28 2598315-7 1989 These results indicate that HA-heparin is the only substance having the ability to catalyze the thrombin/AT III reaction, and that its turnover rate is markedly elevated in the presence of strongly electropositive and electronegative ions because of the decreased affinity of the enzyme for heparin under such conditions. Heparin 31-38 serpin family C member 1 Homo sapiens 105-111 2598315-7 1989 These results indicate that HA-heparin is the only substance having the ability to catalyze the thrombin/AT III reaction, and that its turnover rate is markedly elevated in the presence of strongly electropositive and electronegative ions because of the decreased affinity of the enzyme for heparin under such conditions. Heparin 291-298 serpin family C member 1 Homo sapiens 105-111 2544589-2 1989 Human antithrombin III (AT-III) was partially reduced under mild conditions in the absence or presence of low molecular weight heparin. Heparin 127-134 serpin family C member 1 Homo sapiens 24-30 2544589-4 1989 The study shows that the three disulfide linkages of AT-III can be sequentially reduced, with Cys8-Cys128 being the most sensitive, followed by Cys21-Cys95, while Cys247-Cys430 is the most resistant to the mild reduction conditions. Disulfides 31-40 serpin family C member 1 Homo sapiens 53-59 2544589-7 1989 These results suggest that Cys8-Cys128 is required for the integrity of the heparin binding domain of AT-III and support previous findings that lysyl residues surrounding Cys128 (Lys107, Lys114, Lys125, and Lys136) constitute an important part of the heparin binding site in AT-III. lysyl 144-149 serpin family C member 1 Homo sapiens 102-108 2544589-7 1989 These results suggest that Cys8-Cys128 is required for the integrity of the heparin binding domain of AT-III and support previous findings that lysyl residues surrounding Cys128 (Lys107, Lys114, Lys125, and Lys136) constitute an important part of the heparin binding site in AT-III. lysyl 144-149 serpin family C member 1 Homo sapiens 275-281 2544589-7 1989 These results suggest that Cys8-Cys128 is required for the integrity of the heparin binding domain of AT-III and support previous findings that lysyl residues surrounding Cys128 (Lys107, Lys114, Lys125, and Lys136) constitute an important part of the heparin binding site in AT-III. Heparin 76-83 serpin family C member 1 Homo sapiens 102-108 2806479-8 1989 Antithrombin III and fibronectin inhibited platelet response to heparin, suggesting that these proteins may protect platelets from aggregation by heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 0-16 2818566-3 1989 Using two methods, we have studied the potentiating effects of a series of heparin (poly)saccharides with high affinity for antithrombin and mean Mr ranging from approx. heparin (poly)saccharides 75-100 serpin family C member 1 Homo sapiens 124-136 2818566-5 1989 First, catalytic amounts of heparin (poly)saccharide were added to purified systems containing thrombin and either heparin cofactor II or antithrombin. heparin (poly)saccharide 28-52 serpin family C member 1 Homo sapiens 138-150 2818566-10 1989 In this situation, where the inhibitors competed for thrombin and for the (poly)saccharides, it was found that, provided the latter were of high affinity for antithrombin and exceeded a Mr of 5400, thrombin inhibition in plasma was mediated largely through antithrombin. Polysaccharides 74-91 serpin family C member 1 Homo sapiens 158-170 2818566-10 1989 In this situation, where the inhibitors competed for thrombin and for the (poly)saccharides, it was found that, provided the latter were of high affinity for antithrombin and exceeded a Mr of 5400, thrombin inhibition in plasma was mediated largely through antithrombin. Polysaccharides 74-91 serpin family C member 1 Homo sapiens 257-269 2818566-11 1989 Polysaccharides of Mr exceeding 8000 that were of low affinity for antithrombin accelerated thrombin inhibition in plasma through their interaction with heparin cofactor II. Polysaccharides 0-15 serpin family C member 1 Homo sapiens 67-79 2818566-12 1989 High concentrations of saccharides of Mr 1700-5400 exhibited a size-dependent acceleration of thrombin inhibition, not through their interaction with antithrombin, but through their interaction with heparin cofactor II. Carbohydrates 23-34 serpin family C member 1 Homo sapiens 150-162 2598315-0 1989 Dependence of the rate of thrombin/antithrombin III reaction upon the turnover rate of a catalytic amount of heparin. Heparin 109-116 serpin family C member 1 Homo sapiens 35-51 2598315-1 1989 Commercially available heparin preparations slightly enhanced the rate of thrombin/antithrombin (AT) III reaction at pH 6.05 in the absence of NaCl. Heparin 23-30 serpin family C member 1 Homo sapiens 74-104 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). Heparin 81-88 serpin family C member 1 Homo sapiens 112-118 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). Heparin 81-88 serpin family C member 1 Homo sapiens 201-207 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). Heparin 81-88 serpin family C member 1 Homo sapiens 201-207 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). ha-heparin 120-130 serpin family C member 1 Homo sapiens 112-118 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). histidinoalanine 120-122 serpin family C member 1 Homo sapiens 112-118 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). histidinoalanine 120-122 serpin family C member 1 Homo sapiens 201-207 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). histidinoalanine 120-122 serpin family C member 1 Homo sapiens 201-207 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). Heparin 123-130 serpin family C member 1 Homo sapiens 112-118 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). Heparin 123-130 serpin family C member 1 Homo sapiens 112-118 2598315-2 1989 However, this accelerative activity was significantly lower than that induced by heparin with high affinity for AT III (HA-heparin), probably due to the formation of the binary complexes of HA-heparin-AT III as well as that composed of thrombin and heparin with low affinity for AT III (LA-heparin). la-heparin 287-297 serpin family C member 1 Homo sapiens 112-118 2544589-0 1989 Heparin binding domain of human antithrombin III inferred from the sequential reduction of its three disulfide linkages. Disulfides 101-110 serpin family C member 1 Homo sapiens 32-48 2544589-2 1989 Human antithrombin III (AT-III) was partially reduced under mild conditions in the absence or presence of low molecular weight heparin. Heparin 127-134 serpin family C member 1 Homo sapiens 6-22 2508258-5 1989 After 90 min, in plasma samples containing anti-rt-PA-IgG to inhibit in vitro effects, fibrinogen was decreased to 54%, plasminogen to 52%, alpha 2-antiplasmin to 25%, alpha 2-macroglobulin to 90% and antithrombin III to 85% of initial values. Hydrocortisone 48-50 serpin family C member 1 Homo sapiens 201-217 2508258-5 1989 After 90 min, in plasma samples containing anti-rt-PA-IgG to inhibit in vitro effects, fibrinogen was decreased to 54%, plasminogen to 52%, alpha 2-antiplasmin to 25%, alpha 2-macroglobulin to 90% and antithrombin III to 85% of initial values. Protactinium 51-53 serpin family C member 1 Homo sapiens 201-217 2781509-2 1989 The variant antithrombin was isolated from plasma of the propositus by chromatography on heparin-Sepharose, followed by passage through thrombin-Sepharose to remove the normal antithrombin component that is present. Heparin 89-96 serpin family C member 1 Homo sapiens 12-24 2799755-1 1989 We investigated the effect on thrombin generation in plasma of the pentasaccharide that represent the AT III/binding site in heparin. pentasaccharide 67-82 serpin family C member 1 Homo sapiens 102-108 2799755-1 1989 We investigated the effect on thrombin generation in plasma of the pentasaccharide that represent the AT III/binding site in heparin. Heparin 125-132 serpin family C member 1 Homo sapiens 102-108 2722856-1 1989 Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation. Heparin 12-19 serpin family C member 1 Homo sapiens 142-148 2722856-10 1989 243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin. Heparin 21-29 serpin family C member 1 Homo sapiens 220-226 2722856-10 1989 243, 31-37), all the heparins showed a 5-fold higher rate of inhibition of factor Xa when compared with the inhibition of prothrombinase, indicating that the factor Va-mediated protection of factor Xa from inhibition by AT III/heparin is independent of the molecular size of the heparin. Heparin 21-28 serpin family C member 1 Homo sapiens 220-226 2722856-11 1989 Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way. Heparin 130-138 serpin family C member 1 Homo sapiens 180-186 2722856-11 1989 Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way. Heparin 130-138 serpin family C member 1 Homo sapiens 308-314 2722856-11 1989 Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way. Heparin 206-214 serpin family C member 1 Homo sapiens 180-186 2722856-11 1989 Our original approach has also revealed a hitherto unrecognized phenomenon, namely, in addition to the accelerating effect of the heparins on the rate of formation of the inactive AT III-factor Xa complex, heparins with Mr greater than 4,500 reduce the initial rate of thrombin generation in the presence of AT III in a concentration-dependent way. Heparin 206-214 serpin family C member 1 Homo sapiens 308-314 2722864-1 1989 Antithrombin pescara, ARG393 to pro, caused by a CGT to CCT mutation. Proline 32-35 serpin family C member 1 Homo sapiens 0-12 2722864-11 1989 Using specific oligonucleotide hybridization, we demonstrated that the molecular defect of antithrombin Pescara is caused by a CGT to CCT mutation in codon 393. Oligonucleotides 15-30 serpin family C member 1 Homo sapiens 91-103 2732232-4 1989 A potentially complex reaction mechanism is suggested by the binding of both neutrophil elastase and antithrombin to heparin. Heparin 117-124 serpin family C member 1 Homo sapiens 101-113 2732232-8 1989 Maximum acceleratory effects of heparin on the inactivation of antithrombin occur at heparin concentrations significantly lower than those required to saturate antithrombin. Heparin 32-39 serpin family C member 1 Homo sapiens 63-75 2732232-8 1989 Maximum acceleratory effects of heparin on the inactivation of antithrombin occur at heparin concentrations significantly lower than those required to saturate antithrombin. Heparin 32-39 serpin family C member 1 Homo sapiens 160-172 2732232-8 1989 Maximum acceleratory effects of heparin on the inactivation of antithrombin occur at heparin concentrations significantly lower than those required to saturate antithrombin. Heparin 85-92 serpin family C member 1 Homo sapiens 63-75 2732232-9 1989 The divergence in acceleratory effect and antithrombin binding contrasts with the anticoagulant functioning of heparin in promoting the formation of covalent antithrombin-enzyme complexes and is likely to derive from the fact that neutrophil elastase is not consumed in the inactivation reaction. Heparin 111-118 serpin family C member 1 Homo sapiens 158-170 2732232-10 1989 A size dependence was observed for the heparin effect since an anticoagulantly active octasaccharide fragment of heparin, with avid antithrombin binding activity, was without effect on the inactivation of antithrombin by neutrophil elastase. Octasaccharide 86-100 serpin family C member 1 Homo sapiens 132-144 2732232-10 1989 A size dependence was observed for the heparin effect since an anticoagulantly active octasaccharide fragment of heparin, with avid antithrombin binding activity, was without effect on the inactivation of antithrombin by neutrophil elastase. Heparin 113-120 serpin family C member 1 Homo sapiens 132-144 2722856-1 1989 Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation. Heparin 0-7 serpin family C member 1 Homo sapiens 124-140 2722856-1 1989 Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation. Heparin 0-7 serpin family C member 1 Homo sapiens 142-148 2722856-1 1989 Heparin and heparin fragments in the molecular mass range 1,700-20,000 Da were examined for their ability to accelerate the antithrombin III (AT III)-dependent inhibition of human factor Xa and the prothrombin converting complex (prothrombinase) during human prothrombin activation. Heparin 12-19 serpin family C member 1 Homo sapiens 124-140 2781509-2 1989 The variant antithrombin was isolated from plasma of the propositus by chromatography on heparin-Sepharose, followed by passage through thrombin-Sepharose to remove the normal antithrombin component that is present. Sepharose 97-106 serpin family C member 1 Homo sapiens 12-24 2781509-2 1989 The variant antithrombin was isolated from plasma of the propositus by chromatography on heparin-Sepharose, followed by passage through thrombin-Sepharose to remove the normal antithrombin component that is present. Sepharose 145-154 serpin family C member 1 Homo sapiens 12-24 2796953-5 1989 However, there was close relationship between PFN and antithrombin III, alpha 2-plasmin inhibitor, factor XIII, retinol binding protein and transferrin, which represent hemostasis, fibrinolytic system and nutritional status, respectively. (R)-Fenoprofen 46-49 serpin family C member 1 Homo sapiens 54-70 2615648-4 1989 These occurred in individuals with a history of thromboembolic disease due to functional abnormalities of circulating antithrombin: ten had decreased heparin binding and activation, two had decreased inhibitory activity. Heparin 150-157 serpin family C member 1 Homo sapiens 118-130 2615648-5 1989 The amino acid abnormality in ten out of 12 cases had arisen at a CpG dinucleotide; this confirms the CpG sequence as a "hotspot" in the antithrombin gene and explains the observed frequency of occurrence of the same variant antithrombins in diverse populations. Dinucleoside Phosphates 70-82 serpin family C member 1 Homo sapiens 137-149 2742816-13 1989 The simulated rate of formation and final concentration of a particular oligosaccharide which contains a portion of heparin"s ATIII binding site were similar to those observed experimentally. Oligosaccharides 72-87 serpin family C member 1 Homo sapiens 126-131 2763270-0 1989 C-terminal peptide alcohol, acid and amide analogs of desulfato hirudin54-65 as antithrombin agents. Amides 37-42 serpin family C member 1 Homo sapiens 80-92 2503646-5 1989 As our patient had multiple risk factors for the development of vitamin K deficiency including malabsorption, decreased food intake, and antibiotic use, we postulate that the small amount of heparin precipitated the coagulopathy by increasing the antiprotease activity of antithrombin III on abnormal factors X and II formed in the vitamin K deficient state. Heparin 191-198 serpin family C member 1 Homo sapiens 272-288 2749614-0 1989 Dissociation of the thrombin/antithrombin III reaction from amidolytic activity of the enzyme at high salt concentration. Salts 102-106 serpin family C member 1 Homo sapiens 29-45 2749614-2 1989 Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations. Sodium Chloride 85-89 serpin family C member 1 Homo sapiens 30-46 2749614-2 1989 Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations. Sodium Chloride 85-89 serpin family C member 1 Homo sapiens 48-54 2749614-2 1989 Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations. Sodium Chloride 121-125 serpin family C member 1 Homo sapiens 30-46 2749614-2 1989 Neutralization of thrombin by antithrombin III (AT III) was maximum in 0.1 to 0.15 M NaCl, but completely absent at high NaCl concentrations. Sodium Chloride 121-125 serpin family C member 1 Homo sapiens 48-54 2678856-6 1989 In the high-dose corticosteroid group the values of antithrombin and functional kallikrein inhibition was significantly higher than in the non-steroid group. Steroids 24-31 serpin family C member 1 Homo sapiens 52-64 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 267-289 serpin family C member 1 Homo sapiens 134-139 2726317-6 1989 However, de novo generation of thrombin activity was very susceptible to inhibition by heparin, even in neonatal plasmas with physiologically low AT III levels. Heparin 87-94 serpin family C member 1 Homo sapiens 146-152 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 55-62 serpin family C member 1 Homo sapiens 127-143 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 55-62 serpin family C member 1 Homo sapiens 127-143 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 152-159 serpin family C member 1 Homo sapiens 29-45 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 152-159 serpin family C member 1 Homo sapiens 127-143 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 152-159 serpin family C member 1 Homo sapiens 127-143 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 152-159 serpin family C member 1 Homo sapiens 127-143 2466666-9 1989 Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced. Heparin 135-142 serpin family C member 1 Homo sapiens 15-31 2466666-9 1989 Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced. Heparin 185-192 serpin family C member 1 Homo sapiens 15-31 2466666-9 1989 Its binding to antithrombin III induces a conformational change that enhances antithrombin III activity in a manner that resembles the heparin effect, but its effect is additive to the heparin effect, since when it was added to a reaction mixture which contained a saturating amount of heparin, inhibition of thrombin was enhanced. Heparin 185-192 serpin family C member 1 Homo sapiens 15-31 2466666-10 1989 The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds. Disulfides 188-197 serpin family C member 1 Homo sapiens 96-112 2466666-10 1989 The epitope for monoclonal antibody A5 is located within residues 1-393, and its recognition of antithrombin III or antithrombin-III-thrombin is strongly dependent on the integrity of the disulfide bonds. Disulfides 188-197 serpin family C member 1 Homo sapiens 116-132 2650580-3 1989 The authors investigated the effect of two heparin regimens (regimen I: 2,000 U/hr and regimen II: 500 U/hr) upon plasma antithrombin level (IU/mL) and activated thromboplastin time (sec). Heparin 43-50 serpin family C member 1 Homo sapiens 121-133 2466666-6 1989 If A36 is first reacted with antithrombin III and then heparin is added to the reaction mixture, A36 fixes the conformation of antithrombin III so that heparin binds to antithrombin III, but is not able to induce the conformational change in the antithrombin III molecule required for the enhanced activity. Heparin 55-62 serpin family C member 1 Homo sapiens 127-143 2752479-6 1989 Inhibition of thrombin activity by the ATIII-APC-heparin mixture was weak as compared with that by the ATIII-heparin mixture after a 1-min incubation, but after a 2-min incubation the inhibitory activities were equal. Heparin 49-56 serpin family C member 1 Homo sapiens 39-44 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Heparin 50-57 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Heparin 50-57 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Heparin 50-57 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Heparin 144-151 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 267-289 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 267-289 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 291-294 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 291-294 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. Sodium Dodecyl Sulfate 291-294 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. polyacrylamide 296-310 serpin family C member 1 Homo sapiens 40-45 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. polyacrylamide 296-310 serpin family C member 1 Homo sapiens 134-139 2752479-7 1989 Suppression of thrombin activity by the ATIII-APC-heparin mixture was supposed to be due to the inhibition of the interaction between ATIII and heparin on thrombin by APC because the APC-ATIII-heparin complex was detected by crossed immuno-electrophoresis but not by sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis. polyacrylamide 296-310 serpin family C member 1 Homo sapiens 134-139 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 92-95 serpin family C member 1 Homo sapiens 34-46 2466846-2 1989 The anticoagulant action of heparin is mediated through antithrombin III, and the postoperative decrease in the plasma concentration of antithrombin III may contribute to the relative ineffectiveness of prophylaxis with low-dose heparin in preventing venous thrombosis after total hip arthroplasty. Heparin 28-35 serpin family C member 1 Homo sapiens 56-72 2466846-2 1989 The anticoagulant action of heparin is mediated through antithrombin III, and the postoperative decrease in the plasma concentration of antithrombin III may contribute to the relative ineffectiveness of prophylaxis with low-dose heparin in preventing venous thrombosis after total hip arthroplasty. Heparin 229-236 serpin family C member 1 Homo sapiens 136-152 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 146-152 serpin family C member 1 Homo sapiens 34-46 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 92-95 serpin family C member 1 Homo sapiens 34-46 2492530-0 1989 Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Heparin 11-18 serpin family C member 1 Homo sapiens 28-44 2492530-12 1989 At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. Lysine 71-74 serpin family C member 1 Homo sapiens 13-25 2749590-4 1989 Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin. Heparin 67-74 serpin family C member 1 Homo sapiens 154-160 2492530-12 1989 At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. Lysine 83-86 serpin family C member 1 Homo sapiens 13-25 2492530-12 1989 At a heparin/antithrombin molar ratio of 1, the extent of shielding of Lys-125 and Lys-136 and the unmasking of Lys-236 were 25-33%. Lysine 83-86 serpin family C member 1 Homo sapiens 13-25 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 17-20 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 17-20 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 17-20 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Heparin 71-78 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Heparin 71-78 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Heparin 71-78 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Heparin 134-141 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Heparin 134-141 serpin family C member 1 Homo sapiens 145-157 2492530-0 1989 Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Lysine 90-96 serpin family C member 1 Homo sapiens 28-44 2492530-1 1989 Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. Lysine 0-3 serpin family C member 1 Homo sapiens 78-94 2492530-1 1989 Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. Lysine 9-12 serpin family C member 1 Homo sapiens 78-94 2492530-1 1989 Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III. Lysine 9-12 serpin family C member 1 Homo sapiens 78-94 2492530-2 1989 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. Water 6-11 serpin family C member 1 Homo sapiens 150-166 2492530-2 1989 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. 4-n,n-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid 35-97 serpin family C member 1 Homo sapiens 150-166 2492530-2 1989 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 99-107 serpin family C member 1 Homo sapiens 150-166 2492530-2 1989 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. Lysine 131-137 serpin family C member 1 Homo sapiens 150-166 2492530-2 1989 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. Heparin 203-210 serpin family C member 1 Homo sapiens 150-166 2492530-3 1989 Antithrombin, modified with S-DABITC in the presence and absence of low molecular weight heparin (Mr 5000) was reduced, carboxymethylated, and digested with trypsin. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 28-36 serpin family C member 1 Homo sapiens 0-12 2492530-3 1989 Antithrombin, modified with S-DABITC in the presence and absence of low molecular weight heparin (Mr 5000) was reduced, carboxymethylated, and digested with trypsin. Heparin 89-96 serpin family C member 1 Homo sapiens 0-12 2492530-6 1989 When antithrombin was preincubated with heparin (2-fold by weight), followed by S-DABITC modification, the recovery of peptide T4 remained unchanged, but the recoveries of T1, T2, and T3 were reduced by 93, 86, and 98%, respectively. Heparin 40-47 serpin family C member 1 Homo sapiens 5-17 2492530-6 1989 When antithrombin was preincubated with heparin (2-fold by weight), followed by S-DABITC modification, the recovery of peptide T4 remained unchanged, but the recoveries of T1, T2, and T3 were reduced by 93, 86, and 98%, respectively. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 82-88 serpin family C member 1 Homo sapiens 5-17 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Heparin 134-141 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. Lysine 26-29 serpin family C member 1 Homo sapiens 145-157 2749590-0 1989 Homozygous variant of antithrombin III that lacks affinity for heparin, AT III Kumamoto. Heparin 63-70 serpin family C member 1 Homo sapiens 22-38 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 249-255 serpin family C member 1 Homo sapiens 101-113 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 249-255 serpin family C member 1 Homo sapiens 145-157 2492530-14 1989 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 249-255 serpin family C member 1 Homo sapiens 145-157 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Heparin 17-24 serpin family C member 1 Homo sapiens 34-46 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate 60-66 serpin family C member 1 Homo sapiens 34-46 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 83-86 serpin family C member 1 Homo sapiens 34-46 2492530-9 1989 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. Lysine 92-95 serpin family C member 1 Homo sapiens 34-46 2749590-4 1989 Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin. Heparin 106-113 serpin family C member 1 Homo sapiens 154-160 2749590-4 1989 Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin. Sepharose 114-123 serpin family C member 1 Homo sapiens 154-160 2749590-4 1989 Analysis by crossed-immunoelectrophoresis (CIE) in the presence of heparin and affinity chromatography on heparin-Sepharose revealed that the propositus" AT III did not bind to heparin. Heparin 106-113 serpin family C member 1 Homo sapiens 154-160 2749590-7 1989 The patient"s parents and three of her brothers demonstrated qualitative abnormality of AT III; heparin cofactor activity was 30-50% of normal levels in the presence of both thrombin and F.Xa. Heparin 96-103 serpin family C member 1 Homo sapiens 88-94 2749590-8 1989 These findings indicate that the propositus" AT III lacks affinity for heparin and the mode of its inheritance seems to be autosomal dominant and, hence, the propositus would be a homozygote. Heparin 71-78 serpin family C member 1 Homo sapiens 45-51 2713360-1 1989 The binding of heparin to high molecular weight kininogen (H-kininogen) was analyzed by the effect of kininogen in decreasing the heparin-induced enhancement of the rate of inactivation of thrombin by antithrombin. Heparin 15-22 serpin family C member 1 Homo sapiens 201-213 2713360-2 1989 The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration. Heparin 41-48 serpin family C member 1 Homo sapiens 59-71 2713360-1 1989 The binding of heparin to high molecular weight kininogen (H-kininogen) was analyzed by the effect of kininogen in decreasing the heparin-induced enhancement of the rate of inactivation of thrombin by antithrombin. Heparin 130-137 serpin family C member 1 Homo sapiens 201-213 2713360-2 1989 The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration. 4-aminobenzamidine 154-172 serpin family C member 1 Homo sapiens 59-71 2909522-0 1989 Location of the antithrombin-binding sequence in the heparin chain. Heparin 53-60 serpin family C member 1 Homo sapiens 16-28 2713360-2 1989 The conditions were arranged so that the heparin-catalyzed antithrombin-thrombin reaction, monitored in the presence of the reversible thrombin inhibitor p-aminobenzamidine, followed pseudo-first-order kinetics and the observed rate constant (kappa obsd) varied linearly with the heparin concentration. Heparin 280-287 serpin family C member 1 Homo sapiens 59-71 2713360-3 1989 In the absence of metal ions, H-kininogen minimally affected kappa obsd, measured at a constant concentration of heparin with high affinity for antithrombin (30 nM), at I = 0.15, pH 7.4 and 25 degrees C. However, at a saturating concentration of Zn2+ (10 microM), kappa obsd was reduced to 50% at approximately 20 nM H-kininogen and to that of the uncatalyzed reaction at greater than or equal to approximately 0.2 microM H-kininogen. Heparin 113-120 serpin family C member 1 Homo sapiens 144-156 2798989-2 1989 The mean of AT III level in patients with COBP was 40.5% and was 96.8% in the controls. cobp 42-46 serpin family C member 1 Homo sapiens 12-18 2713873-1 1989 spectroscopy, of the binding of a synthetic, high-affinity heparin pentasaccharide to human antithrombin III. IC 831423 59-82 serpin family C member 1 Homo sapiens 92-108 2713873-6 1989 The resonance of the H-2 atom of the histidine, considered to be the N-terminal residue and to be located in the heparin binding-site, is strongly perturbed by heparin binding both to native and modified antithrombin. Histidine 37-46 serpin family C member 1 Homo sapiens 204-216 2713873-6 1989 The resonance of the H-2 atom of the histidine, considered to be the N-terminal residue and to be located in the heparin binding-site, is strongly perturbed by heparin binding both to native and modified antithrombin. Heparin 113-120 serpin family C member 1 Homo sapiens 204-216 2713873-6 1989 The resonance of the H-2 atom of the histidine, considered to be the N-terminal residue and to be located in the heparin binding-site, is strongly perturbed by heparin binding both to native and modified antithrombin. Heparin 160-167 serpin family C member 1 Homo sapiens 204-216 2713873-8 1989 Resonances from two of the remaining four histidine units are sensitive to longer-range conformational changes, and show differences between binding of the two heparin species both in native and modified ATIII. Histidine 42-51 serpin family C member 1 Homo sapiens 204-209 2713873-8 1989 Resonances from two of the remaining four histidine units are sensitive to longer-range conformational changes, and show differences between binding of the two heparin species both in native and modified ATIII. Heparin 160-167 serpin family C member 1 Homo sapiens 204-209 2713873-10 1989 This is particularly significant as regards the mechanism of action of heparin, because the synthetic pentasaccharide activates ATIII towards Factor Xa, but not towards thrombin. Heparin 71-78 serpin family C member 1 Homo sapiens 128-133 2713873-10 1989 This is particularly significant as regards the mechanism of action of heparin, because the synthetic pentasaccharide activates ATIII towards Factor Xa, but not towards thrombin. pentasaccharide 102-117 serpin family C member 1 Homo sapiens 128-133 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. Heparin 35-42 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. pentasaccharide 48-63 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 105-111 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. 6-oso3 112-118 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. glca-glcnso3 120-132 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. 3,6-di-oso3) 133-145 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. ido a 146-151 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. 2-oso3)- glcnso3 152-168 serpin family C member 1 Homo sapiens 4-16 2909522-1 1989 The antithrombin-binding region of heparin is a pentasaccharide sequence with the predominant structure -GlcNAc(6-OSO3)-GlcA-GlcNSO3(3,6-di-OSO3)-Ido A(2-OSO3)- GlcNSO3(6-OSO3)-. 6-oso3 169-175 serpin family C member 1 Homo sapiens 4-16 2909522-6 1989 Such units were present in small, intermediate-sized as well as large fragments, suggesting that the antithrombin-binding regions were randomly distributed along the heparin chains. Heparin 166-173 serpin family C member 1 Homo sapiens 101-113 2909522-8 1989 The molecular weight distributions of such labeled LA-fragments, determined by gel chromatography, again conformed to a random distribution of the antithrombin-binding sequence within the heparin chains. Heparin 188-195 serpin family C member 1 Homo sapiens 147-159 2909522-15 1989 263, 262-266) which suggest that the antithrombin-binding region is preferentially located at the nonreducing terminus of the heparin molecule. Heparin 126-133 serpin family C member 1 Homo sapiens 37-49 2561387-3 1989 The definite mode of action remains unknown, but LMWH act at different steps like coagulation (by AT III), fibrinolysis, blood cells, endothelial cells. Heparin, Low-Molecular-Weight 49-53 serpin family C member 1 Homo sapiens 98-104 2735662-8 1989 Drugs which act primarily on factor Xa (oligosaccharides) or thrombin by non-ATIII pathways (dermatan sulfate) are less efficient than UFH as antithrombotic drugs. Dermatan Sulfate 93-109 serpin family C member 1 Homo sapiens 77-82 2786690-4 1989 Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex). Heparin 118-125 serpin family C member 1 Homo sapiens 79-84 2786690-4 1989 Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex). Heparin 118-125 serpin family C member 1 Homo sapiens 112-117 2786690-4 1989 Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex). Heparin 118-125 serpin family C member 1 Homo sapiens 112-117 2730347-2 1989 Commercial heparin has now been shown to be a mixture of over 100 different closely related sulfated polysaccharides of which only 10% activate antithrombin-III. Heparin 11-18 serpin family C member 1 Homo sapiens 144-160 2786690-4 1989 Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex). Heparin 235-242 serpin family C member 1 Homo sapiens 79-84 2786690-4 1989 Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex). Heparin 235-242 serpin family C member 1 Homo sapiens 112-117 2786690-4 1989 Because the mechanism of augmentation of the inactivation rate of an enzyme by ATIII occurs via formation of an ATIII-heparin complex, the degree of potentiation can be predicted by knowing the binding capacity (sites per mole) of the heparin preparation and the concentration of heparin in the reaction (to calculate the concentration of the ATIII-heparin complex). Heparin 235-242 serpin family C member 1 Homo sapiens 112-117 2786690-6 1989 The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex. Heparin 20-27 serpin family C member 1 Homo sapiens 79-84 2786690-6 1989 The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex. Heparin 20-27 serpin family C member 1 Homo sapiens 196-201 2786690-6 1989 The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex. Heparin 202-209 serpin family C member 1 Homo sapiens 79-84 2786690-6 1989 The augmentation by heparin of the inactivation rate of a particular enzyme by ATIII is dependent upon the presence of other enzymes with higher kassoc, since these would strongly compete for the ATIII-heparin complex. Heparin 202-209 serpin family C member 1 Homo sapiens 196-201 2463827-4 1989 Predictions were then made as to the heparin-binding domains in endothelial cell growth factor, purpurin, and antithrombin-III. Heparin 37-44 serpin family C member 1 Homo sapiens 110-126 2481530-7 1989 In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin doses required might entail an unexceptable bleeding risk, e.g. in simultaneous thrombocytopenia. Heparin 122-129 serpin family C member 1 Homo sapiens 46-62 2481530-7 1989 In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin doses required might entail an unexceptable bleeding risk, e.g. in simultaneous thrombocytopenia. Heparin 191-198 serpin family C member 1 Homo sapiens 21-33 2730347-2 1989 Commercial heparin has now been shown to be a mixture of over 100 different closely related sulfated polysaccharides of which only 10% activate antithrombin-III. Polysaccharides 101-116 serpin family C member 1 Homo sapiens 144-160 2481530-7 1989 In cases of acquired antithrombin deficiency, antithrombin III substitution is indicated only when the anticoagulation by heparin alone or in combination with FFP is insufficient or when the heparin doses required might entail an unexceptable bleeding risk, e.g. in simultaneous thrombocytopenia. Heparin 191-198 serpin family C member 1 Homo sapiens 46-62 2713428-0 1989 Activity toward thrombin-antithrombin of heparin immobilized on two hydrogels. Heparin 41-48 serpin family C member 1 Homo sapiens 25-37 2920011-4 1989 Association rate constants of both gdN and antithrombin III with alpha-thrombin were obtained using unfractionated, low- and high-affinity heparin types. Heparin 139-146 serpin family C member 1 Homo sapiens 43-59 2713428-2 1989 We found that as tresyl chloride activation of PVA increased, the specific activity of the bound heparin toward thrombin and antithrombin decreased by nearly a factor of 10 and that commercial heparin bound to PEO had nearly ten-fold greater activity than when bound to PVA at comparable concentrations. 2,2,2-trifluoroethanesulfonyl chloride 17-32 serpin family C member 1 Homo sapiens 125-137 2713428-2 1989 We found that as tresyl chloride activation of PVA increased, the specific activity of the bound heparin toward thrombin and antithrombin decreased by nearly a factor of 10 and that commercial heparin bound to PEO had nearly ten-fold greater activity than when bound to PVA at comparable concentrations. Heparin 97-104 serpin family C member 1 Homo sapiens 125-137 2713428-3 1989 These findings suggest that the long "leash" provided by PEO hydrogels may give the heparin more access to the thrombin-antithrombin pair than the tight bond to PVA, and that crowding of heparin units on a surface limits access of the thrombin-antithrombin pair. Heparin 84-91 serpin family C member 1 Homo sapiens 120-132 2713428-3 1989 These findings suggest that the long "leash" provided by PEO hydrogels may give the heparin more access to the thrombin-antithrombin pair than the tight bond to PVA, and that crowding of heparin units on a surface limits access of the thrombin-antithrombin pair. Heparin 187-194 serpin family C member 1 Homo sapiens 120-132 2917133-4 1989 The antithrombin was isolated by heparin Sepharose affinity chromatography. Heparin 33-40 serpin family C member 1 Homo sapiens 4-16 2910358-8 1989 Cell surface bound heparin was functionally active and markedly accelerated the inactivation of thrombin by antithrombin III. Heparin 19-26 serpin family C member 1 Homo sapiens 108-124 2910359-2 1989 The effects of this heparin-neutralizing protein on the interaction between antithrombin III and cultured porcine aortic endothelial cells were examined. Heparin 20-27 serpin family C member 1 Homo sapiens 76-92 2917133-4 1989 The antithrombin was isolated by heparin Sepharose affinity chromatography. Sepharose 41-50 serpin family C member 1 Homo sapiens 4-16 2910359-3 1989 Displacement of 125I-labeled antithrombin III specifically bound to endothelial cells by unlabeled histidine-rich glycoprotein was much less potent than that by unlabeled antithrombin III. Iodine-125 16-20 serpin family C member 1 Homo sapiens 29-45 2917133-7 1989 The antithrombin was further purified by chromatography on thrombin-Sepharose (to remove the normal component), reduced, S-carboxymethylated and fragmented with cyanogen bromide. Sepharose 68-77 serpin family C member 1 Homo sapiens 4-16 2917133-7 1989 The antithrombin was further purified by chromatography on thrombin-Sepharose (to remove the normal component), reduced, S-carboxymethylated and fragmented with cyanogen bromide. Cyanogen Bromide 161-177 serpin family C member 1 Homo sapiens 4-16 2910581-1 1989 We compared concentrations of antithrombin III (AT-III) in plasma, as determined by an immunological method and by a functional thrombin inhibition method, in the presence of heparin in 160 blood samples from Type I diabetics. Heparin 175-182 serpin family C member 1 Homo sapiens 30-46 2910581-1 1989 We compared concentrations of antithrombin III (AT-III) in plasma, as determined by an immunological method and by a functional thrombin inhibition method, in the presence of heparin in 160 blood samples from Type I diabetics. Heparin 175-182 serpin family C member 1 Homo sapiens 48-54 2686903-5 1989 We thus found that MD805 could be used as an anticoagulant drug when an AT III-deficient patient required anticoagulation in the extracorporeal circulation. argatroban 19-24 serpin family C member 1 Homo sapiens 72-78 2910581-6 1989 We suggest that the high concentrations of heparin cofactor II, 117 (SD 17)%, might have caused an overestimation of AT III in this group of patients with diabetes Type I, and should not be overlooked in other clinical situations. Heparin 43-50 serpin family C member 1 Homo sapiens 117-123 2483705-6 1989 The assay is based on the inactivation of factor Xa by antithrombin III which is catalysed by heparin or smaller fragments of it. Heparin 94-101 serpin family C member 1 Homo sapiens 55-71 2488845-1 1989 Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes. Heparin 0-7 serpin family C member 1 Homo sapiens 128-144 2488845-1 1989 Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes. Polyvinyl Alcohol 24-41 serpin family C member 1 Homo sapiens 128-144 2488845-1 1989 Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes. Glutaral 59-73 serpin family C member 1 Homo sapiens 128-144 2488845-1 1989 Heparin, immobilized to polyvinyl alcohol by reaction with glutaraldehyde (heparin-PVA), retained its ability to accelerate the antithrombin III inactivation of thrombin, in a recirculating flow loop using heparin-PVA coated polyethylene tubes. Heparin 75-82 serpin family C member 1 Homo sapiens 128-144 2807044-4 1989 During pyridoxine and folate treatment, antithrombin III activity rapidly returned to normal; factor VII increased and beta-thromboglobulin decreased. Pyridoxine 7-17 serpin family C member 1 Homo sapiens 40-56 2807044-4 1989 During pyridoxine and folate treatment, antithrombin III activity rapidly returned to normal; factor VII increased and beta-thromboglobulin decreased. Folic Acid 22-28 serpin family C member 1 Homo sapiens 40-56 2920976-9 1989 The low antithrombin III concentration (0.44 +/- 0.13 mg/dl) in protein-poor dialysate seems to be sufficient to inhibit the thrombin activity after acceleration by heparin. Heparin 165-172 serpin family C member 1 Homo sapiens 8-24 2488845-2 1989 The extent of inactivation, for a constant flow time, was approximately constant over ten cycles of exposure to thrombin and antithrombin III, suggesting that the immobilized heparin was reusable, as expected from the catalytic nature of non-immobilized heparin. Heparin 175-182 serpin family C member 1 Homo sapiens 125-141 2483706-0 1989 A new AT III-heparin-complex preparation: in vitro and in vivo characterisation. Heparin 13-20 serpin family C member 1 Homo sapiens 6-12 2483706-1 1989 The in vitro experiments show that the anticoagulant affect of a new AT III-Heparin-complex preparation in plasma is similar to heparin. Heparin 76-83 serpin family C member 1 Homo sapiens 69-75 2483706-1 1989 The in vitro experiments show that the anticoagulant affect of a new AT III-Heparin-complex preparation in plasma is similar to heparin. Heparin 128-135 serpin family C member 1 Homo sapiens 69-75 2562205-3 1989 The anticoagulant activity of heparin arises primarily from its ability to bind to antithrombin III (AT III), altering the conformation and enhancing the activity of this major protease inhibitor. Heparin 30-37 serpin family C member 1 Homo sapiens 83-99 2562205-3 1989 The anticoagulant activity of heparin arises primarily from its ability to bind to antithrombin III (AT III), altering the conformation and enhancing the activity of this major protease inhibitor. Heparin 30-37 serpin family C member 1 Homo sapiens 101-107 2562205-4 1989 Passage of heparin through an immobilised AT III column yields two fractions: a high affinity fraction with 300-350 iu mg-1 anticoagulant activity, comprising one-third of the total, and a low affinity fraction with an activity of less than 10 iu mg-1, comprising the remaining two-thirds. Heparin 11-18 serpin family C member 1 Homo sapiens 42-48 2562205-5 1989 Studies in several laboratories have demonstrated that a specific pentasaccharide sequence is required for AT III binding. pentasaccharide 66-81 serpin family C member 1 Homo sapiens 107-113 2922702-1 1989 Heparins from different species and tissues show similar levels of ATIII and HCII mediated anti-IIa activities. Heparin 0-8 serpin family C member 1 Homo sapiens 67-72 2522237-0 1989 Effects of high dose medroxyprogesterone acetate treatment on antithrombin III and other plasma proteins in males with renal cell or prostatic carcinoma. Medroxyprogesterone Acetate 21-48 serpin family C member 1 Homo sapiens 62-78 2522237-1 1989 In 18 patients, 12 with renal cell and 6 with prostatic carcinoma treatment with high dose medroxyprogesterone acetate (MPA) significantly increased serum antithrombin III and haptoglobin concentrations. Medroxyprogesterone Acetate 91-118 serpin family C member 1 Homo sapiens 155-171 2530427-6 1989 Antithrombin III inhibition of activated Hageman factor is augmented by heparin which is also an activator of Hageman factor. Heparin 72-79 serpin family C member 1 Homo sapiens 0-16 2922702-3 1989 Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. Oligosaccharides 0-15 serpin family C member 1 Homo sapiens 116-121 2922702-3 1989 Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. Oligosaccharides 0-15 serpin family C member 1 Homo sapiens 184-189 2922702-3 1989 Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. Oligosaccharides 66-81 serpin family C member 1 Homo sapiens 116-121 2922702-3 1989 Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. Oligosaccharides 66-81 serpin family C member 1 Homo sapiens 184-189 2922702-3 1989 Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. Heparin 106-113 serpin family C member 1 Homo sapiens 116-121 2922702-3 1989 Oligosaccharide mapping demonstrates that the concentration of an oligosaccharide comprising a portion of heparin"s ATIII binding site in a particular heparin fraction correlates with ATIII mediated anti-IIa activity, but does not correlate with HCII mediated anti-IIa activity. Heparin 106-113 serpin family C member 1 Homo sapiens 184-189 2922702-6 1989 Although oligosaccharides of degree of polymerization (dp) 18 and 20 showed significant ATIII and HCII mediated anti-IIa activities no separation of these activities resulted. Oligosaccharides 9-25 serpin family C member 1 Homo sapiens 88-93 3265623-1 1988 The effect of various well-characterized heparin preparations on the inactivation of human Factor XIa by human antithrombin III was studied. Heparin 41-48 serpin family C member 1 Homo sapiens 111-127 3238650-1 1988 Antithrombin Milano is an unusual antithrombin variant, exhibiting an abnormal, fast moving component on crossed immunoelectrophoresis (in the absence of heparin). Heparin 154-161 serpin family C member 1 Homo sapiens 0-12 3238650-5 1988 These and other results established the approximately 120,000 Mr component to be an inactive, disulphide-linked variant antithrombin and albumin complex. disulphide 94-104 serpin family C member 1 Homo sapiens 120-132 3238652-1 1988 Three patients with familial antithrombin III (ATIII) deficiency, who also have histories of thromboembolism, were treated with oxymetholone in combination with warfarin. Oxymetholone 128-140 serpin family C member 1 Homo sapiens 29-45 3238652-1 1988 Three patients with familial antithrombin III (ATIII) deficiency, who also have histories of thromboembolism, were treated with oxymetholone in combination with warfarin. Oxymetholone 128-140 serpin family C member 1 Homo sapiens 47-52 3238652-4 1988 The levels of plasma ATIII, alpha 1-antitrypsin, plasminogen and Cl-inactivator were significantly increased in all patients after the introduction of oxymetholone therapy. Oxymetholone 151-163 serpin family C member 1 Homo sapiens 21-26 3265623-0 1988 The heparin-catalysed inhibition of human factor XIa by antithrombin III is dependent on the heparin type. Heparin 4-11 serpin family C member 1 Homo sapiens 56-72 3265623-4 1988 Enhancement of the rate of inhibition of Factor XIa in the presence of unfractionated heparin correlated to the binding of antithrombin III to heparin. Heparin 86-93 serpin family C member 1 Homo sapiens 123-139 3265623-0 1988 The heparin-catalysed inhibition of human factor XIa by antithrombin III is dependent on the heparin type. Heparin 93-100 serpin family C member 1 Homo sapiens 56-72 3265623-4 1988 Enhancement of the rate of inhibition of Factor XIa in the presence of unfractionated heparin correlated to the binding of antithrombin III to heparin. Heparin 143-150 serpin family C member 1 Homo sapiens 123-139 3265623-7 1988 The rate enhancement achieved in the presence of each of the heparin fractions could also be correlated to the binding of antithrombin III to the heparin. Heparin 61-68 serpin family C member 1 Homo sapiens 122-138 3265623-8 1988 The binding constant inferred from the kinetic data varied from 0.10 to 0.28 microM and the number of binding sites for antithrombin III varied from 0.06 to 0.74 site per heparin molecule. Heparin 171-178 serpin family C member 1 Homo sapiens 120-136 2973992-1 1988 Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 X 10(7) M-1.min-1) and the prothrombinase:ATIII interaction by 2900-fold (k2, 2.5 X 10(7) M-1.min-1). Heparitin Sulfate 0-16 serpin family C member 1 Homo sapiens 56-61 3232125-1 1988 Previous theoretical and experimental evidence led to the formulation of a specific pentasaccharide structure which represents the site in heparin for binding to antithrombin III. pentasaccharide 84-99 serpin family C member 1 Homo sapiens 162-178 3232125-1 1988 Previous theoretical and experimental evidence led to the formulation of a specific pentasaccharide structure which represents the site in heparin for binding to antithrombin III. Heparin 139-146 serpin family C member 1 Homo sapiens 162-178 3232125-4 1988 Previous biochemical studies showed the 3-O-desulfated pentasaccharide to have a low affinity binding to AT III and to be devoid of the high anti-factor Xa activity characteristic of the pentasaccharide. 3-o-desulfated pentasaccharide 40-70 serpin family C member 1 Homo sapiens 105-111 2973992-4 1988 From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present. Heparitin Sulfate 36-52 serpin family C member 1 Homo sapiens 214-219 3232125-4 1988 Previous biochemical studies showed the 3-O-desulfated pentasaccharide to have a low affinity binding to AT III and to be devoid of the high anti-factor Xa activity characteristic of the pentasaccharide. pentasaccharide 55-70 serpin family C member 1 Homo sapiens 105-111 2973992-1 1988 Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 X 10(7) M-1.min-1) and the prothrombinase:ATIII interaction by 2900-fold (k2, 2.5 X 10(7) M-1.min-1). Heparitin Sulfate 0-16 serpin family C member 1 Homo sapiens 115-120 2973992-4 1988 From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present. Heparitin Sulfate 36-52 serpin family C member 1 Homo sapiens 379-395 2973992-4 1988 From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present. Heparitin Sulfate 269-285 serpin family C member 1 Homo sapiens 214-219 2973992-1 1988 Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 X 10(7) M-1.min-1) and the prothrombinase:ATIII interaction by 2900-fold (k2, 2.5 X 10(7) M-1.min-1). Heparitin Sulfate 0-16 serpin family C member 1 Homo sapiens 115-120 2973992-4 1988 From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIII interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present. Heparin 332-339 serpin family C member 1 Homo sapiens 214-219 3196877-6 1988 The inhibition of thrombin generation by the LMWH was comparable with that of standard heparin on the basis of their respective antithrombin specific activities, but not on the basis of their antifactor Xa activities. Heparin, Low-Molecular-Weight 45-49 serpin family C member 1 Homo sapiens 128-140 3266555-2 1988 Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI). chloramine-T 60-72 serpin family C member 1 Homo sapiens 196-212 3266555-2 1988 Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI). chloramine-T 60-72 serpin family C member 1 Homo sapiens 214-220 3228593-0 1988 Adjuvant tamoxifen in primary breast cancer: influence on plasma lipids and antithrombin III levels. Tamoxifen 9-18 serpin family C member 1 Homo sapiens 76-92 3266555-2 1988 Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI). chloramine-T 74-76 serpin family C member 1 Homo sapiens 196-212 3266555-2 1988 Mimicking this oxidation in normal human plasma by usage of chloramine T (CT), we observed an oxidant concentration-dependent inactivating effect on plasma alpha 2-plasmin inhibitor (alpha 2-PI), antithrombin III (AT III), and alpha 1-proteinase inhibitor (alpha 1-PI). chloramine-T 74-76 serpin family C member 1 Homo sapiens 214-220 3266555-4 1988 The inactivation of alpha 1-PI, alpha 2-PI and AT III in plasma by oxidants is the result of a specific oxidative damage since C1-inhibitor, serine proteinases and complexes of plasmin and alpha 2-PI were chloramine resistant under the conditions used. chloramine 205-215 serpin family C member 1 Homo sapiens 47-53 2464199-2 1988 In contrast to a current hypothesis the antithrombin III independent effect of PPS on blood coagulation is not caused by preventing the binding of the factors IX, IXa, X, Xa, VIII, V, Va and II onto procoagulant phospholipids. Pentosan Sulfuric Polyester 79-82 serpin family C member 1 Homo sapiens 40-56 3179438-0 1988 Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Adenine 68-75 serpin family C member 1 Homo sapiens 0-16 3179438-4 1988 Two dimensional immunoelectrophoresis of antithrombin-III-Hamilton in the presence of heparin is normal. Heparin 86-93 serpin family C member 1 Homo sapiens 41-57 3179438-9 1988 Codon 382 codes for alanine in the normal allele and for threonine in the antithrombin-III-Hamilton allele. Alanine 20-27 serpin family C member 1 Homo sapiens 74-90 3179438-9 1988 Codon 382 codes for alanine in the normal allele and for threonine in the antithrombin-III-Hamilton allele. Threonine 57-66 serpin family C member 1 Homo sapiens 74-90 3179438-11 1988 We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases. Threonine 54-63 serpin family C member 1 Homo sapiens 79-95 3179438-11 1988 We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases. Threonine 54-63 serpin family C member 1 Homo sapiens 316-332 3179438-11 1988 We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases. Alanine 68-75 serpin family C member 1 Homo sapiens 79-95 3179438-11 1988 We postulate that, as a result of the substitution of threonine for alanine in antithrombin-III-Hamilton, either the tertiary structure or the hydrophobicity of the thrombin-binding region is altered, causing aberrant conformation of the Arg-393-Ser-394 bond at the reactive center impairing the interaction between antithrombin-III-Hamilton and the activated serine proteases. Alanine 68-75 serpin family C member 1 Homo sapiens 316-332 3179448-4 1988 Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393. Oligonucleotides 46-62 serpin family C member 1 Homo sapiens 212-217 3179448-4 1988 Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393. Oligonucleotides 46-62 serpin family C member 1 Homo sapiens 292-297 3179448-4 1988 Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393. Oligonucleotides 46-61 serpin family C member 1 Homo sapiens 212-217 3179448-4 1988 Consequently, we synthesized two 22-base-long oligonucleotides specific for the single-base substitutions in the region of codon 393 and demonstrated by oligonucleotide hybridization that the molecular defect of ATIII Northwick Park is caused by the CGT----TGT mutation at codon 393 and that ATIII Glasgow is caused by the CGT----CAT mutation at codon 393. Oligonucleotides 46-61 serpin family C member 1 Homo sapiens 292-297 3179448-5 1988 These oligonucleotide probes should prove useful as an alternative method for early detection of the ATIII variants. Oligonucleotides 6-21 serpin family C member 1 Homo sapiens 101-106 2851191-6 1988 This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma. Glycosaminoglycans 27-44 serpin family C member 1 Homo sapiens 193-209 2851191-6 1988 This concentration of each glycosaminoglycan completely inhibited prothrombin activation for 45 s after CaCl2 was added to contact-activated plasma; accelerated thrombin inhibition by purified antithrombin III by approximately 50-fold; and accelerated thrombin inhibition equally by antithrombin III in undiluted plasma. Glycosaminoglycans 27-44 serpin family C member 1 Homo sapiens 283-299 2851191-7 1988 This concentration of the three LMW heparins increased, by approximately 70-fold, the rate of factor Xa inhibition by purified antithrombin III compared to the 50-fold increase seen with the two unfractionated heparins. Heparin, Low-Molecular-Weight 32-44 serpin family C member 1 Homo sapiens 127-143 2851191-7 1988 This concentration of the three LMW heparins increased, by approximately 70-fold, the rate of factor Xa inhibition by purified antithrombin III compared to the 50-fold increase seen with the two unfractionated heparins. Heparin 36-44 serpin family C member 1 Homo sapiens 127-143 3186090-2 1988 The purpose of this study was to evaluate the relationship between plasma antithrombin III activity and both clotting parameters (platelet count and fibrinopeptide A) and renal parameters (serum creatinine and uric acid concentration). Creatinine 195-205 serpin family C member 1 Homo sapiens 74-90 3186090-2 1988 The purpose of this study was to evaluate the relationship between plasma antithrombin III activity and both clotting parameters (platelet count and fibrinopeptide A) and renal parameters (serum creatinine and uric acid concentration). Uric Acid 210-219 serpin family C member 1 Homo sapiens 74-90 3179438-0 1988 Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity. Guanine 57-64 serpin family C member 1 Homo sapiens 0-16 3183496-7 1988 Heparin recovery in cord plasma was significantly improved by raising the AT-III concentration to normal adult levels in both assays. Heparin 0-7 serpin family C member 1 Homo sapiens 74-80 3186758-7 1988 The model accounted for enzymatic degradation as well as the binding of heparin and its breakdown products to antithrombin. Heparin 72-79 serpin family C member 1 Homo sapiens 110-122 2464199-11 1988 We postulate therefore that the antithrombin III independent inhibitory effect of PPS on thrombin generation on blood coagulation is by interaction with factor VIIIa. Pentosan Sulfuric Polyester 82-85 serpin family C member 1 Homo sapiens 32-48 3262615-11 1988 Unfractionated heparin (1 micrograms/ml) stimulated the antithrombin III-dependent inhibition of factor IXa during factor X activation 400-fold. Heparin 15-22 serpin family C member 1 Homo sapiens 56-72 2464199-12 1988 This effect is additional to the heparin-like action of PPS, i.e. potentiation of the activity of antithrombin III and/or heparin cofactor II. Heparin 33-40 serpin family C member 1 Homo sapiens 98-114 2464199-12 1988 This effect is additional to the heparin-like action of PPS, i.e. potentiation of the activity of antithrombin III and/or heparin cofactor II. Pentosan Sulfuric Polyester 56-59 serpin family C member 1 Homo sapiens 98-114 3201396-7 1988 Calcium (1 mM) increased the inhibition reaction rates of native and modified forms of factor Xa with antithrombin III by 20-30%. Calcium 0-7 serpin family C member 1 Homo sapiens 102-118 3218731-0 1988 Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin. Heparin 33-41 serpin family C member 1 Homo sapiens 115-131 3218731-0 1988 Measurement of the affinities of heparins, naturally occurring glycosaminoglycans, and other sulfated polymers for antithrombin III and thrombin. Glycosaminoglycans 63-81 serpin family C member 1 Homo sapiens 115-131 3218731-3 1988 This has been used to compare the binding of a range of glycosaminoglycans and other sulfated polymers to antithrombin III and thrombin, a major inhibitor of and a central protease in the coagulation system, respectively. Glycosaminoglycans 56-74 serpin family C member 1 Homo sapiens 106-122 3218731-3 1988 This has been used to compare the binding of a range of glycosaminoglycans and other sulfated polymers to antithrombin III and thrombin, a major inhibitor of and a central protease in the coagulation system, respectively. Polymers 94-102 serpin family C member 1 Homo sapiens 106-122 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. Glycosaminoglycans 67-85 serpin family C member 1 Homo sapiens 89-105 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. Glycosaminoglycans 67-85 serpin family C member 1 Homo sapiens 138-154 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. pentasaccharide 163-178 serpin family C member 1 Homo sapiens 89-105 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. pentasaccharide 163-178 serpin family C member 1 Homo sapiens 138-154 3218731-4 1988 The results are consistent with the binding of naturally occurring glycosaminoglycans to antithrombin III solely through the well-defined antithrombin III-binding pentasaccharide found in heparin, the apparent affinity of a preparation depending upon its content of this pentasaccharide. pentasaccharide 271-286 serpin family C member 1 Homo sapiens 89-105 3218731-5 1988 Highly sulfated synthetic polymers will, however, bind antithrombin III by a second mechanism. Polymers 26-34 serpin family C member 1 Homo sapiens 55-71 3169017-2 1988 A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups. pentasaccharide 12-27 serpin family C member 1 Homo sapiens 108-124 3169017-2 1988 A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups. Heparin 70-77 serpin family C member 1 Homo sapiens 108-124 3169017-2 1988 A synthetic pentasaccharide corresponding to the sequence involved in heparin for binding and activation of antithrombin III contains eight sulfate groups. Sulfates 140-147 serpin family C member 1 Homo sapiens 108-124 3169017-6 1988 This suggests that they belong to a secondary sub-region of interaction with antithrombin III, the primary one being accounted for by other critical parts of the structure and particularly the trisaccharide sequence placed at the non-reducing end of the pentasaccharide. Trisaccharides 193-206 serpin family C member 1 Homo sapiens 77-93 3169017-6 1988 This suggests that they belong to a secondary sub-region of interaction with antithrombin III, the primary one being accounted for by other critical parts of the structure and particularly the trisaccharide sequence placed at the non-reducing end of the pentasaccharide. pentasaccharide 254-269 serpin family C member 1 Homo sapiens 77-93 3169232-0 1988 New carbohydrate site in mutant antithrombin (7 Ile----Asn) with decreased heparin affinity. Heparin 75-82 serpin family C member 1 Homo sapiens 32-44 3169238-0 1988 Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II. Phosphates 43-52 serpin family C member 1 Homo sapiens 0-12 3187966-0 1988 Prevention of thrombin/antithrombin III reaction in the presence of protamine or polybrene. Hexadimethrine Bromide 81-90 serpin family C member 1 Homo sapiens 23-39 3187966-1 1988 The rate of the thrombin/antithrombin III (AT III) reaction was decreased in the presence of free polybrene or protamine. Hexadimethrine Bromide 98-107 serpin family C member 1 Homo sapiens 16-41 3169238-0 1988 Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II. polyanions 64-74 serpin family C member 1 Homo sapiens 0-12 3187966-1 1988 The rate of the thrombin/antithrombin III (AT III) reaction was decreased in the presence of free polybrene or protamine. Hexadimethrine Bromide 98-107 serpin family C member 1 Homo sapiens 43-49 3187966-3 1988 The reaction was also prevented when either thrombin or AT III was transferred into noncoated tubes after instantaneous contact with protamine-coated tubes or tubes with polybrene. Hexadimethrine Bromide 170-179 serpin family C member 1 Homo sapiens 56-62 3169238-1 1988 We have examined the antithrombin effects of various phosphate-containing polyanions (including linear polyphosphates, polynucleotides and the phosphoserine glycoprotein, phosvitin) on the glycosaminoglycan-binding plasma proteinase inhibitors, antithrombin III (ATIII) and heparin cofactor II (HCII). Phosphates 53-62 serpin family C member 1 Homo sapiens 21-33 3169238-1 1988 We have examined the antithrombin effects of various phosphate-containing polyanions (including linear polyphosphates, polynucleotides and the phosphoserine glycoprotein, phosvitin) on the glycosaminoglycan-binding plasma proteinase inhibitors, antithrombin III (ATIII) and heparin cofactor II (HCII). polyanions 74-84 serpin family C member 1 Homo sapiens 21-33 2458152-9 1988 Both non-disulfide-bonded and disulfide-bonded vitronectin bound to antibody-Sepharose from a mixture of vitronectin and thrombin-antithrombin III. Disulfides 30-39 serpin family C member 1 Homo sapiens 130-146 2458152-12 1988 The change in vitronectin induced by thrombin-antithrombin III, therefore, is a physiological correlate of urea treatment and of adsorption of vitronectin onto tissue culture plastic (as is done in cell adhesion assays). Urea 107-111 serpin family C member 1 Homo sapiens 46-62 2902851-0 1988 Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II. Chondroitin 24-35 serpin family C member 1 Homo sapiens 102-118 3060987-1 1988 The effect on plasma antithrombin III (AT III) and protein C on a supplement with polyunsaturated fatty acids (PUFA"s) was investigated in a double-blind study in 36 patients with stable angina pectoris. Fatty Acids, Unsaturated 82-109 serpin family C member 1 Homo sapiens 21-37 2902851-0 1988 Effect of oversulphated chondroitin and dermatan sulphate upon thrombin and factor Xa inactivation by antithrombin III or heparin cofactor II. Dermatan Sulfate 40-57 serpin family C member 1 Homo sapiens 102-118 2902851-6 1988 The antithrombin III-Factor Xa interaction was potentiated by all other GAGs studied to a degree similar to that of heparin pentasaccharide with high affinity for antithrombin III. IC 831423 116-139 serpin family C member 1 Homo sapiens 4-20 2902851-6 1988 The antithrombin III-Factor Xa interaction was potentiated by all other GAGs studied to a degree similar to that of heparin pentasaccharide with high affinity for antithrombin III. IC 831423 116-139 serpin family C member 1 Homo sapiens 163-179 3224125-5 1988 Desorption of proteins from the polymeric interface by means of polycations (polybrene and polylysine) showed that the inactive complex T-AT is more quantitatively and easily released than thrombin. Hexadimethrine Bromide 77-86 serpin family C member 1 Homo sapiens 138-140 3224125-5 1988 Desorption of proteins from the polymeric interface by means of polycations (polybrene and polylysine) showed that the inactive complex T-AT is more quantitatively and easily released than thrombin. Polylysine 91-101 serpin family C member 1 Homo sapiens 138-140 3224126-4 1988 In order to ascertain the heparin-like mechanism of this activity, we have studied the interactions of thrombin, antithrombin III and thrombin-antithrombin III complex with the inner face of these treated tubings under controlled-flow conditions. Heparin 26-33 serpin family C member 1 Homo sapiens 143-159 3060987-3 1988 Both oil supplements resulted in a statistically significant decrease in AT III activity, but there were no differences between the two different types of PUFA"s. Oils 5-8 serpin family C member 1 Homo sapiens 73-79 3246651-0 1988 [Interaction between oleic acid and human antithrombin III]. Oleic Acid 21-31 serpin family C member 1 Homo sapiens 42-58 3191114-7 1988 Proline-407 is located 14 amino acids C-terminal to the reactive site arginine of ATIII in a core region of the molecule that has been highly conserved during evolution of the serine protease inhibitor (serpin) gene family. Proline 0-7 serpin family C member 1 Homo sapiens 82-87 3246652-0 1988 [Effect of various kinds of fatty acids on the human antithrombin III activity]. Fatty Acids 28-39 serpin family C member 1 Homo sapiens 53-69 3208245-0 1988 Binding of heparin to antithrombin III: a chemical proof of the critical role played by a 3-sulfated 2-amino-2-deoxy-D-glucose residue. Glucosamine 101-126 serpin family C member 1 Homo sapiens 22-38 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 13-19 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187949-3 1988 Out of the 8 AT III variants investigated, 6 had an abnormal pattern: the three variants with defective binding to heparin (AT III Roma, AT III Barcelona, AT III Malmo) shared a similar abnormal pattern; three variants with defective binding to serine proteases (AT III Pescara, AT III Milano, AT III Tampere) had a common abnormal pattern clearly different from the first one, whereas the other two variants deficient in the inactivation of the serine proteases (AT III Chicago, AT III Milano 2) showed a normal pattern. Heparin 115-122 serpin family C member 1 Homo sapiens 124-130 3187951-1 1988 A decreased plasma antithrombin activity in presence or in absence of heparin was discovered in a 47-year-old patient presenting with recurrent venous thromboembolism. Heparin 70-77 serpin family C member 1 Homo sapiens 19-31 3187951-4 1988 The propositus" AT III was coeluted with normal AT III from an heparin-sepharose column. Heparin 63-70 serpin family C member 1 Homo sapiens 16-22 3187951-4 1988 The propositus" AT III was coeluted with normal AT III from an heparin-sepharose column. Sepharose 71-80 serpin family C member 1 Homo sapiens 16-22 3187951-7 1988 The specific activities measured as heparin cofactor antithrombin or factor Xa inhibition in absence of heparin were decreased to half the normal value. Heparin 36-43 serpin family C member 1 Homo sapiens 53-65 3187951-9 1988 SDS-PAGE experiments performed in purified system and immunoblots obtained from plasma showed that the two variants have different behaviour: in the case of AT III Charleville thrombin induced an apparent 5 k delta increase in molecular mass, probably due to a conformational change. Sodium Dodecyl Sulfate 0-3 serpin family C member 1 Homo sapiens 157-163 3401503-2 1988 A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III). Heparin 31-38 serpin family C member 1 Homo sapiens 195-211 3401503-2 1988 A series of well characterized heparin derivatives were prepared and their activities were measured using human thrombin in the presence of an excess of purified human HC II and, for comparison, antithrombin III (AT III). Heparin 31-38 serpin family C member 1 Homo sapiens 213-219 3191114-7 1988 Proline-407 is located 14 amino acids C-terminal to the reactive site arginine of ATIII in a core region of the molecule that has been highly conserved during evolution of the serine protease inhibitor (serpin) gene family. Arginine 70-78 serpin family C member 1 Homo sapiens 82-87 3191114-8 1988 The location of this proline in the crystal structure of the homologous serpin alpha 1-antitrypsin suggests that the leucine substitution in ATIII-Utah may interfere with correct folding of the mutant gene product, leading to its rapid turnover and the low antithrombin levels observed in patient plasmas. Proline 21-28 serpin family C member 1 Homo sapiens 141-146 3191114-8 1988 The location of this proline in the crystal structure of the homologous serpin alpha 1-antitrypsin suggests that the leucine substitution in ATIII-Utah may interfere with correct folding of the mutant gene product, leading to its rapid turnover and the low antithrombin levels observed in patient plasmas. Proline 21-28 serpin family C member 1 Homo sapiens 257-269 3191114-10 1988 Patient antithrombin III, isolated by affinity chromatography on heparin-Sepharose, was reacted with purified thrombin. Heparin 65-72 serpin family C member 1 Homo sapiens 8-24 3191114-10 1988 Patient antithrombin III, isolated by affinity chromatography on heparin-Sepharose, was reacted with purified thrombin. Sepharose 73-82 serpin family C member 1 Homo sapiens 8-24 3215905-1 1988 The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels. Heparin 56-63 serpin family C member 1 Homo sapiens 34-50 3408687-7 1988 Moreover, the unexpectedly normal level of AT III provides a theoretical basis for the use of heparin to enhance the inactivation of those serine proteases present before antivenom administration. Heparin 94-101 serpin family C member 1 Homo sapiens 43-49 3391345-0 1988 Demonstration of altered antithrombin III activity due to nonenzymatic glycosylation at glucose concentration expected to be encountered in severely diabetic patients. Glucose 88-95 serpin family C member 1 Homo sapiens 25-41 3391345-7 1988 On the basis of these data, it is concluded that glycosylated antithrombin III with 50% depressed heparin cofactor activity is three times weaker than normal antithrombin III as an inhibitor of thrombin. Heparin 98-105 serpin family C member 1 Homo sapiens 62-78 3215905-0 1988 Permeability of a heparin-polyvinyl alcohol hydrogel to thrombin and antithrombin III. Heparin 18-25 serpin family C member 1 Homo sapiens 69-85 3215905-1 1988 The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels. Polyvinyl Alcohol 64-81 serpin family C member 1 Homo sapiens 34-50 3215905-0 1988 Permeability of a heparin-polyvinyl alcohol hydrogel to thrombin and antithrombin III. Polyvinyl Alcohol 26-43 serpin family C member 1 Homo sapiens 69-85 3215905-1 1988 The diffusivities of thrombin and antithrombin III in a heparin-polyvinyl alcohol hydrogel were estimated and used to demonstrate that diffusion limits the effectiveness of the immobilized heparin in the interior of such hydrogels. Heparin 189-196 serpin family C member 1 Homo sapiens 34-50 3413737-4 1988 Two populations of ATIII were detected by affinity chromatography on heparin-sepharose from affected members" plasma. Heparin 69-76 serpin family C member 1 Homo sapiens 19-24 2973155-1 1988 Recent evidence suggests that heparan sulfate on endothelial cell surfaces acts as a catalyst for the neutralization of thrombin by antithrombin III (AT III). Heparitin Sulfate 30-45 serpin family C member 1 Homo sapiens 132-148 2855291-0 1988 [Effect of antithrombin III on the binding of heparin and its low molecular weight fraction CY 216 with endothelium in vitro]. Heparin 46-53 serpin family C member 1 Homo sapiens 11-27 3413737-8 1988 This is the first reported ATIII variant in which a molecular abnormality produces a lack of affinity for heparin but no changes in its isoelectric point. Heparin 106-113 serpin family C member 1 Homo sapiens 27-32 2973155-1 1988 Recent evidence suggests that heparan sulfate on endothelial cell surfaces acts as a catalyst for the neutralization of thrombin by antithrombin III (AT III). Heparitin Sulfate 30-45 serpin family C member 1 Homo sapiens 150-156 2973155-3 1988 We evaluated the ability of cultured human fibroblasts to catalyze the interaction between thrombin and AT III and found that heparan sulfate produced by post-confluent fibroblasts was anticoagulantly active. Heparitin Sulfate 126-141 serpin family C member 1 Homo sapiens 104-110 2973155-5 1988 These results indicate that fibroblasts do produce an anticoagulantly active species of heparan sulfate and that the normal interaction between AT III and thrombin may be driven by initial release of heparan sulfate from the cell surface by thrombin followed by AT III interaction with the soluble thrombin-heparan sulfate complex. Heparitin Sulfate 200-215 serpin family C member 1 Homo sapiens 144-150 2973155-5 1988 These results indicate that fibroblasts do produce an anticoagulantly active species of heparan sulfate and that the normal interaction between AT III and thrombin may be driven by initial release of heparan sulfate from the cell surface by thrombin followed by AT III interaction with the soluble thrombin-heparan sulfate complex. Heparitin Sulfate 200-215 serpin family C member 1 Homo sapiens 144-150 2455567-1 1988 Vitronectin, also known as serum-spreading factor or S-protein, mediates cell adhesion and inhibits formation of the membrane-lytic complex of complement and the rapid inactivation of thrombin by antithrombin III in the presence of heparin. Heparin 232-239 serpin family C member 1 Homo sapiens 196-212 3413737-4 1988 Two populations of ATIII were detected by affinity chromatography on heparin-sepharose from affected members" plasma. Sepharose 77-86 serpin family C member 1 Homo sapiens 19-24 3413737-5 1988 The ATIII unbound to sepharose beads was devoid of heparin cofactor activity and showed a lack of anodal migration in CIE in the presence of heparin. Sepharose 21-30 serpin family C member 1 Homo sapiens 4-9 3410869-6 1988 We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface. Heparin 50-57 serpin family C member 1 Homo sapiens 98-114 3055413-3 1988 An abnormal cathodal peak of antithrombin antigen was found in the presence, but not the absence, of heparin in the first dimension gel. Heparin 101-108 serpin family C member 1 Homo sapiens 29-41 3410869-6 1988 We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface. Heparin 160-167 serpin family C member 1 Homo sapiens 98-114 3410869-6 1988 We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface. Heparin 160-167 serpin family C member 1 Homo sapiens 98-114 3410869-6 1988 We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface. Heparin 160-167 serpin family C member 1 Homo sapiens 98-114 3410869-6 1988 We conclude that: 1) a kinetic assay based on the heparin accelerated inactivation of thrombin by antithrombin III can be used to estimate the amount of active heparin bound to a catheter surface, and 2) thrombin uptake studies do not correlate with heparin activity and do not predict which heparin binding method will result in the highest concentration of active heparin on the catheter surface. Heparin 160-167 serpin family C member 1 Homo sapiens 98-114 3162733-1 1988 Congenital substitution of arginine 393 to cysteine in antithrombin Northwick Park and to histidine in antithrombin Glasgow. Histidine 90-99 serpin family C member 1 Homo sapiens 103-115 3377765-2 1988 The resulting oligosaccharides were fractionated by gel filtration chromatography and tested for the ability to stimulate inhibition of thrombin by purified heparin cofactor II or antithrombin. Oligosaccharides 14-30 serpin family C member 1 Homo sapiens 180-192 3377765-3 1988 Oligosaccharides containing greater than or equal to 18 monosaccharide units were active with antithrombin, while larger oligosaccharides were required for activity with heparin cofactor II. Oligosaccharides 0-16 serpin family C member 1 Homo sapiens 94-106 3377765-3 1988 Oligosaccharides containing greater than or equal to 18 monosaccharide units were active with antithrombin, while larger oligosaccharides were required for activity with heparin cofactor II. Monosaccharides 56-70 serpin family C member 1 Homo sapiens 94-106 3377765-5 1988 The relative specific activities of the unbound heparin molecules were 0.06 with antithrombin and 0.76 with heparin cofactor II in comparison to unfractionated heparin (specific activity = 1.00). Heparin 48-55 serpin family C member 1 Homo sapiens 81-93 3414028-0 1988 [Blood antithrombin III levels after prolonged administration of heparin]. Heparin 65-72 serpin family C member 1 Homo sapiens 7-23 3360140-0 1988 Antithrombin Glasgow, 393 Arg to His: a P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity. Heparin 80-87 serpin family C member 1 Homo sapiens 0-12 3408716-2 1988 These forms have two chains disulfide linked and are of the same molecular weight as native antithrombin III. Disulfides 28-37 serpin family C member 1 Homo sapiens 92-108 3408716-3 1988 1H NMR spectroscopy has been used to characterize these proteins and to compare them to one another and to native antithrombin III. Hydrogen 0-2 serpin family C member 1 Homo sapiens 114-130 3162733-5 1988 Following treatment of these pools with trypsin, fast atom bombardment mass spectrometry identified tryptic peptides (found also in normal antithrombin treated in the same way) that corresponded to amino acid sequences Gly339-Lys370 and Val400-Met423. Peptides 108-116 serpin family C member 1 Homo sapiens 139-151 3360140-3 1988 Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl. Heparin 52-59 serpin family C member 1 Homo sapiens 0-12 3360140-3 1988 Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl. Sepharose 60-69 serpin family C member 1 Homo sapiens 0-12 3162733-6 1988 The tryptic peptides, corresponding to amino acid sequences Ala371-Arg393 and Ser394-Arg399 were present in both variant preparations in greatly reduced amounts compared to a normal antithrombin preparation. Peptides 12-20 serpin family C member 1 Homo sapiens 182-194 3360140-3 1988 Antithrombin Glasgow was purified from plasma using heparin-Sepharose chromatography at pH 7.4 eluting with increasing concentrations of NaCl. Sodium Chloride 137-141 serpin family C member 1 Homo sapiens 0-12 3360140-9 1988 The findings suggest that heparin, on binding, interacts indirectly with the reactive centre region of antithrombin. Heparin 26-33 serpin family C member 1 Homo sapiens 103-115 3162733-7 1988 However, two novel tryptic peptides of molecular mass (M + H)+ 2976 and 2952 were identified in the digests of antithrombin Northwick Park and Glasgow, respectively. Peptides 27-35 serpin family C member 1 Homo sapiens 111-123 3363529-5 1988 Affinity adsorption of affected members" plasma to heparin-sepharose beads revealed one population of ATIII in the supernatant corresponding to the abnormal ATIII, devoid of heparin cofactor activity and showing a peak between pH range: 4.6-4.8 in CIEF. Heparin 51-58 serpin family C member 1 Homo sapiens 102-107 3260695-1 1988 Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction. Arginine 51-59 serpin family C member 1 Homo sapiens 0-16 3260695-1 1988 Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction. Arginine 51-59 serpin family C member 1 Homo sapiens 18-24 3260695-1 1988 Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction. Serine 60-66 serpin family C member 1 Homo sapiens 0-16 3260695-1 1988 Antithrombin III (AT III) inhibits thrombin via an arginine-serine interaction. Serine 60-66 serpin family C member 1 Homo sapiens 18-24 3345487-4 1988 The reduced antithrombin III activity previously described in patients receiving tamoxifen for metastatic breast cancer may reflect disease activity rather than a direct effect of tamoxifen on blood coagulation. Tamoxifen 81-90 serpin family C member 1 Homo sapiens 12-28 2969081-5 1988 In the presence of antithrombin III, thrombin action on adenylate cyclase was blocked by unfractionated and high molecular weight heparin at 0.1 microgram/ml. Heparin 130-137 serpin family C member 1 Homo sapiens 19-35 2969081-8 1988 The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III. Heparin 23-31 serpin family C member 1 Homo sapiens 284-300 2969081-8 1988 The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III. Epinephrine 76-86 serpin family C member 1 Homo sapiens 284-300 2969081-8 1988 The data indicate that heparins discriminate platelet activating factor and adrenaline-induced inhibition of adenylate cyclase from the inhibitory action of thrombin and delineate different structural requirements for the interaction of heparins with the adenylate cyclase system and antithrombin III. Heparin 237-245 serpin family C member 1 Homo sapiens 284-300 3044341-3 1988 The AT III expression vectors carrying the hCMV enhancer were used to establish stable BHK cell-lines by a new and fast G418/methotrexate selection protocol, which express up to 12 micrograms AT III/10(6) cells/24h after 40-50 days. antibiotic G 418 120-124 serpin family C member 1 Homo sapiens 4-10 3044341-3 1988 The AT III expression vectors carrying the hCMV enhancer were used to establish stable BHK cell-lines by a new and fast G418/methotrexate selection protocol, which express up to 12 micrograms AT III/10(6) cells/24h after 40-50 days. Methotrexate 125-137 serpin family C member 1 Homo sapiens 4-10 3400080-4 1988 Our results suggested that heparin-like glycosaminoglycans on endothelial cells play as important a role as heparin does in the regulation of antithrombin activity. Glycosaminoglycans 40-58 serpin family C member 1 Homo sapiens 142-154 3400080-4 1988 Our results suggested that heparin-like glycosaminoglycans on endothelial cells play as important a role as heparin does in the regulation of antithrombin activity. Heparin 27-34 serpin family C member 1 Homo sapiens 142-154 3349100-2 1988 AT-III, isolated from normal human plasma by means of heparin affinity and ion-exchange chromatography, was incubated with 0-0.5 M glucose in neutral phosphate buffer at 37 degrees C. The extent of non-enzymatic glycation could be monitored by uptake of radioactivity as well as by binding to a phenylboronate affinity resin, which effectively retards AT-III containing ketoamine-linked glucose. Glucose 131-138 serpin family C member 1 Homo sapiens 0-6 3349100-6 1988 Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule. Carbon-14 27-30 serpin family C member 1 Homo sapiens 123-129 3349100-6 1988 Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule. Glucose 31-38 serpin family C member 1 Homo sapiens 123-129 3349100-6 1988 Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule. Cyanogen Bromide 63-79 serpin family C member 1 Homo sapiens 123-129 3349100-6 1988 Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule. Carbon-14 147-150 serpin family C member 1 Homo sapiens 123-129 3349100-6 1988 Following incubation with [14C]glucose, structural analyses of cyanogen-bromide-cleaved peptides of enzymatically glycated AT-III showed that the [14C]glucose adducts were distributed over many sites on the molecule. Glucose 151-158 serpin family C member 1 Homo sapiens 123-129 3348170-6 1988 After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference. Sodium Nitrite 6-11 serpin family C member 1 Homo sapiens 108-114 3348170-6 1988 After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference. Dermatan Sulfate 37-39 serpin family C member 1 Homo sapiens 108-114 3348170-6 1988 After NaNO2/acetic acid treatment of DS (to inactivate heparin), there was enough residual heparin to cause AT-III interference. Heparin 91-98 serpin family C member 1 Homo sapiens 108-114 3348170-8 1988 With commercially available reagents, both NaNO2/acetic acid treatment of DS and anti-AT-III treatment of plasma were needed to eliminate heparin/AT-III interference. Acetic Acid 49-60 serpin family C member 1 Homo sapiens 146-152 3383824-5 1988 Negative associations between alcohol, fibrinogen and antithrombin III and positive associations between fibre, polyunsaturated fat and antithrombin III are of possible clinical or public health importance. Alcohols 30-37 serpin family C member 1 Homo sapiens 54-70 3363529-5 1988 Affinity adsorption of affected members" plasma to heparin-sepharose beads revealed one population of ATIII in the supernatant corresponding to the abnormal ATIII, devoid of heparin cofactor activity and showing a peak between pH range: 4.6-4.8 in CIEF. Sepharose 59-68 serpin family C member 1 Homo sapiens 102-107 3363529-5 1988 Affinity adsorption of affected members" plasma to heparin-sepharose beads revealed one population of ATIII in the supernatant corresponding to the abnormal ATIII, devoid of heparin cofactor activity and showing a peak between pH range: 4.6-4.8 in CIEF. Heparin 174-181 serpin family C member 1 Homo sapiens 102-107 3363529-5 1988 Affinity adsorption of affected members" plasma to heparin-sepharose beads revealed one population of ATIII in the supernatant corresponding to the abnormal ATIII, devoid of heparin cofactor activity and showing a peak between pH range: 4.6-4.8 in CIEF. cief 248-252 serpin family C member 1 Homo sapiens 102-107 3363529-8 1988 This abnormal ATIII was characterized by a lack of affinity for heparin. Heparin 64-71 serpin family C member 1 Homo sapiens 14-19 3349502-0 1988 Synthesis of methyl glycoside derivatives of tri- and penta-saccharides related to the antithrombin III-binding sequence of heparin, employing cellobiose as a key starting-material. Methylglycosides 13-29 serpin family C member 1 Homo sapiens 87-103 3339006-0 1988 Behavior of antithrombin III isoforms on immobilized heparins. Heparin 53-61 serpin family C member 1 Homo sapiens 12-28 3339006-2 1988 Antithrombin III exists in plasma as major and minor isoforms differing in affinity for heparin. Heparin 88-95 serpin family C member 1 Homo sapiens 0-16 3339006-7 1988 Because the modified lower-affinity isoform eluted with the similarly sized bovine serum albumin in these experiments, the difference in isoform affinity for heparin appears to be the result of a unique, secondary heparin-binding site in the higher-affinity isoform that can bind a heparin site with low affinity for antithrombin III. Heparin 158-165 serpin family C member 1 Homo sapiens 317-333 3339006-7 1988 Because the modified lower-affinity isoform eluted with the similarly sized bovine serum albumin in these experiments, the difference in isoform affinity for heparin appears to be the result of a unique, secondary heparin-binding site in the higher-affinity isoform that can bind a heparin site with low affinity for antithrombin III. Heparin 214-221 serpin family C member 1 Homo sapiens 317-333 3339006-7 1988 Because the modified lower-affinity isoform eluted with the similarly sized bovine serum albumin in these experiments, the difference in isoform affinity for heparin appears to be the result of a unique, secondary heparin-binding site in the higher-affinity isoform that can bind a heparin site with low affinity for antithrombin III. Heparin 214-221 serpin family C member 1 Homo sapiens 317-333 3339006-11 1988 A general model of heparin-antithrombin III interaction is proposed in which a high-affinity heparin site initially interacts with a primary site on antithrombin III. Heparin 19-26 serpin family C member 1 Homo sapiens 27-43 3339006-11 1988 A general model of heparin-antithrombin III interaction is proposed in which a high-affinity heparin site initially interacts with a primary site on antithrombin III. Heparin 19-26 serpin family C member 1 Homo sapiens 149-165 3339006-12 1988 The subsequent conformational change leads to a cooperative, entropy-driven association between secondary sites on the protein and low-affinity sites on heparin, stabilizing antithrombin III in its activated form. Heparin 153-160 serpin family C member 1 Homo sapiens 174-190 3349502-0 1988 Synthesis of methyl glycoside derivatives of tri- and penta-saccharides related to the antithrombin III-binding sequence of heparin, employing cellobiose as a key starting-material. tri- and penta-saccharides 45-71 serpin family C member 1 Homo sapiens 87-103 3349502-6 1988 The pentasaccharide 3 binds strongly to antithrombin III with an association constant almost equivalent to that of high-affinity heparin, but the trisaccharide 4 appears not to bind. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 40-56 3178141-3 1988 Genetically determined structural polymorphism of antithrombin III has been observed using ultra narrow pH polyacrylamide isoelectric focusing gels, followed by immunoblotting. polyacrylamide 107-121 serpin family C member 1 Homo sapiens 50-66 2459037-1 1988 The effect of hirudin and heparin on thrombin-induced consumption of antithrombin III, fibrinogen and platelets was studied in a rat model. Heparin 26-33 serpin family C member 1 Homo sapiens 69-85 2962557-3 1988 Antithrombin III inhibits the serine proteases (factors II, IX, X, XI, and XII); its anticoagulant action is dramatically enhanced by heparin. Heparin 134-141 serpin family C member 1 Homo sapiens 0-16 3349123-1 1988 Heparin-like materials, characterized by a defined superficial density of functional groups which activate antithrombin III (AT III), when in contact with blood specifically inhibit thrombin as soon as it appears. Heparin 0-7 serpin family C member 1 Homo sapiens 107-123 3349123-1 1988 Heparin-like materials, characterized by a defined superficial density of functional groups which activate antithrombin III (AT III), when in contact with blood specifically inhibit thrombin as soon as it appears. Heparin 0-7 serpin family C member 1 Homo sapiens 125-131 3342861-0 1988 Correlation between plasma levels of selenium and antithrombin-III. Selenium 37-45 serpin family C member 1 Homo sapiens 50-66 3342861-2 1988 Patients and controls showed a positive correlation between AT-III and selenium levels (r = 0.27, p = 0.015). Selenium 71-79 serpin family C member 1 Homo sapiens 60-66 3342861-5 1988 The increased AT-III levels were correlated with the use of warfarin and beta blockers in the patients, but these drugs could not explain the comparatively low selenium levels in the patients. Warfarin 60-68 serpin family C member 1 Homo sapiens 14-20 3342861-9 1988 The relation between AT-III and selenium should be further evaluated. Selenium 32-40 serpin family C member 1 Homo sapiens 21-27 2465218-3 1988 The authors observed 5 patients with severe AT III decrease type I, 3 with functional abnormality and 2 with a pathological heparin binding. Heparin 124-131 serpin family C member 1 Homo sapiens 44-50 2465220-0 1988 Investigations of antithrombin III-activity in patients after myocardial infarction and a long-term coumarin therapy. coumarin 100-108 serpin family C member 1 Homo sapiens 18-34 2465220-5 1988 However, we were unable to confirm the comparatively marked increase AT III for dicoumarol treatment found by Roka and Bleyl. Dicumarol 80-90 serpin family C member 1 Homo sapiens 69-75 2465220-7 1988 Our values of the mean AT III-activity were in the lower normal range for patients with long-term coumarin therapy. coumarin 98-106 serpin family C member 1 Homo sapiens 23-29 3166432-12 1988 At 5 U/ml (approximately 8.6 x 10(-8) M) antithrombin III markedly inhibited contractions of basilar arteries to prostaglandin E2 but had no effect of contractions elicited by 10(-6) M serotonin in the umbilical artery, nor did aprotinin (5 x 10(-4) M). Dinoprostone 113-129 serpin family C member 1 Homo sapiens 41-57 3335825-8 1988 The titer of antithrombin III was reduced in the group given 20 micrograms ethinyl estradiol, but not in the groups given 5 or 10 micrograms. Ethinyl Estradiol 75-92 serpin family C member 1 Homo sapiens 13-29 3166432-12 1988 At 5 U/ml (approximately 8.6 x 10(-8) M) antithrombin III markedly inhibited contractions of basilar arteries to prostaglandin E2 but had no effect of contractions elicited by 10(-6) M serotonin in the umbilical artery, nor did aprotinin (5 x 10(-4) M). Serotonin 185-194 serpin family C member 1 Homo sapiens 41-57 3280421-10 1988 Antithrombin III can be isolated by linkage to its cofactor, heparin, on heparin-Sepharose. Heparin 61-68 serpin family C member 1 Homo sapiens 0-16 3280421-10 1988 Antithrombin III can be isolated by linkage to its cofactor, heparin, on heparin-Sepharose. Heparin 73-80 serpin family C member 1 Homo sapiens 0-16 3280421-10 1988 Antithrombin III can be isolated by linkage to its cofactor, heparin, on heparin-Sepharose. Sepharose 81-90 serpin family C member 1 Homo sapiens 0-16 2840374-5 1988 Studying the ADP-induced fibrinogen binding to platelets in vivo, we were able to show that the effect of heparin on platelets is antibody- and antithrombin-III-independent. Adenosine Diphosphate 13-16 serpin family C member 1 Homo sapiens 144-160 2840374-5 1988 Studying the ADP-induced fibrinogen binding to platelets in vivo, we were able to show that the effect of heparin on platelets is antibody- and antithrombin-III-independent. Heparin 106-113 serpin family C member 1 Homo sapiens 144-160 3132590-4 1988 AT III isoforms were examined by isoelectric focusing in polyacrylamide gels (IEF/PA) and immunoblotting, and no changes were observed throughout the study period. polyacrylamide 57-71 serpin family C member 1 Homo sapiens 0-6 3361696-5 1988 When low dose heparin was administered to patients with AF, plasma FPA levels were decreased to the near normal range, accompanied by an increase in heparin-AT III complex activity and heparin concentration 0.5-1.0 h after injection. Heparin 14-21 serpin family C member 1 Homo sapiens 157-163 3361696-5 1988 When low dose heparin was administered to patients with AF, plasma FPA levels were decreased to the near normal range, accompanied by an increase in heparin-AT III complex activity and heparin concentration 0.5-1.0 h after injection. Heparin 149-156 serpin family C member 1 Homo sapiens 157-163 3361696-5 1988 When low dose heparin was administered to patients with AF, plasma FPA levels were decreased to the near normal range, accompanied by an increase in heparin-AT III complex activity and heparin concentration 0.5-1.0 h after injection. Heparin 149-156 serpin family C member 1 Homo sapiens 157-163 3041550-3 1988 Increased activity of vitamin K-dependent clotting factors partially counterbalanced by a rather high level of antithrombin III were also detected. Vitamin K 22-31 serpin family C member 1 Homo sapiens 111-127 3481885-0 1987 Antithrombin III binding to surface immobilized heparin and its relation to F Xa inhibition. Heparin 48-55 serpin family C member 1 Homo sapiens 0-16 3121595-2 1987 Heparin binds to human antithrombin III and accelerates its inhibitory activity in the blood coagulation system. Heparin 0-7 serpin family C member 1 Homo sapiens 23-39 3121595-7 1987 259, 935-938) have shown that selective chemical modification of a limited number of lysine residues in antithrombin III causes drastic loss of its heparin cofactor activity. Lysine 85-91 serpin family C member 1 Homo sapiens 104-120 3121595-8 1987 We have performed chemical modification of antithrombin III with trinitrobenzene sulfonic acid in order to determine the location of these lysine residues. Trinitrobenzenesulfonic Acid 65-94 serpin family C member 1 Homo sapiens 43-59 3121595-8 1987 We have performed chemical modification of antithrombin III with trinitrobenzene sulfonic acid in order to determine the location of these lysine residues. Lysine 139-145 serpin family C member 1 Homo sapiens 43-59 3121595-9 1987 When antithrombin III was treated with 100 M excess of trinitrobenzene sulfonic acid for 10 min, about 3.2 mol of amino group per mol of antithrombin III were modified. Trinitrobenzenesulfonic Acid 55-84 serpin family C member 1 Homo sapiens 5-21 3121595-9 1987 When antithrombin III was treated with 100 M excess of trinitrobenzene sulfonic acid for 10 min, about 3.2 mol of amino group per mol of antithrombin III were modified. Trinitrobenzenesulfonic Acid 55-84 serpin family C member 1 Homo sapiens 137-153 3121595-12 1987 These results were obtained by comparing and analyzing the cyanogen bromide fragments derived from native antithrombin III and the 10-min modified antithrombin III. Cyanogen Bromide 59-75 serpin family C member 1 Homo sapiens 106-122 3121595-13 1987 When antithrombin III was pretreated with heparin, followed by trinitrobenzene sulfonic acid modification, the extent of modification at Lys114 and Lys125 decreased from 75% and 94% to 20% and 40%, respectively, whereas the modification at Lys287 remained nearly quantitative (greater than 95%). Heparin 42-49 serpin family C member 1 Homo sapiens 5-21 3121595-13 1987 When antithrombin III was pretreated with heparin, followed by trinitrobenzene sulfonic acid modification, the extent of modification at Lys114 and Lys125 decreased from 75% and 94% to 20% and 40%, respectively, whereas the modification at Lys287 remained nearly quantitative (greater than 95%). Trinitrobenzenesulfonic Acid 63-92 serpin family C member 1 Homo sapiens 5-21 3481885-2 1987 Affinity chromatography revealed that one fourth of the heparin used in surface coating had high affinity for antithrombin III (AT). Heparin 56-63 serpin family C member 1 Homo sapiens 110-126 2445746-4 1987 The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin. Heparin 17-24 serpin family C member 1 Homo sapiens 76-88 3481885-2 1987 Affinity chromatography revealed that one fourth of the heparin used in surface coating had high affinity for antithrombin III (AT). Heparin 56-63 serpin family C member 1 Homo sapiens 128-130 2445746-4 1987 The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin. Heparin 17-24 serpin family C member 1 Homo sapiens 193-205 3481885-3 1987 The heparin surface adsorbed AT from both human plasma and solutions of purified AT. Heparin 4-11 serpin family C member 1 Homo sapiens 29-31 2445746-4 1987 The abilities of heparin fractions, Mr 7,800-18,800, with high affinity for antithrombin, and of the International Heparin Standard, to accelerate the inactivation of thrombin and Factor Xa by antithrombin were readily neutralized by S protein/vitronectin. Heparin 115-122 serpin family C member 1 Homo sapiens 193-205 2445746-5 1987 Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site. Heparin 30-37 serpin family C member 1 Homo sapiens 110-122 3481885-3 1987 The heparin surface adsorbed AT from both human plasma and solutions of purified AT. Heparin 4-11 serpin family C member 1 Homo sapiens 81-83 2445746-5 1987 Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site. Heparin 80-87 serpin family C member 1 Homo sapiens 110-122 2445746-10 1987 These findings suggest that S protein/vitronectin may interact through its glycosaminoglycan binding domain(s) with various functional domains of the heparin (heparan sulfate) molecule, including the antithrombin-binding pentasaccharide sequence. pentasaccharide 221-236 serpin family C member 1 Homo sapiens 200-212 3481885-8 1987 With AT adsorbed on both high and low affinity heparin the surface had the capacity to inhibit several consecutive aliquots of F Xa exposed to the surface. Heparin 47-54 serpin family C member 1 Homo sapiens 5-7 2445746-5 1987 Binding and neutralization of heparin by S protein/vitronectin was inhibited by heparin with low affinity for antithrombin, indicating that S protein/vitronectin can interact with a region on the heparin chain that might serve as a proteinase binding site. Heparin 80-87 serpin family C member 1 Homo sapiens 110-122 3481885-10 1987 It was demonstrated that the density of AT on both high and low affinity heparin determines the F Xa inhibition capacity whereas the amount of AT on high affinity sites limits the rate of the reaction. Heparin 73-80 serpin family C member 1 Homo sapiens 40-42 2445746-7 1987 Furthermore, S protein/vitronectin neutralized the anti-Factor Xa activity of a synthetic pentasaccharide comprising the antithrombin-binding sequence of heparin. pentasaccharide 90-105 serpin family C member 1 Homo sapiens 121-133 2445746-7 1987 Furthermore, S protein/vitronectin neutralized the anti-Factor Xa activity of a synthetic pentasaccharide comprising the antithrombin-binding sequence of heparin. Heparin 154-161 serpin family C member 1 Homo sapiens 121-133 2445746-10 1987 These findings suggest that S protein/vitronectin may interact through its glycosaminoglycan binding domain(s) with various functional domains of the heparin (heparan sulfate) molecule, including the antithrombin-binding pentasaccharide sequence. Heparin 150-157 serpin family C member 1 Homo sapiens 200-212 3481885-12 1987 The ability of the immobilized heparin to catalyze inhibition of F Xa is likely to be an important component for the thromboresistant properties of a heparin coating with non-compromised AT binding sequences. Heparin 31-38 serpin family C member 1 Homo sapiens 187-189 2445746-10 1987 These findings suggest that S protein/vitronectin may interact through its glycosaminoglycan binding domain(s) with various functional domains of the heparin (heparan sulfate) molecule, including the antithrombin-binding pentasaccharide sequence. Heparitin Sulfate 159-174 serpin family C member 1 Homo sapiens 200-212 3426230-10 1987 HCII differs from antithrombin III, which contains an essential disulfide bond for heparin-dependent thrombin inhibition (Longas, M. O., et al. Disulfides 64-73 serpin family C member 1 Homo sapiens 18-34 3691497-2 1987 Three forms of heparin fractionated on the basis of their affinity for antithrombin III and unfractionated heparin were found to act as noncompetitive inhibitors of the formation of the thrombin-hirudin complex. Heparin 15-22 serpin family C member 1 Homo sapiens 71-87 3689206-0 1987 Modulation of glycosaminoglycan production and antithrombin III binding by cultured aortic endothelial cells treated with 4-methylumbelliferyl-beta-D-xyloside. methylumbelliferyl-beta-D-xyloside 122-158 serpin family C member 1 Homo sapiens 47-63 3680513-5 1987 The mean F1 + 2 level in antithrombin-deficient individuals on warfarin was significantly elevated (mean = 0.714 nM) as compared with that in anticoagulated subjects with protein C deficiency (mean = 0.205 nM) or in those without an inherited thrombotic disorder (P less than 0.01) at equivalent levels of intensity of oral anticoagulation. Warfarin 63-71 serpin family C member 1 Homo sapiens 25-37 3680513-6 1987 We therefore conclude that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-antithrombin mechanism. Warfarin 41-49 serpin family C member 1 Homo sapiens 129-141 3680513-6 1987 We therefore conclude that the effect of warfarin on hemostatic system activation is modulated by the endogenous heparan sulfate-antithrombin mechanism. Heparitin Sulfate 113-128 serpin family C member 1 Homo sapiens 129-141 2962279-6 1987 When BTG was again elevated, the dose of heparin was increased stepwise to 2 x 15,000 IU/d; in this way functional AT III levels remained in the range of 28-50%. Heparin 41-48 serpin family C member 1 Homo sapiens 115-121 3689206-4 1987 This binding was displaced by heparin and was completely abolished by selective removal of heparan sulfate from cells with heparitinase, indicating that antithrombin III binds to heparan sulfate on the surface of endothelial cells. Heparin 30-37 serpin family C member 1 Homo sapiens 153-169 3689206-4 1987 This binding was displaced by heparin and was completely abolished by selective removal of heparan sulfate from cells with heparitinase, indicating that antithrombin III binds to heparan sulfate on the surface of endothelial cells. Heparitin Sulfate 91-106 serpin family C member 1 Homo sapiens 153-169 3689206-4 1987 This binding was displaced by heparin and was completely abolished by selective removal of heparan sulfate from cells with heparitinase, indicating that antithrombin III binds to heparan sulfate on the surface of endothelial cells. Heparitin Sulfate 179-194 serpin family C member 1 Homo sapiens 153-169 3689206-5 1987 Incubation of cell cultures with beta-D-xyloside resulted in a reduction of maximum antithrombin III binding by approximately 65% with little alteration in binding affinity. xylosides 33-48 serpin family C member 1 Homo sapiens 84-100 3689206-8 1987 Whereas the size of heparan sulfate chains derived from the cell surface was not altered by xyloside treatment, they appeared to have slightly less net negative charge and a significantly reduced proportion of the molecule with high affinity for antithrombin III in the presence of xyloside. Heparitin Sulfate 20-35 serpin family C member 1 Homo sapiens 246-262 3689206-11 1987 These results suggest that beta-D-xyloside caused a dose-dependent decrease in production as well as some subtle structural alterations of cell-surface-associated heparan sulfate, which could serve as binding sites for antithrombin III on the endothelial cells and mediate enhancing the anticoagulant activity of this protein. xylosides 27-42 serpin family C member 1 Homo sapiens 219-235 3689206-11 1987 These results suggest that beta-D-xyloside caused a dose-dependent decrease in production as well as some subtle structural alterations of cell-surface-associated heparan sulfate, which could serve as binding sites for antithrombin III on the endothelial cells and mediate enhancing the anticoagulant activity of this protein. Heparitin Sulfate 163-178 serpin family C member 1 Homo sapiens 219-235 3653103-6 1987 Heparin activation of the p68 kinase is reversible since it can be prevented by addition of antithrombin III, heparin-binding protein. Heparin 0-7 serpin family C member 1 Homo sapiens 92-108 3667601-5 1987 The fraction of biologically active ATIII has been purified from total ATIII by affinity fractionation on heparin-Sepharose. Heparin 106-113 serpin family C member 1 Homo sapiens 36-41 3667601-5 1987 The fraction of biologically active ATIII has been purified from total ATIII by affinity fractionation on heparin-Sepharose. Sepharose 114-123 serpin family C member 1 Homo sapiens 36-41 3667601-6 1987 This fractionation indicates that the differences in the active and inactive forms of expressed ATIII result from differences in their ability to bind heparin. Heparin 151-158 serpin family C member 1 Homo sapiens 96-101 3667601-7 1987 Purified ATIII has a specific activity very similar to that of plasma-derived ATIII and exhibits typical heparin-accelerated ATIII activity. Heparin 105-112 serpin family C member 1 Homo sapiens 9-14 3654616-0 1987 Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park". Disulfides 24-33 serpin family C member 1 Homo sapiens 41-53 3654616-0 1987 Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park". Disulfides 24-33 serpin family C member 1 Homo sapiens 76-88 3654616-0 1987 Formation of a covalent disulfide-linked antithrombin-albumin complex by an antithrombin variant, antithrombin "Northwick Park". Disulfides 24-33 serpin family C member 1 Homo sapiens 76-88 3654616-6 1987 In this communication, we present evidence that this Mr approximately 120,000 variant component is comprised of an antithrombin-albumin covalent disulfide-linked complex. Disulfides 145-154 serpin family C member 1 Homo sapiens 115-127 3624272-5 1987 The amidolytic and proteolytic activities of the enzyme were readily inhibited by phenylmethanesulfonyl fluoride, p-amidinophenylmethanesulfonyl fluoride, chloromethyl ketones, and human antithrombin III. Phenylmethylsulfonyl Fluoride 82-112 serpin family C member 1 Homo sapiens 187-203 3427019-0 1987 Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III. 3-o 16-19 serpin family C member 1 Homo sapiens 107-123 3427019-0 1987 Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III. Glucosamine 38-49 serpin family C member 1 Homo sapiens 107-123 3427019-0 1987 Contribution of 3-O- and 6-O-sulfated glucosamine residues in the heparin-induced conformational change in antithrombin III. Heparin 66-73 serpin family C member 1 Homo sapiens 107-123 3427019-2 1987 The octasaccharide produced a maximum 48% increase in intrinsic fluorescence at 37 degrees C and a rate of factor Xa inhibition of 6 X 10(5) M-1 s-1 as measured by stopped-flow fluorometry at 25 degrees C. The basal rate of the antithrombin-factor Xa interaction observed in the absence of oligosaccharide was 2 X 10(3) M-1 s-1. Octasaccharide 4-18 serpin family C member 1 Homo sapiens 228-240 3424283-5 1987 The AT III fraction with normal affinity to heparin displayed H-CIE and CIEF patterns identical to the control AT III. Heparin 44-51 serpin family C member 1 Homo sapiens 4-10 3317985-5 1987 However, heparin (1-10 ug/ml) strongly accelerated the rate of antithrombin III inactivation and slightly protected heparin cofactor II, thus reversing the order of inactivation. Heparin 9-16 serpin family C member 1 Homo sapiens 63-79 3305015-0 1987 Probing the heparin-binding domain of human antithrombin III with V8 protease. Heparin 12-19 serpin family C member 1 Homo sapiens 44-60 2442161-0 1987 Neutralization and binding of heparin by S protein/vitronectin in the inhibition of factor Xa by antithrombin III. Heparin 30-37 serpin family C member 1 Homo sapiens 97-113 2442161-2 1987 The interference of the heparin-neutralizing plasma component S protein (vitronectin) (Mr = 78,000) with heparin-catalyzed inhibition of coagulation factor Xa by antithrombin III was investigated in plasma and in a purified system. Heparin 105-112 serpin family C member 1 Homo sapiens 162-178 2442161-4 1987 Using purified components in the presence of heparin, S protein induced a concentration-dependent reduction of the inhibition rate of factor Xa by antithrombin III. Heparin 45-52 serpin family C member 1 Homo sapiens 147-163 2442161-12 1987 These data provide evidence that the heparin-binding domain of S protein appears to be unique in binding to heparin and thereby neutralizing its anticoagulant activity in the inhibition of coagulation factors by antithrombin III. Heparin 37-44 serpin family C member 1 Homo sapiens 212-228 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Glutamic Acid 50-53 serpin family C member 1 Homo sapiens 255-271 3690577-0 1987 Synthesis of heparin fragments: a methyl alpha-pentaoside with high affinity for antithrombin III. Heparin 13-20 serpin family C member 1 Homo sapiens 81-97 3690577-0 1987 Synthesis of heparin fragments: a methyl alpha-pentaoside with high affinity for antithrombin III. methyl alpha-pentaoside 34-57 serpin family C member 1 Homo sapiens 81-97 3690577-1 1987 The synthesis is described of the methyl alpha-glycoside of the pentasaccharide which represents the sequence in heparin responsible for binding and activation of the anticoagulant protein Antithrombin III. methyl alpha-glycoside 34-56 serpin family C member 1 Homo sapiens 189-205 3690577-1 1987 The synthesis is described of the methyl alpha-glycoside of the pentasaccharide which represents the sequence in heparin responsible for binding and activation of the anticoagulant protein Antithrombin III. pentasaccharide 64-79 serpin family C member 1 Homo sapiens 189-205 3690577-1 1987 The synthesis is described of the methyl alpha-glycoside of the pentasaccharide which represents the sequence in heparin responsible for binding and activation of the anticoagulant protein Antithrombin III. Heparin 113-120 serpin family C member 1 Homo sapiens 189-205 3621562-1 1987 We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III). Heparin 62-69 serpin family C member 1 Homo sapiens 158-174 3621562-1 1987 We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III). Heparin 62-69 serpin family C member 1 Homo sapiens 176-182 3621562-1 1987 We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III). Heparin 99-106 serpin family C member 1 Homo sapiens 158-174 3621562-1 1987 We describe a fully automated assay for determining effective heparin activity in plasma, based on heparin-catalyzed inhibition of Factor Xa (EC 3.4.21.6) by antithrombin III (AT III). Heparin 99-106 serpin family C member 1 Homo sapiens 176-182 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Alanine 54-57 serpin family C member 1 Homo sapiens 255-271 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Glutamic Acid 50-53 serpin family C member 1 Homo sapiens 255-271 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Leucine 83-86 serpin family C member 1 Homo sapiens 255-271 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Glutamic Acid 50-53 serpin family C member 1 Homo sapiens 255-271 3305015-9 1987 259, 939-941], the heparin-binding site of antithrombin III has been suggested to be in the region of Pro-41, Arg-47 and Trp-49. Heparin 19-26 serpin family C member 1 Homo sapiens 43-59 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Alanine 197-200 serpin family C member 1 Homo sapiens 255-271 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Glutamic Acid 50-53 serpin family C member 1 Homo sapiens 255-271 3305015-9 1987 259, 939-941], the heparin-binding site of antithrombin III has been suggested to be in the region of Pro-41, Arg-47 and Trp-49. Proline 102-105 serpin family C member 1 Homo sapiens 43-59 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Leucine 213-216 serpin family C member 1 Homo sapiens 255-271 3305015-9 1987 259, 939-941], the heparin-binding site of antithrombin III has been suggested to be in the region of Pro-41, Arg-47 and Trp-49. Arginine 110-113 serpin family C member 1 Homo sapiens 43-59 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Heparin 294-301 serpin family C member 1 Homo sapiens 255-271 3305015-15 1987 Both high-affinity and low-affinity antithrombin-III-binding heparins were shown to inhibit the V8 protease digestion of native antithrombin III, but the high-affinity sample exhibited a higher inhibition activity than the low-affinity heparin. Heparin 61-69 serpin family C member 1 Homo sapiens 128-144 3305015-9 1987 259, 939-941], the heparin-binding site of antithrombin III has been suggested to be in the region of Pro-41, Arg-47 and Trp-49. Tryptophan 121-124 serpin family C member 1 Homo sapiens 43-59 3305015-15 1987 Both high-affinity and low-affinity antithrombin-III-binding heparins were shown to inhibit the V8 protease digestion of native antithrombin III, but the high-affinity sample exhibited a higher inhibition activity than the low-affinity heparin. Heparin 61-68 serpin family C member 1 Homo sapiens 128-144 3305015-16 1987 These findings (a) imply that the segment containing residues 34-51 is among the most exposed region of native antithrombin III and (b) support the previous conclusions that this region may play a pivotal role in the heparin binding. Heparin 217-224 serpin family C member 1 Homo sapiens 111-127 3305015-10 1987 In this study the heparin-binding site was probed by preferential cleavage of V8 protease on heparin-treated and non-treated native antithrombin III. Heparin 18-25 serpin family C member 1 Homo sapiens 132-148 3305015-10 1987 In this study the heparin-binding site was probed by preferential cleavage of V8 protease on heparin-treated and non-treated native antithrombin III. Heparin 93-100 serpin family C member 1 Homo sapiens 132-148 3305015-11 1987 The study has been based on the presumption that the heparin-binding site of antithrombin III is situated at exposed surface domain and may be preferentially attacked during limited proteolytic digestion. Heparin 53-60 serpin family C member 1 Homo sapiens 77-93 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Glutamic Acid 24-27 serpin family C member 1 Homo sapiens 255-271 3305015-14 1987 The results reveal that Glu-Gly (residues 34-35), Glu-Ala (residues 42-43) and Glu-Leu (residues 50-51) are three preferential cleavage sites for V8 protease and their cleavage, especially the Glu-Ala and the Glu-Leu sites, was drastically inhibited when antithrombin III was preincubated with heparin. Glycine 28-31 serpin family C member 1 Homo sapiens 255-271 2448885-1 1987 Decreases in platelet count, fibrinogen concentration, factor VIII, antithrombin III and alpha 2-antiplasmin activities, increase in FDP-D fraction, and pleural effusion were observed transiently at early fever stage of DHF at grade II, indicating DHF patients had manifestations of the acute type of DIC with increased permeability of vascular wall. dhf 220-223 serpin family C member 1 Homo sapiens 68-84 3607780-0 1987 Long-term adjuvant therapy with tamoxifen: effects on sex hormone binding globulin and antithrombin III. Tamoxifen 32-41 serpin family C member 1 Homo sapiens 87-103 3624220-0 1987 Structure and antithrombin-binding properties of heparin isolated from the clams Anomalocardia brasiliana and Tivela mactroides. Heparin 49-56 serpin family C member 1 Homo sapiens 14-26 3624220-2 1987 A large portion of the polysaccharide chains of both preparations bound with high affinity to immobilized antithrombin. Polysaccharides 23-37 serpin family C member 1 Homo sapiens 106-118 3624220-3 1987 Titrations monitored by tryptophan fluorescence showed that clam polysaccharide chains with Mr approximately 22,500 contained up to three binding sites for antithrombin and that the binding constants for the interaction of these chains with antithrombin were higher than those reported for mammalian heparin of comparable size. Polysaccharides 65-79 serpin family C member 1 Homo sapiens 156-168 3624220-3 1987 Titrations monitored by tryptophan fluorescence showed that clam polysaccharide chains with Mr approximately 22,500 contained up to three binding sites for antithrombin and that the binding constants for the interaction of these chains with antithrombin were higher than those reported for mammalian heparin of comparable size. Polysaccharides 65-79 serpin family C member 1 Homo sapiens 241-253 3624220-5 1987 The content of these saccharide sequences was found to increase with increasing affinity of the parent polysaccharide for antithrombin. Carbohydrates 21-31 serpin family C member 1 Homo sapiens 122-134 3624220-5 1987 The content of these saccharide sequences was found to increase with increasing affinity of the parent polysaccharide for antithrombin. Polysaccharides 103-117 serpin family C member 1 Homo sapiens 122-134 3611110-7 1987 Heparin catalyzed the AT III inhibition of thrombin but not meizothrombin(des F1) formed during the prothrombin activation. Heparin 0-7 serpin family C member 1 Homo sapiens 22-28 3611110-8 1987 Thrombin, generated by (Xa-Va-phospholipid-Ca2+) was inhibited by AT III/heparin more slowly than purified thrombin, and the saturation kinetics of the inhibition with respect to AT III differed from those found with purified thrombin. Heparin 73-80 serpin family C member 1 Homo sapiens 66-72 2955820-10 1987 Efficiency of low-mol-wt heparins to inhibit degradation of heparan sulfate in ECM decreased with their main molecular size, and a synthetic pentasaccharide, representing the binding site to antithrombin III, was devoid of inhibitory activity. pentasaccharide 141-156 serpin family C member 1 Homo sapiens 191-207 3649921-0 1987 Heparin promotes the inactivation of antithrombin by neutrophil elastase. Heparin 0-7 serpin family C member 1 Homo sapiens 37-49 3649921-1 1987 Heparin is an acceleratory cofactor for antithrombin, a circulating inhibitor of blood coagulation enzymes. Heparin 0-7 serpin family C member 1 Homo sapiens 40-52 3649921-3 1987 In apparent opposition to this function, heparin was found to greatly accelerate the in vitro inactivation of antithrombin by neutrophil elastase. Heparin 41-48 serpin family C member 1 Homo sapiens 110-122 3649921-5 1987 Although the data suggest that a heparin-antithrombin complex is essential for the inactivation by elastase to occur, the enzyme itself interacts tightly with heparin. Heparin 33-40 serpin family C member 1 Homo sapiens 41-53 3618551-1 1987 Antithrombin-III assays are performed to assess response to heparin therapy and efficacy of antithrombin concentrate therapy and in diagnosing hereditary thrombophilia, deep venous thrombosis, pulmonary embolus, and disseminated intravascular coagulation. Heparin 60-67 serpin family C member 1 Homo sapiens 0-16 3663508-0 1987 An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy. Heparin 47-54 serpin family C member 1 Homo sapiens 12-28 3428662-0 1987 [Effect of heparin treatment on antithrombin III (AT III) activity]. Heparin 11-18 serpin family C member 1 Homo sapiens 32-48 3663508-0 1987 An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy. Heparin 47-54 serpin family C member 1 Homo sapiens 30-36 3663508-0 1987 An abnormal antithrombin III (AT III) with low heparin affinity: AT III Clichy. Heparin 47-54 serpin family C member 1 Homo sapiens 65-71 3663509-0 1987 Antithrombin III Glasgow: a variant with increased heparin affinity and reduced ability to inactivate thrombin, associated with familial thrombosis. Heparin 51-58 serpin family C member 1 Homo sapiens 0-16 3663509-4 1987 Plasma from the propositus was precipitated with dextran sulphate, applied to heparin-Sepharose and the AT III stepwise eluted with NaCl. Sodium Chloride 132-136 serpin family C member 1 Homo sapiens 104-110 3663509-5 1987 The AT III had a reduced ability to inactivate thrombin, when this was monitored by substrate hydrolysis or by SDS polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 111-114 serpin family C member 1 Homo sapiens 4-10 3663509-5 1987 The AT III had a reduced ability to inactivate thrombin, when this was monitored by substrate hydrolysis or by SDS polyacrylamide gel electrophoresis. polyacrylamide 115-129 serpin family C member 1 Homo sapiens 4-10 3663509-7 1987 AT III from the patient was reapplied to heparin-Sepharose and eluted with a NaCl gradient. Heparin 41-48 serpin family C member 1 Homo sapiens 0-6 3663509-7 1987 AT III from the patient was reapplied to heparin-Sepharose and eluted with a NaCl gradient. Sepharose 49-58 serpin family C member 1 Homo sapiens 0-6 3663509-7 1987 AT III from the patient was reapplied to heparin-Sepharose and eluted with a NaCl gradient. Sodium Chloride 77-81 serpin family C member 1 Homo sapiens 0-6 3663509-9 1987 It is concluded that this variant, designated AT III Glasgow, has increased affinity for heparin but reduced ability to inactivate thrombin. Heparin 89-96 serpin family C member 1 Homo sapiens 46-52 3428662-0 1987 [Effect of heparin treatment on antithrombin III (AT III) activity]. Heparin 11-18 serpin family C member 1 Homo sapiens 50-56 3499176-1 1987 The inactivation of human factor XIa by human antithrombin III was studied under pseudo-first-order reaction conditions (excess antithrombin III) both in the absence and in the presence of heparin. Heparin 189-196 serpin family C member 1 Homo sapiens 46-62 3609301-0 1987 Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135. Carbohydrates 48-60 serpin family C member 1 Homo sapiens 25-41 3609301-0 1987 Physiological variant of antithrombin-III lacks carbohydrate sidechain at Asn 135. Asparagine 74-77 serpin family C member 1 Homo sapiens 25-41 2442830-0 1987 Mechanism of potentiation of antithrombin III [AT-III] inhibition by sulfated xylans. Xylans 78-84 serpin family C member 1 Homo sapiens 29-45 2442830-0 1987 Mechanism of potentiation of antithrombin III [AT-III] inhibition by sulfated xylans. Xylans 78-84 serpin family C member 1 Homo sapiens 47-53 2442830-3 1987 The sulfated xylans were more effective than heparin or SP-54 in potentiating the AT-III inhibition of amidolysis of H-D-Phe-Pip-Arg-pNa (S-2238) by thrombin (IIa) or amidolysis of Bz-Ile-Glu-Gly-Arg-pNa (S-2222) by Xa. Xylans 13-19 serpin family C member 1 Homo sapiens 82-88 2442830-3 1987 The sulfated xylans were more effective than heparin or SP-54 in potentiating the AT-III inhibition of amidolysis of H-D-Phe-Pip-Arg-pNa (S-2238) by thrombin (IIa) or amidolysis of Bz-Ile-Glu-Gly-Arg-pNa (S-2222) by Xa. Heparin 45-52 serpin family C member 1 Homo sapiens 82-88 2442830-3 1987 The sulfated xylans were more effective than heparin or SP-54 in potentiating the AT-III inhibition of amidolysis of H-D-Phe-Pip-Arg-pNa (S-2238) by thrombin (IIa) or amidolysis of Bz-Ile-Glu-Gly-Arg-pNa (S-2222) by Xa. Pentosan Sulfuric Polyester 56-61 serpin family C member 1 Homo sapiens 82-88 2442830-3 1987 The sulfated xylans were more effective than heparin or SP-54 in potentiating the AT-III inhibition of amidolysis of H-D-Phe-Pip-Arg-pNa (S-2238) by thrombin (IIa) or amidolysis of Bz-Ile-Glu-Gly-Arg-pNa (S-2222) by Xa. benzoyl-Ile-Glu-Gly-Arg-p-nitroanilide 181-203 serpin family C member 1 Homo sapiens 82-88 2442830-4 1987 Study of the high affinity binding of the xylan sulfates to AT-III-Sepharose column showed that the amount of the xylan sulfate recovered in the eluates from this peak was greatly increased with an increase in molecular weight (MW). Pentosan Sulfuric Polyester 42-56 serpin family C member 1 Homo sapiens 60-66 2442830-4 1987 Study of the high affinity binding of the xylan sulfates to AT-III-Sepharose column showed that the amount of the xylan sulfate recovered in the eluates from this peak was greatly increased with an increase in molecular weight (MW). Sepharose 67-76 serpin family C member 1 Homo sapiens 60-66 2442830-4 1987 Study of the high affinity binding of the xylan sulfates to AT-III-Sepharose column showed that the amount of the xylan sulfate recovered in the eluates from this peak was greatly increased with an increase in molecular weight (MW). Pentosan Sulfuric Polyester 42-55 serpin family C member 1 Homo sapiens 60-66 3609301-5 1987 Chromatography of total tryptic digests on concanavalin A-Sepharose confirmed that the high heparin affinity form of antithrombin lacked an oligosaccharide moiety at Asn 135. Sepharose 58-67 serpin family C member 1 Homo sapiens 117-129 3609301-5 1987 Chromatography of total tryptic digests on concanavalin A-Sepharose confirmed that the high heparin affinity form of antithrombin lacked an oligosaccharide moiety at Asn 135. Heparin 92-99 serpin family C member 1 Homo sapiens 117-129 3609301-5 1987 Chromatography of total tryptic digests on concanavalin A-Sepharose confirmed that the high heparin affinity form of antithrombin lacked an oligosaccharide moiety at Asn 135. Oligosaccharides 140-155 serpin family C member 1 Homo sapiens 117-129 3609301-5 1987 Chromatography of total tryptic digests on concanavalin A-Sepharose confirmed that the high heparin affinity form of antithrombin lacked an oligosaccharide moiety at Asn 135. Asparagine 166-169 serpin family C member 1 Homo sapiens 117-129 2442830-7 1987 The results also suggested an interaction between larchwood xylan sulfate and IIa which may potentiate an interaction between AT-III and IIa. larchwood xylan sulfate 50-73 serpin family C member 1 Homo sapiens 126-132 3499176-9 1987 From the kinetic data, a binding constant (Kd) of 0.14 microM was inferred for the binding of antithrombin III to heparin. Heparin 114-121 serpin family C member 1 Homo sapiens 94-110 3663595-2 1987 The denaturation of human and bovine antithrombin III by guanidine hydrochloride has been followed by 1H NMR spectroscopy. Guanidine 57-80 serpin family C member 1 Homo sapiens 37-53 3664518-0 1987 Conformation of the pentasaccharide corresponding to the binding site of heparin to antithrombin-III. pentasaccharide 20-35 serpin family C member 1 Homo sapiens 84-100 3664518-0 1987 Conformation of the pentasaccharide corresponding to the binding site of heparin to antithrombin-III. Heparin 73-80 serpin family C member 1 Homo sapiens 84-100 3306136-5 1987 An increase of the activity of plasminogen, alpha 2-antiplasmin, and antithrombin III, and in the concentration of alpha 1-protease inhibitor in ascites was induced by the dexamethasone injection. Dexamethasone 172-185 serpin family C member 1 Homo sapiens 69-85 3109497-1 1987 The interactions of antithrombin III with two heparin-dye conjugates have been compared using their fluorescence anisotropy. Heparin 46-53 serpin family C member 1 Homo sapiens 20-36 3109497-2 1987 The first, heparin labelled with 5-isothiocyanatofluorescein, where the dye was mostly bound to unsulphated glucosamine residues, exhibited binding which was characteristic of heparin with a low affinity for antithrombin III. Heparin 11-18 serpin family C member 1 Homo sapiens 208-224 3109497-2 1987 The first, heparin labelled with 5-isothiocyanatofluorescein, where the dye was mostly bound to unsulphated glucosamine residues, exhibited binding which was characteristic of heparin with a low affinity for antithrombin III. Fluorescein-5-isothiocyanate 33-60 serpin family C member 1 Homo sapiens 208-224 3109497-2 1987 The first, heparin labelled with 5-isothiocyanatofluorescein, where the dye was mostly bound to unsulphated glucosamine residues, exhibited binding which was characteristic of heparin with a low affinity for antithrombin III. Heparin 176-183 serpin family C member 1 Homo sapiens 208-224 3109497-4 1987 However, when the heparin was treated with an amino group blocking agent prior to labelling with DENMT, the resultant heparin-dye conjugate showed binding behaviour, the strength of which was consistent with heparin molecules having both high and low affinity for antithrombin III. Heparin 18-25 serpin family C member 1 Homo sapiens 264-280 3109497-4 1987 However, when the heparin was treated with an amino group blocking agent prior to labelling with DENMT, the resultant heparin-dye conjugate showed binding behaviour, the strength of which was consistent with heparin molecules having both high and low affinity for antithrombin III. Heparin 118-125 serpin family C member 1 Homo sapiens 264-280 3109497-4 1987 However, when the heparin was treated with an amino group blocking agent prior to labelling with DENMT, the resultant heparin-dye conjugate showed binding behaviour, the strength of which was consistent with heparin molecules having both high and low affinity for antithrombin III. Heparin 118-125 serpin family C member 1 Homo sapiens 264-280 3109497-5 1987 Heparin molecules with a high affinity for antithrombin III did not possess free amino groups. Heparin 0-7 serpin family C member 1 Homo sapiens 43-59 3663595-2 1987 The denaturation of human and bovine antithrombin III by guanidine hydrochloride has been followed by 1H NMR spectroscopy. Hydrogen 102-104 serpin family C member 1 Homo sapiens 37-53 3663595-5 1987 258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III. Histidine 155-165 serpin family C member 1 Homo sapiens 175-191 3663595-5 1987 258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III. Histidine 155-165 serpin family C member 1 Homo sapiens 237-253 3663595-5 1987 258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III. Histidine 216-226 serpin family C member 1 Homo sapiens 175-191 3663595-5 1987 258, 14048-14053] at low denaturant concentration was detected here by discontinuous changes in the chemical shifts of the C(2) protons of two of the five histidines in human antithrombin III and of three of the six histidines in bovine antithrombin III. Histidine 216-226 serpin family C member 1 Homo sapiens 237-253 3663595-6 1987 These two histidines in human antithrombin III are assigned to residue 1 and, more tentatively, to residue 65. Histidine 10-20 serpin family C member 1 Homo sapiens 30-46 3663595-10 1987 From the tentative assignment of one of these resonances to histidine-1, it is proposed that the heparin binding site of antithrombin III is located in the N-terminal region and that this region forms a separate domain from the rest of the protein. Histidine 60-69 serpin family C member 1 Homo sapiens 121-137 3663595-10 1987 From the tentative assignment of one of these resonances to histidine-1, it is proposed that the heparin binding site of antithrombin III is located in the N-terminal region and that this region forms a separate domain from the rest of the protein. Heparin 97-104 serpin family C member 1 Homo sapiens 121-137 3663595-12 1987 Thermal denaturation also leads to major perturbation of these two histidine resonances in human antithrombin III, though stable intermediates in the unfolding were not detected. Histidine 67-76 serpin family C member 1 Homo sapiens 97-113 3584126-2 1987 Does cleavage by thrombin induce structural changes in the heparin-binding region of antithrombin? Heparin 59-66 serpin family C member 1 Homo sapiens 85-97 3310396-4 1987 AT III became functionally active in presence of heparin, which operates as a catalyst and accelerates significantly the formation of inactive complexes between AT III and proteinases, which usually developed slowly in absence of the activator. Heparin 49-56 serpin family C member 1 Homo sapiens 0-6 3310396-4 1987 AT III became functionally active in presence of heparin, which operates as a catalyst and accelerates significantly the formation of inactive complexes between AT III and proteinases, which usually developed slowly in absence of the activator. Heparin 49-56 serpin family C member 1 Homo sapiens 161-167 3110143-0 1987 Identification of a lysyl residue in antithrombin which is essential for heparin binding. lysyl 20-25 serpin family C member 1 Homo sapiens 37-49 3110143-0 1987 Identification of a lysyl residue in antithrombin which is essential for heparin binding. Heparin 73-80 serpin family C member 1 Homo sapiens 37-49 3110143-1 1987 Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent pyridoxal 5"-phosphate. lysyl 18-23 serpin family C member 1 Homo sapiens 51-63 3110143-1 1987 Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent pyridoxal 5"-phosphate. Heparin 88-95 serpin family C member 1 Homo sapiens 51-63 3110143-1 1987 Identification of lysyl residue(s) in human plasma antithrombin required for binding of heparin was approached using chemical modification with the amino-group reagent pyridoxal 5"-phosphate. Pyridoxal Phosphate 168-190 serpin family C member 1 Homo sapiens 51-63 3110143-2 1987 Modification of antithrombin with limiting amounts of reagent yields an average incorporation of the phosphopyridoxyl label into 1 lysine/protein molecule (Pecon, J. M., and Blackburn, M. N. (1984) J. Biol. phosphopyridoxyl 101-117 serpin family C member 1 Homo sapiens 16-28 3110143-2 1987 Modification of antithrombin with limiting amounts of reagent yields an average incorporation of the phosphopyridoxyl label into 1 lysine/protein molecule (Pecon, J. M., and Blackburn, M. N. (1984) J. Biol. Lysine 131-137 serpin family C member 1 Homo sapiens 16-28 3110143-5 1987 Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin. Heparin 72-79 serpin family C member 1 Homo sapiens 29-41 3110143-5 1987 Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin. Heparin 72-79 serpin family C member 1 Homo sapiens 123-135 3110143-5 1987 Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin. Sepharose 80-89 serpin family C member 1 Homo sapiens 29-41 3110143-5 1987 Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin. Sepharose 80-89 serpin family C member 1 Homo sapiens 123-135 3110143-5 1987 Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin. Heparin 154-161 serpin family C member 1 Homo sapiens 29-41 3110143-5 1987 Fractionation of the labeled antithrombin by affinity chromatography on heparin-Sepharose separated a phosphopyridoxylated antithrombin species devoid of heparin binding from modified protein which retained affinity for heparin. Heparin 154-161 serpin family C member 1 Homo sapiens 29-41 3110143-9 1987 This peptide corresponds to a tryptic fragment including residues 115-129 in the sequence of antithrombin, with the modified residue identified as Lys-125. Lysine 147-150 serpin family C member 1 Homo sapiens 93-105 3110143-10 1987 Additionally, phosphopyridoxylation of antithrombin in the presence of added heparin indicated that several other lysyl residues were "protected" from modification. Heparin 77-84 serpin family C member 1 Homo sapiens 39-51 3110143-11 1987 Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein. Lysine 32-38 serpin family C member 1 Homo sapiens 141-153 3110143-11 1987 Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein. Heparin 43-50 serpin family C member 1 Homo sapiens 141-153 3110143-11 1987 Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein. Heparin 115-122 serpin family C member 1 Homo sapiens 141-153 3584126-14 1987 The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin. Heparin 57-64 serpin family C member 1 Homo sapiens 182-194 3584126-14 1987 The thrombin-promoted alteration of the structure in the heparin-binding region is presumably responsible for recycling of heparin, allowing it to catalyze further reactions between antithrombin and thrombin. Heparin 123-130 serpin family C member 1 Homo sapiens 182-194 3584127-2 1987 Is the heparin-induced conformational change in antithrombin required for rapid inactivation of thrombin? Heparin 7-14 serpin family C member 1 Homo sapiens 48-60 3584127-3 1987 The role of antithrombin conformation in heparin-catalyzed inhibition of thrombin was investigated using antithrombins modified with the tryptophan reagent dimethyl (2-hydroxy-5-nitrobenzyl) sulfonium bromide (HNB). Heparin 41-48 serpin family C member 1 Homo sapiens 12-24 3584127-4 1987 Affinity fractionation of HNB-labeled antithrombin (0.6-0.7 mol of HNB/mol of protein) on heparin-Sepharose using a linear salt gradient allowed separation of three singly labeled protein species and a fourth HNB-antithrombin species which co-eluted with unlabeled protein. Heparin 90-97 serpin family C member 1 Homo sapiens 38-50 3584127-4 1987 Affinity fractionation of HNB-labeled antithrombin (0.6-0.7 mol of HNB/mol of protein) on heparin-Sepharose using a linear salt gradient allowed separation of three singly labeled protein species and a fourth HNB-antithrombin species which co-eluted with unlabeled protein. Sepharose 98-107 serpin family C member 1 Homo sapiens 38-50 3584127-9 1987 The kinetic analysis indicated that each of these HNB-antithrombin derivatives, which undergo the heparin-induced changes to varying extents, can react with thrombin at the same maximal rate. Heparin 98-105 serpin family C member 1 Homo sapiens 54-66 3584127-10 1987 Thus, this series of chemically modified antithrombin species demonstrated that the conformational change which is induced in antithrombin by heparin does not render the protein intrinsically more reactive toward thrombin. Heparin 142-149 serpin family C member 1 Homo sapiens 41-53 3584127-10 1987 Thus, this series of chemically modified antithrombin species demonstrated that the conformational change which is induced in antithrombin by heparin does not render the protein intrinsically more reactive toward thrombin. Heparin 142-149 serpin family C member 1 Homo sapiens 126-138 2955807-0 1987 Comparative effect of heparin and heparan sulphate on two abnormal antithrombin III type 3 variants. Heparin 22-29 serpin family C member 1 Homo sapiens 67-83 2955807-0 1987 Comparative effect of heparin and heparan sulphate on two abnormal antithrombin III type 3 variants. Heparitin Sulfate 34-50 serpin family C member 1 Homo sapiens 67-83 2955807-2 1987 The abnormal species were purified using affinity chromatography on Sepharose bound anti-AT III antibodies. Sepharose 68-77 serpin family C member 1 Homo sapiens 89-95 2955807-4 1987 In an attempt to explain the thrombotic tendency observed in this abnormality we compared the effect of heparin and heparan sulphate on these abnormal AT III, since, unlike heparin, heparan sulphate is a naturally occurring anticoagulant in the human. Heparin 104-111 serpin family C member 1 Homo sapiens 151-157 2955807-4 1987 In an attempt to explain the thrombotic tendency observed in this abnormality we compared the effect of heparin and heparan sulphate on these abnormal AT III, since, unlike heparin, heparan sulphate is a naturally occurring anticoagulant in the human. Heparitin Sulfate 116-132 serpin family C member 1 Homo sapiens 151-157 2955807-7 1987 At this concentration of heparan sulphate the two abnormal AT III still exhibit a heparin cofactor activity below 10%. Heparitin Sulfate 25-41 serpin family C member 1 Homo sapiens 59-65 2955307-0 1987 [Effect of a cyproterone-estradiol combination administered cutaneously on antithrombin III]. cyproterone-estradiol 13-34 serpin family C member 1 Homo sapiens 75-91 3038185-3 1987 Heparin-like structures of the vessel wall have been proposed as another regulatory mechanism catalyzing the inhibition of thrombin by antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 135-151 3038185-4 1987 In the present study, the interaction of antithrombin III with the thrombin-TM complex and its interference with heparin and polycations were investigated by using human components and TM isolated from the microvasculature of rabbit lung. Heparin 113-120 serpin family C member 1 Homo sapiens 41-57 3110143-11 1987 Identification of this critical lysine for heparin binding strongly supports previous data which indicate that the heparin-binding domain of antithrombin is located at the NH2 terminus within one of the disulfide cross-linked loops of the protein. Disulfides 203-212 serpin family C member 1 Homo sapiens 141-153 3660328-1 1987 Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II). Heparin 0-7 serpin family C member 1 Homo sapiens 57-73 3660328-1 1987 Heparin enhances the inhibition rate of thrombin by both antithrombin III (AT III) and heparin cofactor II (HC II). Heparin 0-7 serpin family C member 1 Homo sapiens 75-81 3660328-8 1987 The decrease of AT III induced by heparin administrated during dialysis is likely to account for this relative decrease of AT III activity. Heparin 34-41 serpin family C member 1 Homo sapiens 16-22 3660328-8 1987 The decrease of AT III induced by heparin administrated during dialysis is likely to account for this relative decrease of AT III activity. Heparin 34-41 serpin family C member 1 Homo sapiens 123-129 3473488-7 1987 In a two-stage chromogenic thrombin inactivation assay, under pseudo-first-order conditions, at 16 nM antithrombin III the t1/2 was 74 min and 50 min for plasma and COS cell-derived antithrombin III, respectively, in the absence of heparin. Heparin 232-239 serpin family C member 1 Homo sapiens 102-118 3473488-7 1987 In a two-stage chromogenic thrombin inactivation assay, under pseudo-first-order conditions, at 16 nM antithrombin III the t1/2 was 74 min and 50 min for plasma and COS cell-derived antithrombin III, respectively, in the absence of heparin. Heparin 232-239 serpin family C member 1 Homo sapiens 182-198 3567355-0 1987 Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His. Heparin 0-7 serpin family C member 1 Homo sapiens 32-48 3584126-3 1987 Heparin has been shown to exhibit lower affinity for the antithrombin-thrombin complex than for antithrombin alone (Carlstrom, A.-S., Lieden, K., and Bjork, I. Heparin 0-7 serpin family C member 1 Homo sapiens 57-69 3567355-1 1987 Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. Heparin 126-133 serpin family C member 1 Homo sapiens 0-16 3567355-1 1987 Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. Heparin 126-133 serpin family C member 1 Homo sapiens 18-24 3584126-7 1987 The hydroxy-nitrobenzyl (HNB) group attached to a unique tryptophan has been used in the present study as an extrinsic probe for localization of conformational changes to the heparin-binding region within antithrombin III using immunochemical and spectral techniques. hydroxy-nitrobenzyl 4-23 serpin family C member 1 Homo sapiens 205-221 3567355-1 1987 Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. Heparin 126-133 serpin family C member 1 Homo sapiens 57-69 3567355-4 1987 By heparin-Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. Heparin 3-10 serpin family C member 1 Homo sapiens 37-43 3567355-4 1987 By heparin-Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. Sepharose 11-20 serpin family C member 1 Homo sapiens 37-43 3584126-7 1987 The hydroxy-nitrobenzyl (HNB) group attached to a unique tryptophan has been used in the present study as an extrinsic probe for localization of conformational changes to the heparin-binding region within antithrombin III using immunochemical and spectral techniques. (2S,5R)-5-pentyltetrahydrofuran-2-ol 25-28 serpin family C member 1 Homo sapiens 205-221 3567355-4 1987 By heparin-Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. Sodium Chloride 138-142 serpin family C member 1 Homo sapiens 37-43 3584126-7 1987 The hydroxy-nitrobenzyl (HNB) group attached to a unique tryptophan has been used in the present study as an extrinsic probe for localization of conformational changes to the heparin-binding region within antithrombin III using immunochemical and spectral techniques. Tryptophan 57-67 serpin family C member 1 Homo sapiens 205-221 3584126-7 1987 The hydroxy-nitrobenzyl (HNB) group attached to a unique tryptophan has been used in the present study as an extrinsic probe for localization of conformational changes to the heparin-binding region within antithrombin III using immunochemical and spectral techniques. Heparin 175-182 serpin family C member 1 Homo sapiens 205-221 3584126-8 1987 Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol. Tryptophan 30-40 serpin family C member 1 Homo sapiens 47-59 3584126-8 1987 Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol. hydroxynitrobenzyl 69-87 serpin family C member 1 Homo sapiens 47-59 3584126-8 1987 Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol. Heparin 103-110 serpin family C member 1 Homo sapiens 47-59 3584126-8 1987 Site-specific modification of tryptophan-49 in antithrombin with the hydroxynitrobenzyl reagent blocks heparin binding to the protein and provides a chemical label in the heparin-binding region of the protein (Blackburn, M. N., Smith, R. L., Carson, J., and Sibley, C. C. (1984) J. Biol. Heparin 171-178 serpin family C member 1 Homo sapiens 47-59 3584126-11 1987 Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin. hydroxynitrobenzyl 28-46 serpin family C member 1 Homo sapiens 90-102 3584126-11 1987 Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin. hydroxynitrobenzyl 28-46 serpin family C member 1 Homo sapiens 218-230 3584126-11 1987 Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin. Tryptophan 73-83 serpin family C member 1 Homo sapiens 90-102 3584126-11 1987 Antibodies specific for the hydroxynitrobenzyl hapten, which bind to HNB-tryptophan-49 in antithrombin, were used to detect a change in conformation in the region of tryptophan-49 which occurs upon thrombin binding to antithrombin. Tryptophan 73-83 serpin family C member 1 Homo sapiens 218-230 3494558-1 1987 Our observation that the effect of a patient"s autoantibody with a potent antithrombin activity could be inhibited by toluidine blue and methylene blue led us to investigate the effect of these dyes in several immunochemical reactions in vitro. Tolonium Chloride 118-132 serpin family C member 1 Homo sapiens 74-86 3572202-7 1987 The AT III recovered in urine was almost all inactive, as demonstrated by the quantitative assays and by the H-CIE runs; on the contrary, the findings obtained by functional assays, H-CIE, and CIEF runs on dialysate samples failed to demonstrate any major alteration in the AT III molecule. h-cie 109-114 serpin family C member 1 Homo sapiens 4-10 3494558-1 1987 Our observation that the effect of a patient"s autoantibody with a potent antithrombin activity could be inhibited by toluidine blue and methylene blue led us to investigate the effect of these dyes in several immunochemical reactions in vitro. Methylene Blue 137-151 serpin family C member 1 Homo sapiens 74-86 3572202-7 1987 The AT III recovered in urine was almost all inactive, as demonstrated by the quantitative assays and by the H-CIE runs; on the contrary, the findings obtained by functional assays, H-CIE, and CIEF runs on dialysate samples failed to demonstrate any major alteration in the AT III molecule. h-cie 182-187 serpin family C member 1 Homo sapiens 4-10 3603738-0 1987 [Antithrombin activity of methyl esters of arginine-containing peptides]. methyl esters 26-39 serpin family C member 1 Homo sapiens 1-13 3603738-0 1987 [Antithrombin activity of methyl esters of arginine-containing peptides]. Arginine 43-51 serpin family C member 1 Homo sapiens 1-13 2443128-1 1987 Heparin catalyses the inhibition of two key enzymes of blood coagulation, namely Factor Xa and thrombin, by enhancing the antiproteinase activities of plasma antithrombin III and heparin cofactor II. Heparin 0-7 serpin family C member 1 Homo sapiens 158-174 2443128-12 1987 Reversal of the inhibitory effects of heparin and pentosan polysulphate was associated with the accelerated formation of 125I-thrombin-antithrombin III and 125I-thrombin-heparin cofactor complexes respectively. Heparin 38-45 serpin family C member 1 Homo sapiens 135-151 2443128-12 1987 Reversal of the inhibitory effects of heparin and pentosan polysulphate was associated with the accelerated formation of 125I-thrombin-antithrombin III and 125I-thrombin-heparin cofactor complexes respectively. Pentosan Sulfuric Polyester 50-71 serpin family C member 1 Homo sapiens 135-151 3606581-6 1987 These results indicate that in the presence of Ca2+/phospholipid/Factor V optimum inhibition of Factor Xa requires a saccharide sequence of heparin additional to that involved in binding to antithrombin III. Phospholipids 52-64 serpin family C member 1 Homo sapiens 190-206 3603409-2 1987 The unusual circumstances of apparition, the age and the increased heparin requirements suggested an antithrombin III (AT III) deficiency. Heparin 67-74 serpin family C member 1 Homo sapiens 101-117 3603409-6 1987 Affinity chromatography on heparin-Sepharose revealed two populations of AT III, one of which was devoid of heparin cofactor activity. Heparin 27-34 serpin family C member 1 Homo sapiens 73-79 3603409-6 1987 Affinity chromatography on heparin-Sepharose revealed two populations of AT III, one of which was devoid of heparin cofactor activity. Sepharose 35-44 serpin family C member 1 Homo sapiens 73-79 3603409-7 1987 The toponym AT III Geneva is proposed for this new familial abnormal AT III with defective heparin cofactor activity. Heparin 91-98 serpin family C member 1 Homo sapiens 12-18 3603409-7 1987 The toponym AT III Geneva is proposed for this new familial abnormal AT III with defective heparin cofactor activity. Heparin 91-98 serpin family C member 1 Homo sapiens 69-75 3496682-3 1987 In the presence of heparin, factor VIIa activity was inhibited 50% by purified antithrombin III and plasma in 90 min and 75 min, respectively. Heparin 19-26 serpin family C member 1 Homo sapiens 79-95 3496682-6 1987 These data indicate that antithrombin III appears to be the sole plasma protease inhibitor of human factor VIIa, and the expression of its inhibitory activity against factor VIIa is absolutely dependent upon the presence of exogenous heparin. Heparin 234-241 serpin family C member 1 Homo sapiens 25-41 3606566-1 1987 S protein, a plasma glycoprotein with Mr 78,000, has been shown to interfere with the heparin-catalysed inhibition of thrombin by antithrombin III. Heparin 86-93 serpin family C member 1 Homo sapiens 130-146 3606566-8 1987 Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS. polyacrylamide 180-194 serpin family C member 1 Homo sapiens 56-72 3580302-0 1987 Antithrombin III Northwick Park: demonstration of an inactive high MW complex with increased affinity for heparin. Heparin 106-113 serpin family C member 1 Homo sapiens 0-16 3606566-8 1987 Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS. Sodium Dodecyl Sulfate 242-245 serpin family C member 1 Homo sapiens 56-72 3472589-5 1987 The effects of thrombin and heparin on the mutant ATIII were similar to controls. Heparin 28-35 serpin family C member 1 Homo sapiens 50-55 3580302-4 1987 Furthermore, this variant component is present in plasma as an approximately 120,000 MW inactive antithrombin III complex that can be reduced with dithiothreitol to MW approximately 60,000, indicating disulphide bridging. Dithiothreitol 147-161 serpin family C member 1 Homo sapiens 97-113 3580302-4 1987 Furthermore, this variant component is present in plasma as an approximately 120,000 MW inactive antithrombin III complex that can be reduced with dithiothreitol to MW approximately 60,000, indicating disulphide bridging. disulphide 201-211 serpin family C member 1 Homo sapiens 97-113 3615614-1 1987 The systematic search for a deficiency in antithrombin III must be considered in case of: venous thrombosis in a young patient, recurrent venous thrombosis especially if these occurred under Heparin, venous mesenteric infarction since this type of thrombosis is rare and seems relatively frequent in case of congenital deficiency in antithrombin III, familial past history of venous thrombosis in a woman desiring to undergo estrogen-progesterone therapy. Heparin 191-198 serpin family C member 1 Homo sapiens 42-58 3581111-2 1987 experiments conducted on synthetic fragments of glycosaminoglycans, one of them representing the pentasaccharidic sequence present in heparin and responsible for the binding to antithrombin III, and the others being related to this sequence. Glycosaminoglycans 48-66 serpin family C member 1 Homo sapiens 177-193 3615614-1 1987 The systematic search for a deficiency in antithrombin III must be considered in case of: venous thrombosis in a young patient, recurrent venous thrombosis especially if these occurred under Heparin, venous mesenteric infarction since this type of thrombosis is rare and seems relatively frequent in case of congenital deficiency in antithrombin III, familial past history of venous thrombosis in a woman desiring to undergo estrogen-progesterone therapy. estrogen-progesterone 425-446 serpin family C member 1 Homo sapiens 42-58 3615614-3 1987 Anti-vitamin K treatment is the only effective therapy proposed to patients suffering from a hereditary deficiency in antithrombin III. Vitamin K 5-14 serpin family C member 1 Homo sapiens 118-134 3826410-1 1987 Unlike in the case of some other species, the plasma curve of iodine-labeled antithrombin III (I-AT-III) in rabbits requires fitting with a three-term exponential function for obtaining reliable estimates of the catabolic rate and distribution of I-AT-III among various body compartments (Carlson, Atencio, and Simon. Iodine 62-68 serpin family C member 1 Homo sapiens 97-103 3590108-0 1987 Affinity of antithrombin III for insoluble modified polystyrene. Polystyrenes 52-63 serpin family C member 1 Homo sapiens 12-28 3590108-7 1987 Furthermore, insoluble sulfonated polystyrenes grafted with different amino acid were shown to possess an heparin-like behaviour and catalyse the generation of thrombin-AT III complex. Polystyrenes 34-46 serpin family C member 1 Homo sapiens 169-175 3590108-7 1987 Furthermore, insoluble sulfonated polystyrenes grafted with different amino acid were shown to possess an heparin-like behaviour and catalyse the generation of thrombin-AT III complex. Heparin 106-113 serpin family C member 1 Homo sapiens 169-175 3590108-9 1987 When thrombin is adsorbed on the surface of the polymer, AT III cannot interact with the specific seryl residue of the enzyme. Polymers 48-55 serpin family C member 1 Homo sapiens 57-63 3567176-2 1987 1H NMR has been used to characterize and compare the structures of antithrombin III from human, bovine, and porcine plasma as well as to investigate the interactions of each of these proteins with heparin fragments of defined length. Hydrogen 0-2 serpin family C member 1 Homo sapiens 67-83 2437972-2 1987 Sephadex derivatives bearing carboxymethyl, sulphonated benzylamine and amino acid groups exhibit heparin-like behaviour as demonstrated by the kinetic study of the thrombin inactivation in the presence of antithrombin III. sephadex 0-8 serpin family C member 1 Homo sapiens 206-222 3590093-1 1987 The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III). Heparin 22-29 serpin family C member 1 Homo sapiens 195-211 2437972-2 1987 Sephadex derivatives bearing carboxymethyl, sulphonated benzylamine and amino acid groups exhibit heparin-like behaviour as demonstrated by the kinetic study of the thrombin inactivation in the presence of antithrombin III. carboxymethyl-coenzyme A 29-42 serpin family C member 1 Homo sapiens 206-222 2437972-2 1987 Sephadex derivatives bearing carboxymethyl, sulphonated benzylamine and amino acid groups exhibit heparin-like behaviour as demonstrated by the kinetic study of the thrombin inactivation in the presence of antithrombin III. benzylamine 56-67 serpin family C member 1 Homo sapiens 206-222 2437972-2 1987 Sephadex derivatives bearing carboxymethyl, sulphonated benzylamine and amino acid groups exhibit heparin-like behaviour as demonstrated by the kinetic study of the thrombin inactivation in the presence of antithrombin III. Heparin 98-105 serpin family C member 1 Homo sapiens 206-222 3803739-4 1987 Heparin infusion was able to significantly preserve ATIII activity from glycemia-induced alterations. Heparin 0-7 serpin family C member 1 Homo sapiens 52-57 3590093-1 1987 The neutralization of heparin by active site blocked meizothrombin and thrombin, prothrombin fragment 1.2, fragment 1 and fragment 2 was probed by the heparin-dependent factor Xa inactivation by antithrombin III (AT III). Heparin 22-29 serpin family C member 1 Homo sapiens 213-219 2433298-5 1987 AT III (1-6 U/ml) reduced basal tone and significantly inhibited, in a concentration-dependent manner, the contractile responses to K+, 5-HT, PGD2, PGF2 alpha, and plasmin. Prostaglandin D2 142-146 serpin family C member 1 Homo sapiens 0-6 3812352-1 1987 Neutralization by protamine of the heparin activation of antithrombin III in plasma, in vitro, represents an equilibrium reaction in which by mass action heparin remains complexed only in the presence of an excess of protamine. Heparin 35-42 serpin family C member 1 Homo sapiens 57-73 3812352-1 1987 Neutralization by protamine of the heparin activation of antithrombin III in plasma, in vitro, represents an equilibrium reaction in which by mass action heparin remains complexed only in the presence of an excess of protamine. Heparin 154-161 serpin family C member 1 Homo sapiens 57-73 3812352-2 1987 Loss of this excess through enzymatic breakdown of the free protamine leads to instability of the complexes with liberation of the heparin, reestablishing antithrombin activity. Heparin 131-138 serpin family C member 1 Homo sapiens 155-167 3812352-3 1987 This "heparin rebound" can also be produced by an increase in heparin levels or increased amounts of antithrombin III. Heparin 6-13 serpin family C member 1 Homo sapiens 101-117 3812352-5 1987 A larger excess of protamine does not itself act as an anticoagulant but produces large heparin-protamine complexes that can still activate antithrombin III. Heparin 88-95 serpin family C member 1 Homo sapiens 140-156 3812468-0 1987 An autoantibody with potent antithrombin activity whose action could be inhibited by toluidine blue or methylene blue. Tolonium Chloride 85-99 serpin family C member 1 Homo sapiens 28-40 3812468-0 1987 An autoantibody with potent antithrombin activity whose action could be inhibited by toluidine blue or methylene blue. Methylene Blue 103-117 serpin family C member 1 Homo sapiens 28-40 3812468-5 1987 However, the antithrombin activity of this anticoagulant could be neutralized by toluidine blue or methylene blue ex vivo. Tolonium Chloride 81-95 serpin family C member 1 Homo sapiens 13-25 3812468-5 1987 However, the antithrombin activity of this anticoagulant could be neutralized by toluidine blue or methylene blue ex vivo. Methylene Blue 99-113 serpin family C member 1 Homo sapiens 13-25 2433298-1 1987 Isolated human basilar arteries were used in this study to evaluate the inhibitory effect of antithrombin III (AT III), thrombin, and alpha 2-macroglobulin (alpha 2-M) on contractions elicited by K+, serotonin (5-HT), prostaglandin (PG) D2, PGF2 alpha, and plasmin. Serotonin 200-209 serpin family C member 1 Homo sapiens 93-109 3602050-3 1987 In contrast to the antithrombin activity, toxicity and side effects of the amidino compounds are not dependent on the position of the amidino group within the molecule. amidino 75-82 serpin family C member 1 Homo sapiens 19-31 3790599-1 1987 Significant differences between saturation kinetic properties of heparin-stimulated reactions between thrombin and antithrombin III from human and bovine species were observed. Heparin 65-72 serpin family C member 1 Homo sapiens 115-131 3790599-2 1987 In both systems, the apparent Km for antithrombin III was higher than the KD for antithrombin III-heparin interaction, monitored by intrinsic protein fluorescence change. Heparin 98-105 serpin family C member 1 Homo sapiens 81-97 3801671-9 1987 Interaction of thrombin Tokushima with antithrombin III was much slower than "thrombin" when followed by SDS-PAGE. Sodium Dodecyl Sulfate 105-108 serpin family C member 1 Homo sapiens 39-55 3569629-0 1987 Daily rapid blood glucose variations may condition antithrombin III biologic activity but not its plasma concentration in insulin-dependent diabetes. Blood Glucose 12-25 serpin family C member 1 Homo sapiens 51-67 3569629-3 1987 The variations of both plasma glucose and labile HbA1 were inversely correlated to the alterations of ATIII activity (r = -0.71 and r = -0.73, respectively, p less than 0.001), while no change in ATIII plasma concentration was present. Glucose 30-37 serpin family C member 1 Homo sapiens 102-107 3569629-4 1987 These data suggest a direct role of glucose in determining rapid alteration of ATIII biologic activity, in vivo, in diabetes, probably mediated by labile non-enzymatic glycation. Glucose 36-43 serpin family C member 1 Homo sapiens 79-84 2955429-5 1987 Introduction of amino acids between the arylsulfonyl blocking group and amino nitrogen influence particularly the antithrombin activity. hydrazine 72-86 serpin family C member 1 Homo sapiens 114-126 2955429-8 1987 It is concluded that the N alpha-moiety is of decisive importance for the antithrombin activity of derivatives of 4-amidinophenylalanine. 4-carbamimidoyl-L-phenylalanine 114-136 serpin family C member 1 Homo sapiens 74-86 3105116-3 1987 Sephacryl S-200 gel chromatography of serum demonstrated that the neoantigen eluted with the first two, early eluting protein peaks; thus the neoantigen had a higher molecular weight than native antithrombin. sephacryl S 200 0-15 serpin family C member 1 Homo sapiens 195-207 3105116-5 1987 Sephacryl S-200 chromatography of factor IX concentrate-treated hemophilic plasma also showed an early eluting peak of antithrombin antigen of more cathodal mobility than normal in crossed immunoelectrophoresis. sephacryl s 0-11 serpin family C member 1 Homo sapiens 119-131 2433298-5 1987 AT III (1-6 U/ml) reduced basal tone and significantly inhibited, in a concentration-dependent manner, the contractile responses to K+, 5-HT, PGD2, PGF2 alpha, and plasmin. Dinoprost 148-152 serpin family C member 1 Homo sapiens 0-6 3565746-14 1987 125I-Fluoresceinamine-derivatized heparin retains its ability to interact specifically with heparin-binding proteins such as human protease nexin-I and antithrombin III. 125i-fluoresceinamine 0-21 serpin family C member 1 Homo sapiens 152-168 3619144-6 1987 II is likely that its antithrombin activity in vivo is restricted to the areas rich in dermatan sulfate. Dermatan Sulfate 87-103 serpin family C member 1 Homo sapiens 22-34 3565746-14 1987 125I-Fluoresceinamine-derivatized heparin retains its ability to interact specifically with heparin-binding proteins such as human protease nexin-I and antithrombin III. Heparin 34-41 serpin family C member 1 Homo sapiens 152-168 3620582-3 1987 The anticoagulant action of heparin is mainly antithrombin III (AT III) dependent and the binding site of AT III on the heparin molecule has been recently identified. Heparin 28-35 serpin family C member 1 Homo sapiens 46-62 3620582-3 1987 The anticoagulant action of heparin is mainly antithrombin III (AT III) dependent and the binding site of AT III on the heparin molecule has been recently identified. Heparin 28-35 serpin family C member 1 Homo sapiens 64-70 3620582-3 1987 The anticoagulant action of heparin is mainly antithrombin III (AT III) dependent and the binding site of AT III on the heparin molecule has been recently identified. Heparin 28-35 serpin family C member 1 Homo sapiens 106-112 3609485-3 1987 Moderately reduced ATIII activity before or immediately after surgery is neither sensitive nor specific for a high risk of postoperative venous thromboembolism (VTE), while moderately reduced ATIII activity during heparin treatment for VTE fails to indicate an unusually large heparin requirement or to predict recurrence. Heparin 214-221 serpin family C member 1 Homo sapiens 192-197 2441925-4 1987 Polysaccharides are antithrombin-III and heparin co-factor-II dependent or independent regarding their biological activity. Polysaccharides 0-15 serpin family C member 1 Homo sapiens 20-36 3111953-3 1987 In the presence of heparin, AT III is converted from its progressive activity state to an immediate activity state. Heparin 19-26 serpin family C member 1 Homo sapiens 28-34 3301469-2 1987 The latter is also known as antithrombin BM, because of its moderate binding affinity to heparin. Heparin 89-96 serpin family C member 1 Homo sapiens 28-40 3817736-9 1987 In the antithrombin III group and the antithrombin III plus heparin group, however, creatinine clearance was moderately elevated while FENa and CH2O remained unchanged as compared with the values before the burn. Creatinine 84-94 serpin family C member 1 Homo sapiens 38-54 3114102-3 1987 Crossed immunoelectrophoresis of AT III on heparin-agarose was also carried out in plasma and serum. Heparin 43-50 serpin family C member 1 Homo sapiens 33-39 3114102-3 1987 Crossed immunoelectrophoresis of AT III on heparin-agarose was also carried out in plasma and serum. Sepharose 51-58 serpin family C member 1 Homo sapiens 33-39 3114102-7 1987 In all groups all serum AT III parameters were higher than in controls; crossed immunoelectrophoresis of AT III on heparin-agarose indicated that this finding was due to a lower formation of complexed AT III in serum. Heparin 115-122 serpin family C member 1 Homo sapiens 105-111 3114102-7 1987 In all groups all serum AT III parameters were higher than in controls; crossed immunoelectrophoresis of AT III on heparin-agarose indicated that this finding was due to a lower formation of complexed AT III in serum. Heparin 115-122 serpin family C member 1 Homo sapiens 105-111 3114102-7 1987 In all groups all serum AT III parameters were higher than in controls; crossed immunoelectrophoresis of AT III on heparin-agarose indicated that this finding was due to a lower formation of complexed AT III in serum. Sepharose 123-130 serpin family C member 1 Homo sapiens 105-111 3114102-7 1987 In all groups all serum AT III parameters were higher than in controls; crossed immunoelectrophoresis of AT III on heparin-agarose indicated that this finding was due to a lower formation of complexed AT III in serum. Sepharose 123-130 serpin family C member 1 Homo sapiens 105-111 3114102-8 1987 AT III heparin cofactor serum values were the same whatever the INR over a large range (9.3-1.5); the highest anti-Xa heparin cofactor serum levels were noted in the groups treated more intensely (groups 1 and 2). Heparin 7-14 serpin family C member 1 Homo sapiens 0-6 3817736-10 1987 The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, creatinine clearance and CH2O. Creatinine 121-131 serpin family C member 1 Homo sapiens 4-20 3817736-10 1987 The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, creatinine clearance and CH2O. Formaldehyde 146-150 serpin family C member 1 Homo sapiens 4-20 2828272-1 1987 In order to obtain a radioiodinated antithrombin III (AT III) with a good labelling yield and optimal biological properties towards heparin, thrombin and its anti-AT III monoclonal antibodies, we compared the classical labelling methods and found them wanting. Heparin 132-139 serpin family C member 1 Homo sapiens 36-52 2828272-1 1987 In order to obtain a radioiodinated antithrombin III (AT III) with a good labelling yield and optimal biological properties towards heparin, thrombin and its anti-AT III monoclonal antibodies, we compared the classical labelling methods and found them wanting. Heparin 132-139 serpin family C member 1 Homo sapiens 54-60 3794520-1 1987 To test the hypothesis that binding to an endogenous heparin-like substance controls breakdown of antithrombin III (ATIII) in vivo, the metabolic behavior of a commercial ATIII concentrate was investigated in three normal volunteers and five subjects with hereditary ATIII deficiency. Heparin 53-60 serpin family C member 1 Homo sapiens 98-114 3794520-1 1987 To test the hypothesis that binding to an endogenous heparin-like substance controls breakdown of antithrombin III (ATIII) in vivo, the metabolic behavior of a commercial ATIII concentrate was investigated in three normal volunteers and five subjects with hereditary ATIII deficiency. Heparin 53-60 serpin family C member 1 Homo sapiens 116-121 3794520-7 1987 Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction. Heparin 113-120 serpin family C member 1 Homo sapiens 24-29 3794520-7 1987 Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction. Heparin 202-209 serpin family C member 1 Homo sapiens 24-29 3794520-7 1987 Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction. Heparin 202-209 serpin family C member 1 Homo sapiens 86-91 3794520-7 1987 Assuming that antigenic ATIII represented both functional inhibitor and dysfunctional ATIII incapable of binding heparin, these data are consistent with the supposition that interaction with endogenous heparin or a similar substance may regulate a catabolic pathway marking ATIII for destruction. Heparin 202-209 serpin family C member 1 Homo sapiens 86-91 3433205-4 1987 In 72-96 h of treatment intravenous heparin administration resulted in a decrease in a level of blood antithrombin III causing a decrease in the efficacy of heparin therapy. Heparin 36-43 serpin family C member 1 Homo sapiens 102-118 2444745-0 1987 [A modified method of determining antithrombin III activity by diffusion in thrombin agarose]. Sepharose 85-92 serpin family C member 1 Homo sapiens 34-50 3433205-4 1987 In 72-96 h of treatment intravenous heparin administration resulted in a decrease in a level of blood antithrombin III causing a decrease in the efficacy of heparin therapy. Heparin 157-164 serpin family C member 1 Homo sapiens 102-118 3798418-2 1986 The interaction between the immobilized heparin, added thrombin, and antithrombin III [AT] was investigated. Heparin 40-47 serpin family C member 1 Homo sapiens 69-85 2432917-7 1986 The anticoagulant activities of these last four SPS in plasma depleted of both AT III and HC II were similar to their respective activities in normal plasma. Sodium phenolsulfonate 48-51 serpin family C member 1 Homo sapiens 79-85 2436331-2 1986 Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively. Heparin 0-7 serpin family C member 1 Homo sapiens 81-87 2436331-2 1986 Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively. Pentosan Sulfuric Polyester 12-32 serpin family C member 1 Homo sapiens 81-87 2436331-2 1986 Heparin and pentosan polysulfate (PPS) interact in plasma with antithrombin III (AT III) and Heparin cofactor II (HC II) respectively. Pentosan Sulfuric Polyester 34-37 serpin family C member 1 Homo sapiens 81-87 2436331-11 1986 This suggest that clinical conditions associated with heparin treatment may be important for the effect of heparin on AT III metabolism previously reported in patients. Heparin 54-61 serpin family C member 1 Homo sapiens 118-124 2436331-11 1986 This suggest that clinical conditions associated with heparin treatment may be important for the effect of heparin on AT III metabolism previously reported in patients. Heparin 107-114 serpin family C member 1 Homo sapiens 118-124 2432917-3 1986 The SPS varied in their relative activities as catalysts of thrombin inhibition by purified AT III or HC II. Sodium phenolsulfonate 4-7 serpin family C member 1 Homo sapiens 92-98 2432917-4 1986 The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively. Heparin 32-39 serpin family C member 1 Homo sapiens 141-147 2432917-4 1986 The anticoagulant activities of heparin and dermatan sulphate were primarily attributable to their ability to enhance thrombin inhibition by AT III and HC II respectively. Dermatan Sulfate 44-61 serpin family C member 1 Homo sapiens 141-147 2432917-6 1986 Pentosan polysulphate, high molecular weight dextran sulphate, heparin with low affinity for AT III and a sulphated heparin derivative had weaker anticoagulant activities in normal plasma than standard heparin. Heparin 63-70 serpin family C member 1 Homo sapiens 93-99 3790695-8 1986 Antithrombin III, a natural thrombin inhibitor, did not significantly reduce the thrombin concentrations, but antithrombin III accelerated by heparin greatly reduced the local thrombin concentrations. Heparin 142-149 serpin family C member 1 Homo sapiens 110-126 3783325-4 1986 During pyridoxine treatment, antithrombin III activity was rapidly restored to normal; factor VII increased and beta-thromboglobulin decreased. Pyridoxine 7-17 serpin family C member 1 Homo sapiens 29-45 3602697-0 1986 [Antithrombin III levels in patients with acute thromboembolism during treatment with heparin]. Heparin 86-93 serpin family C member 1 Homo sapiens 1-17 3782075-0 1986 Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa. Heparin 36-43 serpin family C member 1 Homo sapiens 55-67 3782075-0 1986 Role of ternary complexes, in which heparin binds both antithrombin and proteinase, in the acceleration of the reactions between antithrombin and thrombin or factor Xa. Heparin 36-43 serpin family C member 1 Homo sapiens 129-141 3782075-1 1986 Oligosaccharides (10-20 monosaccharide units) with high affinity for antithrombin, as well as larger high-affinity heparin fractions (having relative molecular masses between 6,000 and 21,500), all markedly accelerated the inhibition of Factor Xa by antithrombin. Oligosaccharides 0-16 serpin family C member 1 Homo sapiens 69-81 3782075-2 1986 Moreover, all high-affinity oligosaccharides and heparins enhanced, to a similar extent, the amount of free proteolytically modified antithrombin cleaved at the reactive bond by Factor Xa. Oligosaccharides 28-44 serpin family C member 1 Homo sapiens 133-145 3782075-2 1986 Moreover, all high-affinity oligosaccharides and heparins enhanced, to a similar extent, the amount of free proteolytically modified antithrombin cleaved at the reactive bond by Factor Xa. Heparin 49-57 serpin family C member 1 Homo sapiens 133-145 3782075-3 1986 In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme. Heparin 37-44 serpin family C member 1 Homo sapiens 164-176 3782075-3 1986 In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme. Heparin 37-44 serpin family C member 1 Homo sapiens 219-231 3782075-3 1986 In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme. Monosaccharides 70-84 serpin family C member 1 Homo sapiens 164-176 3782075-3 1986 In contrast, a minimum high-affinity heparin size of approximately 18 monosaccharide units was required to significantly accelerate the inactivation of thrombin by antithrombin and to enhance the production of modified antithrombin by this enzyme. Monosaccharides 70-84 serpin family C member 1 Homo sapiens 219-231 3782075-5 1986 In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin. octadecasaccharide 66-84 serpin family C member 1 Homo sapiens 48-60 3782075-5 1986 In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin. Heparin 109-117 serpin family C member 1 Homo sapiens 48-60 3782075-5 1986 In competition experiments, binary complexes of antithrombin with octadecasaccharide or larger high-affinity heparins, but not with smaller oligosaccharides, displaced inactivated 125I-thrombin from matrix-linked low-affinity heparin. Heparin 109-116 serpin family C member 1 Homo sapiens 48-60 3782075-7 1986 These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units. Heparin 95-102 serpin family C member 1 Homo sapiens 52-64 3782075-7 1986 These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units. Heparin 95-102 serpin family C member 1 Homo sapiens 148-160 3782075-7 1986 These results indicate that simultaneous binding of antithrombin and thrombin to high-affinity heparin is a prerequisite to the acceleration of the antithrombin-thrombin reaction and that the minimum heparin sequence capable of binding both proteins comprises approximately 18 monosaccharide units. Monosaccharides 277-291 serpin family C member 1 Homo sapiens 52-64 3798412-6 1986 This suggests that Factor Xa and antithrombin III have similar affinities for this immobilized heparin, unlike the situation for thrombin (Thromb-Res., 20, 543-554, 1980). Heparin 95-102 serpin family C member 1 Homo sapiens 33-49 3771538-5 1986 This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III. hexasaccharide 5-19 serpin family C member 1 Homo sapiens 46-62 3563966-1 1986 Four members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and half-normal antithrombin activity with or without heparin. Heparin 223-230 serpin family C member 1 Homo sapiens 109-125 3563966-1 1986 Four members of an Italian family (two with histories of venous thromboembolism) had a qualitative defect of antithrombin III reflected by normal antigen concentrations and half-normal antithrombin activity with or without heparin. Heparin 223-230 serpin family C member 1 Homo sapiens 109-121 3563966-4 1986 A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Heparin 42-49 serpin family C member 1 Homo sapiens 21-37 3563966-4 1986 A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Heparin 68-75 serpin family C member 1 Homo sapiens 21-37 3563966-4 1986 A normal affinity of antithrombin III for heparin was documented by heparin-sepharose chromatography. Sepharose 76-85 serpin family C member 1 Homo sapiens 21-37 3563966-5 1986 Affinity adsorption of the propositus" plasma to human alpha-thrombin immobilized on sepharose beads revealed defective binding of the antithrombin III to thrombin-sepharose. Sepharose 164-173 serpin family C member 1 Homo sapiens 135-151 3771538-5 1986 This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III. hexasaccharide 5-19 serpin family C member 1 Homo sapiens 249-265 3771538-5 1986 This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III. heparin oligosaccharides 125-149 serpin family C member 1 Homo sapiens 46-62 3771538-5 1986 This hexasaccharide contains a portion of the antithrombin III-binding site and has a Kd of 4 X 10(-5) M. Unlike other small heparin oligosaccharides, which are specific for coagulation factor Xa, it inhibits both factors IIa and Xa equally through antithrombin III. heparin oligosaccharides 125-149 serpin family C member 1 Homo sapiens 249-265 3771538-7 1986 These studies suggest the occurrence of contiguous binding sites on heparin for Xa, antithrombin III, and heparin cofactor II. Heparin 68-75 serpin family C member 1 Homo sapiens 84-100 2429788-5 1986 Incubation of normal plasma with 250 nmol/l glucose (a level approximately 6 X higher than encountered in uncontrolled diabetes) resulted in a 17% and 6% decrease in antithrombin III and alpha 1-proteinase inhibitor activities. Glucose 44-51 serpin family C member 1 Homo sapiens 166-182 2432675-4 1986 On the other hand, dextran sulfate accelerated antithrombin III-thrombin reaction only about 40-fold less than heparin. Dextran Sulfate 19-34 serpin family C member 1 Homo sapiens 47-63 3790498-4 1986 When both factor Va and phospholipid were present during prothrombin activation, factor Xa inhibition by antithrombin III was reduced about 10-fold, with a second-order rate constant of 1.3 X 10(5) M-1 min-1. Phospholipids 24-36 serpin family C member 1 Homo sapiens 105-121 3790498-5 1986 Factor Xa in the prothrombin activation mixture that contained both factor Va and phospholipid was even more protected from inhibition by the antithrombin III-heparin complex. Phospholipids 82-94 serpin family C member 1 Homo sapiens 142-158 3790498-6 1986 The first-order rate constants of these reactions at 200 nM antithrombin III and normalized to heparin at 1 microgram/mL were 0.33 and 9.5 min-1 in the presence and absence of factor Va and phospholipid, respectively. Heparin 95-102 serpin family C member 1 Homo sapiens 60-76 3790498-6 1986 The first-order rate constants of these reactions at 200 nM antithrombin III and normalized to heparin at 1 microgram/mL were 0.33 and 9.5 min-1 in the presence and absence of factor Va and phospholipid, respectively. Phospholipids 190-202 serpin family C member 1 Homo sapiens 60-76 3767984-2 1986 We report here that a synthetic heparin pentasaccharide with high affinity for antithrombin III has the same effect as heparin at about the same concentration. IC 831423 32-55 serpin family C member 1 Homo sapiens 79-95 2432885-7 1986 Fractions of standard heparin with high affinity for antithrombin III also had greater affinity for endothelium. Heparin 22-29 serpin family C member 1 Homo sapiens 53-69 2432885-8 1986 However, these two properties of heparin (affinity for antithrombin III and affinity for endothelial cells) could be dissociated. Heparin 33-40 serpin family C member 1 Homo sapiens 55-71 2432885-10 1986 Synthetic pentasaccharides, bearing the minimal sequence for binding to antithrombin III, did not bind to endothelial cells. pentasaccharides 10-26 serpin family C member 1 Homo sapiens 72-88 3766461-7 1986 The anti-Factor Xa activity of heparin was measured using chromogenic substrate S-2251, purified Factor Xa, and excess antithrombin III. Heparin 31-38 serpin family C member 1 Homo sapiens 119-135 3780071-8 1986 We suggest that the fibrinopeptide A is produced intraperitoneally and the antithrombin III-concentration in dialysate is sufficient to inhibit the fibrin formation after acceleration by heparin. Heparin 187-194 serpin family C member 1 Homo sapiens 75-91 3767984-2 1986 We report here that a synthetic heparin pentasaccharide with high affinity for antithrombin III has the same effect as heparin at about the same concentration. Heparin 32-39 serpin family C member 1 Homo sapiens 79-95 3764810-0 1986 The effect of operation and subcutaneous heparin on plasma levels of antithrombin-III. Heparin 41-48 serpin family C member 1 Homo sapiens 69-85 3743657-2 1986 Only 15% of the biologic activity of the complex carbohydrates derived from human skin fibroblasts was expressed when the heparin-binding domain an antithrombin was chemically modified at the Trp 49 residue. Carbohydrates 49-62 serpin family C member 1 Homo sapiens 148-160 3764810-8 1986 These findings support the hypothesis that AT-III is consumed during coagulation and its utilization is increased in the presence of heparin. Heparin 133-140 serpin family C member 1 Homo sapiens 43-49 3800942-1 1986 The effect of heparin fractions of various Mr, with high affinity for antithrombin III, on the kinetics of the reaction between factor Xa and antithrombin III have been studied using purified human proteins. Heparin 14-21 serpin family C member 1 Homo sapiens 70-86 3800942-1 1986 The effect of heparin fractions of various Mr, with high affinity for antithrombin III, on the kinetics of the reaction between factor Xa and antithrombin III have been studied using purified human proteins. Heparin 14-21 serpin family C member 1 Homo sapiens 142-158 3800942-7 1986 These data suggest that the increased rates of inhibition observed with heparins of higher Mr may be due to an involvement of heparin binding to factor Xa as well as to antithrombin III. Heparin 72-80 serpin family C member 1 Homo sapiens 169-185 3800942-7 1986 These data suggest that the increased rates of inhibition observed with heparins of higher Mr may be due to an involvement of heparin binding to factor Xa as well as to antithrombin III. Heparin 72-79 serpin family C member 1 Homo sapiens 169-185 3743657-2 1986 Only 15% of the biologic activity of the complex carbohydrates derived from human skin fibroblasts was expressed when the heparin-binding domain an antithrombin was chemically modified at the Trp 49 residue. Heparin 122-129 serpin family C member 1 Homo sapiens 148-160 3743657-2 1986 Only 15% of the biologic activity of the complex carbohydrates derived from human skin fibroblasts was expressed when the heparin-binding domain an antithrombin was chemically modified at the Trp 49 residue. Tryptophan 192-195 serpin family C member 1 Homo sapiens 148-160 2425853-2 1986 Affinity chromatography of the fraction with antithrombin III-agarose yielded two chondroitin sulfate proteoglycans of a non-binding (proteoglycan IA) and binding (proteoglycan IB) nature. Sepharose 62-69 serpin family C member 1 Homo sapiens 45-61 3755846-6 1986 In the presence of heparin, measurement of the rate of inhibition under pseudo first order conditions can be made only when the NaCl concentration is at least 0.3 M. The significance of the presented data for designing a functional assay of AT III is discussed. Heparin 19-26 serpin family C member 1 Homo sapiens 241-247 3755846-6 1986 In the presence of heparin, measurement of the rate of inhibition under pseudo first order conditions can be made only when the NaCl concentration is at least 0.3 M. The significance of the presented data for designing a functional assay of AT III is discussed. Sodium Chloride 128-132 serpin family C member 1 Homo sapiens 241-247 3775688-1 1986 A qualitative defect of antithrombin III (AT III) was demonstrated in four members of a large Tunisian family by the discrepancy between a normal amount of antigen and decreased or absent heparin cofactor activity. Heparin 188-195 serpin family C member 1 Homo sapiens 24-40 3775688-1 1986 A qualitative defect of antithrombin III (AT III) was demonstrated in four members of a large Tunisian family by the discrepancy between a normal amount of antigen and decreased or absent heparin cofactor activity. Heparin 188-195 serpin family C member 1 Homo sapiens 42-48 3775688-4 1986 Anti-F. Xa activity was also absent when using low molecular weight heparin or a synthetic pentasaccharide, representing the binding site to AT III. Heparin 68-75 serpin family C member 1 Homo sapiens 141-147 3775688-4 1986 Anti-F. Xa activity was also absent when using low molecular weight heparin or a synthetic pentasaccharide, representing the binding site to AT III. pentasaccharide 91-106 serpin family C member 1 Homo sapiens 141-147 3775688-5 1986 The lack of affinity of the propositus AT III for heparin was demonstrated by two-dimensional immunoelectrophoresis and chromatography on heparin-Sepharose. Heparin 50-57 serpin family C member 1 Homo sapiens 39-45 3775688-6 1986 The parents, first cousins, and the sister of the propositus also demonstrated a qualitative abnormality of AT III, with levels of heparin cofactor activity close to 50% of the normal range. Heparin 131-138 serpin family C member 1 Homo sapiens 108-114 2425853-2 1986 Affinity chromatography of the fraction with antithrombin III-agarose yielded two chondroitin sulfate proteoglycans of a non-binding (proteoglycan IA) and binding (proteoglycan IB) nature. Chondroitin Sulfates 82-101 serpin family C member 1 Homo sapiens 45-61 3800906-0 1986 A fragment of antithrombin that binds both heparin and thrombin. Heparin 43-50 serpin family C member 1 Homo sapiens 14-26 3730427-0 1986 A comparison of the strength of binding of antithrombin III, protamine and poly(L-lysine) to heparin samples of different anticoagulant activities. Heparin 93-100 serpin family C member 1 Homo sapiens 43-59 3730427-1 1986 The limiting concentrations, i.e., those concentrations of sodium chloride required to completely disrupt the complexes of heparin with antithrombin III, protamine and poly(L-lysine), were determined using fluorescence techniques, in order to compare the binding strengths of these complexes. Sodium Chloride 59-74 serpin family C member 1 Homo sapiens 136-152 3730427-1 1986 The limiting concentrations, i.e., those concentrations of sodium chloride required to completely disrupt the complexes of heparin with antithrombin III, protamine and poly(L-lysine), were determined using fluorescence techniques, in order to compare the binding strengths of these complexes. Heparin 123-130 serpin family C member 1 Homo sapiens 136-152 3730427-4 1986 In contrast, the limiting salt concentration values for complexes formed between antithrombin III and heparin did not change with either the degree of sulphation or the biological potency of the heparin samples. Salts 26-30 serpin family C member 1 Homo sapiens 81-97 3730427-4 1986 In contrast, the limiting salt concentration values for complexes formed between antithrombin III and heparin did not change with either the degree of sulphation or the biological potency of the heparin samples. Heparin 102-109 serpin family C member 1 Homo sapiens 81-97 3730427-5 1986 A low-potency heparin simply contained a smaller number of molecules which possessed the intact antithrombin III binding site (thus being fully "anticoagulant active") than a high-potency sample. Heparin 14-21 serpin family C member 1 Homo sapiens 96-112 3730427-6 1986 Low-affinity heparin did not contain these binding sites and thus showed a low affinity for antithrombin III. Heparin 13-20 serpin family C member 1 Homo sapiens 92-108 3730427-7 1986 High-potency heparin, being highly sulphated, possessed a higher affinity for protamine and poly(L-lysine) than for antithrombin III. Heparin 13-20 serpin family C member 1 Homo sapiens 116-132 3730427-8 1986 However, after partial N-desulphation of heparin, the subsequent heparin-protamine complex was more weakly bound than a significant proportion of the corresponding heparin-antithrombin III complexes. Heparin 41-48 serpin family C member 1 Homo sapiens 172-188 3800906-2 1986 These fragments did not exhibit direct thrombin-neutralizing activity; however, one unique fragment was found to bind to heparin-Sepharose and also to interfere with the inhibition of thrombin by intact antithrombin. Heparin 121-128 serpin family C member 1 Homo sapiens 203-215 3800906-2 1986 These fragments did not exhibit direct thrombin-neutralizing activity; however, one unique fragment was found to bind to heparin-Sepharose and also to interfere with the inhibition of thrombin by intact antithrombin. Sepharose 129-138 serpin family C member 1 Homo sapiens 203-215 3800906-4 1986 At a concentration of 46 nM, this product decreased the heparin-enhanced thrombin-inhibitory activity of antithrombin by half, and completely abolished this inhibition when above 300 nM. Heparin 56-63 serpin family C member 1 Homo sapiens 105-117 3800906-9 1986 It is concluded that this peptide possesses portions of the antithrombin molecule that bind to heparin as well as to a site on thrombin. Heparin 95-102 serpin family C member 1 Homo sapiens 60-72 3738858-4 1986 The accelerating effect of heparin or potassium polyvinylsulfate for the inhibitory action of AT III is abolished by charge equivalent amounts of polycation. Heparin 27-34 serpin family C member 1 Homo sapiens 94-100 3731451-0 1986 Polyethylene glycol can be validly omitted from chromogenic peptide substrate assay for antithrombin III. Polyethylene Glycols 0-19 serpin family C member 1 Homo sapiens 88-104 3731451-1 1986 To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants. Polysorbates 161-169 serpin family C member 1 Homo sapiens 72-88 3731451-1 1986 To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants. Polysorbates 161-169 serpin family C member 1 Homo sapiens 100-116 3731451-1 1986 To investigate whether the characteristics of a commercial test kit for antithrombin III (Berichrom Antithrombin III) could be influenced by surfactants such as Tween-80 or polyethylene glycol (PEG), we performed some experiments with the original kit reagents and with the reagents dissolved in surfactants. Polyethylene Glycols 173-192 serpin family C member 1 Homo sapiens 72-88 3526065-1 1986 Urinary antithrombin III (AT III) related antigen was analyzed by SDS-polyacrylamide gel electrophoresis and Western blotting, and the nitrocellulose membrane was scanned with a 2-wavelength TLC scanner. Sodium Dodecyl Sulfate 66-69 serpin family C member 1 Homo sapiens 26-32 3526065-1 1986 Urinary antithrombin III (AT III) related antigen was analyzed by SDS-polyacrylamide gel electrophoresis and Western blotting, and the nitrocellulose membrane was scanned with a 2-wavelength TLC scanner. polyacrylamide 70-84 serpin family C member 1 Homo sapiens 26-32 3526065-5 1986 Further, the "index" revealed a significant proportional correlation with the total bilirubin and direct bilirubin, and also a significant inversely proportional correlation with the plasma AT III, suggesting that the "index" tends to become higher as liver function decreases. Bilirubin 84-93 serpin family C member 1 Homo sapiens 190-196 3526065-5 1986 Further, the "index" revealed a significant proportional correlation with the total bilirubin and direct bilirubin, and also a significant inversely proportional correlation with the plasma AT III, suggesting that the "index" tends to become higher as liver function decreases. Bilirubin 105-114 serpin family C member 1 Homo sapiens 190-196 3738858-4 1986 The accelerating effect of heparin or potassium polyvinylsulfate for the inhibitory action of AT III is abolished by charge equivalent amounts of polycation. polyvinyl sulfate 38-64 serpin family C member 1 Homo sapiens 94-100 3738862-1 1986 The changes that take place when a therapeutic antithrombin III (AT III) concentrate is heated in the presence of citrate ion have been assessed. Citric Acid 114-121 serpin family C member 1 Homo sapiens 47-63 3738862-1 1986 The changes that take place when a therapeutic antithrombin III (AT III) concentrate is heated in the presence of citrate ion have been assessed. Citric Acid 114-121 serpin family C member 1 Homo sapiens 65-71 3095926-0 1986 Acetylation of antithrombin III by aspirin. Aspirin 35-42 serpin family C member 1 Homo sapiens 15-31 3095926-2 1986 Since aspirin (acetylsalicylic acid) is known to acetylate numerous biologic macromolecules, the effect of aspirin on antithrombin III was investigated. Aspirin 107-114 serpin family C member 1 Homo sapiens 118-134 3095926-3 1986 It was found that antithrombin III is irreversibly inactivated by treatment with aspirin. Aspirin 81-88 serpin family C member 1 Homo sapiens 18-34 3095926-8 1986 Amino group analysis of aspirin-treated antithrombin III using trinitrobenzenesulfonic acid revealed that one to two primary amino groups are lost relative to the untreated antithrombin III. Aspirin 24-31 serpin family C member 1 Homo sapiens 40-56 3095926-8 1986 Amino group analysis of aspirin-treated antithrombin III using trinitrobenzenesulfonic acid revealed that one to two primary amino groups are lost relative to the untreated antithrombin III. Aspirin 24-31 serpin family C member 1 Homo sapiens 173-189 3095926-8 1986 Amino group analysis of aspirin-treated antithrombin III using trinitrobenzenesulfonic acid revealed that one to two primary amino groups are lost relative to the untreated antithrombin III. Trinitrobenzenesulfonic Acid 63-91 serpin family C member 1 Homo sapiens 40-56 3095926-9 1986 It is concluded that the reaction of aspirin with antithrombin III results in specific acetylation of lysine residues. Aspirin 37-44 serpin family C member 1 Homo sapiens 50-66 3095926-9 1986 It is concluded that the reaction of aspirin with antithrombin III results in specific acetylation of lysine residues. Lysine 102-108 serpin family C member 1 Homo sapiens 50-66 3754869-9 1986 The protective effect of S-protein on inactivation of thrombin by ATIII was demonstrated in functional assays with purified proteins and in plasma only in the presence of low concentrations of heparin. Heparin 193-200 serpin family C member 1 Homo sapiens 66-71 3754869-10 1986 Thus, S-protein may mediate its effect by scavenging heparin required for ATIII activation. Heparin 53-60 serpin family C member 1 Homo sapiens 74-79 3754869-4 1986 Functionally, S-protein in the presence of low concentrations of heparin, protects thrombin from inactivation by ATIII. Heparin 65-72 serpin family C member 1 Homo sapiens 113-118 3733936-1 1986 Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates. cross 0-5 serpin family C member 1 Homo sapiens 89-105 3754869-5 1986 Complex formation between S-protein and thrombin, and between S-protein, thrombin, and ATIII, was demonstrated by agarose gel electrophoresis and by two-dimensional immunoelectrophoresis of purified proteins and in recalcified, clotted plasma. Sepharose 114-121 serpin family C member 1 Homo sapiens 87-92 3771670-3 1986 Preventive treatment applied involves low-dose heparin (1.5 mg/kg/d) to maintain an antithrombin III concentration of at least 65%. Heparin 47-54 serpin family C member 1 Homo sapiens 84-100 3087016-3 1986 Esterification also abolished the binding of heparin to antithrombin as measured by changes in the intrinsic fluorescence. Heparin 45-52 serpin family C member 1 Homo sapiens 56-68 3733936-1 1986 Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates. Polystyrenes 13-25 serpin family C member 1 Homo sapiens 89-105 3733936-1 1986 Cross-linked polystyrenes modified with L-arginyl methyl ester mimic the binding site of antithrombin III and thrombin substrates. l-arginyl methyl ester 40-62 serpin family C member 1 Homo sapiens 89-105 3699029-12 1986 These findings not only indicate a direct interaction of S protein with heparin in the onset of the inhibition of thrombin by antithrombin-III--heparin, but also a contribution of S protein during enzyme-inhibitor complex formation. Heparin 72-79 serpin family C member 1 Homo sapiens 126-142 3697371-1 1986 Fluorescence polarization has been used to study the interaction of thrombin and heparin, and the catalysis by heparin of the combination of thrombin and antithrombin. Heparin 111-118 serpin family C member 1 Homo sapiens 154-166 3697371-8 1986 The complex formed between thrombin and heparin, to which antithrombin was attached, has a dissociation constant of 1-2 microM, again irrespective of the heparin molecular weight. Heparin 40-47 serpin family C member 1 Homo sapiens 58-70 3697371-8 1986 The complex formed between thrombin and heparin, to which antithrombin was attached, has a dissociation constant of 1-2 microM, again irrespective of the heparin molecular weight. Heparin 154-161 serpin family C member 1 Homo sapiens 58-70 3699029-0 1986 S protein modulates the heparin-catalyzed inhibition of thrombin by antithrombin III. Heparin 24-31 serpin family C member 1 Homo sapiens 68-84 3697371-9 1986 In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin. Heparin 7-14 serpin family C member 1 Homo sapiens 34-46 3697371-9 1986 In the heparin-catalysed thrombin-antithrombin reaction, an increase in the size of heparin leads to a lowering of the observed Km for thrombin. Heparin 84-91 serpin family C member 1 Homo sapiens 34-46 3697371-10 1986 A possible explanation is that thrombin, after initial binding to the heparin, moves rapidly to the site where it combines with antithrombin. Heparin 70-77 serpin family C member 1 Homo sapiens 128-140 3699029-2 1986 The interference of S protein with the heparin-catalyzed inhibition of thrombin by antithrombin III was studied in a purified system and in plasma. Heparin 39-46 serpin family C member 1 Homo sapiens 83-99 3754413-1 1986 Heparin cofactor II and antithrombin III are plasma proteins functionally similar in their ability to inhibit thrombin at accelerated rates in the presence of heparin. Heparin 159-166 serpin family C member 1 Homo sapiens 24-40 3699029-6 1986 While the association constant of thrombin--antithrombin III in the presence of 0.05 U/ml heparin amounted to 2.5 X 10(8) M-1, an approximately 200-fold decrease of this value was observed in the presence of S protein. Heparin 90-97 serpin family C member 1 Homo sapiens 44-60 3699029-7 1986 The fast formation of the covalent complex between thrombin and antithrombin III in the presence of heparin was impaired as a result of the presence of S protein, as was shown by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Heparin 100-107 serpin family C member 1 Homo sapiens 64-80 3699029-7 1986 The fast formation of the covalent complex between thrombin and antithrombin III in the presence of heparin was impaired as a result of the presence of S protein, as was shown by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. polyacrylamide 179-193 serpin family C member 1 Homo sapiens 64-80 3699029-7 1986 The fast formation of the covalent complex between thrombin and antithrombin III in the presence of heparin was impaired as a result of the presence of S protein, as was shown by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. Sodium Dodecyl Sulfate 233-255 serpin family C member 1 Homo sapiens 64-80 3486013-0 1986 Interaction of factor XIa and antithrombin in the presence and absence of heparin. Heparin 74-81 serpin family C member 1 Homo sapiens 30-42 3486013-5 1986 These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor. sodium dodecyl sulfatepolyacrylamide 143-179 serpin family C member 1 Homo sapiens 105-117 3486013-5 1986 These results were confirmed in a qualitative manner by directly monitoring the generation of factor XIa-antithrombin interaction product with sodium dodecyl sulfatepolyacrylamide gel electrophoresis (SDS-PAGE) and Western blot analysis using an antibody population specific for the protease inhibitor. Sodium Dodecyl Sulfate 201-204 serpin family C member 1 Homo sapiens 105-117 3715788-4 1986 Crossed immunoelectrophoresis of AT III in the presence of heparin revealed in the plasma an abnormal slow-moving peak. Heparin 59-66 serpin family C member 1 Homo sapiens 33-39 3715788-5 1986 When tested by affinity chromatography on heparin Sepharose, this abnormal AT III did not bind to heparin. Heparin 42-49 serpin family C member 1 Homo sapiens 75-81 3715788-5 1986 When tested by affinity chromatography on heparin Sepharose, this abnormal AT III did not bind to heparin. Sepharose 50-59 serpin family C member 1 Homo sapiens 75-81 3715788-8 1986 We therefore considered our patient as homozygous for an AT III molecular abnormality affecting the binding site for heparin. Heparin 117-124 serpin family C member 1 Homo sapiens 57-63 3715796-0 1986 Thrombosis prophylaxis in an AT III deficient pregnant woman: application of a low molecular weight heparinoid. Heparinoids 100-110 serpin family C member 1 Homo sapiens 29-35 3711199-1 1986 Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III. Polystyrenes 10-22 serpin family C member 1 Homo sapiens 145-161 3711199-1 1986 Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III. sulphonate 40-50 serpin family C member 1 Homo sapiens 145-161 3711199-1 1986 Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III. l-arginyl methyl ester 55-77 serpin family C member 1 Homo sapiens 145-161 3711199-1 1986 Insoluble polystyrenes substituted with sulphonate and L-arginyl methyl ester (PAOM) present substituents mimicking the reactive binding site of antithrombin III. paom 79-83 serpin family C member 1 Homo sapiens 145-161 3013215-3 1986 The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin. metaperiodate 46-55 serpin family C member 1 Homo sapiens 123-135 3013215-3 1986 The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin. metaperiodate 46-55 serpin family C member 1 Homo sapiens 265-277 3013215-3 1986 The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin. Glycols 166-172 serpin family C member 1 Homo sapiens 123-135 3013215-3 1986 The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin. Glycols 166-172 serpin family C member 1 Homo sapiens 265-277 3013215-3 1986 The drop of anticoagulant activity induced by periodate oxidation was paralleled by a substantial decrease of affinity for antithrombin, and is thought to arise from glycol splitting at the level of the D-glucuronic acid residue that is part of the active site for antithrombin. Glucuronic Acid 203-220 serpin family C member 1 Homo sapiens 265-277 3013215-5 1986 The residual anticoagulant activity of periodate-oxidized heparins obtained from preparations - such as those from beef lung - rich in trisulfated disaccharide sequences is discussed in terms of the influence of charge density on heparin-protease interactions not mediated by antithrombin. metaperiodate 39-48 serpin family C member 1 Homo sapiens 276-288 3013215-5 1986 The residual anticoagulant activity of periodate-oxidized heparins obtained from preparations - such as those from beef lung - rich in trisulfated disaccharide sequences is discussed in terms of the influence of charge density on heparin-protease interactions not mediated by antithrombin. Heparin 58-66 serpin family C member 1 Homo sapiens 276-288 3708627-9 1986 This synthetic pentasaccharide binds to antithrombin III with an association constant similar to that of high-affinity heparin and elicits a potent anti-factor Xa activity in plasma. pentasaccharide 15-30 serpin family C member 1 Homo sapiens 40-56 3949769-0 1986 Dependence of antithrombin III and thrombin binding stoichiometries and catalytic activity on the molecular weight of affinity-purified heparin. Heparin 136-143 serpin family C member 1 Homo sapiens 14-30 3949769-1 1986 Heparin was fractionated by affinity chromatography on immobilized antithrombin III followed by gel filtration on Sephadex G-100. Heparin 0-7 serpin family C member 1 Homo sapiens 67-83 3949769-3 1986 The binding stoichiometries of antithrombin III and thrombin interactions with the heparin of these fractions were measured, using changes in intrinsic and extrinsic fluorescence. Heparin 83-90 serpin family C member 1 Homo sapiens 31-47 3949769-5 1986 As the molecular weight of heparin varied from about 10,000 to 30,000, the average number of antithrombin and thrombin sites/heparin molecule varied from 1.0 to 2.1 and 2.4 to 6.8. Heparin 27-34 serpin family C member 1 Homo sapiens 93-105 3949769-8 1986 This can be explained by assuming that heparin functions as a template for both proteins, that all bound thrombin and antithrombin III molecules are accessible to each other, and that the rate at which a bound molecule reacts is proportional to the number of molecules of its interacting counterpart bound. Heparin 39-46 serpin family C member 1 Homo sapiens 118-134 3949769-12 1986 259, 5670-5677), who demonstrated that the rate at which single molecules of antithrombin III, covalently attached to heparin, react increases as the thrombin binding capacity (chain length) of heparin increases. Heparin 118-125 serpin family C member 1 Homo sapiens 77-93 3949769-12 1986 259, 5670-5677), who demonstrated that the rate at which single molecules of antithrombin III, covalently attached to heparin, react increases as the thrombin binding capacity (chain length) of heparin increases. Heparin 194-201 serpin family C member 1 Homo sapiens 77-93 3698718-5 1986 Low-dose heparin acts through its effect of factor Xa and activation of antithrombin III; DHE selectively increases venous smooth muscle tone to accelerate venous blood flow velocity and minimize venous pooling. Heparin 9-16 serpin family C member 1 Homo sapiens 72-88 3698718-5 1986 Low-dose heparin acts through its effect of factor Xa and activation of antithrombin III; DHE selectively increases venous smooth muscle tone to accelerate venous blood flow velocity and minimize venous pooling. Dihydroergotamine 90-93 serpin family C member 1 Homo sapiens 72-88 3715809-0 1986 Effects of different ions on the interactions of heparin with bovine antithrombin III and thrombin. Heparin 49-56 serpin family C member 1 Homo sapiens 69-85 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. tris-salts 8-18 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Sulfates 37-44 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Phosphates 46-55 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Acetates 60-67 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Acetates 60-67 serpin family C member 1 Homo sapiens 124-130 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Chlorides 70-78 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Chlorides 70-78 serpin family C member 1 Homo sapiens 124-130 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Heparin 139-146 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Heparin 139-146 serpin family C member 1 Homo sapiens 124-130 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Sepharose 147-156 serpin family C member 1 Homo sapiens 106-122 3715809-1 1986 Of four Tris-salts tested (chloride, sulfate, phosphate and acetate), chloride caused complete elution of antithrombin III (AT III) from a heparin-Sepharose column and sulfate caused partial elution. Sepharose 147-156 serpin family C member 1 Homo sapiens 124-130 3715809-2 1986 AT III was also partially eluted from the column with sodium acetate, but not Tris acetate. Sodium Acetate 54-68 serpin family C member 1 Homo sapiens 0-6 3715809-5 1986 These findings indicate that the affinity of heparin to AT III was influenced only by strongly electronegative ions, whereas its affinity to thrombin was affected by both strongly electropositive and strongly electronegative ions. Heparin 45-52 serpin family C member 1 Homo sapiens 56-62 3725864-4 1986 The exchange of the glycine residue by prolin in compounds former described caused a decreased antithrombin effect. Glycine 20-27 serpin family C member 1 Homo sapiens 95-107 3725864-4 1986 The exchange of the glycine residue by prolin in compounds former described caused a decreased antithrombin effect. DL-Proline 39-45 serpin family C member 1 Homo sapiens 95-107 3949798-5 1986 An octasaccharide with characteristic marked ability to accelerate the inactivation of Factor Xa by antithrombin retained greater than 50% of its activity even at a histidine-rich glycoprotein/oligosaccharide molar ratio of 500:1. Octasaccharide 3-17 serpin family C member 1 Homo sapiens 100-112 3949798-8 1986 218, 725-732), therefore requires interaction with saccharide sequences in addition to the antithrombin-binding pentasaccharide of heparin in order to efficiently express its antiheparin activity. pentasaccharide 112-127 serpin family C member 1 Homo sapiens 91-103 3949798-8 1986 218, 725-732), therefore requires interaction with saccharide sequences in addition to the antithrombin-binding pentasaccharide of heparin in order to efficiently express its antiheparin activity. Heparin 131-138 serpin family C member 1 Homo sapiens 91-103 3949807-1 1986 The molecular interactions between components of the heparin-catalyzed antithrombin III/thrombin reaction were investigated by light scattering. Heparin 53-60 serpin family C member 1 Homo sapiens 71-87 3949807-2 1986 When heparin was added to antithrombin III, the molecular weight increased to a maximum and then decreased to that of a 1:1 (antithrombin III X heparin) complex. Heparin 5-12 serpin family C member 1 Homo sapiens 26-42 3949807-2 1986 When heparin was added to antithrombin III, the molecular weight increased to a maximum and then decreased to that of a 1:1 (antithrombin III X heparin) complex. Heparin 5-12 serpin family C member 1 Homo sapiens 26-38 3949807-3 1986 The initial molecular weights at low heparin to antithrombin III ratios were consistent with the formation of a 2:1 (antithrombin III X heparin) complex in which only one antithrombin III molecule had undergone the conformational change measured by protein fluorescence enhancement. Heparin 37-44 serpin family C member 1 Homo sapiens 117-133 3949807-8 1986 In the presence of stoichiometric amounts of heparin, the bovine proteins formed an initial complex of Mr = 230,000 (corresponding to a dimer of heparin-antithrombin III-thrombin) which underwent further aggregation. Heparin 45-52 serpin family C member 1 Homo sapiens 153-165 3949807-9 1986 The human proteins, however, formed a 1:1 (antithrombin III X thrombin) initial complex in the presence of heparin, followed by aggregation. Heparin 107-114 serpin family C member 1 Homo sapiens 43-55 3949807-10 1986 These interactions of thrombin and antithrombin with heparin suggest complex interactions that could relate to heparin function. Heparin 53-60 serpin family C member 1 Homo sapiens 35-47 3949807-10 1986 These interactions of thrombin and antithrombin with heparin suggest complex interactions that could relate to heparin function. Heparin 111-118 serpin family C member 1 Homo sapiens 35-47 3955055-8 1986 When heparin was used in these assays, the rate of inhibition of thrombin by antithrombin was much more rapid and 62% of thrombin activity remained after 1 min. Heparin 5-12 serpin family C member 1 Homo sapiens 77-89 3960724-0 1986 Antithrombin III tours gene: identification of a point mutation leading to an arginine----cysteine replacement in a silent deficiency. arginine----cysteine 78-98 serpin family C member 1 Homo sapiens 0-16 3947650-0 1986 The catalysis by heparin of the reaction between thrombin and antithrombin. Heparin 17-24 serpin family C member 1 Homo sapiens 62-74 3947650-1 1986 Fluorescence polarization has been used to study the kinetics of the combination of thrombin with antithrombin and its catalysis by the polysaccharide heparin. polysaccharide heparin 136-158 serpin family C member 1 Homo sapiens 98-110 3947650-2 1986 The heparin-catalysed combination of thrombin and antithrombin is saturable with respect to both thrombin and antithrombin. Heparin 4-11 serpin family C member 1 Homo sapiens 50-62 3947650-2 1986 The heparin-catalysed combination of thrombin and antithrombin is saturable with respect to both thrombin and antithrombin. Heparin 4-11 serpin family C member 1 Homo sapiens 110-122 3947650-4 1986 The kinetics observed can be explained by proposing that the catalyst of the reaction is not heparin alone but a complex of heparin and antithrombin (bound at the high-affinity site). Heparin 93-100 serpin family C member 1 Homo sapiens 136-148 3754413-3 1986 Both antithrombin and heparin cofactor activities of heparin cofactor II are inactivated by the arginine-specific reagent, 2,3-butanedione. Arginine 96-104 serpin family C member 1 Homo sapiens 5-17 3754413-3 1986 Both antithrombin and heparin cofactor activities of heparin cofactor II are inactivated by the arginine-specific reagent, 2,3-butanedione. Diacetyl 123-138 serpin family C member 1 Homo sapiens 5-17 3754413-5 1986 Quantitation of arginyl residues following butanedione modification shows a loss of about four residues for total inactivation, one of which is essential for antithrombin activity. Diacetyl 43-54 serpin family C member 1 Homo sapiens 158-170 3754413-11 1986 The results indicate that arginyl residues are critical for both antithrombin and heparin binding activities. arginyl 26-33 serpin family C member 1 Homo sapiens 65-77 3961733-5 1986 When heparin was bound to antithrombin III-Sepharose, the aggregating activity eluted totally in the high-affinity fraction. Heparin 5-12 serpin family C member 1 Homo sapiens 26-42 2421433-0 1986 Pentosan polysulphate: activation of heparin cofactor II or antithrombin III according to molecular weight fractionation. Pentosan Sulfuric Polyester 0-21 serpin family C member 1 Homo sapiens 60-76 3512602-4 1986 Purification of the patient"s plasma AT-III by heparin-sepharose affinity chromatography showed a normal protein recovery and elution profile, but the purified AT-III fraction showed only 50% of the normal progressive thrombin neutralization and anti-Xa activity. Heparin 47-54 serpin family C member 1 Homo sapiens 37-43 3512602-4 1986 Purification of the patient"s plasma AT-III by heparin-sepharose affinity chromatography showed a normal protein recovery and elution profile, but the purified AT-III fraction showed only 50% of the normal progressive thrombin neutralization and anti-Xa activity. Sepharose 55-64 serpin family C member 1 Homo sapiens 37-43 3512602-5 1986 When thrombin-antithrombin (TAT) complexes were formed by incubating with excess thrombin, SDS-polyacrylamide gel electrophoresis (PAGE) analysis revealed that half the patient AT-III formed TAT complexes while the remainder migrated as free AT-III. Sodium Dodecyl Sulfate 91-94 serpin family C member 1 Homo sapiens 14-26 3512602-5 1986 When thrombin-antithrombin (TAT) complexes were formed by incubating with excess thrombin, SDS-polyacrylamide gel electrophoresis (PAGE) analysis revealed that half the patient AT-III formed TAT complexes while the remainder migrated as free AT-III. polyacrylamide 95-109 serpin family C member 1 Homo sapiens 14-26 3512602-7 1986 The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa. Sodium Dodecyl Sulfate 104-107 serpin family C member 1 Homo sapiens 26-32 3512602-7 1986 The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa. Sodium Dodecyl Sulfate 104-107 serpin family C member 1 Homo sapiens 34-40 3512602-7 1986 The patient"s nonreacting AT-III (AT-III "Denver"), isolated by affinity chromatography, showed CIE and SDS-PAGE migration patterns characteristic of normal AT-III but failed to bind thrombin or Xa. Sodium Dodecyl Sulfate 104-107 serpin family C member 1 Homo sapiens 34-40 3512602-9 1986 These studies indicate that the patients" variant AT-III molecule was characterized by normal heparin interaction but defective binding and inhibition of thrombin and Xa. Heparin 94-101 serpin family C member 1 Homo sapiens 50-56 3518132-3 1986 QAE-Sephadex A-50 chromatography provides a good separation of HCII from antithrombin III (AT) and most contaminants having a heparin affinity similar to that of HCII. QAE 0-3 serpin family C member 1 Homo sapiens 73-89 3518132-3 1986 QAE-Sephadex A-50 chromatography provides a good separation of HCII from antithrombin III (AT) and most contaminants having a heparin affinity similar to that of HCII. sephadex a 4-14 serpin family C member 1 Homo sapiens 73-89 3961733-5 1986 When heparin was bound to antithrombin III-Sepharose, the aggregating activity eluted totally in the high-affinity fraction. Sepharose 43-52 serpin family C member 1 Homo sapiens 26-42 3961735-2 1986 Functional antithrombin III levels fell to 0.32 U/ml during heparin treatment, but it was possible to achieve a heparin effect, measured by the activated partial thromboplastin time, thrombin clotting time and heparin assay with subcutaneous heparin in doses of 30,000 U to 35,000 U/24 hours. Heparin 60-67 serpin family C member 1 Homo sapiens 11-27 3718405-6 1986 Heparin seems to form a ternary complex with AT III and activated coagulation factors, so acting as a catalyst. Heparin 0-7 serpin family C member 1 Homo sapiens 45-51 3942133-7 1986 The addition of danazol therapy led to a sustained rise in the antithrombin III level. Danazol 16-23 serpin family C member 1 Homo sapiens 63-79 3080419-1 1986 Identification of a Pro-Leu substitution in a hereditary abnormal antithrombin with impaired heparin cofactor activity. prolylleucine 20-27 serpin family C member 1 Homo sapiens 66-78 18555318-0 1986 Application of immobilized heparins for isolation of human antithrombin III. Heparin 27-35 serpin family C member 1 Homo sapiens 59-75 18555318-1 1986 Immobilized heparins were prepared by six different methods, and these were utilized for affinity purification of human antithrombin III (AT-III). Heparin 12-20 serpin family C member 1 Homo sapiens 120-136 18555318-1 1986 Immobilized heparins were prepared by six different methods, and these were utilized for affinity purification of human antithrombin III (AT-III). Heparin 12-20 serpin family C member 1 Homo sapiens 138-144 18555318-2 1986 Affinity support capacities (mg AT-III/g support) were strongly influenced by immobilized active heparin concentrations. Heparin 97-104 serpin family C member 1 Homo sapiens 32-38 3080419-2 1986 Antithrombin III Basel is a hereditary abnormal antithrombin with normal progressive inhibition activity (normal reactive site) and reduced heparin cofactor activity (impaired heparin binding site). Heparin 140-147 serpin family C member 1 Homo sapiens 0-16 3080419-2 1986 Antithrombin III Basel is a hereditary abnormal antithrombin with normal progressive inhibition activity (normal reactive site) and reduced heparin cofactor activity (impaired heparin binding site). Heparin 140-147 serpin family C member 1 Homo sapiens 48-60 3080419-5 1986 The amino acid sequence of the peptide from antithrombin III Basel had a single substitution of Pro (normal) by Leu (abnormal) at position 41. Leucine 112-115 serpin family C member 1 Homo sapiens 44-56 3080419-6 1986 This substitution is close to an Arg (residue 47) and a Trp (residue 49) which have previously been shown to be critical for heparin binding by antithrombin III. Arginine 33-36 serpin family C member 1 Homo sapiens 144-160 3080419-6 1986 This substitution is close to an Arg (residue 47) and a Trp (residue 49) which have previously been shown to be critical for heparin binding by antithrombin III. Tryptophan 56-59 serpin family C member 1 Homo sapiens 144-160 3080419-6 1986 This substitution is close to an Arg (residue 47) and a Trp (residue 49) which have previously been shown to be critical for heparin binding by antithrombin III. Heparin 125-132 serpin family C member 1 Homo sapiens 144-160 3080419-7 1986 Although additional amino acid substitutions in antithrombin III Basel cannot be ruled out, this Pro-Leu replacement could cause a conformational change by increasing both the helical structure and the hydrophobicity around residue 41. prolylleucine 97-104 serpin family C member 1 Homo sapiens 48-64 3080419-8 1986 These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41. Heparin 33-40 serpin family C member 1 Homo sapiens 57-73 3080419-8 1986 These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41. Heparin 33-40 serpin family C member 1 Homo sapiens 184-200 3080419-8 1986 These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41. Heparin 155-162 serpin family C member 1 Homo sapiens 57-73 3000827-0 1986 The heparin-binding site(s) of histidine-rich glycoprotein as suggested by sequence homology with antithrombin III. Heparin 4-11 serpin family C member 1 Homo sapiens 98-114 3080419-8 1986 These data suggest that: (i) the heparin binding site of antithrombin III encompasses the region containing residues 41, 47, and 49; and (ii) the impaired heparin cofactor activity of antithrombin III Basel is likely due to a conformational change of the heparin binding site induced by the Pro-Leu substitution at position 41. Heparin 155-162 serpin family C member 1 Homo sapiens 184-200 3000827-1 1986 A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located. Heparin 174-181 serpin family C member 1 Homo sapiens 129-145 3090830-0 1986 Antithrombin III during high-dose cytosine arabinoside therapy with or without asparaginase. Cytarabine 34-54 serpin family C member 1 Homo sapiens 0-16 3000827-1 1986 A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located. Heparin 174-181 serpin family C member 1 Homo sapiens 147-153 3000827-1 1986 A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein (HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located. Heparin 174-181 serpin family C member 1 Homo sapiens 198-204 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Arginine 56-59 serpin family C member 1 Homo sapiens 66-72 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Heparin 99-106 serpin family C member 1 Homo sapiens 66-72 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Arginine 124-132 serpin family C member 1 Homo sapiens 66-72 3000827-2 1986 The amino acid residue at the position corresponding to Arg-47 of AT III that is essential for the heparin-binding was also arginine (Arg 23 and 78) in the homologous sequences of HRG. Arginine 134-137 serpin family C member 1 Homo sapiens 66-72 3000827-3 1986 These observations strongly suggest that the heparin-binding sites of HRG and AT III are evolutionarily related. Heparin 45-52 serpin family C member 1 Homo sapiens 78-84 2436525-15 1986 Heparan sulfate did not inhibit intrinsic prothrombin activation but catalyzed the inhibition of the thrombin generated by the formation of thrombin-antithrombin III complex. Heparitin Sulfate 0-15 serpin family C member 1 Homo sapiens 149-165 3510115-2 1986 Heparin is a complex polysaccharide, consisting of repeating dissacharide subunits, which exerts its anticoagulant effect by potentiating the inhibition of activated clotting proteins by the naturally occurring inhibitor antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 221-237 3940555-3 1986 Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and crossed immunoelectrophoresis (CIE) showed the purified AT III to be homogeneous. sodium dodecyl sulfate-polyacrylamide 0-37 serpin family C member 1 Homo sapiens 129-135 3510115-2 1986 Heparin is a complex polysaccharide, consisting of repeating dissacharide subunits, which exerts its anticoagulant effect by potentiating the inhibition of activated clotting proteins by the naturally occurring inhibitor antithrombin III. Polysaccharides 21-35 serpin family C member 1 Homo sapiens 221-237 3510115-2 1986 Heparin is a complex polysaccharide, consisting of repeating dissacharide subunits, which exerts its anticoagulant effect by potentiating the inhibition of activated clotting proteins by the naturally occurring inhibitor antithrombin III. dissacharide 61-73 serpin family C member 1 Homo sapiens 221-237 2436996-5 1986 An absence of the heparin effect should always lead to the use of an antithrombin III assay. Heparin 18-25 serpin family C member 1 Homo sapiens 69-85 2430807-9 1986 Antithrombin activity was increased during warfarin treatment. Warfarin 43-51 serpin family C member 1 Homo sapiens 0-12 3583099-6 1986 Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII. Glucose 187-194 serpin family C member 1 Homo sapiens 267-272 3583099-6 1986 Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII. Heparin 199-206 serpin family C member 1 Homo sapiens 71-76 3583099-0 1986 Heparin preserves antithrombin III biological activity from hyperglycemia-induced alterations in insulin-dependent diabetics. Heparin 0-7 serpin family C member 1 Homo sapiens 18-34 3583099-6 1986 Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII. Glucose 187-194 serpin family C member 1 Homo sapiens 71-76 3583099-6 1986 Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII. Heparin 199-206 serpin family C member 1 Homo sapiens 267-272 3583099-2 1986 This alteration is glycemia level-dependent, there existing an inverse correlation between fluctuations of daily blood glucose level, labile glycosylated hemoglobin and ATIII activity. Glucose 119-126 serpin family C member 1 Homo sapiens 169-174 3710297-2 1986 Heparin inhibits blood coagulation by 3 independent mechanisms by augmenting the effect of antithrombin III (the major effect), by augmenting the inhibitory effect of thrombin or heparin cofactor II, and by disrupting the activation of blood coagulation on the platelet surface; it has an additional effect on hemostasis through its interaction with blood platelets. Heparin 0-7 serpin family C member 1 Homo sapiens 91-107 3583099-3 1986 The subcutaneous and endovenous heparin administration restores ATIII activity, but does not modify its plasma concentration in diabetics. Heparin 32-39 serpin family C member 1 Homo sapiens 64-69 3583099-4 1986 Moreover, heparin treatment preserves ATIII activity from glycemia-induced alterations. Heparin 10-17 serpin family C member 1 Homo sapiens 38-43 4096360-11 1985 The determined stability of AT III in autologous plasma--without AT III prophylaxis of thrombosis by Heparin is ineffective--and all other clotting factors leads to an expectancy of a not activated clotting mechanism and at the same time to low thrombosis risks. Heparin 101-108 serpin family C member 1 Homo sapiens 28-34 3583099-5 1986 These data suggest a role for glucose, probably through a labile nonenzymatic glycation process, in determining the alteration of ATIII biological activity. Glucose 30-37 serpin family C member 1 Homo sapiens 130-135 3583099-6 1986 Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII. Heparin 37-44 serpin family C member 1 Homo sapiens 71-76 3583099-6 1986 Moreover, showing the possibility by heparin administration to restore ATIII activity and preserve its biological function from effects of glycemia variations, stress the hypothesis that glucose and heparin compete in vivo, both against the same catalytic residue of ATIII. Heparin 37-44 serpin family C member 1 Homo sapiens 267-272 3733300-1 1986 The anticoagulant activity of heparin is dependent on its affinity for antithrombin III (AT III) and on its molecular weight. Heparin 30-37 serpin family C member 1 Homo sapiens 71-87 3733300-1 1986 The anticoagulant activity of heparin is dependent on its affinity for antithrombin III (AT III) and on its molecular weight. Heparin 30-37 serpin family C member 1 Homo sapiens 89-95 3734344-1 1986 Thrombo-embolic complications in pregnant women who have congenital antithrombin III deficiency are usually prevented by giving injections of sub-cutaneous heparin from the beginning to the end of pregnancy and with the administration of concentrated doses of antithrombin III (A.T. III) at delivery and in the following days. Heparin 156-163 serpin family C member 1 Homo sapiens 68-84 2415521-4 1985 Upon prolonged boiling in SDS it dissociates into 56- and 32-kDa components which co-migrate in SDS-PAGE with purified antithrombin III and thrombin, respectively. Sodium Dodecyl Sulfate 26-29 serpin family C member 1 Homo sapiens 119-135 2415521-6 1985 Thrombin-antithrombin III complex, from either serum or recalcified clotted plasma, bound to vitronectin immobilized on Sepharose or plastic. Sepharose 120-129 serpin family C member 1 Homo sapiens 9-25 3153215-1 1986 Thirteen children with ALL and L-asp-induced alterations of the coagulation system were treated with fresh-frozen plasma and antithrombin III (AT III) concentrate. Aspartic Acid 31-36 serpin family C member 1 Homo sapiens 125-141 3517772-2 1986 It is by potentiating antithrombin III (AT III) a natural inhibitor of coagulation, that heparin exerts its anticoagulant effect. Heparin 89-96 serpin family C member 1 Homo sapiens 22-38 3517772-2 1986 It is by potentiating antithrombin III (AT III) a natural inhibitor of coagulation, that heparin exerts its anticoagulant effect. Heparin 89-96 serpin family C member 1 Homo sapiens 40-46 3517772-3 1986 Actually, it has been demonstrated that only 30% of the molecule in commercial heparin preparations are capable of binding to AT III: moreover, several procedures were used to prepare low molecular weight heparin fractions or fragments. Heparin 79-86 serpin family C member 1 Homo sapiens 126-132 3004419-10 1985 Immunoprecipitation at different chase times with monospecific antisera showed that castanospermine markedly decreased the secretion rates of alpha 1-antitrypsin, caeruloplasmin and, to a lesser extent, that of antithrombin-III. castanospermine 84-99 serpin family C member 1 Homo sapiens 211-227 2416361-7 1985 AT III is a weak inhibitor of polymerization, but its effect is magnified in the presence of PAPP-A or heparin. Heparin 103-110 serpin family C member 1 Homo sapiens 0-6 4063384-3 1985 Three significant quantitative differences were observed for the mollusc heparin when compared with the ones from mammalian origin, namely, a higher degree of binding with antithrombin III (45%), higher molecular weight (27-43 kDa) and higher anticoagulant activity (320 I.U./mg). Heparin 73-80 serpin family C member 1 Homo sapiens 172-188 4089794-7 1985 The changes in heparin kinetics in FHF are likely to be complex with the balance between the proteins that act as cofactors, (e.g. AT III) and the proteins that have heparin neutralising activity, controlling the response of added heparin. Heparin 15-22 serpin family C member 1 Homo sapiens 131-137 3865174-2 1985 The synthetic oligodeoxyribonucleotides obtained were successfully tested in comparison with a classical mixed probe for their capacity to identify specific cDNA clones of human antithrombin III. Oligodeoxyribonucleotides 14-39 serpin family C member 1 Homo sapiens 178-194 4089534-0 1985 Changes in plasma antithrombin (heparin cofactor activity) during intravenous heparin therapy: observations in 198 patients with deep venous thrombosis. Heparin 32-39 serpin family C member 1 Homo sapiens 18-30 4089534-1 1985 Plasma antithrombin (AT) measured as heparin cofactor activity decreased 0.16 +/- 0.13 U/ml (mean +/- SD) in 198 patients who received heparin infusion during 1 wk for deep venous thrombosis (DVT). Heparin 37-44 serpin family C member 1 Homo sapiens 7-19 4071470-0 1985 Analysis of antithrombin III microheterogeneity by isoelectric focusing in polyacrylamide gels and immunoblotting. polyacrylamide 75-89 serpin family C member 1 Homo sapiens 12-28 3937259-4 1985 When stimulated by arachidonic acid, the platelets released AT III antigen together with immunoreactive fibrinogen. Arachidonic Acid 19-35 serpin family C member 1 Homo sapiens 60-66 4071470-4 1985 The reactivity of ATIII with heparin or, thrombin was investigated using this technique. Heparin 29-36 serpin family C member 1 Homo sapiens 18-23 4082851-1 1985 Hypercoagulation caused by decreased antithrombin III level leads to thrombosis inspite of postoperative prophylactic heparin therapy. Heparin 118-125 serpin family C member 1 Homo sapiens 37-53 3863104-4 1985 Arginine-modified heparin cofactor II showed a comparable percentage loss of both antichymotrypsin and antithrombin activities. Arginine 0-8 serpin family C member 1 Homo sapiens 103-115 3901791-7 1985 Heparin achieves its prophylactic benefit by activating antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 56-72 3901791-9 1985 It has been shown that 1 micrograms of antithrombin III inhibits the formation of 1 unit of thrombin; however, in the presence of heparin, 1 micrograms of activated antithrombin III inhibits 750 units of thrombin. Heparin 130-137 serpin family C member 1 Homo sapiens 165-181 3840916-2 1985 HC II was functionally determined by thrombin inhibition in the presence of heparin in AT III-free plasma prepared by immunoadsorption on anti-AT III-Sepharose 4B column. Heparin 76-83 serpin family C member 1 Homo sapiens 87-93 4082851-5 1985 One should always suspect an ATIII deficiency when in spite of full heparin dosage a prolonged plasma thrombin time is not attained. Heparin 68-75 serpin family C member 1 Homo sapiens 29-34 4070344-2 1985 The antithrombin effect decreased by substituting the 1-naphthylsulfonyl by the 8-quinolinesulfonyl residue. 1-naphthylsulfonyl 54-72 serpin family C member 1 Homo sapiens 4-16 4064026-0 1985 Synthesis, from cellobiose, of a trisaccharide closely related to the GlcNAc----GlcA----GlcN segment of the antithrombin-binding sequence of heparin. Trisaccharides 33-46 serpin family C member 1 Homo sapiens 108-120 4064026-0 1985 Synthesis, from cellobiose, of a trisaccharide closely related to the GlcNAc----GlcA----GlcN segment of the antithrombin-binding sequence of heparin. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose 70-76 serpin family C member 1 Homo sapiens 108-120 4070344-2 1985 The antithrombin effect decreased by substituting the 1-naphthylsulfonyl by the 8-quinolinesulfonyl residue. 8-quinolinesulfonyl 80-99 serpin family C member 1 Homo sapiens 4-16 3875633-10 1985 This data suggests that alpha 1-PI does not function as a major inhibitor of factor Xa in vivo, and that a tonically active heparin-dependent mechanism exists in humans for accelerating the neutralization of this enzyme by antithrombin. Heparin 124-131 serpin family C member 1 Homo sapiens 223-235 4026027-8 1985 In addition, transfusion of AT III-rich donor plasma may be necessary when low plasma AT III reduces the effects of heparin. Heparin 116-123 serpin family C member 1 Homo sapiens 28-34 4026027-8 1985 In addition, transfusion of AT III-rich donor plasma may be necessary when low plasma AT III reduces the effects of heparin. Heparin 116-123 serpin family C member 1 Homo sapiens 86-92 3873967-0 1985 Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III. Heparin 10-17 serpin family C member 1 Homo sapiens 76-92 3873967-7 1985 Using purified factor XIIa and ATIII, we found that heparin (0.7 to 34.0 U/mL) increased the rate of inhibition of Factor XIIa. Heparin 52-59 serpin family C member 1 Homo sapiens 31-36 3873967-11 1985 Furthermore, using purified factor XIIf and antithrombin III, heparin (3.6 to 57.2 U/mL) increased the inactivation rate constant of factor XIIf by 1.6 to 14.0 times. Heparin 62-69 serpin family C member 1 Homo sapiens 44-60 4060104-3 1985 Danazol, a 17-alkyl derivative of ethinyl testosterone, which has been used to treat other antiprotease deficiency states, was assessed in the management of two men with antithrombin deficiency. Danazol 0-7 serpin family C member 1 Homo sapiens 170-182 4060104-4 1985 In a dose of 600 mg a day danazol appeared to correct the antithrombin deficiency. Danazol 26-33 serpin family C member 1 Homo sapiens 58-70 4082101-2 1985 Both anti-activated factor X (anti Xa) and antithrombin activity were decreased, in the absence and in the presence of heparin, while protein concentration was normal in an immunological assay. Heparin 119-126 serpin family C member 1 Homo sapiens 43-55 4082101-3 1985 The abnormal AT III copurified with functional AT III using insolubilized heparin affinity chromatography. Heparin 74-81 serpin family C member 1 Homo sapiens 13-19 4082101-3 1985 The abnormal AT III copurified with functional AT III using insolubilized heparin affinity chromatography. Heparin 74-81 serpin family C member 1 Homo sapiens 47-53 4082101-4 1985 Polyacrylamide gel electrophoresis (PAGE) and high pressure liquid chromatography (HPLC) on a TSK column suggest that AT III Charleville forms unstable complexes with thrombin from which a modified protein is rapidly released. polyacrylamide 0-14 serpin family C member 1 Homo sapiens 118-124 4035646-0 1985 The role of the carbohydrate moiety for the inhibitory activity of antithrombin III. Carbohydrates 16-28 serpin family C member 1 Homo sapiens 67-83 4043133-3 1985 The mean rise of AT III activity by 40 U/kg per day heparin was 8.7%. Heparin 52-59 serpin family C member 1 Homo sapiens 17-23 4043133-4 1985 If AT III concentrate (40 U/kg per day) was activated with 200 U/kg per day heparin, excessive anticoagulation effect was only observed in one child. Heparin 76-83 serpin family C member 1 Homo sapiens 3-9 2411030-5 1985 Following infusion of HES and albumin, plasma fibrinogen and antithrombin-III levels fell slightly due to plasma volume expansion and hemodilution. Hydroxyethyl Starch Derivatives 22-25 serpin family C member 1 Homo sapiens 61-77 4049307-0 1985 Antithrombin III "Northwick Park": a variant antithrombin with normal affinity for heparin but reduced heparin cofactor activity. Heparin 83-90 serpin family C member 1 Homo sapiens 0-16 4049307-0 1985 Antithrombin III "Northwick Park": a variant antithrombin with normal affinity for heparin but reduced heparin cofactor activity. Heparin 83-90 serpin family C member 1 Homo sapiens 45-57 4049307-6 1985 Further studies confirmed that the abnormal AT III binds completely to heparin but has no heparin cofactor or progressive antithrombin activity. Heparin 71-78 serpin family C member 1 Homo sapiens 44-50 3995171-4 1985 More factor IXa was inhibited by antithrombin III in the presence of heparin than in its absence, but factor IXa levels sufficient for factor X activation appeared to be present in the heparinized plasma. Heparin 69-76 serpin family C member 1 Homo sapiens 33-49 2408688-3 1985 These derivatives exhibit a heparin-like antithrombic activity which requires the presence of antithrombin III; however they are less effective than heparin on a weight basis. Heparin 28-35 serpin family C member 1 Homo sapiens 94-110 4003344-2 1985 In an antithrombin-III (AT-III) deficient patient suffering from recurrent episodes of venous and arterial thrombosis requiring major surgery an attempt was made to institute antithrombotic protection by long-term stanozolol treatment supplemented during periods of thrombogenic exposure with subcutaneous heparin and, when needed, infusion of AT-III as plasma or concentrate. Stanozolol 214-224 serpin family C member 1 Homo sapiens 6-22 4003344-2 1985 In an antithrombin-III (AT-III) deficient patient suffering from recurrent episodes of venous and arterial thrombosis requiring major surgery an attempt was made to institute antithrombotic protection by long-term stanozolol treatment supplemented during periods of thrombogenic exposure with subcutaneous heparin and, when needed, infusion of AT-III as plasma or concentrate. Stanozolol 214-224 serpin family C member 1 Homo sapiens 24-30 4003344-2 1985 In an antithrombin-III (AT-III) deficient patient suffering from recurrent episodes of venous and arterial thrombosis requiring major surgery an attempt was made to institute antithrombotic protection by long-term stanozolol treatment supplemented during periods of thrombogenic exposure with subcutaneous heparin and, when needed, infusion of AT-III as plasma or concentrate. Stanozolol 214-224 serpin family C member 1 Homo sapiens 344-350 4003344-2 1985 In an antithrombin-III (AT-III) deficient patient suffering from recurrent episodes of venous and arterial thrombosis requiring major surgery an attempt was made to institute antithrombotic protection by long-term stanozolol treatment supplemented during periods of thrombogenic exposure with subcutaneous heparin and, when needed, infusion of AT-III as plasma or concentrate. Heparin 306-313 serpin family C member 1 Homo sapiens 24-30 4003344-3 1985 Stanozolol raised the plasma levels of AT-III, demonstrating a sparing effect on the AT-III needed. Stanozolol 0-10 serpin family C member 1 Homo sapiens 39-45 4003344-3 1985 Stanozolol raised the plasma levels of AT-III, demonstrating a sparing effect on the AT-III needed. Stanozolol 0-10 serpin family C member 1 Homo sapiens 85-91 4003387-7 1985 As an extension of these findings, we examined the effect of Zn+2 on the inhibition of thrombin by antithrombin-III (AT-III). Zinc 61-65 serpin family C member 1 Homo sapiens 99-115 4003387-8 1985 The presence of as little as 0.006 mM Zn+2 in an incubating mixture of thrombin and AT-III severely reduced the inhibitory activity of AT-III towards thrombin. Zinc 38-42 serpin family C member 1 Homo sapiens 84-90 4003387-8 1985 The presence of as little as 0.006 mM Zn+2 in an incubating mixture of thrombin and AT-III severely reduced the inhibitory activity of AT-III towards thrombin. Zinc 38-42 serpin family C member 1 Homo sapiens 135-141 4003387-10 1985 It is suggested that Zn+2 can form a complex with thrombin, which results in altered reactivity towards fibrinogen and decreased inhibition by AT-III. Zinc 21-25 serpin family C member 1 Homo sapiens 143-149 2859508-4 1985 Haemostatic tests in cyclosporin-treated and azathioprine-treated patients and normal subjects (10 in each group) showed increased concentrations of factor VIII C, fibrinogen, antithrombin III, and protein C in the cyclosporin-treated patients. Cyclosporine 21-32 serpin family C member 1 Homo sapiens 176-192 2859508-4 1985 Haemostatic tests in cyclosporin-treated and azathioprine-treated patients and normal subjects (10 in each group) showed increased concentrations of factor VIII C, fibrinogen, antithrombin III, and protein C in the cyclosporin-treated patients. Azathioprine 45-57 serpin family C member 1 Homo sapiens 176-192 2408362-3 1985 Results of in vivo studies were as follows: following infusion of 1 liter of 6 percent HES into healthy subjects, fibrinogen and antithrombin-III concentrations fell slightly due to plasma volume expansion and consequent dilution. Hydroxyethyl Starch Derivatives 87-90 serpin family C member 1 Homo sapiens 129-145 4037242-4 1985 These findings suggest that the administration of AT-III concentrates may significantly enhance the therapeutic efficacy of heparin, and that the use of AT-III concentrates with heparin is a safe and effective regimen for the treatment of childhood DIC. Heparin 124-131 serpin family C member 1 Homo sapiens 50-56 3988727-0 1985 The role of surface charge on the accelerating action of heparin on the antithrombin III-inhibited activity of alpha-thrombin. Heparin 57-64 serpin family C member 1 Homo sapiens 72-88 3988727-8 1985 Heparin acts on the antithrombin III-thrombin reaction through cooperative electrostatic binding to thrombin and nonelectrostatic interaction with antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 20-36 3988727-8 1985 Heparin acts on the antithrombin III-thrombin reaction through cooperative electrostatic binding to thrombin and nonelectrostatic interaction with antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 147-163 3985961-0 1985 Mono- and bidimensional 500 MHz 1H-NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: evidence for conformational peculiarity of the sulfated iduronate residue. pentasaccharide 62-77 serpin family C member 1 Homo sapiens 130-146 3985961-0 1985 Mono- and bidimensional 500 MHz 1H-NMR spectra of a synthetic pentasaccharide corresponding to the binding sequence of heparin to antithrombin-III: evidence for conformational peculiarity of the sulfated iduronate residue. Iduronic Acid 204-213 serpin family C member 1 Homo sapiens 130-146 3985961-5 1985 Such a departure, leading to different orientation and spacing of essential sulfate groups, may have implications for high-affinity binding to AT-III. essential sulfate 66-83 serpin family C member 1 Homo sapiens 143-149 4037242-4 1985 These findings suggest that the administration of AT-III concentrates may significantly enhance the therapeutic efficacy of heparin, and that the use of AT-III concentrates with heparin is a safe and effective regimen for the treatment of childhood DIC. Heparin 178-185 serpin family C member 1 Homo sapiens 153-159 3873118-2 1985 Stanozolol treatment resulted in significant (p less than 0.01) increases between the 14th and 1st preoperative days in the plasma concentrations of plasminogen (3.4 to 4.9 Cu/ml) and antithrombin III (107% to 132%); t-PA levels did not increase significantly (6.0 to 16.0 mU/ml; p greater than 0.1). Stanozolol 0-10 serpin family C member 1 Homo sapiens 184-200 3988937-0 1985 Antithrombotic properties in rabbits of heparin and heparin fragments covalently coupled to human antithrombin III. Heparin 40-47 serpin family C member 1 Homo sapiens 98-114 3988937-0 1985 Antithrombotic properties in rabbits of heparin and heparin fragments covalently coupled to human antithrombin III. Heparin 52-59 serpin family C member 1 Homo sapiens 98-114 3988937-1 1985 Clinical grade heparin is a very heterogeneous mucopolysaccharide, containing molecules with Mr ranging from 6,000 to 30,000 that have either a high affinity or a low affinity for antithrombin III (AT). Heparin 15-22 serpin family C member 1 Homo sapiens 180-196 3988937-1 1985 Clinical grade heparin is a very heterogeneous mucopolysaccharide, containing molecules with Mr ranging from 6,000 to 30,000 that have either a high affinity or a low affinity for antithrombin III (AT). Glycosaminoglycans 47-65 serpin family C member 1 Homo sapiens 180-196 3986191-0 1985 Denaturation behavior of antithrombin in guanidinium chloride. Guanidine 41-61 serpin family C member 1 Homo sapiens 25-37 3986191-2 1985 The structural stability of the protease inhibitor antithrombin from bovine plasma was examined as a function of the concentration of guanidinium chloride (GdmCl). Guanidine 134-154 serpin family C member 1 Homo sapiens 51-63 3986191-4 1985 Spectroscopic and hydrodynamic analyses suggest that the intermediate state which exists at 1.5 M GdmCl involves a partial unfolding of the antithrombin molecule that exposes regions of the polypeptide chain through which slow, intermolecular association subsequently takes place. Guanidine 98-103 serpin family C member 1 Homo sapiens 140-152 3986191-9 1985 Analyses of bovine antithrombin in 6 M GdmCl indicated that the second transition reflects the total unfolding of the protein to a disulfide-cross-linked random coil. Guanidine 39-44 serpin family C member 1 Homo sapiens 19-31 3986191-9 1985 Analyses of bovine antithrombin in 6 M GdmCl indicated that the second transition reflects the total unfolding of the protein to a disulfide-cross-linked random coil. Disulfides 131-140 serpin family C member 1 Homo sapiens 19-31 3988155-2 1985 The antithrombotic effect of heparin is closely related to the presence of Antithrombin III (AT III) as cofactor. Heparin 29-36 serpin family C member 1 Homo sapiens 75-91 3988155-2 1985 The antithrombotic effect of heparin is closely related to the presence of Antithrombin III (AT III) as cofactor. Heparin 29-36 serpin family C member 1 Homo sapiens 93-99 3988155-9 1985 This decrease of AT III can be avoided by application of the AT III factor in an active form during the procedure (AT III in solution with heparin). Heparin 139-146 serpin family C member 1 Homo sapiens 17-23 3988155-9 1985 This decrease of AT III can be avoided by application of the AT III factor in an active form during the procedure (AT III in solution with heparin). Heparin 139-146 serpin family C member 1 Homo sapiens 61-67 3988155-9 1985 This decrease of AT III can be avoided by application of the AT III factor in an active form during the procedure (AT III in solution with heparin). Heparin 139-146 serpin family C member 1 Homo sapiens 61-67 3838304-2 1985 Heparin cofactor II and antithrombin III are functionally similar in that both proteins have been shown to inhibit thrombin at accelerated rates in the presence of heparin. Heparin 164-171 serpin family C member 1 Homo sapiens 24-40 3838304-8 1985 While the similarities in primary structure suggest that heparin cofactor II may be an additional member of the superfamily of proteins consisting of antithrombin III, alpha 1-antitrypsin, alpha 1-antichymotrypsin and ovalbumin, the differences in structure could account for differences in protease specificity and reactivity toward thrombin. Heparin 57-64 serpin family C member 1 Homo sapiens 150-166 3838304-9 1985 In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II. Disulfides 17-26 serpin family C member 1 Homo sapiens 88-104 3838304-9 1985 In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II. Heparin 163-170 serpin family C member 1 Homo sapiens 88-104 3838304-9 1985 In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II. Heparin 245-252 serpin family C member 1 Homo sapiens 88-104 3838304-9 1985 In particular, a disulfide bond which links the COOH-terminal (reactive site) region of antithrombin III to the remainder of the molecule and is important for the heparin-induced conformational change in the protein and high affinity binding of heparin does not appear to exist in heparin cofactor II. Heparin 245-252 serpin family C member 1 Homo sapiens 88-104 3838304-10 1985 This observation provides an initial indication that while the reported kinetic mechanisms of action of heparin in accelerating the heparin cofactor II/thrombin and antithrombin III/thrombin reactions are similar, the mechanisms and effects of heparin binding to the two inhibitors may be different. Heparin 104-111 serpin family C member 1 Homo sapiens 165-181 4035368-1 1985 We have synthesized the pentasaccharide representing the binding site of heparin to AT III. pentasaccharide 24-39 serpin family C member 1 Homo sapiens 84-90 4035368-1 1985 We have synthesized the pentasaccharide representing the binding site of heparin to AT III. Heparin 73-80 serpin family C member 1 Homo sapiens 84-90 4035368-3 1985 A pentasaccharide analogue lacking this 3-0-sulfate group and two different tetrasaccharides, each being part of the pentasaccharide sequence with AT III affinity, have also been synthesized. tetrasaccharides 76-92 serpin family C member 1 Homo sapiens 147-153 4035368-3 1985 A pentasaccharide analogue lacking this 3-0-sulfate group and two different tetrasaccharides, each being part of the pentasaccharide sequence with AT III affinity, have also been synthesized. pentasaccharide 117-132 serpin family C member 1 Homo sapiens 147-153 4035368-4 1985 The pentasaccharide with high affinity for AT III also shows high antifactor Xa activity and, in vivo, antithrombotic activity. pentasaccharide 4-19 serpin family C member 1 Homo sapiens 43-49 3973461-4 1985 Antithrombin (AT) binding by heparinized PMA materials (compared with PMA control beads) ranged from no AT binding for the material heparinized with carbodiimide (PMA-Alb-Hep(EDC] to 3.6 micrograms/ml packed beads for the material heparinized by radical polymerization (PMA-MA-Hep). Tetradecanoylphorbol Acetate 41-44 serpin family C member 1 Homo sapiens 0-12 3967090-1 1985 A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin. Heparin 272-279 serpin family C member 1 Homo sapiens 24-40 3967090-1 1985 A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin. Heparin 272-279 serpin family C member 1 Homo sapiens 42-48 3967090-1 1985 A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin. Heparin 272-279 serpin family C member 1 Homo sapiens 24-36 3967090-3 1985 AT III was purified from normal and propositus plasma by sulfate dextran precipitation followed by heparin affinity chromatography. Dextran Sulfate 57-72 serpin family C member 1 Homo sapiens 0-6 3967090-3 1985 AT III was purified from normal and propositus plasma by sulfate dextran precipitation followed by heparin affinity chromatography. Heparin 99-106 serpin family C member 1 Homo sapiens 0-6 3970857-0 1985 Purification of antithrombin "Vicenza": a molecule with normal heparin affinity and impaired reactivity to thrombin. Heparin 63-70 serpin family C member 1 Homo sapiens 16-28 3970857-1 1985 Antithrombin III (AT) "Vicenza", a previously described dysfunctional AT associated with familial thrombosis, has been isolated by heparin affinity chromatography. Heparin 131-138 serpin family C member 1 Homo sapiens 0-16 3973461-4 1985 Antithrombin (AT) binding by heparinized PMA materials (compared with PMA control beads) ranged from no AT binding for the material heparinized with carbodiimide (PMA-Alb-Hep(EDC] to 3.6 micrograms/ml packed beads for the material heparinized by radical polymerization (PMA-MA-Hep). Carbodiimides 149-161 serpin family C member 1 Homo sapiens 0-12 3973461-4 1985 Antithrombin (AT) binding by heparinized PMA materials (compared with PMA control beads) ranged from no AT binding for the material heparinized with carbodiimide (PMA-Alb-Hep(EDC] to 3.6 micrograms/ml packed beads for the material heparinized by radical polymerization (PMA-MA-Hep). ethylene dichloride 175-178 serpin family C member 1 Homo sapiens 0-12 3973461-5 1985 Heparin-like catalytic activity of these materials (assayed by measuring the generation of thrombin-antithrombin complex in plasma) correlated well with the amount of heparin bound, but not as well with AT binding capacity. Heparin 0-7 serpin family C member 1 Homo sapiens 100-112 2578296-2 1985 Several materials were highly active in factor Xa inhibition and the reaction rate at constant factor Xa concentration appeared to be predicted by the extent of intrinsic antithrombin III fluorescence change induced by the polysaccharide. Polysaccharides 223-237 serpin family C member 1 Homo sapiens 171-187 2578296-3 1985 Heparin fractions of different molecular weight and affinity for antithrombin III showed similar kinetic parameters in catalysis of the thrombin-antithrombin III reaction when these parameters were expressed on the basis of antithrombin III-binding heparin. Heparin 249-256 serpin family C member 1 Homo sapiens 65-81 2578296-4 1985 The latter was determined by stoichiometric titration of the antithrombin III fluorescence change by the heparin preparation. Heparin 105-112 serpin family C member 1 Homo sapiens 61-77 2578296-6 1985 This indicated that functional heparin molecules had similar kinetic properties regardless of size or antithrombin III-binding affinity and is possible because the Km for antithrombin III is determined by diffusion rather than by binding affinity. Heparin 31-38 serpin family C member 1 Homo sapiens 102-118 2578296-6 1985 This indicated that functional heparin molecules had similar kinetic properties regardless of size or antithrombin III-binding affinity and is possible because the Km for antithrombin III is determined by diffusion rather than by binding affinity. Heparin 31-38 serpin family C member 1 Homo sapiens 171-187 2579452-0 1985 Comparison between the effect of pentosan polysulphate heparin and antithrombin III injections in antithrombin III deficient patients. pentosan polysulphate heparin 33-62 serpin family C member 1 Homo sapiens 98-114 2579452-1 1985 Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway. Pentosan Sulfuric Polyester 0-21 serpin family C member 1 Homo sapiens 63-79 2579452-7 1985 The marked effect of pentosan polysulphate on thrombin and factor Xa generation in these patients is due to its AT III independent mechanism of action. Pentosan Sulfuric Polyester 21-42 serpin family C member 1 Homo sapiens 112-118 2579452-1 1985 Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway. Pentosan Sulfuric Polyester 0-21 serpin family C member 1 Homo sapiens 81-87 2579452-1 1985 Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway. Heparin 28-35 serpin family C member 1 Homo sapiens 63-79 2579452-1 1985 Pentosan polysulphate is an heparin analogue which acts via an antithrombin III (AT III) independent pathway. Heparin 28-35 serpin family C member 1 Homo sapiens 81-87 3975871-0 1985 Inhibition of antithrombin III by lipid peroxides. Lipid Peroxides 34-49 serpin family C member 1 Homo sapiens 14-30 3965464-1 1985 Two distinct forms of antithrombin III were isolated by chromatography of normal human plasma on heparin-Sepharose. Sepharose 105-114 serpin family C member 1 Homo sapiens 22-38 3965464-2 1985 The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized. Sodium Chloride 106-110 serpin family C member 1 Homo sapiens 16-28 3965464-2 1985 The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized. Sodium Chloride 106-110 serpin family C member 1 Homo sapiens 46-52 3965464-2 1985 The predominant antithrombin species present (AT-III alpha), which eluted from the affinity column in 1 M NaCl, was identified as the antithrombin III form which has been previously characterized. Sodium Chloride 106-110 serpin family C member 1 Homo sapiens 134-150 3965464-5 1985 Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha. Carbohydrates 0-12 serpin family C member 1 Homo sapiens 161-167 3965464-0 1985 Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. Carbohydrates 75-87 serpin family C member 1 Homo sapiens 37-53 3965464-0 1985 Isolation and characterization of an antithrombin III variant with reduced carbohydrate content and enhanced heparin binding. Heparin 109-116 serpin family C member 1 Homo sapiens 37-53 3965464-1 1985 Two distinct forms of antithrombin III were isolated by chromatography of normal human plasma on heparin-Sepharose. Heparin 97-104 serpin family C member 1 Homo sapiens 22-38 3965464-5 1985 Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha. Hexosamines 114-124 serpin family C member 1 Homo sapiens 161-167 3975871-1 1985 A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids. Lipid Peroxides 76-91 serpin family C member 1 Homo sapiens 38-54 3965464-5 1985 Carbohydrate determination revealed the sole detectable structural difference in the two antithrombins: levels of hexosamine, neutral sugars, and sialic acid in AT-III beta were all 25-30% less than in AT-III alpha. N-Acetylneuraminic Acid 146-157 serpin family C member 1 Homo sapiens 161-167 3975871-1 1985 A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids. Lipid Peroxides 76-91 serpin family C member 1 Homo sapiens 56-62 3965464-6 1985 Kinetic studies of thrombin inactivation by both antithrombins, in the presence of nonsaturating amounts of heparin, indicated that AT-III beta inhibited thrombin more rapidly. Heparin 108-115 serpin family C member 1 Homo sapiens 132-138 3965464-7 1985 AT-III beta is also distinguishable from AT-III alpha on the basis of heparin-binding affinity estimated from titration of protein fluorescence with heparin. Heparin 70-77 serpin family C member 1 Homo sapiens 0-6 3975871-1 1985 A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids. Fatty Acids, Unsaturated 122-145 serpin family C member 1 Homo sapiens 38-54 3965464-7 1985 AT-III beta is also distinguishable from AT-III alpha on the basis of heparin-binding affinity estimated from titration of protein fluorescence with heparin. Heparin 149-156 serpin family C member 1 Homo sapiens 0-6 3975871-1 1985 A study was made of the inhibition of antithrombin III (At III) activity by lipid peroxides prepared from autoxidation of unsaturated fatty acids. Fatty Acids, Unsaturated 122-145 serpin family C member 1 Homo sapiens 56-62 3965464-8 1985 Thus, antithrombin III exists as two molecular entities in human plasma which differ both structurally, in carbohydrate content, and functionally, in their heparin-binding behavior. Carbohydrates 107-119 serpin family C member 1 Homo sapiens 6-22 3965464-8 1985 Thus, antithrombin III exists as two molecular entities in human plasma which differ both structurally, in carbohydrate content, and functionally, in their heparin-binding behavior. Heparin 156-163 serpin family C member 1 Homo sapiens 6-22 3975871-2 1985 Lipid peroxides markedly reduced the thrombin neutralising activity of plasma and purified At III with or without albumin carrier. Lipid Peroxides 0-15 serpin family C member 1 Homo sapiens 91-97 3975871-3 1985 Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site. Heparin 0-7 serpin family C member 1 Homo sapiens 121-127 2944348-5 1985 However, at high concentration of heparin, plasmin inactivation by antithrombin III is accelerated even in the presence of fibrinogen or fibrin. Heparin 34-41 serpin family C member 1 Homo sapiens 67-83 3975871-3 1985 Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site. Sepharose 8-17 serpin family C member 1 Homo sapiens 121-127 3975871-3 1985 Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site. Heparin 37-44 serpin family C member 1 Homo sapiens 121-127 3975871-3 1985 Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site. Lipid Peroxides 98-113 serpin family C member 1 Homo sapiens 121-127 3975871-3 1985 Heparin Sepharose chromatography and heparin cofactor assays suggested that the primary target of lipid peroxides on the At III molecule may be the heparin binding site. Heparin 148-155 serpin family C member 1 Homo sapiens 121-127 3975871-4 1985 Results from electrophoretic studies suggested that interaction between lipid peroxides and At III increased the negative charge of the At III molecule; however, no aggregation of the At III molecule was observed. Lipid Peroxides 72-87 serpin family C member 1 Homo sapiens 92-98 3975871-4 1985 Results from electrophoretic studies suggested that interaction between lipid peroxides and At III increased the negative charge of the At III molecule; however, no aggregation of the At III molecule was observed. Lipid Peroxides 72-87 serpin family C member 1 Homo sapiens 136-142 3975871-4 1985 Results from electrophoretic studies suggested that interaction between lipid peroxides and At III increased the negative charge of the At III molecule; however, no aggregation of the At III molecule was observed. Lipid Peroxides 72-87 serpin family C member 1 Homo sapiens 136-142 3975871-5 1985 Lipid peroxidation is being increasingly recognised as a factor in the pathogenesis of several disease states, and it is possible that local inhibition of At III by lipid peroxides could contribute towards the development of a thrombotic event. Lipid Peroxides 165-180 serpin family C member 1 Homo sapiens 155-161 4026390-5 1985 Whereas catalytic amounts of heparin accelerate greatly the inhibitory effect of ATIII, no accelerating effect of heparin on PP5 could be observed under the same conditions. Heparin 29-36 serpin family C member 1 Homo sapiens 81-86 2409857-8 1985 Follicular PP5, like antithrombin III, interacted reversibly with heparin and thrombin affinity matrices, suggesting a potential biological role as a follicular anticoagulant, whereas PAPP-A, a specific and potent inhibitor of leukocyte elastase, contributes to the maintenance of proteolytic homeostasis and the protection of spermatozoa and embryo against proteolytic attack originating from the maternal leukocytes. Heparin 66-73 serpin family C member 1 Homo sapiens 21-37 3966799-1 1985 The therapeutic anticoagulant action of heparin is mediated by the ability of a multifunctional octadecasaccharide region of the molecule to bind to and differentially alter the conformational integrity of antithrombin, and the sugar sequence of the primary binding domain is known. Heparin 40-47 serpin family C member 1 Homo sapiens 206-218 3966799-1 1985 The therapeutic anticoagulant action of heparin is mediated by the ability of a multifunctional octadecasaccharide region of the molecule to bind to and differentially alter the conformational integrity of antithrombin, and the sugar sequence of the primary binding domain is known. octadecasaccharide 96-114 serpin family C member 1 Homo sapiens 206-218 3919676-11 1985 Not only may platelet aggregation persist with low molecular weight heparin which rekindles the debate as to its pathogenic mechanism, but also low molecular weight heparin may have a slight antithrombin effect which limits its use in patients at high risk of thromboembolism, imposing treatment with fast acting vitamin K antagonists. Heparin 165-172 serpin family C member 1 Homo sapiens 191-203 4007636-0 1985 Treatment of familial antithrombin-III deficiency with danazol. Danazol 55-62 serpin family C member 1 Homo sapiens 22-38 3868345-1 1985 Intraperitoneal application of carbon tetrachloride into rabbits caused high mortality due to liver damage with increase of serum transaminases, coagulation disorders, and decrease of antithrombin III (AT III) blood levels. Carbon Tetrachloride 31-51 serpin family C member 1 Homo sapiens 202-208 3868345-5 1985 AT III 25 U/kg and in combination with heparin showed marginal effects, 50 U/kg AT III resulted in increased survival rate and time, improvement of pathological changes of coagulation parameters and of blood urea nitrogen and serum creatinine levels. Urea 208-212 serpin family C member 1 Homo sapiens 80-86 3868345-5 1985 AT III 25 U/kg and in combination with heparin showed marginal effects, 50 U/kg AT III resulted in increased survival rate and time, improvement of pathological changes of coagulation parameters and of blood urea nitrogen and serum creatinine levels. Nitrogen 213-221 serpin family C member 1 Homo sapiens 80-86 3868345-5 1985 AT III 25 U/kg and in combination with heparin showed marginal effects, 50 U/kg AT III resulted in increased survival rate and time, improvement of pathological changes of coagulation parameters and of blood urea nitrogen and serum creatinine levels. Creatinine 232-242 serpin family C member 1 Homo sapiens 80-86 2581861-3 1985 Now some conditions (AT III Trento, for example) are known to show an abnormal pattern only in the absence of heparin. Heparin 110-117 serpin family C member 1 Homo sapiens 21-27 2581861-6 1985 Therefore, the test should be carried out as a screening procedure both in plasma and serum and in the presence or absence of heparin in every case of suspected AT III abnormality. Heparin 126-133 serpin family C member 1 Homo sapiens 161-167 4007636-1 1985 3 individuals from 2 unrelated families with recurrent thromboses and quantitative deficiencies of antithrombin III (AT-III) were treated with danazol, 600 mg daily for 4 months. Danazol 143-150 serpin family C member 1 Homo sapiens 99-115 4007636-1 1985 3 individuals from 2 unrelated families with recurrent thromboses and quantitative deficiencies of antithrombin III (AT-III) were treated with danazol, 600 mg daily for 4 months. Danazol 143-150 serpin family C member 1 Homo sapiens 117-123 4007636-2 1985 Significant increases of AT-III (p less than 0.025) measured as heparin cofactor activity were noted in 1 female and 1 male patient. Heparin 64-71 serpin family C member 1 Homo sapiens 25-31 2579436-1 1985 There is now considerable evidence that the antithrombotic and the hemorrhagic effects of heparin can be dissociated by using low molecular weight heparins and by using heparin with low affinity to AT III. Heparin 90-97 serpin family C member 1 Homo sapiens 198-204 4008141-3 1985 In this study heparin fractions prepared by affinity chromatography on immobilized AT III and by gel filtration chromatography were compared for their ability to inhibit complement mediated haemolysis and both classical and alternative pathway C3 activation as measured by crossed immunoelectrophoresis. Heparin 14-21 serpin family C member 1 Homo sapiens 83-89 3975640-1 1985 Affinity for antithrombin III and anti-Xa activity of selectively carboxyl esterified heparin. Heparin 86-93 serpin family C member 1 Homo sapiens 13-29 6084876-0 1984 Purification and biological property of heparin cofactor II: activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans. Dextran Sulfate 119-134 serpin family C member 1 Homo sapiens 99-115 4082034-4 1985 The use of small doses of heparin was shown to result in a rise of antithrombin III activity in the plasma irrespective of an obvious clinical effect of treatment. Heparin 26-33 serpin family C member 1 Homo sapiens 67-83 6531759-5 1984 Examination of Lineweaver-Burk plots showed nonlinearity at high concentrations of S-2238 as used in the antithrombin III assays. S 2238 83-89 serpin family C member 1 Homo sapiens 105-121 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Dextran Sulfate 0-15 serpin family C member 1 Homo sapiens 79-85 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Dextran Sulfate 0-15 serpin family C member 1 Homo sapiens 149-155 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Heparin 40-47 serpin family C member 1 Homo sapiens 79-85 3838602-0 1985 Histidine-rich glycoprotein inhibits the antithrombin activity of heparin cofactor II in the presence of heparin or dermatan sulfate. Heparin 66-73 serpin family C member 1 Homo sapiens 41-53 3838602-0 1985 Histidine-rich glycoprotein inhibits the antithrombin activity of heparin cofactor II in the presence of heparin or dermatan sulfate. Dermatan Sulfate 116-132 serpin family C member 1 Homo sapiens 41-53 6442470-3 1984 The patients with CH were further classified into two groups: in group CH-I, whose consciousness state was stupor or further deteriorated including coma on admission, the excretion rate of AT III RA was 18.08 +/- 2.50 X 10(-4) ml/min. Radium 196-198 serpin family C member 1 Homo sapiens 189-195 6084876-0 1984 Purification and biological property of heparin cofactor II: activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans. Glycosaminoglycans 147-165 serpin family C member 1 Homo sapiens 99-115 6084876-3 1984 Chem., 257, 2162, 1982) and abilities of dextran sulfate and various glycosaminoglycans to activate the antithrombin activities of HC II and antithrombin III (AT III) were studied. Glycosaminoglycans 69-87 serpin family C member 1 Homo sapiens 104-116 6530392-1 1984 Whale heparin was partially digested with a purified heparinase and the oligosaccharide fractions with 8-20 monosaccharide units were isolated from the digest by gel filtration on Sephadex G-50, followed by affinity chromatography on a column of antithrombin III immobilized on Sepharose 4B. Oligosaccharides 72-87 serpin family C member 1 Homo sapiens 246-262 6525533-7 1984 In the antithrombin III group and the antithrombin III plus heparin group, however, creatinine clearance (Clcr) was moderately elevated while FENa and CH2O remained unchanged as compared with the values before the burn. Creatinine 84-94 serpin family C member 1 Homo sapiens 38-54 6525533-7 1984 In the antithrombin III group and the antithrombin III plus heparin group, however, creatinine clearance (Clcr) was moderately elevated while FENa and CH2O remained unchanged as compared with the values before the burn. clcr 106-110 serpin family C member 1 Homo sapiens 38-54 6525533-8 1984 The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, Clcr and CH2O. clcr 121-125 serpin family C member 1 Homo sapiens 4-20 6525533-8 1984 The antithrombin III plus heparin group showed slightly better results than the antithrombin III group in Ucr/Pcr ratio, Clcr and CH2O. Formaldehyde 130-134 serpin family C member 1 Homo sapiens 4-20 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Heparin 40-47 serpin family C member 1 Homo sapiens 149-155 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Heparin 126-133 serpin family C member 1 Homo sapiens 79-85 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Heparin 126-133 serpin family C member 1 Homo sapiens 149-155 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Sulfates 8-15 serpin family C member 1 Homo sapiens 79-85 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Sulfates 8-15 serpin family C member 1 Homo sapiens 149-155 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Heparin 126-133 serpin family C member 1 Homo sapiens 79-85 6084876-7 1984 Dextran sulfate was almost as active as heparin in the activation of HC II and AT III, indicating that in the interactions of heparin with HC II and AT III, sulfate groups of heparin are more important than carboxyl groups. Heparin 126-133 serpin family C member 1 Homo sapiens 149-155 6084876-8 1984 When mixed with thrombin in the presence of dermatan sulfate, normal human plasma showed antithrombin activity which was not due to AT III but to HC II only. Dermatan Sulfate 44-60 serpin family C member 1 Homo sapiens 89-101 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. Octasaccharide 169-183 serpin family C member 1 Homo sapiens 79-95 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. Octasaccharide 169-183 serpin family C member 1 Homo sapiens 149-165 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. hexadecasaccharide 198-216 serpin family C member 1 Homo sapiens 79-95 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. hexadecasaccharide 198-216 serpin family C member 1 Homo sapiens 149-165 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. octadecasaccharide 230-248 serpin family C member 1 Homo sapiens 79-95 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. eicosasaccharide 263-279 serpin family C member 1 Homo sapiens 79-95 6530392-2 1984 A marked difference in the inhibitory activity for thrombin in the presence of antithrombin III was observed between the high-affinity fractions for antithrombin III of octasaccharide approximately hexadecasaccharide and those of octadecasaccharide approximately eicosasaccharide. eicosasaccharide 263-279 serpin family C member 1 Homo sapiens 149-165 6150297-0 1984 Danazol raises antithrombin III levels in cases of familial deficiency. Danazol 0-7 serpin family C member 1 Homo sapiens 15-31 6530392-5 1984 The present observations, together with those so far reported, suggest that the presence of the former structural elements, specifically IdUA(2S)alpha 1----4GlcNS(6S), as well as the antithrombin III-binding pentasaccharide at the proper positions in the molecules of whale heparin oligosaccharides is essential for the manifestation of high inhibitory activity for thrombin in the presence of antithrombin III. pentasaccharide 208-223 serpin family C member 1 Homo sapiens 183-199 6530392-5 1984 The present observations, together with those so far reported, suggest that the presence of the former structural elements, specifically IdUA(2S)alpha 1----4GlcNS(6S), as well as the antithrombin III-binding pentasaccharide at the proper positions in the molecules of whale heparin oligosaccharides is essential for the manifestation of high inhibitory activity for thrombin in the presence of antithrombin III. heparin oligosaccharides 274-298 serpin family C member 1 Homo sapiens 183-199 6335402-2 1984 The rate of inactivation of factor Xa by antithrombin III was found to be decreased in the presence of phospholipid vesicles with high affinity for factor Xa. Phospholipids 103-115 serpin family C member 1 Homo sapiens 41-57 6525337-0 1984 Sequence variation in heparin octasaccharides with high affinity for antithrombin III. heparin octasaccharides 22-45 serpin family C member 1 Homo sapiens 69-85 6525337-1 1984 We have isolated from nitrous acid cleavage products of heparin two major octasaccharide fragments which bind with high affinity to human antithrombin. Nitrous Acid 22-34 serpin family C member 1 Homo sapiens 138-150 6209821-0 1984 Identification of heparin cofactor II as the principal plasma cofactor for the antithrombin activity of pentosan polysulphate (SP54). Pentosan Sulfuric Polyester 104-125 serpin family C member 1 Homo sapiens 79-91 6525337-1 1984 We have isolated from nitrous acid cleavage products of heparin two major octasaccharide fragments which bind with high affinity to human antithrombin. Heparin 56-63 serpin family C member 1 Homo sapiens 138-150 6525337-1 1984 We have isolated from nitrous acid cleavage products of heparin two major octasaccharide fragments which bind with high affinity to human antithrombin. Octasaccharide 74-88 serpin family C member 1 Homo sapiens 138-150 6525337-3 1984 When bound to antithrombin, both octasaccharides produce a 40% enhancement in the intrinsic fluorescence of the protease inhibitor and a rate of human factor Xa inhibition of 5 X 10(5) M-1 s-1 as monitored by stopped-flow fluorometry. octasaccharides 33-48 serpin family C member 1 Homo sapiens 14-26 6525337-4 1984 This suggests that the conformation of antithrombin in the region of the factor Xa binding site is similar when the protease inhibitor is complexed with either octasaccharide. Octasaccharide 160-174 serpin family C member 1 Homo sapiens 39-51 6209821-1 1984 In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54). Pentosan Sulfuric Polyester 152-173 serpin family C member 1 Homo sapiens 3-19 6209821-1 1984 In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54). Pentosan Sulfuric Polyester 175-179 serpin family C member 1 Homo sapiens 3-19 6523441-6 1984 Low- and high affinity heparin fractions were obtained by affinity chromatography using immobilized AT III. Heparin 23-30 serpin family C member 1 Homo sapiens 100-106 6395434-1 1984 A technique is described to completely remove antithrombin III (AT) from small amounts of human plasma by immunoaffinity chromatography on antibodies against human AT linked to Sepharose 4B. Sepharose 177-186 serpin family C member 1 Homo sapiens 46-62 6395434-1 1984 A technique is described to completely remove antithrombin III (AT) from small amounts of human plasma by immunoaffinity chromatography on antibodies against human AT linked to Sepharose 4B. Sepharose 177-186 serpin family C member 1 Homo sapiens 64-66 6395434-1 1984 A technique is described to completely remove antithrombin III (AT) from small amounts of human plasma by immunoaffinity chromatography on antibodies against human AT linked to Sepharose 4B. Sepharose 177-186 serpin family C member 1 Homo sapiens 164-166 6395434-3 1984 HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma. Heparin 115-122 serpin family C member 1 Homo sapiens 126-128 6395434-3 1984 HCII activity was then determined by measuring the rate of human thrombin inhibition by 3 ways: a) activation with heparin in AT-free plasma, b) activation with dermatan sulfate in normal plasma and c) activation with dermatan sulfate in AT-free plasma. Dermatan Sulfate 218-234 serpin family C member 1 Homo sapiens 238-240 6209821-0 1984 Identification of heparin cofactor II as the principal plasma cofactor for the antithrombin activity of pentosan polysulphate (SP54). Pentosan Sulfuric Polyester 127-131 serpin family C member 1 Homo sapiens 79-91 6209821-1 1984 In antithrombin III depleted plasma only a slight reduction was observed in thrombin inhibitory activity due to potentiation by dermatan sulphate or by pentosan polysulphate (SP54). Dermatan Sulfate 128-145 serpin family C member 1 Homo sapiens 3-19 6509363-0 1984 Effects of heparin fractions of different affinities to antithrombin III and thrombin on the inactivation of thrombin and factor Xa by antithrombin III. Heparin 11-18 serpin family C member 1 Homo sapiens 56-72 6509363-0 1984 Effects of heparin fractions of different affinities to antithrombin III and thrombin on the inactivation of thrombin and factor Xa by antithrombin III. Heparin 11-18 serpin family C member 1 Homo sapiens 135-151 6509363-2 1984 There was a good correlation between heparin affinity for antithrombin III and its ability to enhance the inactivation of thrombin and factor Xa. Heparin 37-44 serpin family C member 1 Homo sapiens 58-74 6509363-3 1984 In addition, there was a good correlation between affinity of heparin for thrombin and its catalytic activity on the inactivation of thrombin by antithrombin III. Heparin 62-69 serpin family C member 1 Homo sapiens 145-161 6509363-7 1984 A heparin fraction with very low affinity to thrombin and high affinity to antithrombin III was prepared by repeated fractionation of a low molecular weight heparin on the two affinity columns. Heparin 2-9 serpin family C member 1 Homo sapiens 75-91 6509363-9 1984 The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III. Heparin 98-105 serpin family C member 1 Homo sapiens 158-174 6509363-9 1984 The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III. Heparin 207-214 serpin family C member 1 Homo sapiens 158-174 6509363-9 1984 The results of these studies support the concept that, for both standard and low molecular weight heparin, the enhancement of the inactivation of thrombin by antithrombin III requires the interaction of the heparin with both thrombin and antithrombin III. Heparin 207-214 serpin family C member 1 Homo sapiens 238-254 6520110-2 1984 In the eluate from a Sephacryl S-200 column, heparin caused a peak and then a trough in the fluorescence of 48 nM antithrombin III or 63 nM thrombin. Heparin 45-52 serpin family C member 1 Homo sapiens 114-130 6520110-0 1984 A method to determine the affinity of heparin to thrombin and antithrombin III on equilibrium gel permeation chromatography. Heparin 38-45 serpin family C member 1 Homo sapiens 62-78 6520110-1 1984 Equilibrium gel permeation chromatography was employed to determine the ability of heparin to form complexes with thrombin and antithrombin III. Heparin 83-90 serpin family C member 1 Homo sapiens 127-143 6520110-2 1984 In the eluate from a Sephacryl S-200 column, heparin caused a peak and then a trough in the fluorescence of 48 nM antithrombin III or 63 nM thrombin. sephacryl s 21-32 serpin family C member 1 Homo sapiens 114-130 6500155-1 1984 Prophylactic treatment of two asymptomatic antithrombin III (AT III) -deficient women with oral anticoagulants and heparin during pregnancy and after delivery appeared to be feasible. Heparin 115-122 serpin family C member 1 Homo sapiens 43-59 6500155-1 1984 Prophylactic treatment of two asymptomatic antithrombin III (AT III) -deficient women with oral anticoagulants and heparin during pregnancy and after delivery appeared to be feasible. Heparin 115-122 serpin family C member 1 Homo sapiens 61-67 6500155-3 1984 A high dose of heparin intravenously in one of them caused a strong reduction in the AT III level which was corrected by infusion of AT III concentrate during delivery. Heparin 15-22 serpin family C member 1 Homo sapiens 85-91 6500155-3 1984 A high dose of heparin intravenously in one of them caused a strong reduction in the AT III level which was corrected by infusion of AT III concentrate during delivery. Heparin 15-22 serpin family C member 1 Homo sapiens 133-139 6544786-6 1984 Albumin-heparin conjugates with high affinity for antithrombin III gave more prolonged clotting times as low affinity conjugates when used as coatings for glass. Heparin 8-15 serpin family C member 1 Homo sapiens 50-66 6520110-5 1984 The ability to form a complex of heparin preparations with different anticoagulant activities for thrombin and antithrombin III could be determined satisfactorily. Heparin 33-40 serpin family C member 1 Homo sapiens 111-127 6520110-7 1984 Of 4 preparations with one low-affinity and three high-affinity subfractions of heparin for antithrombin III, the species with the lowest affinity for antithrombin III had the highest affinity for thrombin. Heparin 80-87 serpin family C member 1 Homo sapiens 92-108 6520110-7 1984 Of 4 preparations with one low-affinity and three high-affinity subfractions of heparin for antithrombin III, the species with the lowest affinity for antithrombin III had the highest affinity for thrombin. Heparin 80-87 serpin family C member 1 Homo sapiens 151-167 6487338-2 1984 The binding affinity toward antithrombin III decreases in the following order: Heparin greater than heparin methyl ester greater than heparinylglycine greater than heparinylglycine methyl ester. Heparin 79-86 serpin family C member 1 Homo sapiens 28-44 6487338-2 1984 The binding affinity toward antithrombin III decreases in the following order: Heparin greater than heparin methyl ester greater than heparinylglycine greater than heparinylglycine methyl ester. heparin methyl ester 100-120 serpin family C member 1 Homo sapiens 28-44 6487338-2 1984 The binding affinity toward antithrombin III decreases in the following order: Heparin greater than heparin methyl ester greater than heparinylglycine greater than heparinylglycine methyl ester. heparinylglycine 134-150 serpin family C member 1 Homo sapiens 28-44 6487338-2 1984 The binding affinity toward antithrombin III decreases in the following order: Heparin greater than heparin methyl ester greater than heparinylglycine greater than heparinylglycine methyl ester. heparinylglycine methyl ester 164-193 serpin family C member 1 Homo sapiens 28-44 6496919-0 1984 [Antithrombin III substitution for optimization of the heparin effect during extracorporeal circulation in heart surgery]. Heparin 55-62 serpin family C member 1 Homo sapiens 1-17 6207810-0 1984 Effect of a pentosan polysulphate upon thrombin and factor Xa inactivation by antithrombin III. Pentosan Sulfuric Polyester 12-33 serpin family C member 1 Homo sapiens 78-94 6207810-7 1984 In the presence of pentosan polysulphate the dissociation constant for the initial complex of antithrombin III and thrombin was shown to be reduced from approx. Pentosan Sulfuric Polyester 19-40 serpin family C member 1 Homo sapiens 94-110 6207810-9 1984 An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate. Oligosaccharides 3-18 serpin family C member 1 Homo sapiens 102-118 6207810-9 1984 An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate. Oligosaccharides 3-18 serpin family C member 1 Homo sapiens 151-167 6207810-9 1984 An oligosaccharide (primarily 8-10 saccharide units) prepared from heparin and with high affinity for antithrombin III but low potency in the thrombin-antithrombin III interaction did not diminish the rate of interaction catalysed by pentosan polysulphate. 8-10 saccharide 30-45 serpin family C member 1 Homo sapiens 102-118 6207810-10 1984 The catalysis was shown to be due to a weak electrostatic interaction, since it was completely reversed by concentrations of NaCl greater than 0.3 M. It is concluded that the mechanism is independent of the heparin high-affinity binding site on antithrombin III and is probably due to binding of the high-charge-density polysaccharide to the proteinase. Heparin 207-214 serpin family C member 1 Homo sapiens 245-261 6207810-10 1984 The catalysis was shown to be due to a weak electrostatic interaction, since it was completely reversed by concentrations of NaCl greater than 0.3 M. It is concluded that the mechanism is independent of the heparin high-affinity binding site on antithrombin III and is probably due to binding of the high-charge-density polysaccharide to the proteinase. Polysaccharides 320-334 serpin family C member 1 Homo sapiens 245-261 6207810-11 1984 It is calculated that the acceleration in rate achieved, although lower than that of heparin, approaches that required to be of physiological significance and may be of importance in the anticoagulation role of antithrombin III at sites of high charge density which may occur in vivo. Heparin 85-92 serpin family C member 1 Homo sapiens 211-227 6209818-0 1984 Abolition by dextran sulfate of the heparin-accelerated antithrombin III/thrombin reaction. Dextran Sulfate 13-28 serpin family C member 1 Homo sapiens 56-72 6209818-0 1984 Abolition by dextran sulfate of the heparin-accelerated antithrombin III/thrombin reaction. Heparin 36-43 serpin family C member 1 Homo sapiens 56-72 6209818-1 1984 Dextran sulfate did not inhibit the amidolytic activity of thrombin on Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide, but abolished inhibition of the enzyme with antithrombin III (AT III) in the presence of heparin. Dextran Sulfate 0-15 serpin family C member 1 Homo sapiens 157-173 6209818-1 1984 Dextran sulfate did not inhibit the amidolytic activity of thrombin on Boc-Val-Pro-Arg-4-methylcoumaryl-7-amide, but abolished inhibition of the enzyme with antithrombin III (AT III) in the presence of heparin. Dextran Sulfate 0-15 serpin family C member 1 Homo sapiens 175-181 6209818-4 1984 These findings indicate that binding of dextran sulfate to a site other than the active site of thrombin to prevent the approach of AT III in the presence of heparin. Dextran Sulfate 40-55 serpin family C member 1 Homo sapiens 132-138 6209818-4 1984 These findings indicate that binding of dextran sulfate to a site other than the active site of thrombin to prevent the approach of AT III in the presence of heparin. Heparin 158-165 serpin family C member 1 Homo sapiens 132-138 6496919-5 1984 Heparin sensitivity, measured as an increase in the ratio of activated coagulation time (ACT) X IU heparin-1 X kg-1 as a response to initial heparin dose, was found to be significantly higher (1.22 +/- 0.30 sec X IU heparin-1 X kg-1) in patients receiving AT III as measured in the control group (0.95 +/- 0.23 s X IU heparin-1 X kg-1). Heparin 0-7 serpin family C member 1 Homo sapiens 256-262 6235872-1 1984 Heparan with a low affinity for antithrombin III has previously been demonstrated to inhibit thrombin generation in both normal plasma and plasma depleted of antithrombin III. heparan 0-7 serpin family C member 1 Homo sapiens 32-48 6435583-4 1984 The recurrence of local signs of DVT after 12 day"s heparin therapy with AT III levels (B) of 40%, led to a change in management with infusion of purified AT III concentrate at a dose of 40 U per kg (2 500 U per hour). Heparin 52-59 serpin family C member 1 Homo sapiens 73-79 6435583-5 1984 This induced a rise in AT III activity to over 100% and enabled early introduction of anti-vitamin K therapy. Vitamin K 91-100 serpin family C member 1 Homo sapiens 23-29 6235872-8 1984 These results suggest that heparan sulfate acts primarily by potentiating antithrombin III, while dermatan sulfate acts by potentiating heparin cofactor II. Heparitin Sulfate 27-42 serpin family C member 1 Homo sapiens 74-90 6486808-0 1984 The role of tryptophan residues in heparin-antithrombin interactions. Tryptophan 12-22 serpin family C member 1 Homo sapiens 43-55 6486808-1 1984 A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide. Tryptophan 9-19 serpin family C member 1 Homo sapiens 31-43 6486808-1 1984 A single tryptophan residue on antithrombin has been modified with dimethyl-(2-hydroxy-5-nitrobenzyl)sulfonium bromide. dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium 67-118 serpin family C member 1 Homo sapiens 31-43 6486808-2 1984 This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease inhibitor for mucopolysaccharide. Heparin 51-58 serpin family C member 1 Homo sapiens 103-115 6486808-2 1984 This alteration led to a 500-fold reduction in the heparin-dependent acceleration of thrombin-modified antithrombin interactions, as well as a 10-fold decrease in the avidity of the modified protease inhibitor for mucopolysaccharide. Glycosaminoglycans 214-232 serpin family C member 1 Homo sapiens 103-115 6486808-3 1984 Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor. Octasaccharide 39-53 serpin family C member 1 Homo sapiens 17-29 6486808-3 1984 Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor. Heparin 72-79 serpin family C member 1 Homo sapiens 17-29 6486808-3 1984 Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor. dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium 104-156 serpin family C member 1 Homo sapiens 17-29 6486808-3 1984 Preincubation of antithrombin with the octasaccharide binding domain of heparin prior to treatment with dimethyl-(2-hydroxy-5-nitrobenzyl) sulfonium bromide was able to suppress modification of the critical tryptophan and preserve the functional capacities of the protease inhibitor. Tryptophan 207-217 serpin family C member 1 Homo sapiens 17-29 6486808-4 1984 Fluorescence quenching experiments indicated that the modifiable tryptophan groups of antithrombin were exposed to the solvent environment. Tryptophan 65-75 serpin family C member 1 Homo sapiens 86-98 6235872-1 1984 Heparan with a low affinity for antithrombin III has previously been demonstrated to inhibit thrombin generation in both normal plasma and plasma depleted of antithrombin III. heparan 0-7 serpin family C member 1 Homo sapiens 158-174 6486808-5 1984 Based upon these data, it was proposed that the loss of "heparin cofactor" activity of antithrombin must be predominantly due to an inability of the modified protease inhibitor to undergo a conformational transition required for mucopolysaccharide-dependent "activation" of the macromolecule. Glycosaminoglycans 229-247 serpin family C member 1 Homo sapiens 87-99 6235872-2 1984 In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III. Heparin 22-29 serpin family C member 1 Homo sapiens 66-82 6235872-2 1984 In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III. Heparin 22-29 serpin family C member 1 Homo sapiens 189-205 6235872-2 1984 In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III. Heparin 34-41 serpin family C member 1 Homo sapiens 66-82 6235872-2 1984 In addition, standard heparin and heparin with a low affinity for antithrombin III have been demonstrated to have equivalent inhibitory actions on thrombin generation in plasma depleted of antithrombin III. Heparin 34-41 serpin family C member 1 Homo sapiens 189-205 6235872-5 1984 In contrast, dermatan sulfate inhibited thrombin generation in both normal and antithrombin III-depleted plasma. Dermatan Sulfate 13-29 serpin family C member 1 Homo sapiens 79-95 6474360-0 1984 Effect of continuous low-dose intravenous heparin administered during operation on postoperative measurements of antithrombin III and antifactor Xa. Heparin 42-49 serpin family C member 1 Homo sapiens 113-129 6487709-0 1984 Interaction of antithrombin III with preadsorbed albumin-heparin conjugates. Heparin 57-64 serpin family C member 1 Homo sapiens 15-31 6487709-1 1984 The adsorption of antithrombin III (AT III) onto polystyrene surfaces preadsorbed with albumin or albumin-heparin conjugates was studied using a two step enzyme immuno assay. Polystyrenes 49-60 serpin family C member 1 Homo sapiens 18-34 6487709-1 1984 The adsorption of antithrombin III (AT III) onto polystyrene surfaces preadsorbed with albumin or albumin-heparin conjugates was studied using a two step enzyme immuno assay. Polystyrenes 49-60 serpin family C member 1 Homo sapiens 36-42 6487709-1 1984 The adsorption of antithrombin III (AT III) onto polystyrene surfaces preadsorbed with albumin or albumin-heparin conjugates was studied using a two step enzyme immuno assay. Heparin 106-113 serpin family C member 1 Homo sapiens 18-34 6487709-1 1984 The adsorption of antithrombin III (AT III) onto polystyrene surfaces preadsorbed with albumin or albumin-heparin conjugates was studied using a two step enzyme immuno assay. Heparin 106-113 serpin family C member 1 Homo sapiens 36-42 6487709-2 1984 When AT III-buffer solutions were used, the highest adsorption values were measured on high affinity albumin-heparin conjugate pretreated surfaces. Heparin 109-116 serpin family C member 1 Homo sapiens 5-11 6487709-3 1984 Less AT III adsorption was found on nonfractionated albumin-heparin conjugate preadsorbed surfaces. Heparin 60-67 serpin family C member 1 Homo sapiens 5-11 6487709-5 1984 When AT III was adsorbed from plasma or plasma dilutions with buffer, only AT III on surfaces preadsorbed with high affinity or nonfractionated albumin-heparin conjugate was found. Heparin 152-159 serpin family C member 1 Homo sapiens 5-11 6474360-2 1984 The anticoagulant effect of heparin was determined by immunologic measurements of antithrombin III (AT III) and by assay of AT III and antifactor Xa activity on postoperative days 1 and 3. Heparin 28-35 serpin family C member 1 Homo sapiens 82-98 6474360-2 1984 The anticoagulant effect of heparin was determined by immunologic measurements of antithrombin III (AT III) and by assay of AT III and antifactor Xa activity on postoperative days 1 and 3. Heparin 28-35 serpin family C member 1 Homo sapiens 100-106 6474360-2 1984 The anticoagulant effect of heparin was determined by immunologic measurements of antithrombin III (AT III) and by assay of AT III and antifactor Xa activity on postoperative days 1 and 3. Heparin 28-35 serpin family C member 1 Homo sapiens 124-130 6474360-3 1984 Despite lowered plasma AT III levels on postoperative day 3, the patients who had received low-dose heparin had significantly increased plasma antifactor Xa activity when compared with control patients (P less than 0.05). Heparin 100-107 serpin family C member 1 Homo sapiens 23-29 6495266-1 1984 Antithrombin III was purified from normal plasma by DEAE-Sephadex chromatography and heparin affinity chromatography; the protein was subsequently radiolabelled with 125I. 2-diethylaminoethanol 52-56 serpin family C member 1 Homo sapiens 0-16 6495266-1 1984 Antithrombin III was purified from normal plasma by DEAE-Sephadex chromatography and heparin affinity chromatography; the protein was subsequently radiolabelled with 125I. sephadex 57-65 serpin family C member 1 Homo sapiens 0-16 6495266-1 1984 Antithrombin III was purified from normal plasma by DEAE-Sephadex chromatography and heparin affinity chromatography; the protein was subsequently radiolabelled with 125I. Heparin 85-92 serpin family C member 1 Homo sapiens 0-16 6495266-4 1984 In semilogarithmic plots 125I-antithrombin III disappeared according to a double exponential curve with a half-life in the second phase of 56.8 hr in the absence of heparin and of 33.7 hr in the presence of heparin. Heparin 165-172 serpin family C member 1 Homo sapiens 30-46 6484894-1 1984 Effect of purification of AT III-binding sequence of heparin. Heparin 53-60 serpin family C member 1 Homo sapiens 26-32 6495266-4 1984 In semilogarithmic plots 125I-antithrombin III disappeared according to a double exponential curve with a half-life in the second phase of 56.8 hr in the absence of heparin and of 33.7 hr in the presence of heparin. Heparin 207-214 serpin family C member 1 Homo sapiens 30-46 6495266-6 1984 These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III. Heparin 36-43 serpin family C member 1 Homo sapiens 102-118 6495266-6 1984 These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III. Heparin 36-43 serpin family C member 1 Homo sapiens 144-160 6495266-6 1984 These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III. Heparin 63-70 serpin family C member 1 Homo sapiens 102-118 6495266-6 1984 These data support the concept that heparin disappears as free heparin from the equilibrium heparin - antithrombin III in equilibrium heparin + antithrombin III. Heparin 63-70 serpin family C member 1 Homo sapiens 144-160 6495266-7 1984 Immuno-reactive antithrombin III decreased from 100% to 85-90% immediately after injection of 125I-antithrombin III in the presence of heparin and returned to normal values within 30 min. Heparin 135-142 serpin family C member 1 Homo sapiens 16-32 6495266-7 1984 Immuno-reactive antithrombin III decreased from 100% to 85-90% immediately after injection of 125I-antithrombin III in the presence of heparin and returned to normal values within 30 min. Heparin 135-142 serpin family C member 1 Homo sapiens 99-115 6495267-3 1984 The generation of thrombin by lipid peroxides is also enhanced by their inhibitory action on antithrombin III. Lipid Peroxides 30-45 serpin family C member 1 Homo sapiens 93-109 6747440-3 1984 Antithrombin III from two members of this family was purified by dextran sulfate precipitation, affinity chromatography on heparin-Sepharose, and ion-exchange chromatography on DEAE-Sephadex A-50. Dextran Sulfate 65-80 serpin family C member 1 Homo sapiens 0-16 6747440-3 1984 Antithrombin III from two members of this family was purified by dextran sulfate precipitation, affinity chromatography on heparin-Sepharose, and ion-exchange chromatography on DEAE-Sephadex A-50. Heparin 123-130 serpin family C member 1 Homo sapiens 0-16 6747440-3 1984 Antithrombin III from two members of this family was purified by dextran sulfate precipitation, affinity chromatography on heparin-Sepharose, and ion-exchange chromatography on DEAE-Sephadex A-50. Sepharose 131-140 serpin family C member 1 Homo sapiens 0-16 6747440-3 1984 Antithrombin III from two members of this family was purified by dextran sulfate precipitation, affinity chromatography on heparin-Sepharose, and ion-exchange chromatography on DEAE-Sephadex A-50. DEAE-Sephadex A-50 177-195 serpin family C member 1 Homo sapiens 0-16 6747440-4 1984 Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and crossed immunoelectrophoresis showed that only approximately half of the purified antithrombin III was capable of forming a complex with thrombin. sodium dodecyl sulfate-polyacrylamide 0-37 serpin family C member 1 Homo sapiens 144-160 6747440-6 1984 The nonreactive as well as the reactive population of antithrombin III bound heparin with the same affinity as normal antithrombin III. Heparin 77-84 serpin family C member 1 Homo sapiens 54-70 6747440-7 1984 This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence. Salts 116-120 serpin family C member 1 Homo sapiens 141-157 6747440-7 1984 This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence. Heparin 163-170 serpin family C member 1 Homo sapiens 141-157 6747440-7 1984 This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence. Sepharose 171-180 serpin family C member 1 Homo sapiens 141-157 6747440-7 1984 This was shown by crossed immunoelectrophoresis using heparin in the first dimension, by the elution pattern during salt gradient elution of antithrombin III from heparin-Sepharose, and by heparin enhancement of intrinsic fluorescence. Heparin 163-170 serpin family C member 1 Homo sapiens 141-157 6747440-8 1984 Kinetic studies in the absence and in the presence of heparin indicated that the fraction of antithrombin III that could inactivate thrombin was functionally normal. Heparin 54-61 serpin family C member 1 Homo sapiens 93-109 6379981-7 1984 This is also the case with heparins of low and high affinity for antithrombin. Heparin 27-35 serpin family C member 1 Homo sapiens 65-77 6467606-3 1984 The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis. Heparin 33-40 serpin family C member 1 Homo sapiens 23-29 6746897-1 1984 We have examined the role of heparinlike molecules in the regulation of coagulation by perfusing rat hindquarters with purified human thrombin and with its plasma inhibitor, antithrombin. heparinlike 29-40 serpin family C member 1 Homo sapiens 174-186 6746897-6 1984 The above mucopolysaccharides function in a manner similar to commercial heparin, since modification of antithrombin at a site critical for heparin-dependent acceleration of the protease inhibitor resulted in a level of interaction product identical to the uncatalyzed amount. Glycosaminoglycans 10-29 serpin family C member 1 Homo sapiens 104-116 6206589-0 1984 Inhibition of thrombin-induced platelet aggregation and serotonin release by antithrombin III and heparin cofactor II in the presence of standard heparin, dermatan sulfate and pentosan polysulfate. Dermatan Sulfate 155-171 serpin family C member 1 Homo sapiens 77-93 6746897-6 1984 The above mucopolysaccharides function in a manner similar to commercial heparin, since modification of antithrombin at a site critical for heparin-dependent acceleration of the protease inhibitor resulted in a level of interaction product identical to the uncatalyzed amount. Heparin 140-147 serpin family C member 1 Homo sapiens 104-116 6746897-7 1984 Finally, addition of diisofluorophosphate-thrombin to the enzyme perfusion stream reduced the amount of thrombin-antithrombin complex formed in the animal by 30-40%, which suggested that thrombin bound to the endothelium as well as enzyme free in solution are accessible to antithrombin that has interacted with heparinlike molecules present on the endothelium. diisofluorophosphate 21-41 serpin family C member 1 Homo sapiens 113-125 6746897-7 1984 Finally, addition of diisofluorophosphate-thrombin to the enzyme perfusion stream reduced the amount of thrombin-antithrombin complex formed in the animal by 30-40%, which suggested that thrombin bound to the endothelium as well as enzyme free in solution are accessible to antithrombin that has interacted with heparinlike molecules present on the endothelium. diisofluorophosphate 21-41 serpin family C member 1 Homo sapiens 274-286 6206589-0 1984 Inhibition of thrombin-induced platelet aggregation and serotonin release by antithrombin III and heparin cofactor II in the presence of standard heparin, dermatan sulfate and pentosan polysulfate. Serotonin 56-65 serpin family C member 1 Homo sapiens 77-93 6467606-3 1984 The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis. Heparin 33-40 serpin family C member 1 Homo sapiens 124-130 6467606-3 1984 The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis. Heparin 33-40 serpin family C member 1 Homo sapiens 124-130 6467606-3 1984 The binding ability of AT III to heparin was observed by crossed immunoelectrophoresis, and showed a reduced second peak of AT III with a faster AT III with a qualitative defect in its binding ability to heparin due to impaired protein synthesis. Heparin 204-211 serpin family C member 1 Homo sapiens 23-29 6426771-2 1984 In view of this literature, a study of patients on tamoxifen was initiated to determine if a paradoxical estrogenic effect was present as evidenced by lowered levels of antithrombin III (AT III). Tamoxifen 51-60 serpin family C member 1 Homo sapiens 169-185 6329378-9 1984 Vitamin K increased the quantity of prothrombin secreted by twofold, without affecting the rate of secretion over a five-day culture period, and had an apparent transient inhibitory effect on secretion of antithrombin III. Vitamin K 0-9 serpin family C member 1 Homo sapiens 205-221 6145672-6 1984 Among these putrescine-binding proteins, we identified, with the help of corresponding specific antisera, four protease inhibitors: alpha 2-macroglobulin, alpha 1-antitrypsin, alpha 1-antichymotrypsin and antithrombin III. Putrescine 12-22 serpin family C member 1 Homo sapiens 205-221 6426771-13 1984 The finding of lowered functional activity of AT III in 42% of tamoxifen-treated patients is preliminary in nature and will require larger confirmatory studies, including further clinical correlation of this observation. Tamoxifen 63-72 serpin family C member 1 Homo sapiens 46-52 6733045-1 1984 Platelets and phospholipids have been shown to protect factor Xa from inhibition by the heparin--antithrombin III complex. Phospholipids 14-27 serpin family C member 1 Homo sapiens 97-113 6740570-0 1984 Reactivity of heparin with the human plasma heparin-binding proteins thrombin, antithrombin III, and apolipoproteins E and B-100. Heparin 14-21 serpin family C member 1 Homo sapiens 79-95 6740570-1 1984 The heparin-binding properties of human plasma apolipoproteins B-100 and E (apoB-100 and E) of low density lipoproteins (LDL), thrombin, and antithrombin-III (AT-III) were investigated. Heparin 4-11 serpin family C member 1 Homo sapiens 141-157 6740570-1 1984 The heparin-binding properties of human plasma apolipoproteins B-100 and E (apoB-100 and E) of low density lipoproteins (LDL), thrombin, and antithrombin-III (AT-III) were investigated. Heparin 4-11 serpin family C member 1 Homo sapiens 159-165 6740570-4 1984 HRH was fractionated further by chromatography on a column of AT-III bound to concanavalin A-Sepharose. Sepharose 93-102 serpin family C member 1 Homo sapiens 62-68 6740570-5 1984 The unretained fraction of heparin (HRH1) had a low affinity for AT-III. Heparin 27-34 serpin family C member 1 Homo sapiens 65-71 6722352-9 1984 Heparin inhibited the tissue factor-dependent activation of factor IX almost completely, apparently through the effect of antithrombin on the feedback reactions of factors Xa and IXa on factor VII. Heparin 0-7 serpin family C member 1 Homo sapiens 122-134 6740570-6 1984 The bound heparin (HRH2) had a high affinity for AT-III and precipitated LDL in the presence of Ca2+. Heparin 10-17 serpin family C member 1 Homo sapiens 49-55 6740570-10 1984 Denatured AT-III did not bind HRH2, indicating that its heparin recognition site may depend on conformation. Heparin 56-63 serpin family C member 1 Homo sapiens 10-16 6733045-7 1984 These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin. Phospholipids 76-89 serpin family C member 1 Homo sapiens 161-177 6733045-7 1984 These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin. Phospholipids 76-89 serpin family C member 1 Homo sapiens 219-235 6733045-7 1984 These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin. Calcium 129-136 serpin family C member 1 Homo sapiens 161-177 6733045-7 1984 These observations are consistent with the hypothesis that platelets, brain phospholipids, and tissue factor, in the presence of calcium, partition heparin from antithrombin III, and thus prevent full expression of the antithrombin III-dependent anticoagulant activity of heparin. Calcium 129-136 serpin family C member 1 Homo sapiens 219-235 6237371-3 1984 Isomeric compounds of N alpha-arylsulfonylated amides of omega-amidinophenyl-alpha-aminoalkylcarboxylic acids--N alpha-amidinophenylsulfonylated amides or N alpha-arylsulfonylated amidino anilides of omega-phenyl-alpha-aminoalkylcarboxylic acids, respectively--possess weak antithrombin activity as compared to the derivatives of the basic structure. n alpha-arylsulfonylated amides 22-53 serpin family C member 1 Homo sapiens 274-286 6742427-6 1984 The assay has been used to follow the generation of Xa-antithrombin complex in kinetic situations by the addition of 1 microM Ile-Glu-Gly-Arg-chloro- methylketone to the ELISA sampling buffer, and it has also been used in plasma systems, where a 20-fold reduction in the sensitivity of the assay is observed. isoleucyl-glutamyl-glycyl-arginine chloromethyl ketone 126-162 serpin family C member 1 Homo sapiens 55-67 6464516-3 1984 - The sensitivity of the functional AT III test for the recognition of increased heparin tolerances is quite satisfactory, and the test for the answer of this questioning also suitable and more sensitive than the immunological proof method. Heparin 81-88 serpin family C member 1 Homo sapiens 36-42 6724150-0 1984 Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation. Heparin 14-21 serpin family C member 1 Homo sapiens 38-54 6724150-2 1984 The effect of nonenzymatic glycosylation on the biologic function of human antithrombin III was evaluated using a chromogenic thrombin substrate assay in the presence of catalytic amounts of heparin. Heparin 191-198 serpin family C member 1 Homo sapiens 75-91 6724150-4 1984 This glycosylation-induced inhibition of heparin-catalyzed antithrombin III activity was completely reversible by preassay incubation with excess sodium heparin. Heparin 41-48 serpin family C member 1 Homo sapiens 59-75 6724150-4 1984 This glycosylation-induced inhibition of heparin-catalyzed antithrombin III activity was completely reversible by preassay incubation with excess sodium heparin. Heparin 146-160 serpin family C member 1 Homo sapiens 59-75 6426525-0 1984 Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation. Sugars 45-51 serpin family C member 1 Homo sapiens 25-41 6426525-0 1984 Thermal stabilization of antithrombin III by sugars and sugar derivatives and the effects of nonenzymatic glycosylation. Sugars 45-50 serpin family C member 1 Homo sapiens 25-41 6426525-1 1984 A variety of neutral and acidic sugars and related compounds were evaluated in terms of their effect on the midpoint, Td, of the thermal denaturation curve of antithrombin III. Sugars 32-38 serpin family C member 1 Homo sapiens 159-175 6426525-4 1984 Several compounds were shown to be effective in preserving antithrombin III activity during pasteurization for 10 h at 60 degrees C. However, the presence of reducing sugars invariably resulted in a decrease in activity following pasteurization, in spite of their ability to increase Td. Sugars 167-173 serpin family C member 1 Homo sapiens 59-75 6426525-5 1984 In fact, when antithrombin III was pasteurized in the presence of 2 M glucose and 0.5 M citrate, it steadily lost its ability to inhibit thrombin even though Td under these conditions was 10 degrees C higher than in citrate alone where activity was preserved. Glucose 70-77 serpin family C member 1 Homo sapiens 14-30 6426525-5 1984 In fact, when antithrombin III was pasteurized in the presence of 2 M glucose and 0.5 M citrate, it steadily lost its ability to inhibit thrombin even though Td under these conditions was 10 degrees C higher than in citrate alone where activity was preserved. Citric Acid 88-95 serpin family C member 1 Homo sapiens 14-30 6426525-5 1984 In fact, when antithrombin III was pasteurized in the presence of 2 M glucose and 0.5 M citrate, it steadily lost its ability to inhibit thrombin even though Td under these conditions was 10 degrees C higher than in citrate alone where activity was preserved. Citric Acid 216-223 serpin family C member 1 Homo sapiens 14-30 6204398-6 1984 Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel. Heparin 70-77 serpin family C member 1 Homo sapiens 104-116 6204398-6 1984 Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel. Heparin 70-77 serpin family C member 1 Homo sapiens 153-165 6204398-6 1984 Moreover the crossed immunoelectrophoretic pattern in the presence of heparin demonstrated two peaks of antithrombin, the slower one migrating as normal antithrombin when heparin was omitted from the first agarose gel. Heparin 171-178 serpin family C member 1 Homo sapiens 104-116 6204398-7 1984 It was concluded that molecular alteration of the antithrombin molecule seemed to affect only the heparin binding site thus preventing from any rate enhancement of thrombin inactivation. Heparin 98-105 serpin family C member 1 Homo sapiens 50-62 6740566-0 1984 Antithrombin III in patients with acute deep vein thrombosis during heparin treatment (subcutaneous and intravenous) and during and after treatment with oral coumarins. Heparin 68-75 serpin family C member 1 Homo sapiens 0-16 6740566-0 1984 Antithrombin III in patients with acute deep vein thrombosis during heparin treatment (subcutaneous and intravenous) and during and after treatment with oral coumarins. Coumarins 158-167 serpin family C member 1 Homo sapiens 0-16 6740566-4 1984 The AT-III concentration was estimated daily during heparin treatment and repeatedly during the first year. Heparin 52-59 serpin family C member 1 Homo sapiens 4-10 6740566-5 1984 The mean AT-III concentration decreased progressively 25% during 5 days of heparin treatment regardless of whether heparin was given intravenously or subcutaneously. Heparin 75-82 serpin family C member 1 Homo sapiens 9-15 6740566-6 1984 The mean AT-III concentration during coumarin treatment was higher than after coumarin treatment. coumarin 37-45 serpin family C member 1 Homo sapiens 9-15 6740566-6 1984 The mean AT-III concentration during coumarin treatment was higher than after coumarin treatment. coumarin 78-86 serpin family C member 1 Homo sapiens 9-15 6715365-0 1984 Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III. Heparin 15-22 serpin family C member 1 Homo sapiens 87-103 6715365-0 1984 Involvement of heparin chain length in the heparin-catalyzed inhibition of thrombin by antithrombin III. Heparin 43-50 serpin family C member 1 Homo sapiens 87-103 6715365-1 1984 The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200). Heparin 21-28 serpin family C member 1 Homo sapiens 64-80 6715365-1 1984 The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200). Heparin 21-28 serpin family C member 1 Homo sapiens 129-145 6715365-1 1984 The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200). Heparin 172-179 serpin family C member 1 Homo sapiens 64-80 6715365-1 1984 The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200). Heparin 172-179 serpin family C member 1 Homo sapiens 64-80 6715365-1 1984 The mechanism of the heparin-promoted reaction of thrombin with antithrombin III was investigated by using covalent complexes of antithrombin III with either high-affinity heparin (Mr = 15,000) or heparin fragments having an average of 16 and 12 monosaccharide units (Mr = 4,300 and 3,200). Monosaccharides 246-260 serpin family C member 1 Homo sapiens 64-80 6715365-6 1984 Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic. Heparin 75-82 serpin family C member 1 Homo sapiens 58-74 6715365-6 1984 Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic. Heparin 190-197 serpin family C member 1 Homo sapiens 58-74 6715365-6 1984 Active site-blocked thrombin is an antagonist of covalent antithrombin III-heparin complexes: the effect is monophasic and half-maximum at 4 nM of antagonist against the complex with intact heparin, whereas the effect is weaker against complexes with heparin fragments and not monophasic. Heparin 190-197 serpin family C member 1 Homo sapiens 58-74 6715365-7 1984 We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III. Heparin 87-94 serpin family C member 1 Homo sapiens 132-148 6715365-7 1984 We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III. Heparin 87-94 serpin family C member 1 Homo sapiens 355-371 6715365-7 1984 We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III. Heparin 152-159 serpin family C member 1 Homo sapiens 132-148 6715365-7 1984 We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III. Heparin 152-159 serpin family C member 1 Homo sapiens 132-148 6715365-7 1984 We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III. Heparin 152-159 serpin family C member 1 Homo sapiens 132-148 6715365-7 1984 We conclude that virtually all of the activity of high affinity, high molecular weight heparin depends on binding both thrombin and antithrombin III to heparin, and that the exceptionally high activity of heparin results in part from the capacity of thrombin bound nonspecifically to heparin to diffuse in the dimension of the heparin chain towards bound antithrombin III. Heparin 152-159 serpin family C member 1 Homo sapiens 132-148 6237371-3 1984 Isomeric compounds of N alpha-arylsulfonylated amides of omega-amidinophenyl-alpha-aminoalkylcarboxylic acids--N alpha-amidinophenylsulfonylated amides or N alpha-arylsulfonylated amidino anilides of omega-phenyl-alpha-aminoalkylcarboxylic acids, respectively--possess weak antithrombin activity as compared to the derivatives of the basic structure. n alpha-arylsulfonylated amidino anilides 155-196 serpin family C member 1 Homo sapiens 274-286 6729779-5 1984 But the high amount of thrombin needed to obtain a 50% reduction of the circulating AT III required a corresponding high amount of protective heparin. Heparin 142-149 serpin family C member 1 Homo sapiens 84-90 6609435-0 1984 Bleeding tendency possibly related to increased plasma antithrombin III activity in patient treated with piroxicam. Piroxicam 105-114 serpin family C member 1 Homo sapiens 55-71 6740557-1 1984 A preparation of heparin was separated by affinity chromatography into two fractions: one of high ( HAH ) and the other of low (LAH) affinity to antithrombin III. Heparin 17-24 serpin family C member 1 Homo sapiens 145-161 6704544-1 1984 High and low affinity heparin (HA and LA heparin) were prepared from commercial heparin by affinity chromatography to insolubilized antithrombin III. Heparin 22-29 serpin family C member 1 Homo sapiens 132-148 6704544-12 1984 On the basis of these kinetics, we suggest that, after intravenous administration of heparin, the two lipolytic enzymes present in plasma are complexed with heparin, analogous to the heparin-antithrombin III complex. Heparin 85-92 serpin family C member 1 Homo sapiens 191-207 6704544-12 1984 On the basis of these kinetics, we suggest that, after intravenous administration of heparin, the two lipolytic enzymes present in plasma are complexed with heparin, analogous to the heparin-antithrombin III complex. Heparin 157-164 serpin family C member 1 Homo sapiens 191-207 6424998-0 1984 Antithrombin activity of gold sodium thiomalate. Gold Sodium Thiomalate 25-47 serpin family C member 1 Homo sapiens 0-12 6546700-10 1984 Interaction with antithrombin III is slower than normal when followed by SDS gel electrophoresis and inhibition of the amidolytic activity of thrombin on S2238. Sodium Dodecyl Sulfate 73-76 serpin family C member 1 Homo sapiens 17-33 6729779-6 1984 Since the secondary injection of protamin sulphate (after the end of the perfusion with the thrombin-heparin mixture) was precipitating the DIC syndrome, such attempts to decrease AT III in man are not feasible. protamin sulphate 33-50 serpin family C member 1 Homo sapiens 180-186 6721831-7 1984 An octadecasaccharide is therefore the smallest heparin fragment (prepared by nitrous acid depolymerization) that can accelerate thrombin inhibition by antithrombin III. octadecasaccharide 3-21 serpin family C member 1 Homo sapiens 152-168 6739525-4 1984 The greatest antithrombin effect shows N alpha-(2- naphthylsulphonylglycyl )-4- amidinophenylalaninpiperidi d with a Ki-value of 6 X 10(-9) mol/l using S-2238 as a substrate. n alpha-(2- naphthylsulphonylglycyl )-4- amidinophenylalaninpiperidi d 39-109 serpin family C member 1 Homo sapiens 13-25 6739525-4 1984 The greatest antithrombin effect shows N alpha-(2- naphthylsulphonylglycyl )-4- amidinophenylalaninpiperidi d with a Ki-value of 6 X 10(-9) mol/l using S-2238 as a substrate. Sulfur 152-153 serpin family C member 1 Homo sapiens 13-25 6721831-1 1984 Oligosaccharides of well-defined molecular size were prepared from heparin by nitrous acid depolymerization, affinity chromatography on immobilized antithrombin III (see footnote on Nomenclature) and gel chromatography on Sephadex G-50. Oligosaccharides 0-16 serpin family C member 1 Homo sapiens 148-164 6721831-7 1984 An octadecasaccharide is therefore the smallest heparin fragment (prepared by nitrous acid depolymerization) that can accelerate thrombin inhibition by antithrombin III. Heparin 48-55 serpin family C member 1 Homo sapiens 152-168 6721831-2 1984 High affinity (for antithrombin III) octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides were prepared, as well as oligosaccharides of larger size than octadecasaccharide. octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides 37-106 serpin family C member 1 Homo sapiens 19-35 6721831-2 1984 High affinity (for antithrombin III) octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides were prepared, as well as oligosaccharides of larger size than octadecasaccharide. Oligosaccharides 133-149 serpin family C member 1 Homo sapiens 19-35 6721831-10 1984 Such binding results in either steric interference with the formation of antithrombin III-proteinase complexes or in displacement of the antithrombin III molecule from the heparin chain. Heparin 172-179 serpin family C member 1 Homo sapiens 137-153 6721831-2 1984 High affinity (for antithrombin III) octa-, deca-, dodeca-, tetradeca-, hexadeca- and octadeca-saccharides were prepared, as well as oligosaccharides of larger size than octadecasaccharide. octadecasaccharide 170-188 serpin family C member 1 Homo sapiens 19-35 6722255-0 1984 Catalysis of the generation of thrombin-antithrombin complex by insoluble anticoagulant polystyrene derivatives. Polystyrenes 88-99 serpin family C member 1 Homo sapiens 40-52 6721831-3 1984 The inhibition of Factor Xa by antithrombin III was greatly accelerated by all of these oligosaccharides, the specific anti-Factor Xa activity being invariably greater than 1300 units/mumol. Oligosaccharides 88-104 serpin family C member 1 Homo sapiens 31-47 6722255-1 1984 The inhibition of thrombin by antithrombin III is known to be accelerated by heparin through the formation of complexes between the muccopolysaccharide and both proteins. Heparin 77-84 serpin family C member 1 Homo sapiens 30-46 6722255-1 1984 The inhibition of thrombin by antithrombin III is known to be accelerated by heparin through the formation of complexes between the muccopolysaccharide and both proteins. muccopolysaccharide 132-151 serpin family C member 1 Homo sapiens 30-46 6722255-4 1984 The protease-antiprotease complex has an affinity for the polymer surface which is higher than that of antithrombin but lower than that of thrombin. Polymers 58-65 serpin family C member 1 Homo sapiens 103-115 6696918-1 1984 Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene. Carbohydrates 104-116 serpin family C member 1 Homo sapiens 34-50 6747369-1 1984 Heparin anticoagulation during extracorporeal circulation in an antithrombin III deficit patient]. Heparin 0-7 serpin family C member 1 Homo sapiens 64-80 6696918-1 1984 Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene. metaperiodate 155-164 serpin family C member 1 Homo sapiens 34-50 6696918-1 1984 Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene. Fluorescein 217-228 serpin family C member 1 Homo sapiens 34-50 6696918-1 1984 Derivatives of human thrombin and antithrombin III with fluorescent labels covalently attached to their carbohydrate moieties were prepared by reaction of periodate-oxidized proteins with amino derivatives of dansyl, fluorescein and pyrene. pyrene 233-239 serpin family C member 1 Homo sapiens 34-50 6698980-7 1984 Circular dichroism studies showed that the disruption of the first unfolding domain in antithrombin III by low concentration of guanidinium chloride (Villanueva, G. B., and Allen, N. (1983) J. Biol. Guanidine 128-148 serpin family C member 1 Homo sapiens 87-103 6691921-1 1984 Long-term warfarin therapy was changed to subcutaneous heparin to cover a planned pregnancy in a patient with congenital antithrombin III (AT III) deficiency. Warfarin 10-18 serpin family C member 1 Homo sapiens 121-137 6698980-14 1984 A model of the antithrombin III-binding octasaccharide (Lindahl, U., Backstrom, G., Thunberg, L., and Leder, I. G. (1980) Proc. Octasaccharide 40-54 serpin family C member 1 Homo sapiens 15-31 6698980-19 1984 These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III. Lysine 55-61 serpin family C member 1 Homo sapiens 219-235 6698980-19 1984 These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III. Sulfates 144-151 serpin family C member 1 Homo sapiens 219-235 6698980-19 1984 These two models can be positioned such that the three lysine residues in the alpha-helix can be matched for maximal interaction with the three sulfate groups in the octasaccharide demonstrated as essential for binding antithrombin III. Octasaccharide 166-180 serpin family C member 1 Homo sapiens 219-235 6698980-20 1984 Based on these models, it is proposed that the unstable helical segment composed of residues 281-292 is the heparin-binding site in antithrombin III. Heparin 108-115 serpin family C member 1 Homo sapiens 132-148 6422851-5 1984 The products obtained after removal of sugars from antithrombin retained thrombin-neutralizing activity. Sugars 39-45 serpin family C member 1 Homo sapiens 51-63 6422851-7 1984 Thus, the sugar residues of thrombin and antithrombin are not required for the formation of enzyme-inhibitor complexes or for the other activities that were measured. Sugars 10-15 serpin family C member 1 Homo sapiens 41-53 6231919-0 1984 Inhibition by heparin-modulated antithrombin III of amidolysis catalysed by m beta-acrosin. beta-acrosin 78-90 serpin family C member 1 Homo sapiens 32-48 6231919-3 1984 This effect of antithrombin III was potentiated by heparin, and to a modest extent by heparan sulphate, cellulose sulphate, dextran sulphate and xylan sulphate. Heparin 51-58 serpin family C member 1 Homo sapiens 15-31 6231919-3 1984 This effect of antithrombin III was potentiated by heparin, and to a modest extent by heparan sulphate, cellulose sulphate, dextran sulphate and xylan sulphate. Heparitin Sulfate 86-102 serpin family C member 1 Homo sapiens 15-31 6231919-3 1984 This effect of antithrombin III was potentiated by heparin, and to a modest extent by heparan sulphate, cellulose sulphate, dextran sulphate and xylan sulphate. cellulose sulphate 104-122 serpin family C member 1 Homo sapiens 15-31 6231919-3 1984 This effect of antithrombin III was potentiated by heparin, and to a modest extent by heparan sulphate, cellulose sulphate, dextran sulphate and xylan sulphate. Dextran Sulfate 124-140 serpin family C member 1 Homo sapiens 15-31 6231919-3 1984 This effect of antithrombin III was potentiated by heparin, and to a modest extent by heparan sulphate, cellulose sulphate, dextran sulphate and xylan sulphate. xylan sulphate 145-159 serpin family C member 1 Homo sapiens 15-31 6691921-1 1984 Long-term warfarin therapy was changed to subcutaneous heparin to cover a planned pregnancy in a patient with congenital antithrombin III (AT III) deficiency. Heparin 55-62 serpin family C member 1 Homo sapiens 121-137 6232045-0 1984 [Acute effects of sulodexide on the lipid profile and on antithrombin III in patients with chronic renal insufficiency in hemodialysis treatment]. glucuronyl glucosamine glycan sulfate 18-28 serpin family C member 1 Homo sapiens 57-73 6583694-6 1984 We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule. tetrasaccharide 97-112 serpin family C member 1 Homo sapiens 223-235 6583694-6 1984 We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule. n-acetyl glucosamine o6-sulfate 143-174 serpin family C member 1 Homo sapiens 223-235 6719385-1 1984 Interaction of human antithrombin III (AT III) with human alpha-thrombin coupled to Sepharose 4B was investigated. Sepharose 84-93 serpin family C member 1 Homo sapiens 21-37 6719385-1 1984 Interaction of human antithrombin III (AT III) with human alpha-thrombin coupled to Sepharose 4B was investigated. Sepharose 84-93 serpin family C member 1 Homo sapiens 39-45 6719385-7 1984 However, Sepharose-coupled thrombin mixed with plasma in the presence of heparin produced outstanding quantities of residual immunoreactive AT III devoid of inhibitory activity. Sepharose 9-18 serpin family C member 1 Homo sapiens 140-146 6719385-7 1984 However, Sepharose-coupled thrombin mixed with plasma in the presence of heparin produced outstanding quantities of residual immunoreactive AT III devoid of inhibitory activity. Heparin 73-80 serpin family C member 1 Homo sapiens 140-146 6583694-0 1984 Evaluation of critical groups required for the binding of heparin to antithrombin. Heparin 58-65 serpin family C member 1 Homo sapiens 69-81 6583694-1 1984 We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin. Monosaccharides 56-70 serpin family C member 1 Homo sapiens 183-195 6583694-1 1984 We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin. Octasaccharide 86-100 serpin family C member 1 Homo sapiens 183-195 6583694-1 1984 We have examined the quantitative importance of various monosaccharide residues of an octasaccharide domain of heparin that are responsible for the binding of this oligosaccharide to antithrombin. Oligosaccharides 164-179 serpin family C member 1 Homo sapiens 183-195 6583694-2 1984 Different fragments of the octasaccharide were prepared by enzymatic digestion and the avidities of these oligosaccharides for antithrombin were determined by equilibrium dialysis. Octasaccharide 27-41 serpin family C member 1 Homo sapiens 127-139 6693405-2 1984 Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol. Tryptophan 34-44 serpin family C member 1 Homo sapiens 56-72 6583694-2 1984 Different fragments of the octasaccharide were prepared by enzymatic digestion and the avidities of these oligosaccharides for antithrombin were determined by equilibrium dialysis. Oligosaccharides 106-122 serpin family C member 1 Homo sapiens 127-139 6583694-6 1984 We suggest that the lack of sulfation of the two uronic acid moieties within the nonreducing-end tetrasaccharide may be required to permit the N-acetyl glucosamine O6-sulfate group to interact with a specific region on the antithrombin molecule. Uronic Acids 49-60 serpin family C member 1 Homo sapiens 223-235 6420409-0 1984 Pyridoxylation of essential lysines in the heparin-binding site of antithrombin III. Lysine 28-35 serpin family C member 1 Homo sapiens 67-83 6420409-0 1984 Pyridoxylation of essential lysines in the heparin-binding site of antithrombin III. Heparin 43-50 serpin family C member 1 Homo sapiens 67-83 6420409-3 1984 A maximum of 3-4 pyridoxal 5"-phosphate groups per antithrombin molecule are bound at high concentrations of pyridoxal 5"-phosphate. 4 pyridoxal 5"-phosphate 15-39 serpin family C member 1 Homo sapiens 51-63 6420409-3 1984 A maximum of 3-4 pyridoxal 5"-phosphate groups per antithrombin molecule are bound at high concentrations of pyridoxal 5"-phosphate. Pyridoxal Phosphate 17-39 serpin family C member 1 Homo sapiens 51-63 6693405-2 1984 Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol. dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium 78-128 serpin family C member 1 Homo sapiens 56-72 6420409-5 1984 Modification in the presence of added heparin decreased the extent of labeling by 1-2 mol of pyridoxyl phosphate per mol of antithrombin and protected against the loss of heparin cofactor activity. Heparin 38-45 serpin family C member 1 Homo sapiens 124-136 6420409-5 1984 Modification in the presence of added heparin decreased the extent of labeling by 1-2 mol of pyridoxyl phosphate per mol of antithrombin and protected against the loss of heparin cofactor activity. Pyridoxal Phosphate 93-112 serpin family C member 1 Homo sapiens 124-136 6693405-2 1984 Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol. Heparin 136-143 serpin family C member 1 Homo sapiens 56-72 6420409-6 1984 To further examine the role of lysine residues in the interaction of antithrombin III with heparin, the protein was singly labeled with pyridoxyl phosphate and affinity fractionated on heparin-agarose. Lysine 31-37 serpin family C member 1 Homo sapiens 69-85 6420409-6 1984 To further examine the role of lysine residues in the interaction of antithrombin III with heparin, the protein was singly labeled with pyridoxyl phosphate and affinity fractionated on heparin-agarose. Heparin 91-98 serpin family C member 1 Homo sapiens 69-85 6693405-2 1984 Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol. Heparin 160-167 serpin family C member 1 Homo sapiens 56-72 6420409-10 1984 Fluorescence emission spectra of the phosphopyridoxyl-antithrombin derivative that does not bind to heparin-agarose indicated fluorescence energy transfer from tryptophan to the bound phosphopyridoxyl moiety. phosphopyridoxyl 37-53 serpin family C member 1 Homo sapiens 54-66 6420409-1 1984 Pyridoxal 5"-phosphate was used to selectively modify lysine residues on antithrombin III. Pyridoxal Phosphate 0-22 serpin family C member 1 Homo sapiens 73-89 6420409-10 1984 Fluorescence emission spectra of the phosphopyridoxyl-antithrombin derivative that does not bind to heparin-agarose indicated fluorescence energy transfer from tryptophan to the bound phosphopyridoxyl moiety. Heparin 100-107 serpin family C member 1 Homo sapiens 54-66 6693405-2 1984 Chemical modification of a single tryptophan residue in antithrombin III with dimethyl(2-hydroxy-5-nitrobenzyl)sulfonium bromide blocks heparin binding and the heparin-enhanced inhibition of thrombin without altering the heparin-independent rate of thrombin inhibition (Blackburn, M. N., and Sibley, C. C. (1980) J. Biol. Heparin 160-167 serpin family C member 1 Homo sapiens 56-72 6420409-10 1984 Fluorescence emission spectra of the phosphopyridoxyl-antithrombin derivative that does not bind to heparin-agarose indicated fluorescence energy transfer from tryptophan to the bound phosphopyridoxyl moiety. Tryptophan 160-170 serpin family C member 1 Homo sapiens 54-66 6420409-1 1984 Pyridoxal 5"-phosphate was used to selectively modify lysine residues on antithrombin III. Lysine 54-60 serpin family C member 1 Homo sapiens 73-89 6420409-2 1984 Pyridoxal 5"-phosphate was incubated with antithrombin, and the Schiff base was reduced with sodium borohydride. Pyridoxal Phosphate 0-22 serpin family C member 1 Homo sapiens 42-54 6693405-8 1984 The site of labeling corresponds to Trp 49, which is located within the disulfide-stabilized loops near the NH2-terminal end of the antithrombin III molecule. Tryptophan 36-39 serpin family C member 1 Homo sapiens 132-148 6420409-10 1984 Fluorescence emission spectra of the phosphopyridoxyl-antithrombin derivative that does not bind to heparin-agarose indicated fluorescence energy transfer from tryptophan to the bound phosphopyridoxyl moiety. phosphopyridoxyl 184-200 serpin family C member 1 Homo sapiens 54-66 6420409-13 1984 255, 824-826) in the heparin-binding domain of antithrombin III. Heparin 21-28 serpin family C member 1 Homo sapiens 47-63 6693405-8 1984 The site of labeling corresponds to Trp 49, which is located within the disulfide-stabilized loops near the NH2-terminal end of the antithrombin III molecule. Disulfides 72-81 serpin family C member 1 Homo sapiens 132-148 6731952-0 1984 [Automatization of heparin determination using chronometric evaluation of anti-Xa activity of the AT III-heparin complex]. Heparin 19-26 serpin family C member 1 Homo sapiens 98-104 6208738-14 1984 This is the first AT III abnormality to show an abnormal crossed-immunoelectrophoresis in the absence of heparin. Heparin 105-112 serpin family C member 1 Homo sapiens 18-24 6731952-0 1984 [Automatization of heparin determination using chronometric evaluation of anti-Xa activity of the AT III-heparin complex]. Heparin 105-112 serpin family C member 1 Homo sapiens 98-104 6083907-4 1984 In acquired AT III defects the anticoagulant activity of heparin is not necessarily decreased. Heparin 57-64 serpin family C member 1 Homo sapiens 12-18 6233149-3 1984 A significant decrease in antithrombin III (AT-III) activity of 27% (range 7-46%) was found in patients on an initially high-dose estrogen (diethylstilbestrol) treatment regime. Diethylstilbestrol 140-158 serpin family C member 1 Homo sapiens 26-42 6233149-3 1984 A significant decrease in antithrombin III (AT-III) activity of 27% (range 7-46%) was found in patients on an initially high-dose estrogen (diethylstilbestrol) treatment regime. Diethylstilbestrol 140-158 serpin family C member 1 Homo sapiens 44-50 6083907-5 1984 After continuous infusion of doses below 500 USP in patients with DICFS and after administration of heparin doses of 750 USP/h/70 kg in patients undergoing fibrinolytic therapy the AT III content rather increases continuously. Heparin 100-107 serpin family C member 1 Homo sapiens 181-187 6083957-1 1984 In a trial involving 61 patients suffering from shock and DIC, the relations between the concentration of heparin, the effect of heparin on coagulation and the activity of AT III were studied. Heparin 106-113 serpin family C member 1 Homo sapiens 172-178 6083957-2 1984 The effect of heparin decreased to one-half when the activity of AT III was 75 per cent of the average normal level. Heparin 14-21 serpin family C member 1 Homo sapiens 65-71 6083907-6 1984 After extremely high heparin doses during extracorporeal circulation in the heart-lung machine transitorily decreased AT III values return to normal. Heparin 21-28 serpin family C member 1 Homo sapiens 118-124 6083907-7 1984 In certain risk situations, however, such as after bolus injection of comparatively high heparin doses in patients with greatly reduced AT III values, a lowered anticoagulant effect of high heparin doses must be expected. Heparin 89-96 serpin family C member 1 Homo sapiens 136-142 6083907-7 1984 In certain risk situations, however, such as after bolus injection of comparatively high heparin doses in patients with greatly reduced AT III values, a lowered anticoagulant effect of high heparin doses must be expected. Heparin 190-197 serpin family C member 1 Homo sapiens 136-142 6083907-9 1984 However, when enhanced heparin resistance is suspected or diagnosed, treatment with AT III concentrates is justified only when the diagnosis is based on laboratory findings. Heparin 23-30 serpin family C member 1 Homo sapiens 84-90 6083907-10 1984 Cortisone and protamine chloride were found to exert direct effects on AT III function and concentration independent of the AT III defects mentioned. Cortisone 0-9 serpin family C member 1 Homo sapiens 71-77 6724355-3 1984 This type of AT-III deficiency (type 1) was later divided into type 1a and 1b on the basis of the heparin affinity of the AT-III molecule. Heparin 98-105 serpin family C member 1 Homo sapiens 13-19 6735277-8 1984 The extra antithrombin III that is added in the assays had to be freed of heparin neutralising activity to obtain reliable estimates of the heparin concentration in the low range (0-200 U/l). Heparin 140-147 serpin family C member 1 Homo sapiens 10-26 6724356-5 1984 There are several types of AT-III defect; they are characterized by a decrease in amount and function, a functional decrease, or a pathological heparin-binding. Heparin 144-151 serpin family C member 1 Homo sapiens 27-33 6582486-2 1984 Abnormal antithrombin III was reduced, S-pyridylethylated, and treated with cyanogen bromide. Cyanogen Bromide 76-92 serpin family C member 1 Homo sapiens 9-25 6334690-2 1984 In vitro hepatocyte-uptake studies with antithrombin III-proteinase complexes confirmed the hepatocyte uptake and degradation of these complexes, and demonstrated the formation of a disulfide interchange product between the ligand and a cellular protein. Disulfides 182-191 serpin family C member 1 Homo sapiens 40-56 6382162-2 1984 There is now considerable evidence that the antithrombotic and the hemorrhagic effects of heparin can be dissociated by using low molecular weight heparins, and heparinoids, and by using heparin with low affinity to AT III. Heparin 90-97 serpin family C member 1 Homo sapiens 216-222 6473093-1 1984 In order to investigate the specificity of heparin-antithrombin binding and to precisely define the nature of the structural requirements in heparin, we have synthesized several oligosaccharides and have assessed their affinity for antithrombin. Heparin 43-50 serpin family C member 1 Homo sapiens 51-63 6473093-1 1984 In order to investigate the specificity of heparin-antithrombin binding and to precisely define the nature of the structural requirements in heparin, we have synthesized several oligosaccharides and have assessed their affinity for antithrombin. Oligosaccharides 178-194 serpin family C member 1 Homo sapiens 232-244 6582486-0 1984 Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Heparin 115-122 serpin family C member 1 Homo sapiens 0-16 6582486-0 1984 Antithrombin III Toyama: replacement of arginine-47 by cysteine in hereditary abnormal antithrombin III that lacks heparin-binding ability. Heparin 115-122 serpin family C member 1 Homo sapiens 87-103 6442908-6 1984 Abnormality of AT-III was also found in heparin-binding studies. Heparin 40-47 serpin family C member 1 Homo sapiens 15-21 6198531-8 1984 The therapeutic effects of heparin were assessed by prolonged APTT (45-250 sec) and elevated Anti-FXa activity (0.2-1.2 u/ml of plasma heparin concentration) as an indicator for the evaluation of anticoagulation activity and by normalized FPA, Fbg, FDP, Plg and AT III as an indicator for evaluation of antithrombolic activity. Heparin 27-34 serpin family C member 1 Homo sapiens 262-268 6718507-0 1984 [Clinical problems posed by the consumption of antithrombin III induced by heparin]. Heparin 75-82 serpin family C member 1 Homo sapiens 47-63 6718507-1 1984 Two cases of resistance to the heparin treatment, induced by large consumption of antithrombin III, are reported. Heparin 31-38 serpin family C member 1 Homo sapiens 82-98 6718507-2 1984 Normally small, this consumption does not automatically call for the systematic dosage of Antithrombin III for each treatment using heparin. Heparin 132-139 serpin family C member 1 Homo sapiens 90-106 6718507-3 1984 On the other hand, any clinical or biological resistance to higher doses of heparin, any personal or family history of thrombosis necessitate the administration of Antithrombin III. Heparin 76-83 serpin family C member 1 Homo sapiens 164-180 6582486-6 1984 Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama. Arginine 72-80 serpin family C member 1 Homo sapiens 94-110 6582486-6 1984 Amino acid sequence analysis of the abnormal peptide indicated that the arginine-47 of normal antithrombin III had been replaced by cysteine in antithrombin III Toyama. Arginine 72-80 serpin family C member 1 Homo sapiens 94-106 6643505-0 1983 A simple rate law that describes the kinetics of the heparin-catalyzed reaction between antithrombin III and thrombin. Heparin 53-60 serpin family C member 1 Homo sapiens 88-104 6198746-11 1983 We conclude that plasma contains a component(s) which displaces (thrombin-antithrombin-III) complex from immobilised heparin: presumably this leaves the heparin sites free for further use in enzyme inactivation. Heparin 117-124 serpin family C member 1 Homo sapiens 74-90 6198746-11 1983 We conclude that plasma contains a component(s) which displaces (thrombin-antithrombin-III) complex from immobilised heparin: presumably this leaves the heparin sites free for further use in enzyme inactivation. Heparin 153-160 serpin family C member 1 Homo sapiens 74-90 6516292-1 1984 A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS). Heparin 170-177 serpin family C member 1 Homo sapiens 73-89 6516292-1 1984 A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS). Heparin 170-177 serpin family C member 1 Homo sapiens 91-97 6516292-1 1984 A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS). Sepharose 178-187 serpin family C member 1 Homo sapiens 73-89 6516292-1 1984 A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS). Sepharose 178-187 serpin family C member 1 Homo sapiens 91-97 6516292-1 1984 A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS). heparin-sepharose 189-191 serpin family C member 1 Homo sapiens 73-89 6516292-1 1984 A single-step method is described for the isolation of a highly purified antithrombin III (AT III) concentrate at a recovery of over 30% using affinity chromatography on heparin-Sepharose (HS). heparin-sepharose 189-191 serpin family C member 1 Homo sapiens 91-97 6516292-3 1984 Pasteurization of the AT III concentrate in the presence of 0.5 M sodium citrate to minimize the risk of hepatitis decreases the recovery by about 20% and induces changes in the patterns obtained by polyacrylamide gel electrophoresis and by crossed immunoelectrophoresis in heparinized agarose gel. Sodium Citrate 66-80 serpin family C member 1 Homo sapiens 22-28 6516292-3 1984 Pasteurization of the AT III concentrate in the presence of 0.5 M sodium citrate to minimize the risk of hepatitis decreases the recovery by about 20% and induces changes in the patterns obtained by polyacrylamide gel electrophoresis and by crossed immunoelectrophoresis in heparinized agarose gel. polyacrylamide 199-213 serpin family C member 1 Homo sapiens 22-28 6516292-3 1984 Pasteurization of the AT III concentrate in the presence of 0.5 M sodium citrate to minimize the risk of hepatitis decreases the recovery by about 20% and induces changes in the patterns obtained by polyacrylamide gel electrophoresis and by crossed immunoelectrophoresis in heparinized agarose gel. Sepharose 286-293 serpin family C member 1 Homo sapiens 22-28 6643505-1 1983 The kinetics of the reaction between human thrombin and antithrombin III were studied in the presence of heparin fractionated according to its molecular size and affinity for antithrombin III. Heparin 105-112 serpin family C member 1 Homo sapiens 56-72 6643505-1 1983 The kinetics of the reaction between human thrombin and antithrombin III were studied in the presence of heparin fractionated according to its molecular size and affinity for antithrombin III. Heparin 105-112 serpin family C member 1 Homo sapiens 175-191 6643505-2 1983 Reactions were monitored continuously through the loss of fluorescence intensity accompanying the displacement of the reversible inhibitor dansylarginine-N-(3-ethyl-1,5-pentanediyl)amide from thrombin upon its interaction with antithrombin III. dansylarginine N-(3-ethyl-1,5-pentanediyl)amide 139-186 serpin family C member 1 Homo sapiens 227-243 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 20-27 serpin family C member 1 Homo sapiens 269-285 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 20-27 serpin family C member 1 Homo sapiens 388-404 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 269-285 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 388-404 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 269-285 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 388-404 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 269-285 6640109-0 1983 Antithrombin "Chicago": a functionally abnormal molecule with increased heparin affinity causing familial thrombophilia. Heparin 72-79 serpin family C member 1 Homo sapiens 0-12 6640109-7 1983 The abnormal antithrombin ("Chicago") was found to elute from heparin-Sepharose at a higher ionic strength than normal inhibitor. Heparin 62-69 serpin family C member 1 Homo sapiens 13-25 6643505-7 1983 The kinetics of the heparin-catalyzed reaction measured over an appreciable range of protein and heparin concentrations could be rationalized well by the simple rate equation, v = k X fa X fb X [H]t, where k is an intrinsic rate constant for the reaction between bound antithrombin III and thrombin, fa and fb are, respectively, the fractional saturation of available sites on heparin by antithrombin III and thrombin, and [H]t is the total concentration of heparin. Heparin 97-104 serpin family C member 1 Homo sapiens 388-404 6640109-7 1983 The abnormal antithrombin ("Chicago") was found to elute from heparin-Sepharose at a higher ionic strength than normal inhibitor. Sepharose 70-79 serpin family C member 1 Homo sapiens 13-25 6643466-2 1983 The presence of two unfolding domains in antithrombin III during its denaturation in guanidinium chloride has previously been reported (Villanueva, G. B., and Allen, N. (1983) J. Biol. Guanidine 85-105 serpin family C member 1 Homo sapiens 41-57 6640109-8 1983 The functionally defective antithrombin molecules exhibit a reduced ability to neutralize thrombin in the presence or absence of heparin (approximately 10%-20% of normal). Heparin 129-136 serpin family C member 1 Homo sapiens 27-39 6643466-12 1983 On the basis of these data, the binding of heparin to antithrombin III is interpreted in terms of a two-step mechanism. Heparin 43-50 serpin family C member 1 Homo sapiens 54-70 6607710-0 1983 Antithrombin in vertebrate species: conservation of the heparin-dependent anticoagulant mechanism. Heparin 56-63 serpin family C member 1 Homo sapiens 0-12 6607710-1 1983 Heparin is thought to regulate the rate of mammalian blood clotting by enhancing the activity of antithrombin, an inhibitor of coagulation enzymes. Heparin 0-7 serpin family C member 1 Homo sapiens 97-109 6607710-3 1983 In each case, an inhibitor with remarkably similar properties to human antithrombin was isolated by affinity chromatography on immobilized porcine heparin. porcine heparin 139-154 serpin family C member 1 Homo sapiens 71-83 6607710-4 1983 The purified vertebrate inhibitors all show the following physical and functional homologies to human antithrombin: (i) heparin-enhanced inhibition of both bovine thrombin and human Factor Xa, (ii) molecular masses of approximately 60,000, and (iii) heparin-induced increases in ultraviolet fluorescence. Heparin 120-127 serpin family C member 1 Homo sapiens 102-114 6607710-4 1983 The purified vertebrate inhibitors all show the following physical and functional homologies to human antithrombin: (i) heparin-enhanced inhibition of both bovine thrombin and human Factor Xa, (ii) molecular masses of approximately 60,000, and (iii) heparin-induced increases in ultraviolet fluorescence. Heparin 250-257 serpin family C member 1 Homo sapiens 102-114 6607710-5 1983 Also, the heparin-binding interaction of vertebrate antithrombins is highly selective with each demonstrating the same rigid specificity for heparin species fractionated on the basis of their affinity for human antithrombin. Heparin 10-17 serpin family C member 1 Homo sapiens 52-64 6607710-5 1983 Also, the heparin-binding interaction of vertebrate antithrombins is highly selective with each demonstrating the same rigid specificity for heparin species fractionated on the basis of their affinity for human antithrombin. Heparin 141-148 serpin family C member 1 Homo sapiens 52-64 6643466-11 1983 However, the tryptophan-ascribed fluorescence enhancement and absorption difference spectrum which occur when heparin binds to antithrombin III are reduced by 70%. Tryptophan 13-23 serpin family C member 1 Homo sapiens 127-143 6643466-11 1983 However, the tryptophan-ascribed fluorescence enhancement and absorption difference spectrum which occur when heparin binds to antithrombin III are reduced by 70%. Heparin 110-117 serpin family C member 1 Homo sapiens 127-143 6640057-0 1983 Affinity of purified thrombin or antithrombin III for two insoluble anticoagulant polystyrene derivatives: I. Polystyrenes 82-93 serpin family C member 1 Homo sapiens 33-49 6194790-5 1983 In the presence of saturating concentrations of ATIII and heparin, an apparent first-order rate constant of 6.8 X 10(-1) s-1 was calculated for the inhibition of urokinase. Heparin 58-65 serpin family C member 1 Homo sapiens 48-53 6195981-4 1983 Both groups exhibited below normal antithrombin III and plasminogen levels, with significantly lower antithrombin III levels noted in the HES group postoperatively (41.9 +/- 11.8% versus 56.6 +/- 9.9%; p = 0.006). Hydroxyethyl Starch Derivatives 138-141 serpin family C member 1 Homo sapiens 101-117 6651824-3 1983 In contrast, the synthetic pentasaccharide strongly binds to AT-III (Ka: 7.10(6)M-1) forming an equimolar complex and also enhances the AT-III inhibitory activity towards factor Xa. pentasaccharide 27-42 serpin family C member 1 Homo sapiens 61-67 6651824-3 1983 In contrast, the synthetic pentasaccharide strongly binds to AT-III (Ka: 7.10(6)M-1) forming an equimolar complex and also enhances the AT-III inhibitory activity towards factor Xa. pentasaccharide 27-42 serpin family C member 1 Homo sapiens 136-142 6651824-4 1983 These results confirm that the synthetic pentasaccharide with the above structure corresponds to the actual minimal sequence required in heparin for binding to AT-III. pentasaccharide 41-56 serpin family C member 1 Homo sapiens 160-166 6651824-4 1983 These results confirm that the synthetic pentasaccharide with the above structure corresponds to the actual minimal sequence required in heparin for binding to AT-III. Heparin 137-144 serpin family C member 1 Homo sapiens 160-166 6640057-3 1983 In order to ascertain the heparin-like mechanism of this activity we have studied the interactions of thrombin and antithrombin III with two polymers of this series: sulphonated polystyrene and sulphonate-glutamic acid sulphonamide polystyrene. Heparin 26-33 serpin family C member 1 Homo sapiens 115-131 6885810-0 1983 Demonstration of a two-domain structure of antithrombin III during its denaturation in guanidinium chloride. Guanidine 87-107 serpin family C member 1 Homo sapiens 43-59 6192845-1 1983 The inactivation of human coagulation factor Xa by the plasma proteinase inhibitors alpha 1-antitrypsin, antithrombin III and alpha 2-macroglobulin in purified systems was found to be accelerated by the divalent cations Ca2+, Mn2+ and Mg2+. Manganese(2+) 226-230 serpin family C member 1 Homo sapiens 105-121 6192845-1 1983 The inactivation of human coagulation factor Xa by the plasma proteinase inhibitors alpha 1-antitrypsin, antithrombin III and alpha 2-macroglobulin in purified systems was found to be accelerated by the divalent cations Ca2+, Mn2+ and Mg2+. magnesium ion 235-239 serpin family C member 1 Homo sapiens 105-121 6192845-2 1983 The rate constant for the inhibition of factor Xa by antithrombin III rose from 2.62 X 10(4) M-1 X min-1 in the absence of divalent cations to a maximum of 6.40 X 10(4) M-1 X min-1 at 5 mM Ca2+, 8.10 X 10(4) M-1 X min-1 at 5 mM Mn2+, with a slight decrease in rate at higher cation concentrations. Manganese(2+) 228-232 serpin family C member 1 Homo sapiens 53-69 6604220-7 1983 The independence of the new thrombin inhibitor from heparin control explains the bleeding disorder; it also indicates that heparin normally acts directly on antithrombin III, revealing its inherent inhibitory activity. Heparin 123-130 serpin family C member 1 Homo sapiens 157-173 6885810-1 1983 The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy. Urea 46-50 serpin family C member 1 Homo sapiens 26-42 6885810-1 1983 The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy. Guanidine 55-75 serpin family C member 1 Homo sapiens 26-42 6885810-1 1983 The denaturation of human antithrombin III in urea and guanidinium chloride (GdmCl) was investigated by intrinsic fluorescence, circular dichroism, and absorption difference spectroscopy. Guanidine 77-82 serpin family C member 1 Homo sapiens 26-42 6882687-4 1983 These results confirm previous findings of heterogeneity in At III concentrates and show that some concentrates contain substantial amounts of altered At III molecules in which the heparin-binding site has been denatured but the thrombin-neutralizing site left largely intact. Heparin 181-188 serpin family C member 1 Homo sapiens 151-157 6625618-0 1983 Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin. Calcium 0-7 serpin family C member 1 Homo sapiens 39-55 6625618-0 1983 Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin. Heparin 21-28 serpin family C member 1 Homo sapiens 39-55 6625618-0 1983 Calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction by decreasing the apparent binding affinity of heparin for thrombin. Heparin 121-128 serpin family C member 1 Homo sapiens 39-55 6625618-1 1983 The present study has shown that calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction. Calcium 33-40 serpin family C member 1 Homo sapiens 72-88 6625618-1 1983 The present study has shown that calcium inhibits the heparin-catalyzed antithrombin III/thrombin reaction. Heparin 54-61 serpin family C member 1 Homo sapiens 72-88 6625618-2 1983 The initial rate of thrombin (4.0 nM) inhibition by antithrombin III (200 nM) in the presence of heparin (2.5 ng/ml) decreased from 3.6 nM/min (in the absence of calcium) to 0.12 nM/min in the presence of 10 mM calcium. Heparin 97-104 serpin family C member 1 Homo sapiens 52-68 6625618-2 1983 The initial rate of thrombin (4.0 nM) inhibition by antithrombin III (200 nM) in the presence of heparin (2.5 ng/ml) decreased from 3.6 nM/min (in the absence of calcium) to 0.12 nM/min in the presence of 10 mM calcium. Calcium 211-218 serpin family C member 1 Homo sapiens 52-68 6577437-6 1983 The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and heparin cofactor II/thrombin reactions differed in terms of apparent Vmax and apparent heparin-inhibitor dissociation constant values. Heparin 31-38 serpin family C member 1 Homo sapiens 49-65 6625618-4 1983 The heparin-catalyzed antithrombin III/thrombin reaction is described by the general rate equation for a random-order, bireactant, enzyme-catalyzed reaction (M. J. Griffith (1982) J. Biol. Heparin 4-11 serpin family C member 1 Homo sapiens 22-38 6625618-8 1983 The apparent kinetic parameters for the heparin-catalyzed antithrombin III/thrombin reaction were determined in the presence and absence of calcium. Heparin 40-47 serpin family C member 1 Homo sapiens 58-74 6625618-8 1983 The apparent kinetic parameters for the heparin-catalyzed antithrombin III/thrombin reaction were determined in the presence and absence of calcium. Calcium 140-147 serpin family C member 1 Homo sapiens 58-74 6328252-9 1983 It is difficult to determine the optimal dose of heparin because of decreased antithrombin III and metabolism in the liver due to loss of hepatic parenchyma. Heparin 49-56 serpin family C member 1 Homo sapiens 78-94 6577437-4 1983 The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and antithrombin III/factor Xa reactions differed in terms of apparent maximum velocity (Vmax) and apparent heparin-protease dissociation constant values. Heparin 31-38 serpin family C member 1 Homo sapiens 49-65 6577437-4 1983 The kinetic parameters for the heparin-catalyzed antithrombin III/thrombin and antithrombin III/factor Xa reactions differed in terms of apparent maximum velocity (Vmax) and apparent heparin-protease dissociation constant values. Heparin 31-38 serpin family C member 1 Homo sapiens 79-95 6615439-0 1983 Properties of antithrombin-thrombin complex formed in the presence and in the absence of heparin. Heparin 89-96 serpin family C member 1 Homo sapiens 14-26 6415849-0 1983 Interaction of heparin with histidine-rich glycoprotein and with antithrombin III. Heparin 15-22 serpin family C member 1 Homo sapiens 65-81 6415849-1 1983 The interaction between heparin, histidine-rich glycoprotein and antithrombin III was studied in purified systems. Heparin 24-31 serpin family C member 1 Homo sapiens 65-81 6415849-2 1983 Histidine-rich glycoprotein binds heparin and thereby interferes with its interaction with antithrombin III, resulting in neutralization of the anticoagulant activity. Heparin 34-41 serpin family C member 1 Homo sapiens 91-107 6415849-3 1983 This interaction occurs with clinical grade heparin as well as with high affinity (for antithrombin III) heparin and with a high affinity heparin fragment with Mr 4,300. Heparin 105-112 serpin family C member 1 Homo sapiens 87-103 6410910-1 1983 Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage. polyethylene glycol 400 63-86 serpin family C member 1 Homo sapiens 0-16 6410910-1 1983 Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage. polyethylene glycol 400 63-86 serpin family C member 1 Homo sapiens 18-24 6410910-1 1983 Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage. polyethylene glycol 400 88-91 serpin family C member 1 Homo sapiens 0-16 6410910-1 1983 Antithrombin III (AT III) was isolated by two procedures using polyethylene glycol-400 (PEG) precipitation as the first stage. polyethylene glycol 400 88-91 serpin family C member 1 Homo sapiens 18-24 6410910-2 1983 The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated. polyethylene glycol 400 4-7 serpin family C member 1 Homo sapiens 91-97 6410910-2 1983 The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated. polyethylene glycol 400 4-7 serpin family C member 1 Homo sapiens 116-122 6410910-2 1983 The PEG supernatant (PEG-sup) was applied to a heparin-affinity chromatographic system and AT III-heparin cofactor (AT III-HCF) was isolated. peg-sup 21-28 serpin family C member 1 Homo sapiens 91-97 6410910-8 1983 They differed, however, in that the PEG-sup and AT III-HCF demonstrated considerably reduced progressive antithrombin function assessed over 30 min. polyethylene glycol 400 36-39 serpin family C member 1 Homo sapiens 105-117 6410910-10 1983 AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump. Heparin 72-79 serpin family C member 1 Homo sapiens 0-6 6410910-10 1983 AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump. sephacryl 92-101 serpin family C member 1 Homo sapiens 0-6 6410910-10 1983 AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump. Heparin 106-113 serpin family C member 1 Homo sapiens 0-6 6410910-10 1983 AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump. sephacryl 173-182 serpin family C member 1 Homo sapiens 0-6 6410910-10 1983 AT III two-dimensional immunoelectrophoresis (2-DIE) in the presence of heparin of both the Sephacryl and heparin-affinity purified components were very different, with the Sephacryl-purified AT III AGN showing both a fast peak and a very prominent slow-moving hump. sephacryl 173-182 serpin family C member 1 Homo sapiens 192-198 6410910-11 1983 The AT III heparin affinity fraction showed primarily a fast component. Heparin 11-18 serpin family C member 1 Homo sapiens 4-10 6889048-1 1983 In 34 girls who were treated with large doses of ethinylestradiol because of expected excessive tall stature, antithrombin activity in the blood was followed before, during, and after treatment. Ethinyl Estradiol 49-65 serpin family C member 1 Homo sapiens 110-122 6136676-0 1983 Effect of stanozolol on antithrombin III and protein C. Stanozolol 10-20 serpin family C member 1 Homo sapiens 24-40 6885772-0 1983 The antithrombin-binding sequence in heparin. Heparin 37-44 serpin family C member 1 Homo sapiens 4-16 6885772-2 1983 An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit. Octasaccharide 3-17 serpin family C member 1 Homo sapiens 41-53 6885772-2 1983 An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit. l-iduronosyl-n-acetylglucosaminyl-6-o-sulfate 143-188 serpin family C member 1 Homo sapiens 41-53 6885772-2 1983 An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin, was previously found to have an L-iduronosyl-N-acetylglucosaminyl-6-O-sulfate nonreducing terminal disaccharide unit. Disaccharides 210-222 serpin family C member 1 Homo sapiens 41-53 6885772-3 1983 After digestion of this octasaccharide with alpha-L-iduronidase and N-acetylglucosamine-6-sulfate sulfatase, two fractions, with high and low affinity for antithrombin, respectively, were isolated by affinity chromatography on antithrombin-Sepharose. Octasaccharide 24-38 serpin family C member 1 Homo sapiens 155-167 6885772-3 1983 After digestion of this octasaccharide with alpha-L-iduronidase and N-acetylglucosamine-6-sulfate sulfatase, two fractions, with high and low affinity for antithrombin, respectively, were isolated by affinity chromatography on antithrombin-Sepharose. Sepharose 240-249 serpin family C member 1 Homo sapiens 155-167 6885772-6 1983 This less degraded heptasaccharide retained high affinity for antithrombin. Xyloglucan Heptasaccharide 19-34 serpin family C member 1 Homo sapiens 62-74 6885772-7 1983 It is concluded that the 6-sulfate group on the N-acetylglucosamine residue is of critical importance to the interaction between heparin and antithrombin. Sulfates 27-34 serpin family C member 1 Homo sapiens 141-153 6885772-7 1983 It is concluded that the 6-sulfate group on the N-acetylglucosamine residue is of critical importance to the interaction between heparin and antithrombin. Acetylglucosamine 48-67 serpin family C member 1 Homo sapiens 141-153 6885772-7 1983 It is concluded that the 6-sulfate group on the N-acetylglucosamine residue is of critical importance to the interaction between heparin and antithrombin. Heparin 129-136 serpin family C member 1 Homo sapiens 141-153 6603874-3 1983 As a result of fractionation of products on the column with DEAE-Sephadex A-50, some fractions that have thrombin amidase activity (splitting of the substrate S-2238) and high antithrombin activity were obtained. DEAE-Sephadex A-50 60-78 serpin family C member 1 Homo sapiens 176-188 6615439-7 1983 The similar properties of antithrombin-thrombin complexes formed with or without heparin support the concept of a catalytic role for the polysaccharide in the antithrombin-thrombin reaction. Heparin 81-88 serpin family C member 1 Homo sapiens 159-171 6410910-13 1983 On the basis of these observations, it is postulated that AT III purified by PEG precipitation is in an aggregated form and that aggregate formation and dissolution is associated with AT III progressive activity. polyethylene glycol 400 77-80 serpin family C member 1 Homo sapiens 58-64 6615439-1 1983 Purification of antithrombin-thrombin complex by ion-exchange chromatography on DEAE-agarose resulted in predominantly monomeric complex, whereas purification on matrix-linked heparin produced large amounts of aggregated complex. deae-agarose 80-92 serpin family C member 1 Homo sapiens 16-28 6679287-1 1983 The treatment of three patients suffering from carbon tetrachloride intoxication with antithrombin III and plasma derivatives is reported. Carbon Tetrachloride 47-67 serpin family C member 1 Homo sapiens 86-102 6615439-7 1983 The similar properties of antithrombin-thrombin complexes formed with or without heparin support the concept of a catalytic role for the polysaccharide in the antithrombin-thrombin reaction. Polysaccharides 137-151 serpin family C member 1 Homo sapiens 26-38 6615439-7 1983 The similar properties of antithrombin-thrombin complexes formed with or without heparin support the concept of a catalytic role for the polysaccharide in the antithrombin-thrombin reaction. Polysaccharides 137-151 serpin family C member 1 Homo sapiens 159-171 6615439-1 1983 Purification of antithrombin-thrombin complex by ion-exchange chromatography on DEAE-agarose resulted in predominantly monomeric complex, whereas purification on matrix-linked heparin produced large amounts of aggregated complex. Heparin 176-183 serpin family C member 1 Homo sapiens 16-28 6871478-3 1983 The main laboratory features were: normal routine clotting tests, slightly decreased AT III activities in all assays carried out in the presence of heparin. Heparin 148-155 serpin family C member 1 Homo sapiens 85-91 6615439-2 1983 Monomeric antithrombin-thrombin complexes formed in the presence and in the absence of heparin had similar conformations and heparin affinities. Heparin 87-94 serpin family C member 1 Homo sapiens 10-22 6615439-2 1983 Monomeric antithrombin-thrombin complexes formed in the presence and in the absence of heparin had similar conformations and heparin affinities. Heparin 125-132 serpin family C member 1 Homo sapiens 10-22 6135060-0 1983 Effective prophylaxis with oral anticoagulants and low-dose heparin during pregnancy in an antithrombin III deficient woman. Heparin 60-67 serpin family C member 1 Homo sapiens 91-107 6871107-2 1983 The abnormal molecule, called AT III "Vicenza", was characterized by two-dimensional crossed immunoelectrophoresis either in the absence or presence of heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 30-36 6879278-1 1983 A patient with antithrombin III (ATT) deficiency after arterial embolism manifested an increasing requirement for heparin to adjust a partial thromboplastin time. Heparin 114-121 serpin family C member 1 Homo sapiens 15-31 6879278-1 1983 A patient with antithrombin III (ATT) deficiency after arterial embolism manifested an increasing requirement for heparin to adjust a partial thromboplastin time. Heparin 114-121 serpin family C member 1 Homo sapiens 33-36 6636041-4 1983 After administration of aspirin (acetylsalicylic acid), however, AT-III levels increased presumably due to inhibition of coagulation activities. Aspirin 24-31 serpin family C member 1 Homo sapiens 65-71 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Ammonium Sulfate 193-209 serpin family C member 1 Homo sapiens 40-46 6883717-4 1983 Based on the fact that protamine sulfate did not show any direct action on the antithrombin III molecule, the presence of AT III with progressive activity was considered to play an important role in the rebound phenomenon of heparin after heparin neutralization with protamine sulfate. Heparin 225-232 serpin family C member 1 Homo sapiens 122-128 6883717-4 1983 Based on the fact that protamine sulfate did not show any direct action on the antithrombin III molecule, the presence of AT III with progressive activity was considered to play an important role in the rebound phenomenon of heparin after heparin neutralization with protamine sulfate. Heparin 239-246 serpin family C member 1 Homo sapiens 122-128 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Sepharose 265-274 serpin family C member 1 Homo sapiens 22-38 6636041-4 1983 After administration of aspirin (acetylsalicylic acid), however, AT-III levels increased presumably due to inhibition of coagulation activities. Aspirin 33-53 serpin family C member 1 Homo sapiens 65-71 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Sepharose 265-274 serpin family C member 1 Homo sapiens 40-46 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Sepharose 265-274 serpin family C member 1 Homo sapiens 49-65 6636045-6 1983 On crossed immunoelectrophoresis (CIE) containing heparin in the first dimension agarose, patient"s AT-III showed no increase in electrophoretic mobility compared to that in the absence of heparin, suggesting that the patient"s AT-III has no affinity for heparin. Heparin 50-57 serpin family C member 1 Homo sapiens 100-106 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. DEAE-Dextran 284-297 serpin family C member 1 Homo sapiens 22-38 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. barium chloride 173-188 serpin family C member 1 Homo sapiens 22-38 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. DEAE-Dextran 284-297 serpin family C member 1 Homo sapiens 40-46 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. DEAE-Dextran 284-297 serpin family C member 1 Homo sapiens 49-65 6636046-6 1983 These results suggest that in antithrombin III Toyama an amino acid residue at the heparin-binding site has been replaced by less basic or more acidic one which has no ability to interact with heparin, resulting in a loss of heparin cofactor activity of this protein. Heparin 83-90 serpin family C member 1 Homo sapiens 30-46 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. barium chloride 173-188 serpin family C member 1 Homo sapiens 40-46 6636046-6 1983 These results suggest that in antithrombin III Toyama an amino acid residue at the heparin-binding site has been replaced by less basic or more acidic one which has no ability to interact with heparin, resulting in a loss of heparin cofactor activity of this protein. Heparin 193-200 serpin family C member 1 Homo sapiens 30-46 6305982-5 1983 ATIII cDNA clones were identified by hybridization to a mixture of synthetic oligodeoxynucleotides encoding amino acids 251-256 of the ATIII protein sequence. Oligodeoxyribonucleotides 77-98 serpin family C member 1 Homo sapiens 0-5 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. barium chloride 173-188 serpin family C member 1 Homo sapiens 49-65 6636046-1 1983 A hereditary abnormal antithrombin III (AT-III) "Antithrombin III Toyama" was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Ammonium Sulfate 193-209 serpin family C member 1 Homo sapiens 22-38 6193602-1 1983 Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl. Pentosan Sulfuric Polyester 0-21 serpin family C member 1 Homo sapiens 88-93 6305982-5 1983 ATIII cDNA clones were identified by hybridization to a mixture of synthetic oligodeoxynucleotides encoding amino acids 251-256 of the ATIII protein sequence. Oligodeoxyribonucleotides 77-98 serpin family C member 1 Homo sapiens 135-140 6857515-0 1983 Effects of low-dose warfarin on antithrombin III levels in morbidly obese patients. Warfarin 20-28 serpin family C member 1 Homo sapiens 32-48 6193602-1 1983 Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl. Pentosan Sulfuric Polyester 23-26 serpin family C member 1 Homo sapiens 88-93 6193602-1 1983 Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl. Sepharose 94-103 serpin family C member 1 Homo sapiens 88-93 6193602-1 1983 Pentosan polysulphate (PPS, Hemoclar, MW 6,700) was observed to have a low affinity for ATIII-Sepharose eluting at 0.3M NaCl. Sodium Chloride 120-124 serpin family C member 1 Homo sapiens 88-93 6193602-7 1983 The antiheparin effect of PPS was also observed in a purified system in obviating the heparin potentiation of the rate of inhibition of thrombin by antithrombin III. Pentosan Sulfuric Polyester 26-29 serpin family C member 1 Homo sapiens 148-164 6193602-8 1983 Observations showed that at higher concentrations of PPS it acted by directly inhibiting thrombin without the intervention of antithrombin III but also to potentiate the rate of fibrin monomer polymerization. Pentosan Sulfuric Polyester 53-56 serpin family C member 1 Homo sapiens 126-142 6612689-0 1983 The effect of variable fat diets and cholesterol-lowering drugs on Antithrombin III levels in hyperlipoproteinemic and normal subjects. Cholesterol 37-48 serpin family C member 1 Homo sapiens 67-83 6879515-0 1983 Differential AT III-response to oral and parenteral administration of 17 beta-estradiol. Estradiol 70-87 serpin family C member 1 Homo sapiens 13-19 6851887-0 1983 [Perioperative plasma-antithrombin activity during low-dose heparin prophylaxis]. Heparin 60-67 serpin family C member 1 Homo sapiens 22-34 6687888-1 1983 We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Glycosaminoglycans 38-56 serpin family C member 1 Homo sapiens 141-157 6687888-1 1983 We have tested the ability of various glycosaminoglycans to increase the rate of inhibition of thrombin by heparin cofactor II (HCII) and by antithrombin III (ATIII) isolated from human plasma. Glycosaminoglycans 38-56 serpin family C member 1 Homo sapiens 159-164 6223404-4 1983 Heparin, complexed with LDL, retains its enhancing effect on the rate of thrombin and plasmin inactivation by antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 110-126 6846326-2 1983 To date, much work has been done to elucidate the interaction of heparin with thrombin and its physiologic inhibitor, Antithrombin III (ATIII). Heparin 65-72 serpin family C member 1 Homo sapiens 118-134 6846326-2 1983 To date, much work has been done to elucidate the interaction of heparin with thrombin and its physiologic inhibitor, Antithrombin III (ATIII). Heparin 65-72 serpin family C member 1 Homo sapiens 136-141 6833231-6 1983 The mechanism of the interaction between histidine-rich glycoprotein and heparin appeared to be different from that between antithrombin III and heparin, since the former is abolished by EDTA and occurs both with heparin molecules having a high affinity or a low affinity for antithrombin III. Edetic Acid 187-191 serpin family C member 1 Homo sapiens 124-140 6687802-5 1983 The results suggest that heparin cofactor II differs from antithrombin III with respect to the mucopolysaccharide binding site. Glycosaminoglycans 95-113 serpin family C member 1 Homo sapiens 58-74 6831687-3 1983 In the AT III assay the sample is incubated with excess thrombin and heparin to form the functionally inactive AT III-thrombin complex. Heparin 69-76 serpin family C member 1 Homo sapiens 7-13 6831687-3 1983 In the AT III assay the sample is incubated with excess thrombin and heparin to form the functionally inactive AT III-thrombin complex. Heparin 69-76 serpin family C member 1 Homo sapiens 111-117 6870832-0 1983 Electrostatic interactions in the heparin-enhanced reaction between human thrombin and antithrombin. Heparin 34-41 serpin family C member 1 Homo sapiens 87-99 6870832-1 1983 Binding of heparin to thrombin is monitored by means of an aqueous two-phase partition system, and binding of heparin to antithrombin is monitored by means of heparin induced enhancement of the intrinsic fluorescence of the protein. Heparin 110-117 serpin family C member 1 Homo sapiens 121-133 6870832-1 1983 Binding of heparin to thrombin is monitored by means of an aqueous two-phase partition system, and binding of heparin to antithrombin is monitored by means of heparin induced enhancement of the intrinsic fluorescence of the protein. Heparin 110-117 serpin family C member 1 Homo sapiens 121-133 6870832-3 1983 Heparin is displaced from thrombin at lower concentrations of electrolyte than those necessary for its displacement from antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 121-133 6870832-5 1983 The kinetics of the reaction between thrombin and antithrombin in the presence of heparin were studied by using an assay where synthetic peptide substrate is present in the reaction mixture during the reaction between proteinase and inhibitor. Heparin 82-89 serpin family C member 1 Homo sapiens 50-62 6870832-7 1983 The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin. Heparin 57-64 serpin family C member 1 Homo sapiens 68-80 6870832-7 1983 The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin. Heparin 195-202 serpin family C member 1 Homo sapiens 68-80 6870832-7 1983 The results are consistent with a model where binding of heparin to antithrombin causes enhancement of the reaction rate, and where this enhancement is abolished again when additional binding of heparin to thrombin takes place on further addition of heparin. Heparin 195-202 serpin family C member 1 Homo sapiens 68-80 6832015-0 1983 [Perioperative plasma antithrombin activity with "low-dose" heparin prophylaxis. Heparin 60-67 serpin family C member 1 Homo sapiens 22-34 6832015-2 1983 Antithrombin III activity was estimated using a chromogenic substrate perioperatively in the plasma of 200 patients undergoing major elective abdominal surgery during low-dose heparin prophylaxis. Heparin 176-183 serpin family C member 1 Homo sapiens 0-16 6833231-6 1983 The mechanism of the interaction between histidine-rich glycoprotein and heparin appeared to be different from that between antithrombin III and heparin, since the former is abolished by EDTA and occurs both with heparin molecules having a high affinity or a low affinity for antithrombin III. Heparin 73-80 serpin family C member 1 Homo sapiens 276-292 6602754-5 1983 This reaction was complete after 15 s and is comparable with the fast heparin induced formation of modified antithrombin III. Heparin 70-77 serpin family C member 1 Homo sapiens 108-124 6830338-6 1983 The individual, nadir levels of FN, AT III, prealbumin, and transferrin were lower (p less than 0.01) in the septic group A than in B and C. Within the septic group, the nadir levels of AT III, but not those of FN, were lower (p less than 0.01) in the 14 nonsurvivors than in the 19 survivors. nadir 170-175 serpin family C member 1 Homo sapiens 186-192 6830362-3 1983 Analysis of the data revealed that patients with high triglyceride levels also have a high incidence of low antithrombin III activity and increased platelet aggregation. Triglycerides 54-66 serpin family C member 1 Homo sapiens 108-124 6859531-3 1983 The methodologies were extended to investigations on the effects of heparin in the interaction between thrombin and antithrombin III. Heparin 68-75 serpin family C member 1 Homo sapiens 116-132 6830263-0 1983 Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation. Disulfides 20-29 serpin family C member 1 Homo sapiens 44-60 6845270-4 1983 Molecular forms of AT III produced in plasma treated with coagulation enzymes, or in serum, were assessed by measuring immunoreactive AT III in fractions obtained by gel filtration chromatography on Sephadex G-200. sephadex 199-213 serpin family C member 1 Homo sapiens 19-25 6571800-0 1983 Antithrombin III and anti-activated factor X activity in patients with acute promyelocytic leukemia and disseminated intravascular coagulation treated with heparin. Heparin 156-163 serpin family C member 1 Homo sapiens 0-16 6830263-0 1983 Localization of the disulfide bond in human antithrombin III required for heparin-accelerated thrombin inactivation. Heparin 74-81 serpin family C member 1 Homo sapiens 44-60 6830263-1 1983 Heparin accelerates the rate of inhibition of thrombin by antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 58-74 6830263-3 1983 Alkylation of mildly reduced antithrombin III with [3H]iodacetic acid followed by digestion with cyanogen bromide yielded two major labeled peptides. [3h]iodacetic acid 51-69 serpin family C member 1 Homo sapiens 29-45 6830263-7 1983 These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines. Disulfides 39-48 serpin family C member 1 Homo sapiens 57-73 6830263-7 1983 These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines. Disulfides 39-48 serpin family C member 1 Homo sapiens 150-166 6830263-7 1983 These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines. Cysteine 90-93 serpin family C member 1 Homo sapiens 57-73 6830263-7 1983 These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines. Cysteine 90-93 serpin family C member 1 Homo sapiens 150-166 6830263-7 1983 These data indicate that the sensitive disulfide bond in antithrombin III extends between Cys-239 and Cys-422; the site at which thrombin cleaves the antithrombin III is between these two half-cystines. Cysteine 102-105 serpin family C member 1 Homo sapiens 57-73 6845286-0 1983 Antithrombin III-binding capacity of heparin-sepharose as a function of activation temperature and duration. Heparin 37-44 serpin family C member 1 Homo sapiens 0-16 6845286-0 1983 Antithrombin III-binding capacity of heparin-sepharose as a function of activation temperature and duration. Sepharose 45-54 serpin family C member 1 Homo sapiens 0-16 6660606-4 1983 Heparin is prescribed as soon as AT III activity reaches 70%. Heparin 0-7 serpin family C member 1 Homo sapiens 33-39 6822493-0 1983 Two-substrate reaction model for the heparin-catalyzed bovine antithrombin/protease reaction. Heparin 37-44 serpin family C member 1 Homo sapiens 62-74 6822493-2 1983 In this model, heparin is the catalyst; while antithrombin is the first substrate and the protease is the second substrate. Heparin 15-22 serpin family C member 1 Homo sapiens 46-58 6822493-5 1983 Differences between thrombin and Factor Xa at low (nanomolar) concentrations of heparin were evident in this rate constant and the relative affinities for the heparin-antithrombin complex (Km for Factor Xa = 100 nM; Km for thrombin less than or equal to 2 nM). Heparin 80-87 serpin family C member 1 Homo sapiens 167-179 6184096-5 1983 Antithrombin-heparin cofactor, which eluted from heparin-agarose with buffer containing 2.0 M NaCl, was functionally and antigenically identified as antithrombin III. Heparin 13-20 serpin family C member 1 Homo sapiens 149-165 6667245-11 1983 The antithrombotic effect of heparin therapy is determined by FPA as an immediate index and by Fbg, FDP, and AT III as a slow index. Heparin 29-36 serpin family C member 1 Homo sapiens 109-115 6667252-2 1983 About 60% of these 21 patients were effectively treated with AT III concentrates by enhancing the effect of heparin and alleviating the burden of excessive plasma transfusions on the cardiovascular system. Heparin 108-115 serpin family C member 1 Homo sapiens 61-67 6338832-1 1983 The inhibition of thrombin by antithrombin-III involves formation of a 1:1 covalent complex between protease and inhibitor and concomitant cleavage of the antithrombin-III peptide chain after Arg-385. Arginine 192-195 serpin family C member 1 Homo sapiens 30-46 6338832-1 1983 The inhibition of thrombin by antithrombin-III involves formation of a 1:1 covalent complex between protease and inhibitor and concomitant cleavage of the antithrombin-III peptide chain after Arg-385. Arginine 192-195 serpin family C member 1 Homo sapiens 155-171 6184096-5 1983 Antithrombin-heparin cofactor, which eluted from heparin-agarose with buffer containing 2.0 M NaCl, was functionally and antigenically identified as antithrombin III. Sepharose 57-64 serpin family C member 1 Homo sapiens 149-165 6184096-5 1983 Antithrombin-heparin cofactor, which eluted from heparin-agarose with buffer containing 2.0 M NaCl, was functionally and antigenically identified as antithrombin III. Sodium Chloride 94-98 serpin family C member 1 Homo sapiens 149-165 7142182-2 1982 The results have shown that the reaction is saturable with respect to both thrombin (KT = 3.6 x 10(-8) M) and antithrombin III (KAT = 1.0 x 10(-7) M) when the heparin concentration is low relative to the initial protein concentrations. Heparin 159-166 serpin family C member 1 Homo sapiens 110-126 6654191-6 1983 A significant decrease in the AT-III level (p less than 0.01) and a significant increase (p less than 0.01) in the fibrinogen level were observed after heparin-dipyridamole treatment of patients suspected of IUGR. Heparin 152-159 serpin family C member 1 Homo sapiens 30-36 6654191-6 1983 A significant decrease in the AT-III level (p less than 0.01) and a significant increase (p less than 0.01) in the fibrinogen level were observed after heparin-dipyridamole treatment of patients suspected of IUGR. Dipyridamole 160-172 serpin family C member 1 Homo sapiens 30-36 6868150-3 1983 Relations were found connecting polar (delta) and steric (Es) characteristics of substituent (R) in R-C6H4-SO2-Arg-OCH3 esters with their antithrombin activity in vitro or with efficiency of their thrombin-catalyzed hydrolysis. Einsteinium 58-60 serpin family C member 1 Homo sapiens 138-150 6868150-3 1983 Relations were found connecting polar (delta) and steric (Es) characteristics of substituent (R) in R-C6H4-SO2-Arg-OCH3 esters with their antithrombin activity in vitro or with efficiency of their thrombin-catalyzed hydrolysis. r-c6h4-so2-arg-och3 esters 100-126 serpin family C member 1 Homo sapiens 138-150 6132465-4 1982 Studies on binding to Antithrombin III - Sepharose showed that sulphated guaran and a fraction of the aminated and sulphated alginic acid was bound, whereas no binding occurred with sulphated alginic acid. Sepharose 41-50 serpin family C member 1 Homo sapiens 22-38 6132465-4 1982 Studies on binding to Antithrombin III - Sepharose showed that sulphated guaran and a fraction of the aminated and sulphated alginic acid was bound, whereas no binding occurred with sulphated alginic acid. Alginic Acid 125-137 serpin family C member 1 Homo sapiens 22-38 7140568-1 1982 Haemodialysis had become impossible or possible only using high doses of heparin in 20 patients with dialysis-dependent renal insufficiency due to lowering of antithrombin III (AT III). Heparin 73-80 serpin family C member 1 Homo sapiens 159-175 7140568-1 1982 Haemodialysis had become impossible or possible only using high doses of heparin in 20 patients with dialysis-dependent renal insufficiency due to lowering of antithrombin III (AT III). Heparin 73-80 serpin family C member 1 Homo sapiens 177-183 7140568-6 1982 Dialysis was performed with continuous substitution of the AT III-heparin-complex in 6 patients prone to haemorrhage. Heparin 66-73 serpin family C member 1 Homo sapiens 59-65 6403706-8 1983 Minimal alterations were seen with the levonorgestrel preparation, whereas those containing norethindrone or ethynodiol diacetate showed marked increases in factors I, VII, VIII and X and plasminogen, associated with a decrease in antithrombin III. Norethindrone 92-105 serpin family C member 1 Homo sapiens 231-247 6403706-8 1983 Minimal alterations were seen with the levonorgestrel preparation, whereas those containing norethindrone or ethynodiol diacetate showed marked increases in factors I, VII, VIII and X and plasminogen, associated with a decrease in antithrombin III. Ethynodiol Diacetate 109-129 serpin family C member 1 Homo sapiens 231-247 6344178-2 1983 Although heparin activates ATIII, thereby accelerating its consumption, it cannot increase the overall inhibitory capacity towards coagulation. Heparin 9-16 serpin family C member 1 Homo sapiens 27-32 6344178-3 1983 The anticoagulant effect of heparin is in relation with the presence of sufficient amounts of ATIII. Heparin 28-35 serpin family C member 1 Homo sapiens 94-99 6402859-0 1983 The antithrombin III content of cryoprecipitate prepared from blood collected with and without heparin. Heparin 95-102 serpin family C member 1 Homo sapiens 4-20 6402859-6 1983 Using the fluorogenic assay, we also determined the effect of adding heparin to blood on the cryoprecipitation of AT III. Heparin 69-76 serpin family C member 1 Homo sapiens 114-120 6132465-6 1982 The two alginic acid preparations showed Antithrombin III-dependent inhibition of thrombin, whereas the sulphated guaran inhibits both by Antithrombin III-dependent and independent mechanisms. Alginic Acid 8-20 serpin family C member 1 Homo sapiens 41-57 7142182-6 1982 When the heparin-enhanced antithrombin III/thrombin reaction was studied under conditions where the heparin concentration was high relative to the initial protein concentrations the overall reaction was second order. Heparin 9-16 serpin family C member 1 Homo sapiens 26-42 6961402-0 1982 Circular dichroism spectroscopy of heparin-antithrombin interactions. Heparin 35-42 serpin family C member 1 Homo sapiens 43-55 6961402-1 1982 We have utilized circular dichroism spectroscopy to examine the interaction of antithrombin with heparin-derived oligosaccharides and mucopolysaccharides of various sizes. heparin-derived oligosaccharides 97-129 serpin family C member 1 Homo sapiens 79-91 6961402-1 1982 We have utilized circular dichroism spectroscopy to examine the interaction of antithrombin with heparin-derived oligosaccharides and mucopolysaccharides of various sizes. Glycosaminoglycans 134-153 serpin family C member 1 Homo sapiens 79-91 6961402-10 1982 The second of these patterns is apparent when octadecasaccharide, low molecular weight heparin (6,500), and high molecular weight heparin (22,000) interact with antithrombin. octadecasaccharide 46-64 serpin family C member 1 Homo sapiens 161-173 6961402-10 1982 The second of these patterns is apparent when octadecasaccharide, low molecular weight heparin (6,500), and high molecular weight heparin (22,000) interact with antithrombin. Heparin 87-94 serpin family C member 1 Homo sapiens 161-173 6961402-10 1982 The second of these patterns is apparent when octadecasaccharide, low molecular weight heparin (6,500), and high molecular weight heparin (22,000) interact with antithrombin. Heparin 130-137 serpin family C member 1 Homo sapiens 161-173 6961402-15 1982 Given our method for generating the above data, these spectral alterations must be associated with the binding of a second critical domain of the mucopolysaccharide to antithrombin that is required for rapid complex formation with thrombin or the activation of the protease inhibitor with respect to the neutralization of the latter enzyme. Glycosaminoglycans 146-164 serpin family C member 1 Homo sapiens 168-180 7164033-3 1982 This latter inhibitory action of heparin occurs independently of antithrombin III. Heparin 33-40 serpin family C member 1 Homo sapiens 65-81 6957257-0 1982 Antithrombin III and anti-activated factor X activity in patients with acute promyelocytic leukemia and disseminated intravascular coagulation treated with heparin. Heparin 156-163 serpin family C member 1 Homo sapiens 0-16 7164033-0 1982 Heparin with low affinity to antithrombin III inhibits the activation of prothrombin in normal plasma. Heparin 0-7 serpin family C member 1 Homo sapiens 29-45 7164033-4 1982 A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin. Heparin 2-9 serpin family C member 1 Homo sapiens 40-56 7164033-2 1982 Unfractionated heparin enhances the rates at which antithrombin III inactivates activated clotting factors, and inhibits the activation of both Factor X and prothrombin by disrupting the calcium and phospholipid dependent assembly of the Factor X and prothrombin activator complexes. Heparin 15-22 serpin family C member 1 Homo sapiens 51-67 7164033-4 1982 A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin. Heparin 2-9 serpin family C member 1 Homo sapiens 122-138 7164033-4 1982 A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin. Sepharose 139-148 serpin family C member 1 Homo sapiens 40-56 7164033-4 1982 A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin. Sepharose 139-148 serpin family C member 1 Homo sapiens 122-138 7164033-4 1982 A heparin fraction with low affinity to antithrombin III was prepared from standard heparin by affinity chromatography on antithrombin-III-Sepharose and its properties compared with unfractionated heparin. Heparin 84-91 serpin family C member 1 Homo sapiens 40-56 7164033-5 1982 The low affinity heparin fraction and the unfractionated heparin had equivalent inhibitory effects on prothrombin activation in antithrombin III depleted plasma. Heparin 17-24 serpin family C member 1 Homo sapiens 128-144 7164033-5 1982 The low affinity heparin fraction and the unfractionated heparin had equivalent inhibitory effects on prothrombin activation in antithrombin III depleted plasma. Heparin 57-64 serpin family C member 1 Homo sapiens 128-144 7164033-8 1982 This antithrombin III independent inhibition of the activation of prothrombin was also evident when activated platelets were used as the source of the procoagulant phospholipids. Phospholipids 164-177 serpin family C member 1 Homo sapiens 5-21 7164033-9 1982 The antithrombin III independent effect of heparin is unlikely to be important therapeutically, however, if this property of heparin is shared by other naturally occurring glycosaminoglycans, it could be important in maintaining the fluidity of blood under physiological conditions. Heparin 43-50 serpin family C member 1 Homo sapiens 4-20 7164033-9 1982 The antithrombin III independent effect of heparin is unlikely to be important therapeutically, however, if this property of heparin is shared by other naturally occurring glycosaminoglycans, it could be important in maintaining the fluidity of blood under physiological conditions. Heparin 125-132 serpin family C member 1 Homo sapiens 4-20 7158775-0 1982 Preparation of three types of heparin-sepharose and their binding activities to thrombin and antithrombin III. Heparin 30-37 serpin family C member 1 Homo sapiens 93-109 7158775-0 1982 Preparation of three types of heparin-sepharose and their binding activities to thrombin and antithrombin III. Sepharose 38-47 serpin family C member 1 Homo sapiens 93-109 7164033-9 1982 The antithrombin III independent effect of heparin is unlikely to be important therapeutically, however, if this property of heparin is shared by other naturally occurring glycosaminoglycans, it could be important in maintaining the fluidity of blood under physiological conditions. Glycosaminoglycans 172-190 serpin family C member 1 Homo sapiens 4-20 6183640-0 1982 [A study of antithrombin systems during heparin therapy]. Heparin 40-47 serpin family C member 1 Homo sapiens 12-24 6812990-1 1982 Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO). chromozym TH 97-109 serpin family C member 1 Homo sapiens 0-16 6812990-1 1982 Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO). chromozym TH 97-109 serpin family C member 1 Homo sapiens 18-24 6812990-1 1982 Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO). tos-gly-arg-p-nitroanilide 111-137 serpin family C member 1 Homo sapiens 0-16 6812990-1 1982 Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO). boehringer 139-149 serpin family C member 1 Homo sapiens 0-16 6812990-1 1982 Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO). thiobenzyl benzyloxycarbonyl-L-lysinate 164-213 serpin family C member 1 Homo sapiens 0-16 6812990-1 1982 Antithrombin III (AT III) activity was determined with two different new chromogenic substances--Chromozym-TH (Tos-Gly-Arg-p-nitroanilide; Boehringer Mannheim) and alpha-N-carbobenzyl-oxy-L-lysine-thiobenzyl ester (Du Pont)--with both a discrete (aca) and a centrifugal analyzer (COBAS BIO). du pont 215-222 serpin family C member 1 Homo sapiens 0-16 6812990-8 1982 Plasma from 14 of 16 patients with disseminated intravascular coagulopathy showed a decrease in AT III of from 17 to 51% of normal before and during heparin therapy. Heparin 149-156 serpin family C member 1 Homo sapiens 96-102 6183640-2 1982 A decrease in AT III levels was observed during treatment and found to correlate significantly with heparin plasma levels, but there were no significant changes in alpha 2M and alpha 1 AT levels. Heparin 100-107 serpin family C member 1 Homo sapiens 14-20 7115961-0 1982 Effect of heparin on the inactivation rate of human factor XIa by antithrombin-III. Heparin 10-17 serpin family C member 1 Homo sapiens 66-82 7115961-2 1982 Although antithrombin-III, an inhibitor of factor XIa, normally accounts for only one-sixth of the plasma inhibitory activity against factor XIa, its effectiveness has been reported to be enhanced by heparin. Heparin 200-207 serpin family C member 1 Homo sapiens 9-25 7115961-3 1982 We have reinvestigated the ability of heparin to potentiate factor XIa inhibition by both purified antithrombin-III and plasma using synthetic tripeptide amide substrates as well as a coagulant assay. Heparin 38-45 serpin family C member 1 Homo sapiens 99-115 7115961-7 1982 Only at heparin concentrations of 5 and 10 U/ml, was a 2- and 4-fold increase in the inactivation rate of factor XIa by purified antithrombin III observed. Heparin 8-15 serpin family C member 1 Homo sapiens 129-145 7157229-4 1982 In contrast thrombin, antithrombin III and factor Xa adsorb on the surface of such insoluble polymers. Polymers 93-101 serpin family C member 1 Homo sapiens 22-38 7157229-6 1982 The inactivation of thrombin or factor Xa by antithrombin is catalysed by the presence in the mixture of these insoluble materials as it is with soluble heparin. Heparin 153-160 serpin family C member 1 Homo sapiens 45-57 7117524-0 1982 Permanent activation of antithrombin by covalent attachment of heparin oligosaccharides. heparin oligosaccharides 63-87 serpin family C member 1 Homo sapiens 24-36 7107605-5 1982 Furthermore, incubation of the mastocytoma endoglucuronidase with a heparin octasaccharide having high affinity for antithrombin failed to cleave the beta-glucuronidic linkage in the antithrombin-binding region. heparin octasaccharide 68-90 serpin family C member 1 Homo sapiens 116-128 7107605-7 1982 This enzyme has now been found to attack also the beta-glucuronidic linkage in the antithrombin-binding region of the heparin molecule. Heparin 118-125 serpin family C member 1 Homo sapiens 83-95 7107605-8 1982 The loss of bio-affinity resulting from cleavage of this linkage in the antithrombin-binding heparin octasaccharide was utilized to construct a sensitive, specific, and simple assay method for the platelet endoglucuronidase. heparin octasaccharide 93-115 serpin family C member 1 Homo sapiens 72-84 7147215-0 1982 Effect of sulfinpyrazone upon antithrombin III and platelet factor 4 in chronic renal failure. Sulfinpyrazone 10-24 serpin family C member 1 Homo sapiens 30-46 7147215-3 1982 Sulfinpyrazone, a drug capable of reducing the frequency of thrombotic events in uremic patients, allows return toward normal of the AT III while reducing to normal the plasma concentration of PF4. Sulfinpyrazone 0-14 serpin family C member 1 Homo sapiens 133-139 7147215-4 1982 Thus, suppression of platelet function by sulfinpyrazone appears to reduce in vivo clotting, and thus reduces consumption of AT III. Sulfinpyrazone 42-56 serpin family C member 1 Homo sapiens 125-131 7082848-6 1982 Turnover studies were made in the patient using her own purified AT-III labeled with 131I, (*I). Iodine-131 85-89 serpin family C member 1 Homo sapiens 65-71 7109075-3 1982 A loading dose of 15 mg. diethylstilbestrol daily resulted in a marked decrease in plasma antithrombin III activity (mean 0.24 U. per ml.). Diethylstilbestrol 25-43 serpin family C member 1 Homo sapiens 90-106 7110603-2 1982 More specifically, it is shown that a change in these enzymatic systems could determine "functional kidnapping" of heparin or other substances (glicosaminoglycans) engaged in the activation of Antithrombin III, with noteworthy haemorrheological consequences mediated by a variety of mechanisms. Heparin 115-122 serpin family C member 1 Homo sapiens 193-209 7173439-1 1982 Acetylcholine entailed a release of substance possessing activity of the blood plasma antithrombin III into the intestinal vascular bed and activated to some extent the release of antifibrinolytic compounds. Acetylcholine 0-13 serpin family C member 1 Homo sapiens 86-102 7135347-0 1982 On the reliability of the use of heparin immobilized on agarose for the study of the interactions among heparin, thrombin and antithrombin. Heparin 33-40 serpin family C member 1 Homo sapiens 126-138 7135347-0 1982 On the reliability of the use of heparin immobilized on agarose for the study of the interactions among heparin, thrombin and antithrombin. Sepharose 56-63 serpin family C member 1 Homo sapiens 126-138 7135347-1 1982 The extent of inhibition of thrombin was re-examined as a consequence of the sequence of addition of thrombin and antithrombin III to a column of heparin immobilized on agarose. Heparin 146-153 serpin family C member 1 Homo sapiens 114-130 7112497-2 1982 Specific antithrombin activity in plasma showed a negative correlation with triglyceride levels. Triglycerides 76-88 serpin family C member 1 Homo sapiens 9-21 7112497-3 1982 The consumption of antithrombin activity during blood clotting was negatively correlated with both serum total triglyceride and heparin precipitable lipoprotein and positively correlated with serum high density lipoprotein cholesterol. Triglycerides 111-123 serpin family C member 1 Homo sapiens 19-31 7082587-6 1982 In the presence of heparin, two peaks of AT III were observed in the patients" plasmas: the mobility of one peak was similar to that of the control, whereas the other showed a decreased mobility, suggesting a lack of binding to heparin. Heparin 19-26 serpin family C member 1 Homo sapiens 41-47 7082587-7 1982 The two populations of AT III were separated by affinity chromatography on heparin-agarose. Heparin 75-82 serpin family C member 1 Homo sapiens 23-29 6285503-7 1982 Furthermore, a significant decrease in both antithrombin III levels and basal and venostasis-stimulated plasminogen activator levels were seen in glibenclamide patients. Glyburide 146-159 serpin family C member 1 Homo sapiens 44-60 7082587-7 1982 The two populations of AT III were separated by affinity chromatography on heparin-agarose. Sepharose 83-90 serpin family C member 1 Homo sapiens 23-29 7082587-8 1982 50% of the patients" AT III bound to the agarose beads. Sepharose 41-48 serpin family C member 1 Homo sapiens 21-27 7082587-10 1982 This familial AT III variant characterized a reduced affinity for heparin is tentatively named "Antithrombin III Paris". Heparin 66-73 serpin family C member 1 Homo sapiens 14-20 7082587-10 1982 This familial AT III variant characterized a reduced affinity for heparin is tentatively named "Antithrombin III Paris". Heparin 66-73 serpin family C member 1 Homo sapiens 96-112 7068594-0 1982 The rate-determining step of the heparin-catalyzed antithrombin/thrombin reaction is independent of thrombin. Heparin 33-40 serpin family C member 1 Homo sapiens 51-63 7068594-1 1982 The heparin-catalyzed inactivation of thrombin by antithrombin was examined using saturation kinetics and fractional reaction lifetimes. Heparin 4-11 serpin family C member 1 Homo sapiens 50-62 7068594-2 1982 Based solely on kinetic analysis, the reaction binding sequence was determined to be heparin binding to antithrombin followed by binding of thrombin. Heparin 85-92 serpin family C member 1 Homo sapiens 104-116 6896131-3 1982 These findings include the following: (1) On the vascular endothelium, a cofactor for antithrombin III (with an activity comparable to stationary phase heparin) catalyzes thrombin inhibition in vivo. Heparin 152-159 serpin family C member 1 Homo sapiens 86-102 7095150-0 1982 The N-terminal sequence of human plasma histidine-rich glycoprotein homologous to antithrombin with high affinity for heparin. Heparin 118-125 serpin family C member 1 Homo sapiens 82-94 7101236-0 1982 Inhibition of thrombin-neutralizing activity of antithrombin III by steroid hormones. Steroids 68-84 serpin family C member 1 Homo sapiens 48-64 6179183-5 1982 Our data indicate that pentosan polysulphate has more marked effects in vivo than in vitro, that the action of the drug on clotting is mediated mainly via an At III-independent pathway, and that its effects are not confined to the coagulation system. Pentosan Sulfuric Polyester 23-44 serpin family C member 1 Homo sapiens 158-164 7112512-1 1982 The role of antithrombin III (AT III) in heparin-induced potentiation of platelet aggregation was investigated using purified AT III and AT III depleted plasma. Heparin 41-48 serpin family C member 1 Homo sapiens 12-28 7112512-1 1982 The role of antithrombin III (AT III) in heparin-induced potentiation of platelet aggregation was investigated using purified AT III and AT III depleted plasma. Heparin 41-48 serpin family C member 1 Homo sapiens 30-36 7112512-4 1982 When purified AT III was added to AT III depleted plasma at a concentration of 20 microgram/ml, potentiation of platelet aggregation by heparin was clearly demonstrated. Heparin 136-143 serpin family C member 1 Homo sapiens 14-20 7112512-4 1982 When purified AT III was added to AT III depleted plasma at a concentration of 20 microgram/ml, potentiation of platelet aggregation by heparin was clearly demonstrated. Heparin 136-143 serpin family C member 1 Homo sapiens 34-40 7112512-5 1982 These results suggest that the effect of heparin on platelet aggregation is also mediated by AT III. Heparin 41-48 serpin family C member 1 Homo sapiens 93-99 7112514-2 1982 The experiments (thrombin and Factor Xa inactivation, heparin affinity chromatography, modified two dimensional immunoelectrophoresis and gel filtration) showed a distinct difference between the two antithrombin III anomalies. Heparin 54-61 serpin family C member 1 Homo sapiens 199-215 7101236-11 1982 ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone. Cholesterol 76-87 serpin family C member 1 Homo sapiens 12-18 7101236-11 1982 ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone. Cortisone 89-98 serpin family C member 1 Homo sapiens 12-18 7101236-11 1982 ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone. Testosterone 100-112 serpin family C member 1 Homo sapiens 12-18 7101236-11 1982 ACtivity of AT III was also reduced in increasing order of effectiveness by cholesterol, cortisone, testosterone and progesterone. Progesterone 117-129 serpin family C member 1 Homo sapiens 12-18 7101236-12 1982 Our studies suggest a direct effect of estrogens and other steroids on AT III, altering its specific neutralization of thrombin. Steroids 59-67 serpin family C member 1 Homo sapiens 71-77 7112509-0 1982 Preparation of highly stable antithrombin-sepharose and utilization for the fractionation of heparin. Sepharose 42-51 serpin family C member 1 Homo sapiens 29-41 7101237-5 1982 Neutralization of heparin by PF4 and PS probably proceeds by similar mechanisms, but the details of structure outside the antithrombin III-binding oligosaccharide of heparin may enter in differently. Oligosaccharides 147-162 serpin family C member 1 Homo sapiens 122-138 7112509-0 1982 Preparation of highly stable antithrombin-sepharose and utilization for the fractionation of heparin. Heparin 93-100 serpin family C member 1 Homo sapiens 29-41 7101237-5 1982 Neutralization of heparin by PF4 and PS probably proceeds by similar mechanisms, but the details of structure outside the antithrombin III-binding oligosaccharide of heparin may enter in differently. Heparin 166-173 serpin family C member 1 Homo sapiens 122-138 6461438-4 1982 This assay using Bz-Leu-Ala-Arg-NE is a highly sensitive method for detecting prothrombin, thrombin and antithrombin III in human plasma. bz-leu-ala-arg 17-31 serpin family C member 1 Homo sapiens 104-120 7071651-5 1982 We believe the antithrombin III level should be routinely determined for patients receiving heparin therapy. Heparin 92-99 serpin family C member 1 Homo sapiens 15-31 6461438-6 1982 Antithrombin III activity could be determined with 2 microliter of human plasma using human thrombin and heparin as cofactor. Heparin 105-112 serpin family C member 1 Homo sapiens 0-16 6977539-4 1982 As in the latter reaction, the formation of the modified antithrombin by Factor Xa was increased in the presence of heparin, while only small amounts were produced by Factor IXa both in the absence and presence of the polysaccharide. Heparin 116-123 serpin family C member 1 Homo sapiens 57-69 7037067-0 1982 Differential role of fractionated heparin in antithrombin-III proteolysis. Heparin 34-41 serpin family C member 1 Homo sapiens 45-61 6977539-7 1982 The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor. Ammonia 94-101 serpin family C member 1 Homo sapiens 13-25 6977539-7 1982 The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor. Ammonia 94-101 serpin family C member 1 Homo sapiens 41-53 6977539-7 1982 The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor. Hydroxylamine 105-118 serpin family C member 1 Homo sapiens 13-25 6977539-7 1982 The purified antithrombin-Factor IXa and antithrombin-Factor Xa complexes were dissociated by ammonia or hydroxylamine into free enzyme and a modified two-chain form of the inhibitor. Hydroxylamine 105-118 serpin family C member 1 Homo sapiens 41-53 6977539-9 1982 The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin. Arginine 168-171 serpin family C member 1 Homo sapiens 72-84 6977539-9 1982 The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin. Arginine 168-171 serpin family C member 1 Homo sapiens 212-224 6977539-9 1982 The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin. Serine 172-175 serpin family C member 1 Homo sapiens 72-84 6977539-9 1982 The fact that identical results were obtained for the reactions between antithrombin and three enzymes with different specificities strongly suggests that the observed Arg-Ser cleavage site is the active site of antithrombin. Serine 172-175 serpin family C member 1 Homo sapiens 212-224 6807052-3 1982 Antithrombin III (AT III) was always found along the inside of thickened TBM in every atrophic nephron, but not found in the sclerotic GT nor along the thickened BC. metsulfuron methyl 73-76 serpin family C member 1 Homo sapiens 0-16 6807052-3 1982 Antithrombin III (AT III) was always found along the inside of thickened TBM in every atrophic nephron, but not found in the sclerotic GT nor along the thickened BC. metsulfuron methyl 73-76 serpin family C member 1 Homo sapiens 18-24 6807052-6 1982 At III was easily dissociated from the thickened TBM after the incubation in warm (37 degrees C) 0.01 M phosphate buffered saline of various pH (pH 4.0, pH 7.2 or pH 10.0) and cold (4 degrees C) or warm (37 degrees C) 0.75 M hydrazine solutions of the same pH, while alpha 1AT was not dissociated from the atrophic nephrons after the incubation in all solutions. Phosphate-Buffered Saline 104-129 serpin family C member 1 Homo sapiens 0-6 6807052-6 1982 At III was easily dissociated from the thickened TBM after the incubation in warm (37 degrees C) 0.01 M phosphate buffered saline of various pH (pH 4.0, pH 7.2 or pH 10.0) and cold (4 degrees C) or warm (37 degrees C) 0.75 M hydrazine solutions of the same pH, while alpha 1AT was not dissociated from the atrophic nephrons after the incubation in all solutions. hydrazine 225-234 serpin family C member 1 Homo sapiens 0-6 7066204-6 1982 This discrepancy was associated with the presence in the patient"s plasma of an AT III fraction showing a slower mobility than the main AT III peak on two-dimensional immunoelectrophoresis in the presence of heparin. Heparin 208-215 serpin family C member 1 Homo sapiens 80-86 7037067-1 1982 Commercial heparin was fractionated by affinity chromatography on immobilized antithrombin-III (AT-III) into nonbinding (NB), lower affinity (LA), and high affinity (HA) heparin, with specific anticoagulant activity of 9, 205, and 284 U/mg, respectively, Each fraction, in microgram quantities, was examined in the reaction of alpha-thrombin with a molar excess of 125I-labeled AT-III. Heparin 11-18 serpin family C member 1 Homo sapiens 78-94 7037067-1 1982 Commercial heparin was fractionated by affinity chromatography on immobilized antithrombin-III (AT-III) into nonbinding (NB), lower affinity (LA), and high affinity (HA) heparin, with specific anticoagulant activity of 9, 205, and 284 U/mg, respectively, Each fraction, in microgram quantities, was examined in the reaction of alpha-thrombin with a molar excess of 125I-labeled AT-III. Heparin 11-18 serpin family C member 1 Homo sapiens 96-102 7083257-11 1982 It is concluded that the antithrombin binding site in heparin is represented by the pentasaccharide sequence extending from unit 2 to unit 6 of the octasaccharide studied. Octasaccharide 148-162 serpin family C member 1 Homo sapiens 25-37 7037067-2 1982 Proteolysis of residual AT-III was assessed on the basis of distribution of radioactivity in SDS-polyacrylamide gels after electrophoresis. Sodium Dodecyl Sulfate 93-96 serpin family C member 1 Homo sapiens 24-30 7037067-2 1982 Proteolysis of residual AT-III was assessed on the basis of distribution of radioactivity in SDS-polyacrylamide gels after electrophoresis. polyacrylamide 97-111 serpin family C member 1 Homo sapiens 24-30 7083257-0 1982 Further characterization of the antithrombin-binding sequence in heparin. Heparin 65-72 serpin family C member 1 Homo sapiens 32-44 7037067-3 1982 In the presence of HA heparin, 36% of AT-III participating in the reaction was degraded into a 50,000-dalton inactive fragment. Heparin 22-29 serpin family C member 1 Homo sapiens 38-44 7083257-1 1982 An octasaccharide with high affinity for antithrombin, isolated after partial deaminative cleavage of heparin and previously found to have the following predominant structure (see formula in text) has been studied further. Octasaccharide 3-17 serpin family C member 1 Homo sapiens 41-53 7134791-4 1982 The high antithrombin III level in the Eskimos may at least partly be a consequence of a high dietary intake of polyunsaturated fatty acids. Fatty Acids, Unsaturated 112-139 serpin family C member 1 Homo sapiens 9-25 7083257-10 1982 These results suggest that the 6-sulfate group in unit 2 may be involved in antithrombin binding. Sulfates 33-40 serpin family C member 1 Homo sapiens 76-88 7083257-11 1982 It is concluded that the antithrombin binding site in heparin is represented by the pentasaccharide sequence extending from unit 2 to unit 6 of the octasaccharide studied. pentasaccharide 84-99 serpin family C member 1 Homo sapiens 25-37 7071806-1 1982 Antithrombin III (AT-III) was isolated by heparin affinity chromatography from adult venous and newborn term and preterm umbilical cord blood. Heparin 42-49 serpin family C member 1 Homo sapiens 0-16 7071806-1 1982 Antithrombin III (AT-III) was isolated by heparin affinity chromatography from adult venous and newborn term and preterm umbilical cord blood. Heparin 42-49 serpin family C member 1 Homo sapiens 18-24 6802163-2 1982 Normal and sclerotic CSs accelerated the inactivation of thrombin by antithrombin III to an equal extent. Chondroitin Sulfates 21-24 serpin family C member 1 Homo sapiens 69-85 6173074-11 1982 Cephalin was shown to inhibit the rate of reaction between factor Xa and antithrombin III. Phosphatidylethanolamines 0-8 serpin family C member 1 Homo sapiens 73-89 7059522-0 1982 A novel semi-synthetic sulphated polysaccharide with potent antithrombin activity. Polysaccharides 33-47 serpin family C member 1 Homo sapiens 60-72 7059522-10 1982 It is concluded that this new sulphated mucopolysaccharide acts as a pure antithrombin with a potency corresponding to 40--50 iu heparin/mg S-Lim. Glycosaminoglycans 40-58 serpin family C member 1 Homo sapiens 74-86 7059522-10 1982 It is concluded that this new sulphated mucopolysaccharide acts as a pure antithrombin with a potency corresponding to 40--50 iu heparin/mg S-Lim. Heparin 129-136 serpin family C member 1 Homo sapiens 74-86 6175043-0 1982 Antithrombin BM from human plasma: an antithrombin binding moderately to heparin. Heparin 73-80 serpin family C member 1 Homo sapiens 0-12 7073686-0 1982 Potentiation by calcium ions of the antithrombin III inhibition of thrombin. Calcium 16-23 serpin family C member 1 Homo sapiens 36-52 7064134-0 1982 Measurement of the heparin enhanced-antithrombin III/thrombin reaction rate in the presence of synthetic substrate. Heparin 19-26 serpin family C member 1 Homo sapiens 36-52 6175043-0 1982 Antithrombin BM from human plasma: an antithrombin binding moderately to heparin. Heparin 73-80 serpin family C member 1 Homo sapiens 38-50 6175043-3 1982 Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column. Heparin 93-100 serpin family C member 1 Homo sapiens 117-129 6175043-3 1982 Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column. Heparin 157-164 serpin family C member 1 Homo sapiens 117-129 7064134-2 1982 In essence the approach takes advantage of the fact that synthetic substrates, e.g. N-alpha-p-tosyl-L-glycyl-L-prolyl-L-arginine-p-nitroanilide, bind to the active site of thrombin, which slows the rate of reaction with antithrombin III. n-alpha-p-tosyl-l-glycyl-l-prolyl-l-arginine-p-nitroanilide 84-143 serpin family C member 1 Homo sapiens 220-236 6175043-3 1982 Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column. Heparin 157-164 serpin family C member 1 Homo sapiens 117-129 6175043-3 1982 Compared to the similar antithrombin III, this glycoprotein binds only moderately to porcine heparin (hence its name Antithrombin BM), thus requiring higher heparin concentration for full thrombin inhibitor function, and lower ionic strength for elution from a heparin sepharose column. Sepharose 269-278 serpin family C member 1 Homo sapiens 117-129 6175043-5 1982 From AT III, AT BM further differs in its absolute dependency on the presence of heparin(oids) for antithrombin activity, in its more pronounced inhibitory specificity largely restricted to thrombin, and in the absence of substantial immunological crossreaction with antibody to AT III. Heparin 81-88 serpin family C member 1 Homo sapiens 99-111 7053378-0 1982 Heparin with two binding sites for antithrombin or platelet factor 4. Heparin 0-7 serpin family C member 1 Homo sapiens 35-47 7053378-2 1982 This methodology is able to subdivide the active mucopolysaccharide pools of molecular weight 6,000 to 8,000 (LMW) or 18,000 to 22,000 (HMW) into various species with descending affinities for antithrombin as well as decreasing anticoagulant potencies. Glycosaminoglycans 49-67 serpin family C member 1 Homo sapiens 193-205 7053378-8 1982 The avidity of platelet factor 4 for HMW highly active heparin could not be quantitated but appears to be at least 10 to 100 times greater than that of antithrombin for mucopolysaccharide. Glycosaminoglycans 169-187 serpin family C member 1 Homo sapiens 152-164 7053378-6 1982 The stoichiometries of interaction of antithrombin and platelet factor 4 with HMW highly active heparin as determined by fluorescence spectroscopy indicated that 2 molecules of either protein are able to bind to 1 molecule of the mucopolysaccharide. Heparin 96-103 serpin family C member 1 Homo sapiens 38-50 7053378-6 1982 The stoichiometries of interaction of antithrombin and platelet factor 4 with HMW highly active heparin as determined by fluorescence spectroscopy indicated that 2 molecules of either protein are able to bind to 1 molecule of the mucopolysaccharide. Glycosaminoglycans 230-248 serpin family C member 1 Homo sapiens 38-50 7053378-7 1982 These studies also reveal that the binding of antithrombin to HMW highly active heparin is characterized by KDISSHAT = 5.0 X 10(-8) M and KDISSHAT2 = 1.0 x 10(-7) M, respectively. Heparin 80-87 serpin family C member 1 Homo sapiens 46-58 7055531-1 1982 Antithrombin III (At III) levels in plasma samples were determined by incubation of diluted plasma with thrombin, either with or without heparin. Heparin 137-144 serpin family C member 1 Homo sapiens 0-16 7055531-6 1982 Heat defibrination and ancrod defibrination methods are compared using the amidolytic heparin cofactor assay and it is shown that heat defibrination can cause the loss of nearly 50% of the functional At III in a reconstituted freeze-dried plasma which was used as a standard. Heparin 86-93 serpin family C member 1 Homo sapiens 200-206 7035043-0 1982 Paradoxical behaviour of antithrombin III during hemodialysis and its prevention with prostacyclin. Epoprostenol 86-98 serpin family C member 1 Homo sapiens 25-41 6176339-0 1982 [Separation and purification of antithrombin III, thrombin and carboxypeptidase N using affinity sorption on the copolymer hydroxyalkylmethacrylate with immobilized heparin (heparinoid)]. copolymer hydroxyalkylmethacrylate 113-147 serpin family C member 1 Homo sapiens 32-48 6187640-1 1982 Tri-calciumphosphate was found to have not only a known adsorption capacity for factors of the prothrombin complex, but also for antithrombin III. tricalcium phosphate 0-20 serpin family C member 1 Homo sapiens 129-145 6177612-0 1982 Benzamidine derivatives--relationship between antithrombin activity and structure. benzamidine 0-11 serpin family C member 1 Homo sapiens 46-58 7116792-5 1982 The haemorrhagic risk of continuing modest doses of heparin with high dose ATIII therapy appears small. Heparin 52-59 serpin family C member 1 Homo sapiens 75-80 6187640-4 1982 Liberating antithrombin III from calciumphosphate is made with care without using any concentrated salt solutions. calcium phosphate 33-49 serpin family C member 1 Homo sapiens 11-27 6187643-3 1982 Owing to the fact that a certain degree of antithrombin III level can be regarded as a prerequisite for a sufficient heparin effect the missing cofactor, antithrombin III, has to be absolutely substituted, if heparinization is necessary in the newborn period. Heparin 117-124 serpin family C member 1 Homo sapiens 43-59 6187643-3 1982 Owing to the fact that a certain degree of antithrombin III level can be regarded as a prerequisite for a sufficient heparin effect the missing cofactor, antithrombin III, has to be absolutely substituted, if heparinization is necessary in the newborn period. Heparin 117-124 serpin family C member 1 Homo sapiens 154-170 7117919-0 1982 Pregnancy in women with congenital antithrombin III deficiency: experience of treatment with heparin and antithrombin. Heparin 93-100 serpin family C member 1 Homo sapiens 35-47 6460338-4 1981 Treatment with sulphinpyrazone resulted in lengthening of both platelet and fibrinogen survival, a rise in ATIII but no change in the beta tg or PF4 concentrations. Sulfinpyrazone 15-30 serpin family C member 1 Homo sapiens 107-112 7164279-0 1982 Invalidation of concerns with long-term use of heparin: thrombin/antithrombin III interactions. Heparin 47-54 serpin family C member 1 Homo sapiens 65-81 7337233-0 1981 Fractionation of heparin using antithrombin III reversibly bound to concanavalin A-sepharose. Heparin 17-24 serpin family C member 1 Homo sapiens 31-47 7298649-6 1981 The extent of the increase in 8-anilino-1-naphthalene sulfonate fluorescence correlates roughly with the loss of antithrombin activity and with the extent of protein aggregation as determined by high pressure liquid chromatography. 8-anilino-1-naphthalenesulfonic acid 30-63 serpin family C member 1 Homo sapiens 113-125 7308558-0 1981 The antithrombin-binding sequence of heparin. Heparin 37-44 serpin family C member 1 Homo sapiens 4-16 7342649-0 1981 Vitamin K dependent clotting factors and their inhibitor--with special reference to prothrombin and antithrombin III. Vitamin K 0-9 serpin family C member 1 Homo sapiens 100-116 6462134-4 1981 Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx. Heparin 0-7 serpin family C member 1 Homo sapiens 90-106 6462134-4 1981 Heparin results in a minimum 20-fold rate enhancement of the reaction between plasmin and antithrombin III when the concentrations of heparin and plasmin are approx. Heparin 134-141 serpin family C member 1 Homo sapiens 90-106 6462134-7 1981 Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin. Heparin 0-7 serpin family C member 1 Homo sapiens 55-71 6462134-7 1981 Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin. Lysine 121-127 serpin family C member 1 Homo sapiens 55-71 6462134-7 1981 Heparin must bind to plasmin to accelerate the plasmin-antithrombin III reaction, since the modification of four to five lysine residues of the enzyme inhibits the rate-enhancement effect of heparin and the dissociation of heparin-plasmin complex decreases the inactivation rate of plasmin. Heparin 191-198 serpin family C member 1 Homo sapiens 55-71 6462134-8 1981 Increasing the concentration of antithrombin III, at a constant amount of heparin, results in increase of the inactivation rate. Heparin 74-81 serpin family C member 1 Homo sapiens 32-48 6462134-9 1981 By contrast, the effect of increasing the amount of plasmin in the presence of constant amount of heparin and antithrombin III is such that higher plasmin-to-heparin ratios are associated with lower rates of inactivation. Heparin 158-165 serpin family C member 1 Homo sapiens 110-126 6462134-11 1981 Arrhenius plots of the plasmin-antithrombin III reaction are linear both in the absence and presence of heparin, at concentrations of 1 or 2mug/ml, over a range of 26K. Heparin 104-111 serpin family C member 1 Homo sapiens 31-47 6800672-0 1981 Practical requirements for immunochemical analysis of antithrombin III in agarose gels. Sepharose 74-81 serpin family C member 1 Homo sapiens 54-70 6800672-1 1981 This report emphasizes the importance charged groups affixed to the agarose gel matrix have on immunoprecipitation of antithrombin III (AT) and of its protease complexes. Sepharose 68-75 serpin family C member 1 Homo sapiens 118-134 7337233-0 1981 Fractionation of heparin using antithrombin III reversibly bound to concanavalin A-sepharose. Sepharose 83-92 serpin family C member 1 Homo sapiens 31-47 6949499-4 1981 The activity of AT III, a progressive inhibitor of thrombin and cofactor of heparin, is always below 50% after L-asparaginase. Heparin 76-83 serpin family C member 1 Homo sapiens 16-22 7287751-0 1981 Binding of high affinity heparin to antithrombin III. Heparin 25-32 serpin family C member 1 Homo sapiens 36-52 7287752-0 1981 Binding of high affinity heparin to antithrombin III. Heparin 25-32 serpin family C member 1 Homo sapiens 36-52 7287752-2 1981 The kinetics of high affinity heparin binding to human antithrombin III has been studied by stopped flow fluorimetry, using the 40% antithrombin fluorescence enhancement resulting from this interaction. Heparin 30-37 serpin family C member 1 Homo sapiens 55-71 7287752-2 1981 The kinetics of high affinity heparin binding to human antithrombin III has been studied by stopped flow fluorimetry, using the 40% antithrombin fluorescence enhancement resulting from this interaction. Heparin 30-37 serpin family C member 1 Homo sapiens 55-67 7287752-3 1981 At mu 0.15, pH 7.4, and 25 degrees C, the observed pseudo-first order rate constant varies hyperbolically with heparin concentration with a limiting rate constant of 440 +/- 90 s-1, demonstrating that heparin binding is a two-step process involving a conformational change in antithrombin III. Heparin 111-118 serpin family C member 1 Homo sapiens 276-292 7287752-3 1981 At mu 0.15, pH 7.4, and 25 degrees C, the observed pseudo-first order rate constant varies hyperbolically with heparin concentration with a limiting rate constant of 440 +/- 90 s-1, demonstrating that heparin binding is a two-step process involving a conformational change in antithrombin III. Heparin 201-208 serpin family C member 1 Homo sapiens 276-292 6977940-7 1981 Elevation of the antithrombin III inhibitory activity in presence of heparin was apparently responsible for an increase in the antitryptic activity under conditions of severe forms of SH when content of alpha 1-antitrypsin decreased. Heparin 69-76 serpin family C member 1 Homo sapiens 17-33 7287752-4 1981 An identical dependence is produced when antithrombin is varied, consistent with a symmetrical mechanism in which heparin binding induces a conformational change in antithrombin rather than perturbing an equilibrium between two conformational states of the protein. Heparin 114-121 serpin family C member 1 Homo sapiens 41-53 7287752-4 1981 An identical dependence is produced when antithrombin is varied, consistent with a symmetrical mechanism in which heparin binding induces a conformational change in antithrombin rather than perturbing an equilibrium between two conformational states of the protein. Heparin 114-121 serpin family C member 1 Homo sapiens 165-177 7287752-5 1981 The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide. Heparin 55-62 serpin family C member 1 Homo sapiens 42-54 7287752-5 1981 The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide. Heparin 55-62 serpin family C member 1 Homo sapiens 196-208 7287752-5 1981 The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide. Heparin 147-154 serpin family C member 1 Homo sapiens 42-54 7287752-5 1981 The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide. Heparin 147-154 serpin family C member 1 Homo sapiens 42-54 7287752-5 1981 The rate constant for dissociation of the antithrombin-heparin complex is 1.1-1.5 s-1 at mu 0.15, as determined from the ordinate intercept at low heparin concentrations or by dissociation of the antithrombin-heparin complex with iodide. Iodides 230-236 serpin family C member 1 Homo sapiens 42-54 7287752-9 1981 A major function of the conformational change is, thus, to increase the affinity of heparin for antithrombin III greater than 300-fold. Heparin 84-91 serpin family C member 1 Homo sapiens 96-112 7287752-10 1981 The implications of these findings for the mechanism of the heparin-catalyzed inhibition of coagulation proteases by antithrombin III are discussed. Heparin 60-67 serpin family C member 1 Homo sapiens 117-133 7338523-1 1981 Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III. Heparin 19-26 serpin family C member 1 Homo sapiens 122-138 7338523-1 1981 Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III. Octasaccharide 84-98 serpin family C member 1 Homo sapiens 122-138 7338523-1 1981 Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III. Octasaccharide 84-98 serpin family C member 1 Homo sapiens 264-280 7338523-1 1981 Porcine intestinal heparin was partially digested with a purified heparinase and an octasaccharide with high-affinity for antithrombin III was isolated from the digest by gel filtration, followed by affinity chromatography on a column of Sepharose 4B coupled with antithrombin III. Sepharose 238-250 serpin family C member 1 Homo sapiens 122-138 7295594-0 1981 Abnormal migration of serum antithrombin III in patients on coumarin therapy by cross-immunoelectrophoresis. coumarin 60-68 serpin family C member 1 Homo sapiens 28-44 7338523-3 1981 Fifty percent inactivation activities of the octasaccharide for thrombin and factor Xa in the presence of antithrombin III were 2 and 6.5 times, respectively, higher than those of the initial heparin. Octasaccharide 45-59 serpin family C member 1 Homo sapiens 106-122 6800057-0 1981 Antithrombin III levels during heparin therapy. Heparin 31-38 serpin family C member 1 Homo sapiens 0-16 7029926-3 1981 In glomerular proteinuria (20 patients not on steroid therapy) the plasma level of AT III correlated inversely to the renal AT III clearance. Steroids 46-53 serpin family C member 1 Homo sapiens 83-89 7029926-4 1981 In contrast to liver cirrhosis and proteinuria, in septicaemia (33 patients) the ratio between AT III antigen (radial immunodiffusion) and functional AT III (heparin cofactor assay using a chromogenic substrate) demonstrated an excess of AT III antigen probably due to inactive AT III-enzyme complexes. Heparin 158-165 serpin family C member 1 Homo sapiens 150-156 7029926-4 1981 In contrast to liver cirrhosis and proteinuria, in septicaemia (33 patients) the ratio between AT III antigen (radial immunodiffusion) and functional AT III (heparin cofactor assay using a chromogenic substrate) demonstrated an excess of AT III antigen probably due to inactive AT III-enzyme complexes. Heparin 158-165 serpin family C member 1 Homo sapiens 150-156 7029926-4 1981 In contrast to liver cirrhosis and proteinuria, in septicaemia (33 patients) the ratio between AT III antigen (radial immunodiffusion) and functional AT III (heparin cofactor assay using a chromogenic substrate) demonstrated an excess of AT III antigen probably due to inactive AT III-enzyme complexes. Heparin 158-165 serpin family C member 1 Homo sapiens 150-156 7314061-0 1981 Bidimensional immunoelectrophoresis abnormal migration of serum antithrombin III in coumarin-treated patients. coumarin 84-92 serpin family C member 1 Homo sapiens 64-80 7330836-0 1981 Studies on the neutralizing mechanism of antithrombin activity of heparin by protamine. Heparin 66-73 serpin family C member 1 Homo sapiens 41-53 7316178-0 1981 A method for rapid quantitation and preparation of antithrombin III--high-affinity heparin fractions. Heparin 83-90 serpin family C member 1 Homo sapiens 51-67 7272219-3 1981 Their half-time of AT III elimination was 8.4--13.6 h. The patient in whom AT III concentrate was injected at the start of heparin therapy showed a very rapid decrease of AT III activity with a three-fold increase in the elimination rate constant. Heparin 123-130 serpin family C member 1 Homo sapiens 75-81 7325974-0 1981 The structure of heparin oligosaccharide fragments with high anti-(factor Xa) activity containing the minimal antithrombin III-binding sequence. heparin oligosaccharide 17-40 serpin family C member 1 Homo sapiens 110-126 7325974-3 1981 spectra of heparin oligosaccharides (essentially octasaccharides), having high affinity for antithrombin III and high anti-(Factor Xa) activity, prepared by three independent approaches (extraction, partial deaminative cleavage with HNO2 and partial depolymerization with bacterial heparinase), leading to different terminal residues, have been studied and compared with those of the corresponding inactive species. heparin oligosaccharides 11-35 serpin family C member 1 Homo sapiens 92-108 7325974-3 1981 spectra of heparin oligosaccharides (essentially octasaccharides), having high affinity for antithrombin III and high anti-(Factor Xa) activity, prepared by three independent approaches (extraction, partial deaminative cleavage with HNO2 and partial depolymerization with bacterial heparinase), leading to different terminal residues, have been studied and compared with those of the corresponding inactive species. octasaccharides 49-64 serpin family C member 1 Homo sapiens 92-108 6167624-5 1981 The shared antigenic determinant appeared to be carbohydrate in nature in that native and guanidine-treated AT III, but not periodate oxidized AT III, were capable of inhibiting the mitogenic activity of the serum when added continuously to the cultures. Carbohydrates 48-60 serpin family C member 1 Homo sapiens 108-114 6167624-5 1981 The shared antigenic determinant appeared to be carbohydrate in nature in that native and guanidine-treated AT III, but not periodate oxidized AT III, were capable of inhibiting the mitogenic activity of the serum when added continuously to the cultures. Guanidine 90-99 serpin family C member 1 Homo sapiens 108-114 7272219-1 1981 The rate of elimination of injected antithrombin III (AT III) concentrate was investigated by measuring plasma AT III levels in two control subjects and four patients treated with continuous intravenous infusion of heparin. Heparin 215-222 serpin family C member 1 Homo sapiens 36-52 7272219-1 1981 The rate of elimination of injected antithrombin III (AT III) concentrate was investigated by measuring plasma AT III levels in two control subjects and four patients treated with continuous intravenous infusion of heparin. Heparin 215-222 serpin family C member 1 Homo sapiens 54-60 7302889-2 1981 The endothelial cell At-III (EC-At-III) consists of a small fraction similar to plasma At-III and a larger fraction with decreased heparin-binding as tested by crossed immunoelectrophoresis. Heparin 131-138 serpin family C member 1 Homo sapiens 21-27 7302889-3 1981 However, both the anti-Xa and thrombin-neutralizing activities of the EC-At-III were rapid and active even in the absence of added heparin. Heparin 131-138 serpin family C member 1 Homo sapiens 73-79 7026867-1 1981 The paper contains new data on the pharmacodynamics of heparin and its interaction with the Xa factor, antithrombin III and thrombin. Heparin 55-62 serpin family C member 1 Homo sapiens 103-119 7272219-3 1981 Their half-time of AT III elimination was 8.4--13.6 h. The patient in whom AT III concentrate was injected at the start of heparin therapy showed a very rapid decrease of AT III activity with a three-fold increase in the elimination rate constant. Heparin 123-130 serpin family C member 1 Homo sapiens 19-25 7272219-3 1981 Their half-time of AT III elimination was 8.4--13.6 h. The patient in whom AT III concentrate was injected at the start of heparin therapy showed a very rapid decrease of AT III activity with a three-fold increase in the elimination rate constant. Heparin 123-130 serpin family C member 1 Homo sapiens 75-81 6113018-1 1981 1 The ability of several sulphated polysaccharide anticoagulants to prevent alpha 1-antitrypsin inhibition of thrombin paralleled their ability to potentiate antithrombin III inhibition of thrombin. Polysaccharides 35-49 serpin family C member 1 Homo sapiens 158-174 7284440-1 1981 Purified antithrombin III has been reported to have bound glucocerebroside, the major glycolipid of plasma. Glucosylceramides 58-74 serpin family C member 1 Homo sapiens 9-25 7284440-1 1981 Purified antithrombin III has been reported to have bound glucocerebroside, the major glycolipid of plasma. Glycolipids 86-96 serpin family C member 1 Homo sapiens 9-25 6113018-3 1981 2 These results are consistent with the possibility that a direct polysaccharide-proteinase interaction may be involved in the sulphated polysaccharide-modulated inhibition of thrombin by antithrombin III. Polysaccharides 66-80 serpin family C member 1 Homo sapiens 188-204 7267980-3 1981 In the present research, AT III has been determined both as substance concentration, by radial immunodiffusion, and on the base of its activity on a chromogenic substrate (Chromozym) in patients with DIC before and after heparin therapy. Heparin 221-228 serpin family C member 1 Homo sapiens 25-31 6790279-1 1981 Previous studies have shown that a modified form of antithrombin, cleaved at a single Arg-Ser bond near the carboxy-terminal end of the chain, is formed during the reaction with thrombin concurrent with the formation of the inactive enzyme-inhibitor complex. Arginine 86-89 serpin family C member 1 Homo sapiens 52-64 6790279-1 1981 Previous studies have shown that a modified form of antithrombin, cleaved at a single Arg-Ser bond near the carboxy-terminal end of the chain, is formed during the reaction with thrombin concurrent with the formation of the inactive enzyme-inhibitor complex. Serine 90-93 serpin family C member 1 Homo sapiens 52-64 7292454-0 1981 Antithrombin III in patients treated with subcutaneous or intravenous heparin. Heparin 70-77 serpin family C member 1 Homo sapiens 0-16 7245036-8 1981 Antithrombin deficiency should be suspected when there is an unusual propensity to develop thrombus, when heparin cannot prolong coagulation time, and when measurements show reduced levels of antithrombin. Heparin 106-113 serpin family C member 1 Homo sapiens 0-12 7317004-0 1981 Dansyl (5-dimethylaminonaphthalene-1-sulphonyl)-heparin binds antithrombin III and platelet factor 4 at separate sites. dansyl (5-dimethylaminonaphthalene-1-sulphonyl)-heparin 0-55 serpin family C member 1 Homo sapiens 62-78 7317004-1 1981 Antithrombin III binds to, and thereby augments the fluorescence of, dansyl-(5-dimethylaminonaphthalene-1-sulphonyl)-heparin; platelet factor 4 binding to the fluorescent heparin has little of this effect. dansyl-(5-dimethylaminonaphthalene-1-sulphonyl)-heparin 69-124 serpin family C member 1 Homo sapiens 0-16 7317004-1 1981 Antithrombin III binds to, and thereby augments the fluorescence of, dansyl-(5-dimethylaminonaphthalene-1-sulphonyl)-heparin; platelet factor 4 binding to the fluorescent heparin has little of this effect. Heparin 117-124 serpin family C member 1 Homo sapiens 0-16 7317004-2 1981 Competition studies in which antithrombin III competes with platelet factor 4 for heparin binding demonstrate that heparin can simultaneously bind both proteins. Heparin 82-89 serpin family C member 1 Homo sapiens 29-45 7462246-0 1981 The antithrombin-binding sequence of heparin. Heparin 37-44 serpin family C member 1 Homo sapiens 4-16 7238175-1 1981 The low-dose heparin prophylaxis depends upon a low-level activation of antithrombin III to prevent thrombin generation. Heparin 13-20 serpin family C member 1 Homo sapiens 72-88 7236529-0 1981 Thrombin-induced proteolysis of human antithrombin III: an outstanding contribution of heparin. Heparin 87-94 serpin family C member 1 Homo sapiens 38-54 7236529-1 1981 Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin. Heparin 96-103 serpin family C member 1 Homo sapiens 40-56 7236529-1 1981 Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin. Heparin 96-103 serpin family C member 1 Homo sapiens 58-64 7236529-1 1981 Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin. Heparin 96-103 serpin family C member 1 Homo sapiens 152-158 7236529-1 1981 Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin. Heparin 202-209 serpin family C member 1 Homo sapiens 40-56 7236529-1 1981 Products obtained in reaction of excess antithrombin III (AT III) with human alpha-thrombin and heparin were found to contain markedly less of residual AT III than products of similar reactions without heparin. Heparin 202-209 serpin family C member 1 Homo sapiens 58-64 7236529-4 1981 The optimum amount of heparin required to facilitate AT III proteolysis was of 5 microgram/ml (0.8 u/ml). Heparin 22-29 serpin family C member 1 Homo sapiens 53-59 7236529-5 1981 Excessive reduction of the residual inhibitory activity and changes in two-dimensional immunoelectrophoresis suggested that AT III in plasma is also subjected to nonproductive proteolysis and formation of a modified AT III derivative following addition of thrombin and heparin. Heparin 269-276 serpin family C member 1 Homo sapiens 124-130 7236529-5 1981 Excessive reduction of the residual inhibitory activity and changes in two-dimensional immunoelectrophoresis suggested that AT III in plasma is also subjected to nonproductive proteolysis and formation of a modified AT III derivative following addition of thrombin and heparin. Heparin 269-276 serpin family C member 1 Homo sapiens 216-222 7236529-6 1981 These data indicate that the effect of heparin on AT III is more complex than generally recognized. Heparin 39-46 serpin family C member 1 Homo sapiens 50-56 7236529-7 1981 On the one hand, heparin interacting with AT III and thrombin contributes to a rapid binding and neutralization of the enzyme; on the other, heparin facilitates proteolytic degradation of unbound inhibitor even in the presence of small quantities of thrombin accounting for excessive reduction of the overall inhibitory potential of AT III. Heparin 17-24 serpin family C member 1 Homo sapiens 42-48 7236529-7 1981 On the one hand, heparin interacting with AT III and thrombin contributes to a rapid binding and neutralization of the enzyme; on the other, heparin facilitates proteolytic degradation of unbound inhibitor even in the presence of small quantities of thrombin accounting for excessive reduction of the overall inhibitory potential of AT III. Heparin 17-24 serpin family C member 1 Homo sapiens 333-339 7218490-2 1981 Both patients had abnormally low antithrombin III levels, which improved to normal levels with warfarin ;sodium therapy. Warfarin 95-103 serpin family C member 1 Homo sapiens 33-49 7215671-0 1981 Effect of dithiothreitol on the modulation of antithrombin III activity by sulphated polysaccharides. Dithiothreitol 10-24 serpin family C member 1 Homo sapiens 46-62 7226527-1 1981 When compared to values obtained in healthy normolipidemic normal weight control subjects, the plasma antithrombin III level determined by immunological, clotting and thrombin-agarose diffusion techniques was found to be obviously decreased in patients with decompensated cirrhosis of the liver and slightly but significantly increased in hyperlipidemic and especially in hypertriglyceridemic subjects. Sepharose 176-183 serpin family C member 1 Homo sapiens 102-118 7226527-2 1981 Plasma antithrombin III was positively correlated with serum cholesterol level, the logarithm of serum triglyceride concentration and serum pseudocholinesterase activity. Cholesterol 61-72 serpin family C member 1 Homo sapiens 7-23 7226527-2 1981 Plasma antithrombin III was positively correlated with serum cholesterol level, the logarithm of serum triglyceride concentration and serum pseudocholinesterase activity. Triglycerides 103-115 serpin family C member 1 Homo sapiens 7-23 7226527-4 1981 It is suggested that the accelerated fatty acid and lipoprotein turnover occurring in many subjects with type IIb and type IV hyperlipoproteinemia might be accompanied by an enhanced hepatic protein synthesis involving various liver secretion enzymes and clotting factors as well as antithrombin III. Fatty Acids 37-47 serpin family C member 1 Homo sapiens 283-299 7213813-1 1981 Binding constants for the binding of high-affinity heparin to antithrombin at different ionic strengths were determined by fluorescence titrations and were also estimated from dissociation curves of the heparin-antithrombin complex. Heparin 51-58 serpin family C member 1 Homo sapiens 62-74 7213813-1 1981 Binding constants for the binding of high-affinity heparin to antithrombin at different ionic strengths were determined by fluorescence titrations and were also estimated from dissociation curves of the heparin-antithrombin complex. Heparin 51-58 serpin family C member 1 Homo sapiens 211-223 7305940-1 1981 The interaction between bovine antithrombin, a plasma proteinase inhibitor, and heparin species of different molecular weights was studied. Heparin 80-87 serpin family C member 1 Homo sapiens 31-43 7305940-8 1981 difference absorption studies showed that the non-adsorbed heparin fraction bound to antithrombin in solution with a binding constant at physiological ionic strength only slightly lower than that of low-affinity heparin. Heparin 59-66 serpin family C member 1 Homo sapiens 85-97 6914196-0 1981 The molecular-weight dependence of the rate-enhancing effect of heparin on the inhibition of thrombin, factor Xa, factor IXa, factor XIa, factor XIIa and kallikrein by antithrombin. Heparin 64-71 serpin family C member 1 Homo sapiens 168-180 7215671-0 1981 Effect of dithiothreitol on the modulation of antithrombin III activity by sulphated polysaccharides. Polysaccharides 85-100 serpin family C member 1 Homo sapiens 46-62 6160891-2 1981 In the presence of heparin (incorporated into the agarose gel matrix), the AT-III of normal human plasma was separated into four components: two major, faster-moving components, and two minor, slower-moving components. Heparin 19-26 serpin family C member 1 Homo sapiens 75-81 6940150-2 1981 Direct measurements of the kinetic behavior of the hexasaccharides, octasaccharides, and decasaccharides showed that these fractions greatly enhanced the rate of Factor Xa inactivation by antithrombin. hexasaccharides 51-66 serpin family C member 1 Homo sapiens 188-200 6783500-3 1981 Dependent on enzyme concentration, however, granulocytic elastase induced progressive inactivation of antithrombin III leading to an almost complete loss of the thrombin inhibitory activity at a molar ratio of elastase: antithrombin III = 0.4:1 within 5 min at 25 degrees C. Antithrombin III is not drastically degraded by elastase as revealed by polyacrylamide gel electrophoretic and rocket immunoelectrophoretic investigations. polyacrylamide 347-361 serpin family C member 1 Homo sapiens 102-118 6783500-5 1981 This indicates that heparin binding sites of antithrombin III are occupied or affected by the elastase-induced peptide bond cleavage(s). Heparin 20-27 serpin family C member 1 Homo sapiens 45-61 6940150-2 1981 Direct measurements of the kinetic behavior of the hexasaccharides, octasaccharides, and decasaccharides showed that these fractions greatly enhanced the rate of Factor Xa inactivation by antithrombin. decasaccharides 89-104 serpin family C member 1 Homo sapiens 188-200 6940150-5 1981 The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain. hexasaccharides 19-34 serpin family C member 1 Homo sapiens 313-325 6940150-5 1981 The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain. hexasaccharides 19-34 serpin family C member 1 Homo sapiens 367-379 6940150-5 1981 The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain. decasaccharides 57-72 serpin family C member 1 Homo sapiens 313-325 6940150-5 1981 The avidity of the hexasaccharides, octasaccharides, and decasaccharides for the protease inhibitor increased as a function of size with the respective dissociation constants ranging from 5.5 X 10(-6) M to 2.9 X 10(-7) M. These data suggest that the region of the heparin molecule needed for catalyzing Factor Xa-antithrombin interaction is intimately related to the antithrombin binding domain. decasaccharides 57-72 serpin family C member 1 Homo sapiens 367-379 6940150-6 1981 The smallest complex carbohydrate fragment that accelerated the inactivation of thrombin by antithrombin had approximately 14 residues. Carbohydrates 21-33 serpin family C member 1 Homo sapiens 92-104 7471127-0 1981 The antithrombin-binding sequence of heparin studied by n.m.r. Heparin 37-44 serpin family C member 1 Homo sapiens 4-16 6455833-0 1981 The effects of orchiectomy, oestrogens and cyproterone-acetate on the antithrombin-III concentration in carcinoma of the prostate. Cyproterone Acetate 43-62 serpin family C member 1 Homo sapiens 70-86 6943957-9 1981 The antithrombotic action of heparin depends on a normal quantity of plasma AT-III. Heparin 29-36 serpin family C member 1 Homo sapiens 76-82 6783633-0 1981 Preparation of biologically active fluorescent heparin composed of fluorescein-labeled species and its behavior to antithrombin III. Heparin 47-54 serpin family C member 1 Homo sapiens 115-131 6783633-0 1981 Preparation of biologically active fluorescent heparin composed of fluorescein-labeled species and its behavior to antithrombin III. Fluorescein 67-78 serpin family C member 1 Homo sapiens 115-131 6783633-4 1981 The fluorescent heparin was separated into the low-affinity (56.6%) and high-affinity (43.4%) fractions for antithrombin III, and the anticoagulant activities of the two types of fluorescent heparin were compared with those of the starting heparin and the partially N-desulfated heparin, suggesting that FTC-substitution in heparin molecules had no effect on the known biological interaction with mobilized or immobilized antithrombin III. Heparin 16-23 serpin family C member 1 Homo sapiens 108-124 7039127-4 1981 The enhanced activity of antithrombin III, found most frequently in the treatment with indirect anticoagulants, renal transplantations, and application of anabolic steroids, has given no data of clinical importance so far. Steroids 164-172 serpin family C member 1 Homo sapiens 25-41 6168228-0 1981 The interaction of protein-bound heparin and antithrombin III. Heparin 33-40 serpin family C member 1 Homo sapiens 45-61 6168228-1 1981 When commercially prepared porcine mucosal heparin is added to human plasma, some of the heparin fractions form a complex with antithrombin III activating it to an immediate inhibitor of thrombin as well as of other serine proteases. Heparin 43-50 serpin family C member 1 Homo sapiens 127-143 6168228-1 1981 When commercially prepared porcine mucosal heparin is added to human plasma, some of the heparin fractions form a complex with antithrombin III activating it to an immediate inhibitor of thrombin as well as of other serine proteases. Heparin 89-96 serpin family C member 1 Homo sapiens 127-143 6168228-4 1981 Protamine sulfate inactivates those heparin fractions that bind to antithrombin III but not those bound to alpha 2-macroglobulin. Heparin 36-43 serpin family C member 1 Homo sapiens 67-83 6791550-0 1981 Heparin binding and protease inhibitor activity of chemically modified antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 71-87 7225714-2 1981 2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin. Dermatan Sulfate 7-24 serpin family C member 1 Homo sapiens 81-87 7225714-2 1981 2 Only dermatan sulphate preparations of considerable heparin content potentiate AT III inhibition of thrombin, factor Xa and plasmin. Heparin 54-61 serpin family C member 1 Homo sapiens 81-87 7281335-0 1981 [Thrombosis patients with familial antithrombin-III deficiency treated with heparin and antithrombin]. Heparin 76-83 serpin family C member 1 Homo sapiens 35-47 6455833-6 1981 During cyproterone-acetate treatment there was a slight but significant increase in AT-III at 2 months. Cyproterone Acetate 7-26 serpin family C member 1 Homo sapiens 84-90 7469415-0 1980 Binding of heparin to antithrombin III: The use of dansyl and rhodamine labels. Heparin 11-18 serpin family C member 1 Homo sapiens 22-38 6781095-3 1980 Affinity chromatography on antithrombin-Sepharose separated a distinct high-affinity fraction (4-5% of the total material). Sepharose 40-49 serpin family C member 1 Homo sapiens 27-39 7236660-3 1980 Antithrombin III, the major contaminant after affinity chromatography with heparin-Sepharose 4B, could be removed by gel filtration on Bio-Gel A-5m. Heparin 75-82 serpin family C member 1 Homo sapiens 0-16 7236660-3 1980 Antithrombin III, the major contaminant after affinity chromatography with heparin-Sepharose 4B, could be removed by gel filtration on Bio-Gel A-5m. Sepharose 83-95 serpin family C member 1 Homo sapiens 0-16 7213665-5 1980 The data obtained from affinity chromatography of these fractions on antithrombin III-Sepharose also substantiated the observed difference in anticoagulant activity. Sepharose 86-95 serpin family C member 1 Homo sapiens 69-85 7459342-6 1980 The anticoagulant activity of heparin, determined in an antithrombin III activation assay, was markedly reduced after treatment with the heparitinase. Heparin 30-37 serpin family C member 1 Homo sapiens 56-72 7469415-0 1980 Binding of heparin to antithrombin III: The use of dansyl and rhodamine labels. Rhodamines 62-71 serpin family C member 1 Homo sapiens 22-38 6448845-1 1980 A low molecular weight preparation of porcine heparin (specific anticoagulation activity = 125 units/mg) was fractionated to obtain a mucopolysaccharide product of 6500 daltons (specific anticoagulant activity = 373 units/mg) that is homogeneous with respect to its interaction with antithrombin. Glycosaminoglycans 134-152 serpin family C member 1 Homo sapiens 283-295 6448845-3 1980 Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion. Fluorescamine 30-43 serpin family C member 1 Homo sapiens 115-127 6448845-3 1980 Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion. Heparin 44-51 serpin family C member 1 Homo sapiens 115-127 6448845-3 1980 Initially, we showed that the fluorescamine-heparin conjugate and the unlabeled mucopolysaccharide interacted with antithrombin in a virtually identical fashion. Glycosaminoglycans 80-98 serpin family C member 1 Homo sapiens 115-127 6448846-0 1980 The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin. Heparin 100-107 serpin family C member 1 Homo sapiens 34-46 6448846-1 1980 The kinetics of inhibition of four hemostatic system enzymes by antithrombin were examined as a function of heparin concentration. Heparin 108-115 serpin family C member 1 Homo sapiens 64-76 6448846-17 1980 Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor. Heparin 43-50 serpin family C member 1 Homo sapiens 54-66 7457802-1 1980 Dependence of the effect of heparin on the activity of antithrombin III (author"s transl)]. Heparin 28-35 serpin family C member 1 Homo sapiens 55-71 6448846-17 1980 Thus, our data demonstrate that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor. Glycosaminoglycans 87-105 serpin family C member 1 Homo sapiens 54-66 7457802-4 1980 A distinct relation was found between the effect of heparin on the aPTT and on the thrombin clotting time and the activity of antithrombin III. Heparin 52-59 serpin family C member 1 Homo sapiens 126-142 6448846-18 1980 Furthermore, a careful comparison of the various constants suggests that the direct interaction between heparin and antithrombin may be largely responsible for the kinetic effect of this mucopolysaccharide. Heparin 104-111 serpin family C member 1 Homo sapiens 116-128 7457802-6 1980 Since this effect is of primary importance for the efficacy of prophylaxis of DIC, regular assays of antithrombin III are proposed in shock patients receiving heparin. Heparin 159-166 serpin family C member 1 Homo sapiens 101-117 7457881-0 1980 Immobilization of heparin with trichloro-s-triazine: purification of mouse antithrombin. Heparin 18-25 serpin family C member 1 Homo sapiens 75-87 6448846-18 1980 Furthermore, a careful comparison of the various constants suggests that the direct interaction between heparin and antithrombin may be largely responsible for the kinetic effect of this mucopolysaccharide. Glycosaminoglycans 187-205 serpin family C member 1 Homo sapiens 116-128 7449596-9 1980 Our observation that depression of AT III levels in young diabetic females was closely correlated with elevations of fasting serum glucose and HbA1 suggests that strict diabetic control may help prevent hypercoagulability in diabetes. Glucose 131-138 serpin family C member 1 Homo sapiens 35-41 7457881-0 1980 Immobilization of heparin with trichloro-s-triazine: purification of mouse antithrombin. cyanuric chloride 31-51 serpin family C member 1 Homo sapiens 75-87 7239054-0 1980 [Determination of antithrombin III in a group workers with long-term exposure to carbon disulfide (CS2)]. Carbon Disulfide 81-97 serpin family C member 1 Homo sapiens 18-34 7437065-0 1980 The interaction of heparin with thrombin and antithrombin. Heparin 19-26 serpin family C member 1 Homo sapiens 45-57 6776145-7 1980 A complex with antithrombin III is detected by dodecyl sulfate gel electrophoresis. dodecyl sulfate 47-62 serpin family C member 1 Homo sapiens 15-31 6935668-0 1980 Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin. Glucosamine 28-41 serpin family C member 1 Homo sapiens 57-69 6935668-0 1980 Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin. Heparin 90-97 serpin family C member 1 Homo sapiens 57-69 6935668-1 1980 An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid. Octasaccharide 3-17 serpin family C member 1 Homo sapiens 41-53 6935668-1 1980 An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid. Heparin 105-112 serpin family C member 1 Homo sapiens 41-53 6935668-1 1980 An octasaccharide with high affinity for antithrombin was isolated after partial deaminative cleavage of heparin with nitrous acid. Nitrous Acid 118-130 serpin family C member 1 Homo sapiens 41-53 6935668-6 1980 Similar treatment of an analogous tetrasaccharide derived from heparin with low affinity for antithrombin failed to produce any disulfated anhydromannitol. tetrasaccharide 34-49 serpin family C member 1 Homo sapiens 93-105 6935668-7 1980 These results suggest that 3-sulfated glucosamine is a unique component of high-affinity heparin, located at a specific position in the antithrombin-binding sequence of the molecule. 3-sulfated glucosamine 27-49 serpin family C member 1 Homo sapiens 136-148 6935668-7 1980 These results suggest that 3-sulfated glucosamine is a unique component of high-affinity heparin, located at a specific position in the antithrombin-binding sequence of the molecule. Heparin 89-96 serpin family C member 1 Homo sapiens 136-148 6450073-0 1980 Modification by anionic polysaccharides of the antithrombin III inhibition of plasmin. Polysaccharides 24-39 serpin family C member 1 Homo sapiens 47-63 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 0-22 serpin family C member 1 Homo sapiens 71-87 7209874-0 1980 Preparation and partial characterization of human plasma depleted of antithrombin-III by heparin-sepharose affinity chromatography. Heparin 89-96 serpin family C member 1 Homo sapiens 69-85 7209874-0 1980 Preparation and partial characterization of human plasma depleted of antithrombin-III by heparin-sepharose affinity chromatography. Sepharose 97-106 serpin family C member 1 Homo sapiens 69-85 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 0-22 serpin family C member 1 Homo sapiens 145-161 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 24-27 serpin family C member 1 Homo sapiens 71-87 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. Sodium Dodecyl Sulfate 24-27 serpin family C member 1 Homo sapiens 145-161 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. polyacrylamide 29-43 serpin family C member 1 Homo sapiens 71-87 7426659-11 1980 Sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the antithrombin III/venom proteinase reaction mixtures indicated that intact antithrombin III (63 000 daltons) was converted to an inactive form (57 500 daltons) by limited proteolysis. polyacrylamide 29-43 serpin family C member 1 Homo sapiens 145-161 7213342-4 1980 Discontinuous polyacrylamide-gel electrophoresis of the reduced dissociation fragments of the complex in the presence of sodium dodecyl sulphate reveals two antithrombin III bands that do not resolve during electrophoresis without reduction. polyacrylamide 14-28 serpin family C member 1 Homo sapiens 157-173 7426659-13 1980 The inactivating cleavage occurred within a disulfide loop of the antithrombin III molecule, since the lower molecular weight species was detected only under reducing conditions. Disulfides 44-53 serpin family C member 1 Homo sapiens 66-82 7213342-4 1980 Discontinuous polyacrylamide-gel electrophoresis of the reduced dissociation fragments of the complex in the presence of sodium dodecyl sulphate reveals two antithrombin III bands that do not resolve during electrophoresis without reduction. Sodium Dodecyl Sulfate 121-144 serpin family C member 1 Homo sapiens 157-173 7213342-11 1980 The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s). Arginine 117-125 serpin family C member 1 Homo sapiens 50-66 7213342-11 1980 The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s). Arginine 140-148 serpin family C member 1 Homo sapiens 50-66 7213342-2 1980 Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. Carbon-14 63-66 serpin family C member 1 Homo sapiens 22-38 7213342-2 1980 Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. Carbon-14 63-66 serpin family C member 1 Homo sapiens 140-156 7213342-2 1980 Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. methoxyamine 67-93 serpin family C member 1 Homo sapiens 22-38 7349668-5 1980 Thrombin and Factor Xa were instantaneously inhibited by AT III in the presence of soluble heparin. Heparin 91-98 serpin family C member 1 Homo sapiens 57-63 7213342-2 1980 Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. methoxyamine 67-93 serpin family C member 1 Homo sapiens 140-156 7213342-2 1980 Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. Carbon-14 127-130 serpin family C member 1 Homo sapiens 22-38 7213342-2 1980 Cleavage of the human antithrombin III--thrombin complex with [14C]methoxyamine hydrochloride results in inactive thrombin and 14C-labelled antithrombin III. Carbon-14 127-130 serpin family C member 1 Homo sapiens 140-156 7213342-11 1980 The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s). carboxylic ester 165-181 serpin family C member 1 Homo sapiens 50-66 7213342-11 1980 The results indicate that during formation of the antithrombin III--thrombin complex, the inhibitor is cleaved at an arginine--X bond; this arginine residue forms a carboxylic ester with the enzyme, while the excised polypeptide remains bound through a disulphide bridge(s). disulphide 253-263 serpin family C member 1 Homo sapiens 50-66 7444870-1 1980 Correlation between the anticoagulant activity of the fractions and their content of heparin with high affinity for antithrombin. Heparin 85-92 serpin family C member 1 Homo sapiens 116-128 7417484-0 1980 Effects of the reduction and S-carbamidomethylation on the conformation, activity and heparin-binding capacity of human antithrombin III. Heparin 86-93 serpin family C member 1 Homo sapiens 120-136 6159941-1 1980 1 Comparison of the effects of sulphated polysaccharides on thrombin-induced clotting of normal and antithrombin III-deficient plasmas suggests the involvement of antithrombin III (AT III) in the anticoagulant activities of cellulose, dextran and xylan sulphates. Dextrans 235-242 serpin family C member 1 Homo sapiens 181-187 7417484-1 1980 Antithrombin III has been shown to contain three disulphide bridges. disulphide 49-59 serpin family C member 1 Homo sapiens 0-16 7417484-8 1980 The reduction and S-carbamidomethylation of antithrombin III induces some local changes in the tertiary structure affecting the inhibitor activity, heparin binding and near-ultraviolet circular dichroic spectrum, but do not seem to induce any substantial general conformation change. Heparin 148-155 serpin family C member 1 Homo sapiens 44-60 7407200-6 1980 Approximately stoichiometric amounts of heparin completely inhibited the reaction of papain with antithrombin. Heparin 40-47 serpin family C member 1 Homo sapiens 97-109 7409165-0 1980 The molecular size of the antithrombin-binding sequence in heparin. Heparin 59-66 serpin family C member 1 Homo sapiens 26-38 7406509-0 1980 Tryptophan residue at the heparin binding site in antithrombin III. Tryptophan 0-10 serpin family C member 1 Homo sapiens 50-66 7406509-0 1980 Tryptophan residue at the heparin binding site in antithrombin III. Heparin 26-33 serpin family C member 1 Homo sapiens 50-66 6159941-1 1980 1 Comparison of the effects of sulphated polysaccharides on thrombin-induced clotting of normal and antithrombin III-deficient plasmas suggests the involvement of antithrombin III (AT III) in the anticoagulant activities of cellulose, dextran and xylan sulphates. xylan sulphates 247-262 serpin family C member 1 Homo sapiens 181-187 7406510-0 1980 Structural studies of the carbohydrate moiety of human antithrombin III. Carbohydrates 26-38 serpin family C member 1 Homo sapiens 55-71 7007650-4 1980 We suggest that the migrating leucocytes on their cell membranes have receptors, composed of AT III-like molecules, which are blocked or destroyed, by forming complexes with heparin and thrombin. Heparin 174-181 serpin family C member 1 Homo sapiens 93-99 6159941-1 1980 1 Comparison of the effects of sulphated polysaccharides on thrombin-induced clotting of normal and antithrombin III-deficient plasmas suggests the involvement of antithrombin III (AT III) in the anticoagulant activities of cellulose, dextran and xylan sulphates. Cellulose 224-233 serpin family C member 1 Homo sapiens 181-187 6157479-3 1980 In several ways PN resembles antithrombin III (AT3), a prominent inhibitor of thrombin in serum: PN links thrombin, probably via an ester bond; PN does not link thrombin blocked at its catalytic site serine; PN has a high-affinity heparin-binding site; and heparin greatly accelerates the rate of linkage between soluble PN and thrombin. Heparin 231-238 serpin family C member 1 Homo sapiens 47-50 6157479-3 1980 In several ways PN resembles antithrombin III (AT3), a prominent inhibitor of thrombin in serum: PN links thrombin, probably via an ester bond; PN does not link thrombin blocked at its catalytic site serine; PN has a high-affinity heparin-binding site; and heparin greatly accelerates the rate of linkage between soluble PN and thrombin. Heparin 257-264 serpin family C member 1 Homo sapiens 47-50 7444377-4 1980 The patient was treated with human AT III concentrate as a result of the development of progressive disseminated intravascular coagulation (DIC), the further deterioration of renal function, the risk for thromboembolic complications and the possible adverse effects of heparin therapy. Heparin 269-276 serpin family C member 1 Homo sapiens 35-41 7372626-0 1980 Structural studies on the carbohydrate portion of human antithrombin III. Carbohydrates 26-38 serpin family C member 1 Homo sapiens 56-72 7455972-2 1980 We obtained different antithrombin III patterns in the plasma of the affected members of the two families with the modified two dimensional immunoelectrophoresis method (heparin in agarose). Heparin 170-177 serpin family C member 1 Homo sapiens 22-38 7455972-2 1980 We obtained different antithrombin III patterns in the plasma of the affected members of the two families with the modified two dimensional immunoelectrophoresis method (heparin in agarose). Sepharose 181-188 serpin family C member 1 Homo sapiens 22-38 7455972-5 1980 The relatively low affinity of this antithrombin III to heparin could be directly proved by the heparin-agarose affinity chromatography, too. Sepharose 104-111 serpin family C member 1 Homo sapiens 36-52 7455979-0 1980 Stanazolol treatment in an AT III deficient patient. Stanozolol 0-10 serpin family C member 1 Homo sapiens 27-33 7372626-1 1980 Human antithrombin III has been shown to contain four identical N-glycosidically linked carbohydrate chain per molecule. Nitrogen 64-65 serpin family C member 1 Homo sapiens 6-22 7372626-4 1980 As a result of these studies, the following structures is proposed for the carbohydrate chains in human antithrombin III: (formula: see text). Carbohydrates 75-87 serpin family C member 1 Homo sapiens 104-120 7455972-4 1980 In the other, the antithrombin III displayed a decreased electrophoretic mobility in the heparinized agarose gel. Sepharose 101-108 serpin family C member 1 Homo sapiens 18-34 7455972-5 1980 The relatively low affinity of this antithrombin III to heparin could be directly proved by the heparin-agarose affinity chromatography, too. Heparin 56-63 serpin family C member 1 Homo sapiens 36-52 7455972-5 1980 The relatively low affinity of this antithrombin III to heparin could be directly proved by the heparin-agarose affinity chromatography, too. Heparin 96-103 serpin family C member 1 Homo sapiens 36-52 7372626-1 1980 Human antithrombin III has been shown to contain four identical N-glycosidically linked carbohydrate chain per molecule. Carbohydrates 88-100 serpin family C member 1 Homo sapiens 6-22 6966584-1 1980 The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively. Glycine 101-104 serpin family C member 1 Homo sapiens 60-76 6155418-0 1980 The effect of a sulfated polysaccharide on antithrombin III. Polysaccharides 25-39 serpin family C member 1 Homo sapiens 43-59 6155418-2 1980 We have investigated the potentiation of AT-III inhibition of factors Xa, IIa, and plasmin by the heparinoid substance SP-54. Heparinoids 98-118 serpin family C member 1 Homo sapiens 41-47 6155418-2 1980 We have investigated the potentiation of AT-III inhibition of factors Xa, IIa, and plasmin by the heparinoid substance SP-54. Pentosan Sulfuric Polyester 119-124 serpin family C member 1 Homo sapiens 41-47 6155418-4 1980 SP-54 potentiated AT-III inhibition of factors Xa and IIa in the absence of heparin. Pentosan Sulfuric Polyester 0-5 serpin family C member 1 Homo sapiens 18-24 6155418-6 1980 SP-54 also potentiated the AT-III inhibition of plasmin action. Pentosan Sulfuric Polyester 0-5 serpin family C member 1 Homo sapiens 27-33 6966584-1 1980 The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively. Arginine 105-108 serpin family C member 1 Homo sapiens 60-76 6966584-1 1980 The C-terminal amino acid sequences of human and of porcine antithrombin III have been determined as Gly-Arg-Val-Ala-Asn-Pro-Cys-Val-Lys and Gly-Arg-Val-Ala-Asn-Pro-Cys, respectively. ala-asn 113-120 serpin family C member 1 Homo sapiens 60-76 6993082-1 1980 Heparin binds reversibly to its target sites of action, antithrombin and the other serine proteases involved in coagulation, especially activated factor X. Heparin 0-7 serpin family C member 1 Homo sapiens 56-68 7377131-3 1980 The thrombin remaining after neutralization by AT-III cleaves a chromophore, p-nitroaniline, from the substrate, which can then te quantified in a spectrophotometer. 4-nitroaniline 77-91 serpin family C member 1 Homo sapiens 47-53 7377145-0 1980 Heparin anticoagulation during cardiopulmonary bypass in an antithrombin-III deficient patient. Heparin 0-7 serpin family C member 1 Homo sapiens 60-76 7377145-2 1980 A case of antithrombin-III (AT-III) deficiency was diagnosed on the basis of a diminished anticoagulant effect following the administration of heparin for cardiopulmonary bypass. Heparin 143-150 serpin family C member 1 Homo sapiens 10-26 7378640-0 1980 Evidence for antithrombin III involvement in the anticoagulant activity of cellulose sulphate. cellulose sulphate 75-93 serpin family C member 1 Homo sapiens 13-29 7436418-0 1980 Studies on the interaction of heparin with thrombin, antithrombin, and other plasma proteins. Heparin 30-37 serpin family C member 1 Homo sapiens 53-65 6102938-0 1980 Effect of sulphated polysaccharides on clotting of plasma deficient in antithrombin III [proceedings]. Polysaccharides 20-35 serpin family C member 1 Homo sapiens 71-87 6772690-7 1980 The thrombin agarose (total antithrombin) gel diffusion technique correlated less well with the chromogenic (r = 0.65; P less than 0.01) and Mancini immunoassay (r = 0.45; P less than 0.01) methods. Sepharose 13-20 serpin family C member 1 Homo sapiens 28-40 7378640-1 1980 1 Cellulose sulphate, like heparin, prolonged the clotting time in partial thromboplastin time (PTT) assays, inhibited the amidolytic activity of thrombin, was without effect on amidolysis catalysed by activated coagulation factor X(Xa), and potentiated the inhibition of both thrombin and Xa by antithrombin III (AT). cellulose sulphate 2-20 serpin family C member 1 Homo sapiens 296-312 7368150-1 1980 The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides. Heparin 123-130 serpin family C member 1 Homo sapiens 94-110 7353045-0 1980 Exposure to solvent of tyrosyl and tryptophanyl residues of bovine antithrombin in the absence and presence of high-affinity and low-affinity heparin. cyclo(tyrosyl-tyrosyl) 23-30 serpin family C member 1 Homo sapiens 67-79 7404500-0 1980 A versatile assay method of antithrombin III using thrombin and Tos-Gly-Pro-Arg-Pna. chromozym TH 64-83 serpin family C member 1 Homo sapiens 28-44 6444419-8 1980 The isolated proteoglycan was indistinguishable from commercial heparin when analyzed in terms of its ability to act as a cofactor in the antithrombin III inhibition of thrombin. Heparin 64-71 serpin family C member 1 Homo sapiens 138-154 7368150-6 1980 An antiserum made against purifed At III contained antibodies with different cross-reactivities against heparin bound and non-heparin bound At III. Heparin 126-133 serpin family C member 1 Homo sapiens 34-40 7368151-3 1980 The method allows the specific determination of heparin concentrations from 0.02 USP to 0.8 USP/ml of plasma in the presence of normal At III levels. Heparin 48-55 serpin family C member 1 Homo sapiens 135-141 7353045-0 1980 Exposure to solvent of tyrosyl and tryptophanyl residues of bovine antithrombin in the absence and presence of high-affinity and low-affinity heparin. tryptophanyl 35-47 serpin family C member 1 Homo sapiens 67-79 7368150-1 1980 The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides. Heparin 123-130 serpin family C member 1 Homo sapiens 112-118 7353045-0 1980 Exposure to solvent of tyrosyl and tryptophanyl residues of bovine antithrombin in the absence and presence of high-affinity and low-affinity heparin. Heparin 142-149 serpin family C member 1 Homo sapiens 67-79 7368150-1 1980 The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides. Glycosaminoglycans 141-160 serpin family C member 1 Homo sapiens 94-110 7353045-1 1980 The exposure to solvent of the aromatic amino acid residues of free bovine antithrombin was probed by three different methods, which gave comparable results. Amino Acids, Aromatic 31-50 serpin family C member 1 Homo sapiens 75-87 7368150-1 1980 The technique of crossed immunoelectrophoresis has been used to study the binding to purified antithrombin III (At III) of heparin and other mucopolysaccharides. Glycosaminoglycans 141-160 serpin family C member 1 Homo sapiens 112-118 7353045-3 1980 Fluorescence quenching experiments indicated that 60% of the tryptophanyl fluorescence of antithrombin arose from exposed residues. tryptophanyl 61-73 serpin family C member 1 Homo sapiens 90-102 7368150-3 1980 A semi-synthetic heparin analogue showed no evidence of binding to At III, but a sample of heparan sulphate did interact with At III at a concentration 3 times that of heparin. Heparitin Sulfate 91-107 serpin family C member 1 Homo sapiens 126-132 7353045-6 1980 The binding of low-affinity of high-affinity heparin to antithrombin had neglibible effects on the solvent perturbation spectra and on the spectrophotometric titration curves. Heparin 45-52 serpin family C member 1 Homo sapiens 56-68 7368150-4 1980 Samples of purified At III from four different manufacturers all displayed heterogeneity with respect to heparin binding. Heparin 105-112 serpin family C member 1 Homo sapiens 20-26 7353045-8 1980 The binding of heparin to antithrombin therefore apparently leads to, at most, minimal changes of the exposure of the aromatic amino acids of the protein to the surrounding solvent. Heparin 15-22 serpin family C member 1 Homo sapiens 26-38 7353045-8 1980 The binding of heparin to antithrombin therefore apparently leads to, at most, minimal changes of the exposure of the aromatic amino acids of the protein to the surrounding solvent. Amino Acids, Aromatic 118-138 serpin family C member 1 Homo sapiens 26-38 7368150-6 1980 An antiserum made against purifed At III contained antibodies with different cross-reactivities against heparin bound and non-heparin bound At III. Heparin 104-111 serpin family C member 1 Homo sapiens 34-40 7356660-0 1980 The heparin binding site of antithrombin III. Heparin 4-11 serpin family C member 1 Homo sapiens 28-44 6154613-0 1980 Involvement of antithrombin III in anticoagulant effects of sulphated polysaccharides [proceedings]. Polysaccharides 70-85 serpin family C member 1 Homo sapiens 15-31 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. Tryptophan 89-99 serpin family C member 1 Homo sapiens 25-41 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. Tryptophan 89-99 serpin family C member 1 Homo sapiens 238-254 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide 108-158 serpin family C member 1 Homo sapiens 25-41 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide 108-158 serpin family C member 1 Homo sapiens 238-254 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. hydroxynitrobenzyl 196-214 serpin family C member 1 Homo sapiens 25-41 7356660-2 1980 Chemical modification of antithrombin III, the major plasma protease inhibitor, with the tryptophan reagent dimethy(2-hydroxy-5-nitrobenzyl) sulfonium bromide, results in the incorporation of one hydroxynitrobenzyl moiety per molecule of antithrombin III. hydroxynitrobenzyl 196-214 serpin family C member 1 Homo sapiens 238-254 7356660-8 1980 These results indicate that the integrity of a specific tryptophan residue is critical to the binding of heparin to antithrombin III. Tryptophan 56-66 serpin family C member 1 Homo sapiens 116-132 7356660-8 1980 These results indicate that the integrity of a specific tryptophan residue is critical to the binding of heparin to antithrombin III. Heparin 105-112 serpin family C member 1 Homo sapiens 116-132 7371952-0 1980 Inhibition by antithrombin III of carrageenan- and xylan SP54-induced aggregation of human blood platelets [proceedings]. Carrageenan 34-45 serpin family C member 1 Homo sapiens 14-30 6158827-6 1980 Together with the increased concentration of antithrombin III this might explain the potentiating effect of DHE or prophylactic treatment with low-dose heparin. Dihydroergotamine 108-111 serpin family C member 1 Homo sapiens 45-61 7371952-0 1980 Inhibition by antithrombin III of carrageenan- and xylan SP54-induced aggregation of human blood platelets [proceedings]. Pentosan Sulfuric Polyester 51-61 serpin family C member 1 Homo sapiens 14-30 7368180-0 1980 A differential effect of low-affinity heparin on the inhibition of thrombin and factor Xa by antithrombin. Heparin 38-45 serpin family C member 1 Homo sapiens 93-105 6768161-0 1980 Altered inactivation of trinitrophenylated thrombin by antithrombin III in the presence of heparin. Heparin 91-98 serpin family C member 1 Homo sapiens 55-71 6158827-6 1980 Together with the increased concentration of antithrombin III this might explain the potentiating effect of DHE or prophylactic treatment with low-dose heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 45-61 7417594-3 1980 Heparin stimulates the inactivation of Factor Xa and thrombin by AT III. Heparin 0-7 serpin family C member 1 Homo sapiens 65-71 7191289-5 1980 The amidolytic method using chromogenic substrates S-2222 for factor Xa and S-2238 for thrombin demonstrated that the new heparin was also at least two times more effective than commercial heparin in increasing the rate of inactivation of these serin proteases through antithrombin III. Heparin 122-129 serpin family C member 1 Homo sapiens 269-285 7192096-1 1980 5th Communication: Further characterization by affinity chromatography on antithrombin-sepharose and its comparison with a commercially available heparin. Sepharose 87-96 serpin family C member 1 Homo sapiens 74-86 7417594-4 1980 Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure. Sepharose 47-59 serpin family C member 1 Homo sapiens 5-11 7192096-2 1980 A highly potent heparin (Heparin Schering) was characterized in comparison to commercial heparin by affinity chromatography on antithrombin-III-sepharose. Heparin 16-23 serpin family C member 1 Homo sapiens 127-143 7192096-2 1980 A highly potent heparin (Heparin Schering) was characterized in comparison to commercial heparin by affinity chromatography on antithrombin-III-sepharose. Heparin 25-32 serpin family C member 1 Homo sapiens 127-143 7417594-4 1980 Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure. Polyvinyl Alcohol 61-78 serpin family C member 1 Homo sapiens 5-11 7192096-2 1980 A highly potent heparin (Heparin Schering) was characterized in comparison to commercial heparin by affinity chromatography on antithrombin-III-sepharose. Sepharose 144-153 serpin family C member 1 Homo sapiens 127-143 7192096-4 1980 The specific biological activities per microgram uronic acid and elution pattern on antithrombin-sepharose of high affinity heparin fraction were similar for both heparin preparations. Sepharose 97-106 serpin family C member 1 Homo sapiens 84-96 7417594-4 1980 Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure. Polyhydroxyethyl Methacrylate 80-110 serpin family C member 1 Homo sapiens 5-11 7417594-4 1980 Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure. Silicones 115-123 serpin family C member 1 Homo sapiens 5-11 7417594-4 1980 Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure. Nylons 131-136 serpin family C member 1 Homo sapiens 5-11 7417594-4 1980 Thus AT III and heparin were co-immobilized on Sepharose 4B, polyvinyl alcohol, polyhydroxy-ethyl methacrylate and silicone-coated nylon by the cyanogen bromide procedure. Cyanogen Bromide 144-160 serpin family C member 1 Homo sapiens 5-11 7376137-0 1980 Effect of monovalent cations on the heparin-enhanced antithrombin III/thrombin reaction. Heparin 36-43 serpin family C member 1 Homo sapiens 53-69 7350242-3 1980 A minor heparin fraction binds free AT III selectively and firmly but not its protease complexes. Heparin 8-15 serpin family C member 1 Homo sapiens 36-42 6792695-4 1980 In the presence of coagulation inhibitors such as heparin, hirudin and antithrombin III the DP reaction was inhibited, suggesting that the precipitation zone represents coagulation. dp 92-94 serpin family C member 1 Homo sapiens 71-87 527591-0 1979 Evidence by chemical modification for the involvement of one or more tryptophanyl residues of bovine antithrombin in the binding of high-affinity heparin. tryptophanyl 69-81 serpin family C member 1 Homo sapiens 101-113 527591-0 1979 Evidence by chemical modification for the involvement of one or more tryptophanyl residues of bovine antithrombin in the binding of high-affinity heparin. Heparin 146-153 serpin family C member 1 Homo sapiens 101-113 527591-1 1979 Tryptophanyl residues of bovine antithrombin were modified with N-bromosuccinimide at near-neutral pH. tryptophanyl 0-12 serpin family C member 1 Homo sapiens 32-44 527591-1 1979 Tryptophanyl residues of bovine antithrombin were modified with N-bromosuccinimide at near-neutral pH. Bromosuccinimide 64-82 serpin family C member 1 Homo sapiens 32-44 527591-4 1979 Modification of an average of about one tryptophanyl residue per protein molecule did not affect antithrombin activity measured in the absence of heparin, but decreased the activity assayed in the presence of heparin to about half the value given by unmodified antithrombin. tryptophanyl 40-52 serpin family C member 1 Homo sapiens 261-273 527591-5 1979 Addition of an excess of high-affinity heparin to a similarly modified antithrombin sample resulted in much smaller circular dichroism, ultraviolet absorption and fluorescence changes than those observed with the intact protein. Heparin 39-46 serpin family C member 1 Homo sapiens 71-83 316698-0 1979 Carboxy terminal fragment of human alpha-1-antitrypsin from hydroxylamine cleavage: homology with antithrombin III. Hydroxylamine 60-73 serpin family C member 1 Homo sapiens 98-114 6243142-5 1980 Fractionation of heparin yielded preparations that varied in molecular weight and, within a given molecular weight fraction, in affinity for antithrombin III. Heparin 17-24 serpin family C member 1 Homo sapiens 141-157 527591-7 1979 These studies thus reinforce the conclusion from previous spectroscopic analyses that one or more tryptophanyl residues of antithrombin are involved in the binding of high-affinity heparin, presumably by being located at or close to the heparin binding site. tryptophanyl 98-110 serpin family C member 1 Homo sapiens 123-135 6243142-10 1980 These results suggest that formation of an antithrombin-heparin complex protected platelets from aggregation by heparin. Heparin 56-63 serpin family C member 1 Homo sapiens 43-55 6243142-10 1980 These results suggest that formation of an antithrombin-heparin complex protected platelets from aggregation by heparin. Heparin 112-119 serpin family C member 1 Homo sapiens 43-55 527591-7 1979 These studies thus reinforce the conclusion from previous spectroscopic analyses that one or more tryptophanyl residues of antithrombin are involved in the binding of high-affinity heparin, presumably by being located at or close to the heparin binding site. Heparin 181-188 serpin family C member 1 Homo sapiens 123-135 6243142-11 1980 Selection of heparin fractions of low molecular weight and high antithrombin affinity may improve anticoagulant therapy and development of thromboresistant heparin-coated artificial materials. Heparin 13-20 serpin family C member 1 Homo sapiens 64-76 527591-7 1979 These studies thus reinforce the conclusion from previous spectroscopic analyses that one or more tryptophanyl residues of antithrombin are involved in the binding of high-affinity heparin, presumably by being located at or close to the heparin binding site. Heparin 237-244 serpin family C member 1 Homo sapiens 123-135 118968-2 1979 Human, porcine, rabbit, and rat antithrombin III have been purified by affinity chromatography using heparin-agarose. Heparin 101-108 serpin family C member 1 Homo sapiens 32-48 118968-5 1979 Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid. Glucosamine 99-110 serpin family C member 1 Homo sapiens 32-48 500822-4 1979 Antithrombin affinity chromatography of purified heparin with an anticoagulant activity of 137 U/mg, revealed that the one-third that was bound and eluted had a 273 U/mg sp act, whereas the unbound activity was 31 U/mg. Heparin 49-56 serpin family C member 1 Homo sapiens 0-12 500822-4 1979 Antithrombin affinity chromatography of purified heparin with an anticoagulant activity of 137 U/mg, revealed that the one-third that was bound and eluted had a 273 U/mg sp act, whereas the unbound activity was 31 U/mg. TFF2 protein, human 170-172 serpin family C member 1 Homo sapiens 0-12 500822-5 1979 Thus, the previously observed heterogeneity of commercial porcine heparin for binding to human antithrombin was also observed with human heparin. porcine heparin 58-73 serpin family C member 1 Homo sapiens 95-107 500822-5 1979 Thus, the previously observed heterogeneity of commercial porcine heparin for binding to human antithrombin was also observed with human heparin. Heparin 66-73 serpin family C member 1 Homo sapiens 95-107 118968-5 1979 Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid. Neuraminic Acids 116-131 serpin family C member 1 Homo sapiens 32-48 118968-2 1979 Human, porcine, rabbit, and rat antithrombin III have been purified by affinity chromatography using heparin-agarose. Sepharose 109-116 serpin family C member 1 Homo sapiens 32-48 118968-7 1979 The total carbohydrate contents were 17, 16, 14, and 15% for human, porcine, rabbit, and rat antithrombin III, respectively. Carbohydrates 10-22 serpin family C member 1 Homo sapiens 93-109 118968-13 1979 Human, porcine, and rabbit antithrombin III have a histidine residue at the amino-terminus, while rat antithrombin III contains an amino-terminal asparagine residue. Asparagine 146-156 serpin family C member 1 Homo sapiens 102-118 118968-5 1979 Human, porcine, rabbit, and rat antithrombin III are single-chain glycoproteins containing hexose, glucosamine, and neuraminic acid. Hexoses 91-97 serpin family C member 1 Homo sapiens 32-48 508327-0 1979 The effects of phospholipid and factor Va on the inhibition of factor Xa by antithrombin III. Phospholipids 15-27 serpin family C member 1 Homo sapiens 76-92 161807-2 1979 The antitrypsin, antiplasmin and antithrombin activities of bis(amidinobenzylidene)- and bis(amidinobenzyl)cycloalkanones are not markedly affected if the amidino group is substituted by an uncharged residue (H, OCH3, Cl, Br, NO2). bis(amidinobenzylidene) 60-83 serpin family C member 1 Homo sapiens 33-45 161807-2 1979 The antitrypsin, antiplasmin and antithrombin activities of bis(amidinobenzylidene)- and bis(amidinobenzyl)cycloalkanones are not markedly affected if the amidino group is substituted by an uncharged residue (H, OCH3, Cl, Br, NO2). bis(amidinobenzyl)cycloalkanones 89-121 serpin family C member 1 Homo sapiens 33-45 161807-2 1979 The antitrypsin, antiplasmin and antithrombin activities of bis(amidinobenzylidene)- and bis(amidinobenzyl)cycloalkanones are not markedly affected if the amidino group is substituted by an uncharged residue (H, OCH3, Cl, Br, NO2). amidino 64-71 serpin family C member 1 Homo sapiens 33-45 489712-7 1979 3) Transferrin, antithrombin III, prothrombin, and plasminogen showed marked increases after administration of danazol and during pregnancy. Danazol 111-118 serpin family C member 1 Homo sapiens 16-32 120212-0 1979 Chromatography of heparin on sepharose-lysine: molecular size fractionation and its relevance to thrombin and antithrombin III binding. Heparin 18-25 serpin family C member 1 Homo sapiens 110-126 120212-0 1979 Chromatography of heparin on sepharose-lysine: molecular size fractionation and its relevance to thrombin and antithrombin III binding. sepharose-lysine 29-45 serpin family C member 1 Homo sapiens 110-126 477560-7 1979 Antithrombin III levels should be determined in all cases of increased heparin tolerance. Heparin 71-78 serpin family C member 1 Homo sapiens 0-16 111639-7 1979 Pretreatment with heparin prevents the consumption of fibrinogen and antithrombin III but does not prevent the increase in fibrin split products which was observed. Heparin 18-25 serpin family C member 1 Homo sapiens 69-85 476156-0 1979 Evidence for a plasma inhibitor of the heparin accelerated inhibition of factor Xa by antithrombin III. Heparin 39-46 serpin family C member 1 Homo sapiens 86-102 476156-1 1979 The ability of heparin fractions of different molecular weight to potentiate the action of antithrombin III against the coagulation factors thrombin and Xa has been examined in purified reaction mixtures and in plasma. Heparin 15-22 serpin family C member 1 Homo sapiens 91-107 486155-1 1979 The inactivation of thrombin and factor Xa by antithrombin was determined in the presence of heparin fractions of different molecular weights and with high affinity for antithrombin. Heparin 93-100 serpin family C member 1 Homo sapiens 46-58 486155-1 1979 The inactivation of thrombin and factor Xa by antithrombin was determined in the presence of heparin fractions of different molecular weights and with high affinity for antithrombin. Heparin 93-100 serpin family C member 1 Homo sapiens 169-181 160589-0 1979 Effects of PGI2 on the inactivation of thrombin, factor Xa, and plasmin by antithrombin-III and heparin. Epoprostenol 11-15 serpin family C member 1 Homo sapiens 75-91 316999-7 1979 The molecular weight estimated on SDS electrophoresis for AT-III and alpha 1-AT was 63,000 and 50,000, respectively. Sodium Dodecyl Sulfate 34-37 serpin family C member 1 Homo sapiens 58-64 223567-0 1979 Effect of polyanetholesulphonic acid and xylan sulphate on antithrombin III activity. polyanetholesulphonic acid 10-36 serpin family C member 1 Homo sapiens 59-75 223567-0 1979 Effect of polyanetholesulphonic acid and xylan sulphate on antithrombin III activity. xylan sulphate 41-55 serpin family C member 1 Homo sapiens 59-75 116567-2 1979 The importance of antithrombin III as a cofactor of heparin is stressed. Heparin 52-59 serpin family C member 1 Homo sapiens 18-34 420768-4 1979 The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment. Sodium Dodecyl Sulfate 65-87 serpin family C member 1 Homo sapiens 12-24 469001-1 1979 To clarify the action of dextran sulphate, a heparin analogue, in the clotting of fibrinogen by thrombin, determinations were carried out on the clotting activity, the release of fibrinopeptides from fibrinogen, and the hydrolytic activity of thrombin against a peptide chromogenic substrate in the absence or presence of antithrombin III (heparin cofactor). Dextran Sulfate 25-41 serpin family C member 1 Homo sapiens 322-338 469001-3 1979 Although heparin markedly enhanced the antithrombin activity of antithrombin III, dextran sulphate did not activate antithrombin III. Heparin 9-16 serpin family C member 1 Homo sapiens 39-51 469001-3 1979 Although heparin markedly enhanced the antithrombin activity of antithrombin III, dextran sulphate did not activate antithrombin III. Heparin 9-16 serpin family C member 1 Homo sapiens 64-80 89015-0 1979 [Heparin inhibition of the antithrombin activity of alpha-2-macroglobulin]. Heparin 1-8 serpin family C member 1 Homo sapiens 27-39 89015-5 1979 These data show that heparin paradoxically protects thrombin from inhibition by alpha-2-macroglobulin whereas it increases the enzyme inhibition by antithrombin III. Heparin 21-28 serpin family C member 1 Homo sapiens 148-164 429327-0 1979 Fractionation of low molecular weight heparin species and their interaction with antithrombin. Heparin 38-45 serpin family C member 1 Homo sapiens 81-93 429327-5 1979 The binding of highly active heparin to antithrombin is accurately described by a single-site binding model with a KHep-ATDISS of approximately 1 X 10(-7) M. Variations in this binding parameter secondary to changes in environmental variables indicate that charge-charge interactions as well as an increase in entropy are critical to the formation of the highly active heparin-antithrombin complex. Heparin 29-36 serpin family C member 1 Homo sapiens 40-52 429327-5 1979 The binding of highly active heparin to antithrombin is accurately described by a single-site binding model with a KHep-ATDISS of approximately 1 X 10(-7) M. Variations in this binding parameter secondary to changes in environmental variables indicate that charge-charge interactions as well as an increase in entropy are critical to the formation of the highly active heparin-antithrombin complex. Heparin 29-36 serpin family C member 1 Homo sapiens 377-389 429327-7 1979 The ability of the highly active heparin to accelerate the thrombin-antithrombin interaction was also examined. Heparin 33-40 serpin family C member 1 Homo sapiens 68-80 473117-3 1979 The antithrombin activity of the copolymer corresponded to 1% of grafted heparin. copolymer 33-42 serpin family C member 1 Homo sapiens 4-16 473117-3 1979 The antithrombin activity of the copolymer corresponded to 1% of grafted heparin. Heparin 73-80 serpin family C member 1 Homo sapiens 4-16 473117-6 1979 The heparin part of the copolymer was responsible for antithrombin III adsorption and for decrease of factor V activity. Heparin 4-11 serpin family C member 1 Homo sapiens 54-70 473117-6 1979 The heparin part of the copolymer was responsible for antithrombin III adsorption and for decrease of factor V activity. copolymer 24-33 serpin family C member 1 Homo sapiens 54-70 420817-4 1979 These spectral results indicate that the thrombin-antithrombin III complex formed in the presence of heparin differs in its conformation from that produced in its absence. Heparin 101-108 serpin family C member 1 Homo sapiens 50-66 420768-4 1979 The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment. nadodso4 89-97 serpin family C member 1 Homo sapiens 12-24 420768-4 1979 The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment. nadodso4 107-115 serpin family C member 1 Homo sapiens 12-24 420768-4 1979 The enzyme--antithrombin complexes could not be dissociated with sodium dodecyl sulfate (NaDodSO4) but the NaDodSO4-denatured complexes were dissociated by hydroxylamine treatment. Hydroxylamine 156-169 serpin family C member 1 Homo sapiens 12-24 436823-0 1979 Studies on the mechanism of the rate-enhancing effect of heparin on the thrombin-antithrombin III reaction. Heparin 57-64 serpin family C member 1 Homo sapiens 81-97 160191-7 1979 Antithrombin III was promoted by heparin in its inhibitory effect. Heparin 33-40 serpin family C member 1 Homo sapiens 0-16 436823-1 1979 The rate of the reaction between thrombin and antithrombin III is greatly increased in the presence of heparin. Heparin 103-110 serpin family C member 1 Homo sapiens 46-62 436823-4 1979 The strength of the binding of the two heparin fractions to antithrombin III and thrombin, respectively, was determined by a crossed immunoelectrophoresis technique. Heparin 39-46 serpin family C member 1 Homo sapiens 60-76 436823-7 1979 The ability of the two heparin fractions to catalyse the inhibition of thrombin by antithrombin III was determined and was found to be much greater for the high activity heparin fraction. Heparin 23-30 serpin family C member 1 Homo sapiens 83-99 436823-7 1979 The ability of the two heparin fractions to catalyse the inhibition of thrombin by antithrombin III was determined and was found to be much greater for the high activity heparin fraction. Heparin 170-177 serpin family C member 1 Homo sapiens 83-99 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 103-110 serpin family C member 1 Homo sapiens 50-66 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 103-110 serpin family C member 1 Homo sapiens 133-149 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 103-110 serpin family C member 1 Homo sapiens 133-149 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 162-169 serpin family C member 1 Homo sapiens 50-66 553509-7 1979 In the treatment of DIC priority is given to intravenous application of AT-III complex human, concentrated and purified, activated in vitro with heparin. Heparin 145-152 serpin family C member 1 Homo sapiens 72-78 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 162-169 serpin family C member 1 Homo sapiens 133-149 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 162-169 serpin family C member 1 Homo sapiens 133-149 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 162-169 serpin family C member 1 Homo sapiens 50-66 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 162-169 serpin family C member 1 Homo sapiens 133-149 436823-8 1979 A mechanism for the reaction between thrombin and antithrombin III in the presence of small amounts of heparin is suggested, whereby antithrombin III first binds heparin and this complex then inhibits thrombin by interaction with both the bound heparin and the antithrombin III. Heparin 162-169 serpin family C member 1 Homo sapiens 133-149 504072-5 1979 Heparin cofactor activity was demonstrated by immediate inactivation of thrombin by antithrombin III in the presence of minute quantities of heparin. Heparin 0-7 serpin family C member 1 Homo sapiens 84-100 456150-3 1979 In this situation special emphasis should be placed on the levels of antithrombin III regarding application of heparin. Heparin 111-118 serpin family C member 1 Homo sapiens 69-85 511016-6 1979 Serum samples showed two antithrombin III peaks due to a decreased heparin binding of the slower peak (2.1-3.9 times), which was probably antithrombin III-activated procoagulant complexes. Heparin 67-74 serpin family C member 1 Homo sapiens 25-41 511016-6 1979 Serum samples showed two antithrombin III peaks due to a decreased heparin binding of the slower peak (2.1-3.9 times), which was probably antithrombin III-activated procoagulant complexes. Heparin 67-74 serpin family C member 1 Homo sapiens 138-154 511016-7 1979 Heparin analogue (A 73025) also bound antithrombin III in vitro but the mobility of the peak was slower than with mucosal heparin and only a single peak was obtained in serum samples. Heparin 0-7 serpin family C member 1 Homo sapiens 38-54 511016-10 1979 Heparin therapy gave rise to a double peak in the plasma antithrombin III profile and with continuous infusion, quantitative decreases were noted in all subjects studied, two of whom rethrombosed at the end of 7 days therapy. Heparin 0-7 serpin family C member 1 Homo sapiens 57-73 216717-0 1979 Measurement of antithrombin III in healthy subjects studied before and after taking aspirin and dipyridamole. Aspirin 84-91 serpin family C member 1 Homo sapiens 15-31 216717-0 1979 Measurement of antithrombin III in healthy subjects studied before and after taking aspirin and dipyridamole. Dipyridamole 96-108 serpin family C member 1 Homo sapiens 15-31 531528-4 1979 A negative correlation was found between AT-III and serum creatinine and between AT-III and serum albumin. Creatinine 58-68 serpin family C member 1 Homo sapiens 41-47 462917-5 1979 It consists of the following steps: (a) partial purification by precipitation of impurities with 20% polyethylene glycol (PEG) 4000; (b) isolation of AT III from the PEG supernatant by batch adsorption and elution on heparin-Sepharose at a ratio corresponding to 45 vol of plasma or 80 vol of 10% Fr. Polyethylene Glycols 166-169 serpin family C member 1 Homo sapiens 150-156 483282-0 1979 Enhancement of antithrombin III activity by carrageenans. Carrageenan 44-56 serpin family C member 1 Homo sapiens 15-31 504072-6 1979 It also could be demonstrated that thrombin inactivation by antithrombin III occurs by formation of a bimolecular complex whose rate of formation is markedly enhanced by minute quantities of heparin. Heparin 191-198 serpin family C member 1 Homo sapiens 60-76 743219-1 1978 It is proposed that the anti-coagulant activity of heparin is related to the probability of finding, in a random distribution of different disaccharides, a dodecasaccharide with the sequence required for binding to antithrombin. Heparin 51-58 serpin family C member 1 Homo sapiens 215-227 217091-3 1978 25 patients receiving heparin therapy had low antithrombin III concentration. Heparin 22-29 serpin family C member 1 Homo sapiens 46-62 217091-6 1978 Antithrombin III decreased activity induced by heparin treatment is pointed out. Heparin 47-54 serpin family C member 1 Homo sapiens 0-16 743219-1 1978 It is proposed that the anti-coagulant activity of heparin is related to the probability of finding, in a random distribution of different disaccharides, a dodecasaccharide with the sequence required for binding to antithrombin. Disaccharides 139-152 serpin family C member 1 Homo sapiens 215-227 743219-1 1978 It is proposed that the anti-coagulant activity of heparin is related to the probability of finding, in a random distribution of different disaccharides, a dodecasaccharide with the sequence required for binding to antithrombin. dodecasaccharide 156-172 serpin family C member 1 Homo sapiens 215-227 743219-6 1978 The probability that any randomly chosen dodecasaccharide sequence in heparin should bind to antithrombin was calculated to 0.022. dodecasaccharide 41-57 serpin family C member 1 Homo sapiens 93-105 743219-6 1978 The probability that any randomly chosen dodecasaccharide sequence in heparin should bind to antithrombin was calculated to 0.022. Heparin 70-77 serpin family C member 1 Homo sapiens 93-105 743219-10 1978 The activity of high-affinity heparin (i.e. molecules containing high-affinity binding sites for antithrombin), determined either by a whole-blood clotting procedure or by thrombin inactivation in the presence of antithrombin, thus remained dependent on molecular weight. Heparin 30-37 serpin family C member 1 Homo sapiens 97-109 743219-10 1978 The activity of high-affinity heparin (i.e. molecules containing high-affinity binding sites for antithrombin), determined either by a whole-blood clotting procedure or by thrombin inactivation in the presence of antithrombin, thus remained dependent on molecular weight. Heparin 30-37 serpin family C member 1 Homo sapiens 213-225 743219-12 1978 One explanation could be a requirement for binding of thrombin to the heparin chain adjacent to antithrombin. Heparin 70-77 serpin family C member 1 Homo sapiens 96-108 570737-0 1978 Inhibition of thrombin by antithrombin III in the presence of certain glycosaminoglycans found in the mammalian aorta. Glycosaminoglycans 70-88 serpin family C member 1 Homo sapiens 26-42 107070-0 1978 The influence of heparin on the immunochemical evaluation of antithrombin III by electroimmunoassay. Heparin 17-24 serpin family C member 1 Homo sapiens 61-77 698151-2 1978 Quinestrol therapy was associated with increased levels of factors VII and IX and decreased antithrombin activity on the sixth postpartum day, and increased factor IX and plasminogen levels on the fourteenth postpartum day. Quinestrol 0-10 serpin family C member 1 Homo sapiens 92-104 710412-0 1978 The binding of low-affinity and high-affinity heparin to antithrombin. Heparin 46-53 serpin family C member 1 Homo sapiens 57-69 710412-2 1978 The interaction between antithrombin and two forms of heparin, differing in their affinity for the matrix-linked protein, has been studied by fluorescence. Heparin 54-61 serpin family C member 1 Homo sapiens 24-36 710412-3 1978 The binding of the high-affinity heparin fraction to antithrombin leads to activation of the inhibitor, allowing it to react more rapidly with a number of serine proteases of the coagulation cascade. Heparin 33-40 serpin family C member 1 Homo sapiens 53-65 710412-5 1978 The binding of either fraction to antithrombin was found to result in an increase of the tryptophan fluorescence of the protein. Tryptophan 89-99 serpin family C member 1 Homo sapiens 34-46 710412-7 1978 The fluorescence enhancement caused by high-affinity heparin is consistent with a conformational change of antithrombin related to its activation. Heparin 53-60 serpin family C member 1 Homo sapiens 107-119 710412-9 1978 These showed high-affinity heparin to bind to antithrombin with a stoichiometry of about one and with a binding constant at physiological ionic strength of about 8 X 10(7) M-1. Heparin 27-34 serpin family C member 1 Homo sapiens 46-58 710423-0 1978 The binding of low-affinity and high-affinity heparin to antithrombin. Heparin 46-53 serpin family C member 1 Homo sapiens 57-69 708377-0 1978 Effect of heparin on thrombin inactivation by antithrombin-III. Heparin 10-17 serpin family C member 1 Homo sapiens 46-62 708377-1 1978 The inactivation of thrombin by heat and by its physiological inhibitor, antithrombin-III, shows quite different dependence on heparin concentration. Heparin 127-134 serpin family C member 1 Homo sapiens 73-89 708377-5 1978 On the other hand, heparin at 0.125-2.5 microgram/ml accelerates the thrombin-antithrombin-III reaction. Heparin 19-26 serpin family C member 1 Homo sapiens 78-94 708377-9 1978 On the basis of these data we suggest a mechanism of action of heparin in the thrombin-antithrombin-III reaction which accounts for all the important features of the latter and seems to unify the different hypotheses that have been advanced. Heparin 63-70 serpin family C member 1 Homo sapiens 87-103 741437-0 1978 Appearance of heparin antithrombin-active chains in vivo after injection of commercial heparin and in anaphylaxis. Heparin 14-21 serpin family C member 1 Homo sapiens 22-34 705689-3 1978 At III levels measured with six methods in 36 people: 10 healthy controls, 10 women taking a progestagen Lynestrenol and 16 women taking a combined oestrogen-progestagen contraceptive pill. Lynestrenol 105-116 serpin family C member 1 Homo sapiens 0-6 687588-0 1978 Binding of low-affinity and high-affinity heparin to antithrombin. Heparin 42-49 serpin family C member 1 Homo sapiens 53-65 705690-0 1978 Inhibition of urokinase by complex formation with human antithrombin III in absence and presence of heparin. Heparin 100-107 serpin family C member 1 Homo sapiens 56-72 705690-1 1978 Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis. Heparin 90-97 serpin family C member 1 Homo sapiens 6-22 705690-1 1978 Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis. Sepharose 98-107 serpin family C member 1 Homo sapiens 6-22 705690-1 1978 Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis. Sepharose 151-160 serpin family C member 1 Homo sapiens 6-22 705690-1 1978 Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis. deae a 228-234 serpin family C member 1 Homo sapiens 6-22 705690-1 1978 Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis. sephadex 238-246 serpin family C member 1 Homo sapiens 6-22 705690-1 1978 Human antithrombin III was purified from fresh human plasma by affinity chromatography on heparin-Sepharose, affinity chromatography on concanavalin A Sepharose, gel filtration on Ultrogel AcA 34, ion exchange chromatography on DEAE A-50 Sephadex and preparative agarose gel electrophoresis. Sepharose 263-270 serpin family C member 1 Homo sapiens 6-22 705690-2 1978 The hydrolytic activity of urokinase (plasminogen activator from urine) on acetyl-glycyl-L-lysine methylester acetate (Ac-gly-lys-OMeAc) was inhibited by antithrombin III in a slow time-dependent manner. acetyl-glycyl-l-lysine methylester acetate 75-117 serpin family C member 1 Homo sapiens 154-170 705690-2 1978 The hydrolytic activity of urokinase (plasminogen activator from urine) on acetyl-glycyl-L-lysine methylester acetate (Ac-gly-lys-OMeAc) was inhibited by antithrombin III in a slow time-dependent manner. ac-gly-lys-omeac 119-135 serpin family C member 1 Homo sapiens 154-170 673830-7 1978 Thus, in the polysulphate group, heparin has the highest affinity for antithrombin III, liquoid for fibrinogen and dextran sulphate for beta 2-glycoprotein I. polysulphate 13-25 serpin family C member 1 Homo sapiens 70-86 656463-0 1978 The increase in human antithrombin III tryptophan fluorescence produced by heparin. Tryptophan 39-49 serpin family C member 1 Homo sapiens 22-38 656463-0 1978 The increase in human antithrombin III tryptophan fluorescence produced by heparin. Heparin 75-82 serpin family C member 1 Homo sapiens 22-38 656463-1 1978 The increase in fluorescence of human antithrombin III has been used to study the binding of a semi-synthetic heparin analogue. Heparin 110-117 serpin family C member 1 Homo sapiens 38-54 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Heparin 64-71 serpin family C member 1 Homo sapiens 57-63 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Quinuclidinyl Benzilate 136-138 serpin family C member 1 Homo sapiens 45-51 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Quinuclidinyl Benzilate 136-138 serpin family C member 1 Homo sapiens 57-63 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. H-Pro-Phe-OH 139-146 serpin family C member 1 Homo sapiens 45-51 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. H-Pro-Phe-OH 139-146 serpin family C member 1 Homo sapiens 57-63 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Arginine 147-150 serpin family C member 1 Homo sapiens 45-51 97200-5 1978 Time dependent inactivation of kallikrein by AT III, and AT III-heparin complex was shown by means of a synthetic kallikrein substrate: Bz-Pro-Phe-Arg-pNan. Arginine 147-150 serpin family C member 1 Homo sapiens 57-63 149555-4 1978 The extent of plasmin-antithrombin-(heparin) complex formation was studied by intravenous injection of iodine-labelled antithrombin (5-20 muCi) and quantitation of the amount of antithrombin bound to plasmin. Iodine 103-109 serpin family C member 1 Homo sapiens 119-131 149555-4 1978 The extent of plasmin-antithrombin-(heparin) complex formation was studied by intravenous injection of iodine-labelled antithrombin (5-20 muCi) and quantitation of the amount of antithrombin bound to plasmin. Iodine 103-109 serpin family C member 1 Homo sapiens 119-131 149555-6 1978 Thus only between 3 and 11% of the in vivo formed plasmin is neutralized by antithrombin-heparin complex. Heparin 89-96 serpin family C member 1 Homo sapiens 76-88 149555-7 1978 Repeated activation of the fibrinolytic system resulted in a shortening of the plasma radioactivity half-life of labelled antithrombin from 2.45 to 2.03 d in the absence of heparin (three patients), and from 3.13 to 2.35 d following heparin administration (two patients). Heparin 173-180 serpin family C member 1 Homo sapiens 122-134 149555-7 1978 Repeated activation of the fibrinolytic system resulted in a shortening of the plasma radioactivity half-life of labelled antithrombin from 2.45 to 2.03 d in the absence of heparin (three patients), and from 3.13 to 2.35 d following heparin administration (two patients). Heparin 233-240 serpin family C member 1 Homo sapiens 122-134 347919-5 1978 Heparin tremendously accelerates the inhibitory function of antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 60-76 347919-7 1978 Heparin retards the thrombin-fibrinogen reaction, but otherwise the effectiveness of heparin as an anticoagulant depends on antithrombin III in laboratory experiments, as well as in therapeutics. Heparin 85-92 serpin family C member 1 Homo sapiens 124-140 673830-7 1978 Thus, in the polysulphate group, heparin has the highest affinity for antithrombin III, liquoid for fibrinogen and dextran sulphate for beta 2-glycoprotein I. Heparin 33-40 serpin family C member 1 Homo sapiens 70-86 631129-1 1978 Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable. 5--6 arginine 16-29 serpin family C member 1 Homo sapiens 174-190 638885-3 1978 Exercise on a treadmill induced similar changes in both groups, but during the use of Demulen the levels of fibrinogen and plasminogen were higher, antithrombin level was lower, and the recalcified clotting and dilute whole blood lysis times were shorter in group 2 than in the corresponding samples obtained from the nonpill users. SC-11800 EE 86-93 serpin family C member 1 Homo sapiens 148-160 662621-5 1978 The various aspects of this disorder discovered by Egeberg are reviewed: early onset, in several members of the same family, or recurrent thrombo-embolic problems, accompanied by a decrease in functional activity of one of the principal inhibitors of thrombin (AT III), with autosomal dominant transmission and treatment based upon anti-vitamin K agents. Vitamin K 337-346 serpin family C member 1 Homo sapiens 261-267 631129-1 1978 Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable. 5--6 arginine 16-29 serpin family C member 1 Homo sapiens 204-220 631129-1 1978 Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable. 1,2-cyclohexanedione 56-76 serpin family C member 1 Homo sapiens 174-190 631129-1 1978 Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable. Heparin 124-131 serpin family C member 1 Homo sapiens 174-190 631129-1 1978 Modification of 5--6 arginine residues of thrombin with 1,2-cyclohexanedione has resulted in the selective abolition of the heparin sensitivity of the enzyme"s reaction with antithrombin-III, whereas the antithrombin-III sensitivity of native and modified thrombin was indistinguishable. Heparin 124-131 serpin family C member 1 Homo sapiens 204-220 631129-2 1978 It is suggested that heparin accelerates the thrombin antithrombin-III reaction by interacting with thrombin. Heparin 21-28 serpin family C member 1 Homo sapiens 54-70 652506-0 1978 [Changes in antithrombin III during treatment with heparin]. Heparin 51-58 serpin family C member 1 Homo sapiens 12-28 75564-6 1978 These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography. Heparin 134-141 serpin family C member 1 Homo sapiens 43-59 75564-6 1978 These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography. Heparin 152-159 serpin family C member 1 Homo sapiens 43-59 75564-6 1978 These results indicate that the removal of antithrombin III is the major problem in the purification of H-TGL and LPL from human post-heparin plasma by heparin-Sepharose affinity chromatography. Sepharose 160-169 serpin family C member 1 Homo sapiens 43-59 74632-0 1978 Heparin-induced decrease in circulating antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 40-56 735880-8 1978 Prophylactic treatment, preferably oral anticoagulants and/or dextran, is recommended for all persons with a low AT III concentration in any situation known to increase the predisposition to thrombosis. Dextrans 62-69 serpin family C member 1 Homo sapiens 113-119 618863-2 1978 Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1. Acetylglucosamine 62-81 serpin family C member 1 Homo sapiens 6-22 618863-2 1978 Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1. Mannose 83-90 serpin family C member 1 Homo sapiens 6-22 618863-2 1978 Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1. Galactose 92-101 serpin family C member 1 Homo sapiens 6-22 618863-2 1978 Human antithrombin III was found to contain covalently linked N-acetylglucosamine, mannose, galactose, and sialic acid in a molar ratio of approximately 1:1:0.6:1. N-Acetylneuraminic Acid 107-118 serpin family C member 1 Homo sapiens 6-22 618863-5 1978 Antithrombin III isolated by different procedures was also found to contain glucose in an approximately equimolar ratio with N-acetylglucosamine. Glucose 76-83 serpin family C member 1 Homo sapiens 0-16 618863-5 1978 Antithrombin III isolated by different procedures was also found to contain glucose in an approximately equimolar ratio with N-acetylglucosamine. Acetylglucosamine 125-144 serpin family C member 1 Homo sapiens 0-16 618863-8 1978 Although it remains to be established whether the inhibitory actions of antithrombin III are affected by glucosylceramide, the relative amounts which are bound suggest that antithrombin III may be a significant carrier of the glycolipid. Glucosylceramides 105-121 serpin family C member 1 Homo sapiens 72-88 618863-8 1978 Although it remains to be established whether the inhibitory actions of antithrombin III are affected by glucosylceramide, the relative amounts which are bound suggest that antithrombin III may be a significant carrier of the glycolipid. Glycolipids 226-236 serpin family C member 1 Homo sapiens 72-88 618863-8 1978 Although it remains to be established whether the inhibitory actions of antithrombin III are affected by glucosylceramide, the relative amounts which are bound suggest that antithrombin III may be a significant carrier of the glycolipid. Glycolipids 226-236 serpin family C member 1 Homo sapiens 173-189 735880-9 1978 The effect of heparin in these patients is impaired since the heparin co-factor, which is identical with AT III, is lowered. Heparin 14-21 serpin family C member 1 Homo sapiens 105-111 742337-1 1978 (A clinico-pharmacological study of the relationship between antithrombin-III activity and steroid cholestasis). Steroids 91-98 serpin family C member 1 Homo sapiens 61-77 742337-2 1978 The relationship between steroid cholestasis and antithrombin-III activity were examined in users of oral contraceptives (Infecundin or Bisecurin) and in patients receiving anabolic hormone therapy (Nerobol). Steroids 25-32 serpin family C member 1 Homo sapiens 49-65 720957-2 1978 When factor Xa was added to a system containing antithrombin III in excess and heparin in low concentration, the amount of factor Xa immediately inactivated was found to be a function of the concentration of heparin. Heparin 208-215 serpin family C member 1 Homo sapiens 48-64 618990-8 1978 The results suggest that a surface with covalently bonded heparin is reactive toward platelets but can be passivated by formation of a heparin/AT III complex. Heparin 58-65 serpin family C member 1 Homo sapiens 143-149 350729-3 1978 The inactivation is accelerated by heparin, permitting assay systems which rapidly measure the At-III content of diluted plasma. Heparin 35-42 serpin family C member 1 Homo sapiens 95-101 658785-4 1978 Heparin accelerates the saturation of antithrombin with factor Xa. Heparin 0-7 serpin family C member 1 Homo sapiens 38-50 618990-8 1978 The results suggest that a surface with covalently bonded heparin is reactive toward platelets but can be passivated by formation of a heparin/AT III complex. Heparin 135-142 serpin family C member 1 Homo sapiens 143-149 73931-0 1977 Effect of heparin and warfarin on antithrombin III. Heparin 10-17 serpin family C member 1 Homo sapiens 34-50 73931-0 1977 Effect of heparin and warfarin on antithrombin III. Warfarin 22-30 serpin family C member 1 Homo sapiens 34-50 303667-5 1977 Evidence is presented which supports previous findings that C1-INH, alpha1-AT, and antithrombin (in the presence of heparin) contribute to factor XIIa and XI a inactivation in ellagic acid-activated plasma and that plasma albumin may compete with factor XII for ellagic acid binding. Heparin 116-123 serpin family C member 1 Homo sapiens 83-95 303667-5 1977 Evidence is presented which supports previous findings that C1-INH, alpha1-AT, and antithrombin (in the presence of heparin) contribute to factor XIIa and XI a inactivation in ellagic acid-activated plasma and that plasma albumin may compete with factor XII for ellagic acid binding. Ellagic Acid 176-188 serpin family C member 1 Homo sapiens 83-95 303667-5 1977 Evidence is presented which supports previous findings that C1-INH, alpha1-AT, and antithrombin (in the presence of heparin) contribute to factor XIIa and XI a inactivation in ellagic acid-activated plasma and that plasma albumin may compete with factor XII for ellagic acid binding. Ellagic Acid 262-274 serpin family C member 1 Homo sapiens 83-95 146278-0 1977 Role of heparin in the inactivation of thrombin, factor Xa, and plasmin by antithrombin III. Heparin 8-15 serpin family C member 1 Homo sapiens 75-91 353657-5 1977 A purified antithrombin III, prepared by affinity chromatography, contained an immunoreactive material of higher molecular size which has no activity and a higher mobility in agarose gel. Sepharose 175-182 serpin family C member 1 Homo sapiens 11-27 353657-6 1977 When heparin is incorporated in the agarose plate, the electrophoretic mobility of this polymerized antithrombin III is not modified. Heparin 5-12 serpin family C member 1 Homo sapiens 100-116 353657-6 1977 When heparin is incorporated in the agarose plate, the electrophoretic mobility of this polymerized antithrombin III is not modified. Sepharose 36-43 serpin family C member 1 Homo sapiens 100-116 148659-2 1977 Antitrypsin, antiplasmin and antithrombin effect of 2-amino-6-alkoxy- and aralkoxynaphthalenes]. 2-amino-6-alkoxy- and aralkoxynaphthalenes 52-94 serpin family C member 1 Homo sapiens 29-41 353657-0 1977 [Electrophoretic mobility of antithrombin III in an agarose gel with heparin. Sepharose 52-59 serpin family C member 1 Homo sapiens 29-45 353657-0 1977 [Electrophoretic mobility of antithrombin III in an agarose gel with heparin. Heparin 69-76 serpin family C member 1 Homo sapiens 29-45 353657-2 1977 The electrophoretic mobility of several forms of antithrombin III in an agarose gel has been compared with the mobility in a gel containing heparin. Sepharose 72-79 serpin family C member 1 Homo sapiens 49-65 353657-4 1977 The inactige antithrombin III with higher molecular size, separated by gel filtration, was found to be homogenous even if there was heparin in the gel. Heparin 132-139 serpin family C member 1 Homo sapiens 13-29 601748-0 1977 Heparin-like effect of polymethacrylic acid on the reaction between thrombin and antithrombin-III. Heparin 0-7 serpin family C member 1 Homo sapiens 81-97 601748-0 1977 Heparin-like effect of polymethacrylic acid on the reaction between thrombin and antithrombin-III. polymethacrylic acid 23-43 serpin family C member 1 Homo sapiens 81-97 601749-0 1977 Decreased binding of heparin to antithrombin following the interaction between antithrombin and thrombin. Heparin 21-28 serpin family C member 1 Homo sapiens 32-44 601749-0 1977 Decreased binding of heparin to antithrombin following the interaction between antithrombin and thrombin. Heparin 21-28 serpin family C member 1 Homo sapiens 79-91 74248-3 1977 Heparin facilitated complex-formation between alpha-thrombin and antithrombin-III, whereas inactivation of beta-thrombin by antithrombin was only slightly influenced, even at a heparin concentration two orders of magnitude higher. Heparin 0-7 serpin family C member 1 Homo sapiens 65-81 72924-0 1977 Heparin-induced decrease in circulating antithrombin-III. Heparin 0-7 serpin family C member 1 Homo sapiens 40-56 74248-3 1977 Heparin facilitated complex-formation between alpha-thrombin and antithrombin-III, whereas inactivation of beta-thrombin by antithrombin was only slightly influenced, even at a heparin concentration two orders of magnitude higher. Heparin 0-7 serpin family C member 1 Homo sapiens 65-77 579514-0 1977 Studies of heparin affinity to antithrombin III and other proteins in vitro and in vivo. Heparin 11-18 serpin family C member 1 Homo sapiens 31-47 24016-0 1977 Quenching of tryptophan fluorescence in human antithrombin III by iodide ion. Tryptophan 13-23 serpin family C member 1 Homo sapiens 46-62 24016-0 1977 Quenching of tryptophan fluorescence in human antithrombin III by iodide ion. Iodides 66-72 serpin family C member 1 Homo sapiens 46-62 24016-1 1977 Iodide is an efficient quencher of antithrombin III intrinsic tryptophan fluorescence. Iodides 0-6 serpin family C member 1 Homo sapiens 35-51 24016-1 1977 Iodide is an efficient quencher of antithrombin III intrinsic tryptophan fluorescence. Tryptophan 62-72 serpin family C member 1 Homo sapiens 35-51 24016-4 1977 The binding of heparin to antithrombin III influences the number of solvent-exposed tryptophan residues. Heparin 15-22 serpin family C member 1 Homo sapiens 26-42 24016-4 1977 The binding of heparin to antithrombin III influences the number of solvent-exposed tryptophan residues. Tryptophan 84-94 serpin family C member 1 Homo sapiens 26-42 579516-7 1977 A possible explanation may be that the normal liver removes heparin bound to antithrombin III, and that this function is impaired in liver cirrhosis. Heparin 60-67 serpin family C member 1 Homo sapiens 77-93 410640-9 1977 In conclusion, the marked structural similarity of human and bovine antithrombin indicates that the two proteins may also exhibit extensive functional similarities in the binding of heparin and the inhibition of various coagulation factors. Heparin 182-189 serpin family C member 1 Homo sapiens 68-80 603757-2 1977 A study has been made of a low molecular weight semi-synthetic heparin analogue, A73025, that may be clinically useful as an antithrombotic agent because of its reported high specificity for antithrombin III. Heparin 63-70 serpin family C member 1 Homo sapiens 191-207 603757-2 1977 A study has been made of a low molecular weight semi-synthetic heparin analogue, A73025, that may be clinically useful as an antithrombotic agent because of its reported high specificity for antithrombin III. A73025 81-87 serpin family C member 1 Homo sapiens 191-207 71399-0 1977 Heparin-induced decrease in circulating antithrombin-III. Heparin 0-7 serpin family C member 1 Homo sapiens 40-56 71399-2 1977 In all patients, including 1 with congenital AT-III deficiency, heparin therapy was associated with a considerable progressive reduction in AT-III-binding capacity and antigenic protein. Heparin 64-71 serpin family C member 1 Homo sapiens 45-51 71399-4 1977 Plasma-AT-III returned to normal two to three days after heparin was stopped. Heparin 57-64 serpin family C member 1 Homo sapiens 7-13 71399-6 1977 When present in blood for long periods heparin significantly reduced AT-III, the proteinase inhibitor that is responsible for the anticoagulant effect of this drug. Heparin 39-46 serpin family C member 1 Homo sapiens 69-75 71399-7 1977 The finding is very relevant to the interpretation of clinical data in patients treated with heparin and suggests that AT-III depletion may underly the thromboembolic complications sometimes encountered during heparin therapy. Heparin 93-100 serpin family C member 1 Homo sapiens 119-125 71399-7 1977 The finding is very relevant to the interpretation of clinical data in patients treated with heparin and suggests that AT-III depletion may underly the thromboembolic complications sometimes encountered during heparin therapy. Heparin 210-217 serpin family C member 1 Homo sapiens 119-125 579490-6 1977 This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex. Heparin 139-146 serpin family C member 1 Homo sapiens 201-207 579490-7 1977 These results suggest that acceleration of binding and increased utilization of binding capacity are the two regular effects of heparin on thrombin-involving reactions of AT III. Heparin 128-135 serpin family C member 1 Homo sapiens 171-177 579490-8 1977 Both of these effects may be abolished by quantitative binding of heparin to thrombin-AT III complex. Heparin 66-73 serpin family C member 1 Homo sapiens 86-92 579491-2 1977 In the first step of the preparation, using heparin-agarose chromatography, we observed that the complexed form of AT III bound less strongly to the gel than the free form and that about half of the AT III was free. Heparin 44-51 serpin family C member 1 Homo sapiens 115-121 579491-2 1977 In the first step of the preparation, using heparin-agarose chromatography, we observed that the complexed form of AT III bound less strongly to the gel than the free form and that about half of the AT III was free. Sepharose 52-59 serpin family C member 1 Homo sapiens 115-121 579490-5 1977 Heparin itself was neutralized in thrombin-AT III reaction losing its anticoagulant property in proportion to the amount of thrombin bound by inhibitor. Heparin 0-7 serpin family C member 1 Homo sapiens 43-49 579490-6 1977 This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex. Heparin 36-43 serpin family C member 1 Homo sapiens 110-116 579490-6 1977 This quantitative neutralization of heparin occurred not only when the anticoagulant participated in thrombin-AT III binding but also when heparin was added to a medium containing a preformed thrombin-AT III complex. Heparin 36-43 serpin family C member 1 Homo sapiens 201-207 330064-5 1977 The basis for this phenomenon is most probably the binding of the heparin-antithrombin cofactor (AT III) to a complex with heparin and thrombin. Heparin 66-73 serpin family C member 1 Homo sapiens 97-103 872292-7 1977 In the high salt system the relative contributions of antithrombin III to Xa neutralization in human and rabbit plasma are different. Salts 12-16 serpin family C member 1 Homo sapiens 54-70 872292-8 1977 However, in experiments in which Xa inhibitory activity of antithrombin III is altered by heparin, a simple formula, Total activity (%) = 65% + 0.35 x human plasma (%), permits translation of rabbit data on the Xa-antithrombin III-heparin reaction to man. Heparin 90-97 serpin family C member 1 Homo sapiens 59-75 142314-0 1977 The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin. Sepharose 80-89 serpin family C member 1 Homo sapiens 44-60 560216-0 1977 Effect of heparin modification on its activity in enhancing the inhibition of thrombin by antithrombin III. Heparin 10-17 serpin family C member 1 Homo sapiens 90-106 560216-5 1977 Heparin methyl ester is more potent than heparinylglycine in activating antithrombin III, as exhibited by its immediate effect on the thrombin-fibrinogen reaction. heparin methyl ester 0-20 serpin family C member 1 Homo sapiens 72-88 560216-5 1977 Heparin methyl ester is more potent than heparinylglycine in activating antithrombin III, as exhibited by its immediate effect on the thrombin-fibrinogen reaction. heparinylglycine 41-57 serpin family C member 1 Homo sapiens 72-88 560216-6 1977 However, heparinylglycine is the more effective of the two, in increasing the rate of thrombin deactivation by antithrombin III. heparinylglycine 9-25 serpin family C member 1 Homo sapiens 111-127 560216-8 1977 In contrast, N-sulfates are critical for the interaction of heparin with antithrombin III. n-sulfates 13-23 serpin family C member 1 Homo sapiens 73-89 142314-0 1977 The inactivation of thrombin and plasmin by antithrombin III in the presence of sepharose-heparin. Heparin 90-97 serpin family C member 1 Homo sapiens 44-60 407761-0 1977 [The studies on the influence of heparin on the reaction of antithrombin with thrombin, and the optimal dosis of heparin in the reaction (author"s transl)]. Heparin 33-40 serpin family C member 1 Homo sapiens 60-72 65182-0 1977 Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence. Heparin 11-18 serpin family C member 1 Homo sapiens 28-44 849484-3 1977 Thus, the unique specificity for heparin in the anticoagulation system (which involves two or more lysine residues on the antithrombin molecule) is not paralleled by the findings with the basic homopolymers. Heparin 33-40 serpin family C member 1 Homo sapiens 122-134 849484-3 1977 Thus, the unique specificity for heparin in the anticoagulation system (which involves two or more lysine residues on the antithrombin molecule) is not paralleled by the findings with the basic homopolymers. Lysine 99-105 serpin family C member 1 Homo sapiens 122-134 857429-1 1977 Antithrombin III (AT III) was determined in 290 patients with deep venous thrombosis and/or pulmonary embolism by immunological methods (radial immunodiffusion, Laurell technique) and by biological activity (heparin cofactor activity and anti-Xa activity). Heparin 208-215 serpin family C member 1 Homo sapiens 0-16 853045-4 1977 After contact with plasma, the copolymer lost part of its antithrombin activity which could be restored by a high ionic-strength medium. copolymer 31-40 serpin family C member 1 Homo sapiens 58-70 854877-0 1977 Evaluation of an amidolytic heparin assay method: increased sensitivity by adding purified antithrombin III. Heparin 28-35 serpin family C member 1 Homo sapiens 91-107 12845-6 1977 Heparin and antithrombin III not only neutralized the thrombogenic materials present in the thrombogenic concentrate, but also inhibited the de novo generation of coagulant enzymes during incubation with calcium. Calcium 204-211 serpin family C member 1 Homo sapiens 12-28 65284-0 1977 Metabolism of antithrombin III (heparin cofactor) in man: effects of venous thrombosis and of heparin administration. Heparin 32-39 serpin family C member 1 Homo sapiens 14-30 65284-2 1977 The labelled antithrombin III has a high specific activity (5.75 units/mg) and displayed a single band on SDS-polyacrylamide gel electrophoresis. Sodium Dodecyl Sulfate 106-109 serpin family C member 1 Homo sapiens 13-29 65284-2 1977 The labelled antithrombin III has a high specific activity (5.75 units/mg) and displayed a single band on SDS-polyacrylamide gel electrophoresis. polyacrylamide 110-124 serpin family C member 1 Homo sapiens 13-29 65284-12 1977 In three patients with venous thrombosis not treated with heparin, the turnover of labelled antithrombin III was in the normal range. Heparin 58-65 serpin family C member 1 Homo sapiens 92-108 65284-14 1977 In one of these patients, the labelled antithrombin III had been incubated with an equimolar amount of heparin prior to injection. Heparin 103-110 serpin family C member 1 Homo sapiens 39-55 402555-4 1977 Since disorders of hemostasis due to therapy occur sporadically, early postoperative raising of the dose of heparin should only be done under regular laboratory controll, to which activated PTT and antithrombin time is well suited. Heparin 108-115 serpin family C member 1 Homo sapiens 198-210 836042-0 1977 Small-angle x-ray scattering studies on human antithrombin III and its complex with heparin. Heparin 84-91 serpin family C member 1 Homo sapiens 46-62 65182-0 1977 Binding of heparin to human antithrombin III as studied by measurements of tryptophan fluorescence. Tryptophan 75-85 serpin family C member 1 Homo sapiens 28-44 65182-4 1977 The binding of heparin to antithrombin III caused a marked fluorescence enhancement by about 30% of the intrinsic protein emission intensity. Heparin 15-22 serpin family C member 1 Homo sapiens 26-42 65182-6 1977 Heparin fractionated by gel filtration seemed to be bound to two sites on antithrombin III with association constants of 0.6-10(6)m-1 and 0.2-10(6)M-1 respectively. Heparin 0-7 serpin family C member 1 Homo sapiens 74-90 65182-7 1977 Heparin, prepared by affinity chromatography on matrix-bound antithrombin III appeared to be bound to only one site with an association constant of 2.3-10(6)M-1. Heparin 0-7 serpin family C member 1 Homo sapiens 61-77 64653-0 1977 A heparin analogue with specific action on antithrombin III. Heparin 2-9 serpin family C member 1 Homo sapiens 43-59 64653-3 1977 When given by parenteral injection, the heparin analogue had almost the same potentiating effect on antithrombin III as mucous heparin, but without a comparable effect on the K.C.C.T. Heparin 40-47 serpin family C member 1 Homo sapiens 100-116 65891-4 1977 Immunoreactive AT III showed a positive correlation to both AT III and heparin cofactor activities. Heparin 71-78 serpin family C member 1 Homo sapiens 15-21 754468-5 1977 Thrombin inactivation by antithrombin did not proceed at 0 degrees C in 60 min, but the interaction between thrombin and antithrombin was facilitated in the presence of heparin. Heparin 169-176 serpin family C member 1 Homo sapiens 25-37 754468-5 1977 Thrombin inactivation by antithrombin did not proceed at 0 degrees C in 60 min, but the interaction between thrombin and antithrombin was facilitated in the presence of heparin. Heparin 169-176 serpin family C member 1 Homo sapiens 121-133 16544-5 1977 Furthermore, the fall in antithrombin III level then its rise can contribute to the "heparine rebound" occurring in certain cases after neutralization of heparinemia with protamine. Heparin 85-93 serpin family C member 1 Homo sapiens 25-41 869991-1 1977 The nature of platelet antithrombin was elucidated by comparison of thrombin binding and antithrombin activities of intact platelets and by purification of antithrombin from platelet lysates using glycerol osmotic lysis, ethanol precipitation and Sephadex gel filtration techniques. Glycerol 197-205 serpin family C member 1 Homo sapiens 23-35 869991-1 1977 The nature of platelet antithrombin was elucidated by comparison of thrombin binding and antithrombin activities of intact platelets and by purification of antithrombin from platelet lysates using glycerol osmotic lysis, ethanol precipitation and Sephadex gel filtration techniques. Ethanol 221-228 serpin family C member 1 Homo sapiens 23-35 869991-1 1977 The nature of platelet antithrombin was elucidated by comparison of thrombin binding and antithrombin activities of intact platelets and by purification of antithrombin from platelet lysates using glycerol osmotic lysis, ethanol precipitation and Sephadex gel filtration techniques. sephadex 247-255 serpin family C member 1 Homo sapiens 23-35 869991-5 1977 However, the PGE1 treatment produced slight (less than 30%) but significant decrease of antithrombin activity of intact platelets, whereas the binding of thrombin to platelets was not affected by PGE1 treatment. Alprostadil 13-17 serpin family C member 1 Homo sapiens 88-100 830556-0 1977 Interaction of heparin with thrombin and antithrombin III. Heparin 15-22 serpin family C member 1 Homo sapiens 41-57 557071-1 1977 The binding of heparin to antithrombin III and the antithrombin III--thrombin complex. Heparin 15-22 serpin family C member 1 Homo sapiens 26-42 557071-1 1977 The binding of heparin to antithrombin III and the antithrombin III--thrombin complex. Heparin 15-22 serpin family C member 1 Homo sapiens 51-67 557071-2 1977 A two-dimensional immunoelectrophoretic method has been used to obtain information on the binding of heparin to purified antithrombin III and the antithrombin III--thrombin complex. Heparin 101-108 serpin family C member 1 Homo sapiens 121-137 557071-2 1977 A two-dimensional immunoelectrophoretic method has been used to obtain information on the binding of heparin to purified antithrombin III and the antithrombin III--thrombin complex. Heparin 101-108 serpin family C member 1 Homo sapiens 146-162 557071-3 1977 The difference in mobility of the components in a gel containing heparin enables distinction between free and complexed forms of antithrombin III. Heparin 65-72 serpin family C member 1 Homo sapiens 129-145 557071-4 1977 The results obtained with purified preparations show that heparin is bound more strongly to antithrombin III than to the antithrombin III--thrombin complex. Heparin 58-65 serpin family C member 1 Homo sapiens 92-108 557071-4 1977 The results obtained with purified preparations show that heparin is bound more strongly to antithrombin III than to the antithrombin III--thrombin complex. Heparin 58-65 serpin family C member 1 Homo sapiens 121-137 557071-5 1977 In plasma heparin is bound to several components, only a fraction being bound to antithrombin III. Heparin 10-17 serpin family C member 1 Homo sapiens 81-97 836327-0 1977 Evidence for a heparin-induced conformational change on antithrombin III. Heparin 15-22 serpin family C member 1 Homo sapiens 56-72 151469-0 1977 Role of heparin in the interaction of serine proteinases with antithrombin III. Heparin 8-15 serpin family C member 1 Homo sapiens 62-78 151469-1 1977 To characterize the mode of action of heparin, the kinetics of inhibition of thrombin, factor Xa, and plasmin by antithrombin III was studied without and in the presence of heparin. Heparin 38-45 serpin family C member 1 Homo sapiens 113-129 151469-5 1977 Thus, heparin acts obviously as an activator of the enzymes and enhances their affinity for antithrombin III. Heparin 6-13 serpin family C member 1 Homo sapiens 92-108 754468-4 1977 Thrombin inactivation by antithrombin was also accelerated at calcium or magnesium chloride concentrations above 0.04 M. Antithrombin was inactivated at pH 7.3 at 65 degrees C in some minutes and heparin failed to protect it against heat denaturation. Calcium 62-69 serpin family C member 1 Homo sapiens 25-37 754468-4 1977 Thrombin inactivation by antithrombin was also accelerated at calcium or magnesium chloride concentrations above 0.04 M. Antithrombin was inactivated at pH 7.3 at 65 degrees C in some minutes and heparin failed to protect it against heat denaturation. Calcium 62-69 serpin family C member 1 Homo sapiens 121-133 754468-4 1977 Thrombin inactivation by antithrombin was also accelerated at calcium or magnesium chloride concentrations above 0.04 M. Antithrombin was inactivated at pH 7.3 at 65 degrees C in some minutes and heparin failed to protect it against heat denaturation. Magnesium Chloride 73-91 serpin family C member 1 Homo sapiens 25-37 754468-4 1977 Thrombin inactivation by antithrombin was also accelerated at calcium or magnesium chloride concentrations above 0.04 M. Antithrombin was inactivated at pH 7.3 at 65 degrees C in some minutes and heparin failed to protect it against heat denaturation. Magnesium Chloride 73-91 serpin family C member 1 Homo sapiens 121-133 63389-0 1977 Structural requirements for the interaction of heparin with antithrombin III. Heparin 47-54 serpin family C member 1 Homo sapiens 60-76 75141-0 1977 [The role of heparin in thrombin inhibition by antithrombin]. Heparin 13-20 serpin family C member 1 Homo sapiens 47-59 402327-2 1977 Antithrombin III (AT-III), being an alpha2-globulin, will have an electrophoretic mobility in the presence of heparin like prealbumin in agarose gels. Heparin 110-117 serpin family C member 1 Homo sapiens 0-16 402327-2 1977 Antithrombin III (AT-III), being an alpha2-globulin, will have an electrophoretic mobility in the presence of heparin like prealbumin in agarose gels. Heparin 110-117 serpin family C member 1 Homo sapiens 18-24 402327-2 1977 Antithrombin III (AT-III), being an alpha2-globulin, will have an electrophoretic mobility in the presence of heparin like prealbumin in agarose gels. Sepharose 137-144 serpin family C member 1 Homo sapiens 0-16 402327-2 1977 Antithrombin III (AT-III), being an alpha2-globulin, will have an electrophoretic mobility in the presence of heparin like prealbumin in agarose gels. Sepharose 137-144 serpin family C member 1 Homo sapiens 18-24 402327-3 1977 This phenomenon was utilized to quantitate AT-III from serum and plasma by electroimmunodiffusion (EID) for 90 min agarose gels containing 75 USP units of heparin/ml gel. Sepharose 115-122 serpin family C member 1 Homo sapiens 43-49 402327-3 1977 This phenomenon was utilized to quantitate AT-III from serum and plasma by electroimmunodiffusion (EID) for 90 min agarose gels containing 75 USP units of heparin/ml gel. Heparin 155-162 serpin family C member 1 Homo sapiens 43-49 402327-4 1977 The method permits a rapid quantitation of AT-III from serum, citrated plasma and EDTA plasma, and a positive correlation was observed between these values and those obtained by single radial immunodiffusion (SRI). Edetic Acid 82-86 serpin family C member 1 Homo sapiens 43-49 65798-3 1976 Heparin facilitated the complex formation between alpha-thrombin and antithrombin-III, whereas beta-thrombin inactivation was only slightly affected. Heparin 0-7 serpin family C member 1 Homo sapiens 69-85 974107-0 1976 The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III. 1-anilino-8-naphthalenesulfonate 15-47 serpin family C member 1 Homo sapiens 92-108 1006626-0 1976 Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin iii and by gel filtration. Heparin 28-35 serpin family C member 1 Homo sapiens 92-108 974107-0 1976 The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III. Caprylates 73-82 serpin family C member 1 Homo sapiens 92-108 982357-0 1976 Studies on human plasma antithrombin isolated on heparin gel. Heparin 49-56 serpin family C member 1 Homo sapiens 24-36 974107-0 1976 The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III. Heparin 49-56 serpin family C member 1 Homo sapiens 92-108 974107-1 1976 The binding of 1-anilino-8-naphthalenesulfonate to human antithrombin III was studied by fluorescence enhancement of the fluorophor and fluorescence quenching of the protein emission. 1-anilino-8-naphthalenesulfonate 15-47 serpin family C member 1 Homo sapiens 57-73 974107-0 1976 The binding of 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate by human antithrombin III. Salicylates 58-68 serpin family C member 1 Homo sapiens 92-108 974107-2 1976 Two molecules of 1-anilino-8-naphthalenesulfonate were found to bind per antithrombin molecule with an average dissociation constant of 4.4-10(-5) M. The binding of heparin to antithrombin was studied by ultraviolet difference spectroscopy. 1-anilino-8-naphthalenesulfonate 17-49 serpin family C member 1 Homo sapiens 73-85 974107-2 1976 Two molecules of 1-anilino-8-naphthalenesulfonate were found to bind per antithrombin molecule with an average dissociation constant of 4.4-10(-5) M. The binding of heparin to antithrombin was studied by ultraviolet difference spectroscopy. 1-anilino-8-naphthalenesulfonate 17-49 serpin family C member 1 Homo sapiens 176-188 60879-1 1976 An assay technic for measuring heparin cofactor activity in which antithrombin activity can be assessed without plasma attenuation even in the presence of therapeutic levels of heparin is presented. Heparin 31-38 serpin family C member 1 Homo sapiens 66-78 974107-2 1976 Two molecules of 1-anilino-8-naphthalenesulfonate were found to bind per antithrombin molecule with an average dissociation constant of 4.4-10(-5) M. The binding of heparin to antithrombin was studied by ultraviolet difference spectroscopy. Heparin 165-172 serpin family C member 1 Homo sapiens 73-85 974107-2 1976 Two molecules of 1-anilino-8-naphthalenesulfonate were found to bind per antithrombin molecule with an average dissociation constant of 4.4-10(-5) M. The binding of heparin to antithrombin was studied by ultraviolet difference spectroscopy. Heparin 165-172 serpin family C member 1 Homo sapiens 176-188 974107-3 1976 The stoichiometry of the heparin binding indicated 1.8 binding sites with an average dissociation constant of 4.3 - 10(-6) M. Further the fluorometric competition experiments with 1-anilino-8-naphthalenesulfonate, heparin, salicylate and caprylate indicated two different classes of anion binding sites on the antithrombin molecule. Heparin 25-32 serpin family C member 1 Homo sapiens 310-322 976270-2 1976 It was demonstrated that one molecule of heparin was able to promote the binding of a large number of antithrombin molecules to thrombin. Heparin 41-48 serpin family C member 1 Homo sapiens 102-114 976270-3 1976 Thus heparin may affect the rate of the inactivation of thrombin by antithrombin in a catalytic manner. Heparin 5-12 serpin family C member 1 Homo sapiens 68-80 976270-0 1976 Acceleration of the reaction between thrombin and antithrombin III by non-stoichiometric amounts of heparin. Heparin 100-107 serpin family C member 1 Homo sapiens 50-66 976270-1 1976 The accelerating effect of heparin on the reaction between purified human antithrombin and thrombin has been investigated by measuring the amount of thrombin inactivated during a short incubation of the enzyme with the inhibitor in the presence and absence of non-stoichiometric amounts of heparin. Heparin 27-34 serpin family C member 1 Homo sapiens 74-86 982345-0 1976 Inhibition of the activated Cls subunit of the first component of complement by antithrombin III in the presence of heparin. Heparin 116-123 serpin family C member 1 Homo sapiens 80-96 968810-0 1976 Effect of calcium phosphate on thrombin and on its sensitivity to heparin and antithrombin-III. calcium phosphate 10-27 serpin family C member 1 Homo sapiens 78-94 1036800-5 1976 In vitro, abnormal III was seen: however an enhanced antithrombin III activity in vitro was not found with carbenicillin and various penicillin derivatives. Penicillins 133-143 serpin family C member 1 Homo sapiens 53-69 982345-0 1976 Inhibition of the activated Cls subunit of the first component of complement by antithrombin III in the presence of heparin. Chlorine 28-31 serpin family C member 1 Homo sapiens 80-96 989640-5 1976 Ethinyl oestradiol treatment resulted in much more widespread changes with marked increases in coagulation factors VII, VIII, IX and X, decreased levels of antithrombin and dramatic increases in circulating plasminogen levels and euglobulin lysis activity. Ethinyl Estradiol 0-18 serpin family C member 1 Homo sapiens 156-168 1278445-0 1976 Anticoagulant activity of heparin: separation of high-activity and low-activity heparin species by affinity chromatography on immobilized antithrombin. Heparin 26-33 serpin family C member 1 Homo sapiens 138-150 1273513-5 1976 The antithrombin clotting time is shown to be inversely related to the level of circulating serine procoagulants, directly related to the level of antithrombin, and results from a procoagulant-antithrombin inter-molecular reaction. Serine 92-98 serpin family C member 1 Homo sapiens 147-159 61631-1 1976 Antithrombin III, purified to homogeneity according to polyacrylamide gel disc electrophoresis and immunoelectrophoresis, inhibited the activity of purified factor IXa and Xa, whereas factor VII was not inhibited either in the active or in the native form. polyacrylamide 55-69 serpin family C member 1 Homo sapiens 0-16 55783-9 1976 The intra-operative fall in antithrombin-III activity was prevented by a small preoperative dose of subcutaneous heparin. Heparin 113-120 serpin family C member 1 Homo sapiens 28-44 1273513-5 1976 The antithrombin clotting time is shown to be inversely related to the level of circulating serine procoagulants, directly related to the level of antithrombin, and results from a procoagulant-antithrombin inter-molecular reaction. Serine 92-98 serpin family C member 1 Homo sapiens 4-16 1273513-5 1976 The antithrombin clotting time is shown to be inversely related to the level of circulating serine procoagulants, directly related to the level of antithrombin, and results from a procoagulant-antithrombin inter-molecular reaction. Serine 92-98 serpin family C member 1 Homo sapiens 147-159 1194266-5 1975 This activated species is added to purified antithrombin-heparin cofactor and the interaction is studied in the presence and absence of heparin. Heparin 57-64 serpin family C member 1 Homo sapiens 44-56 789043-5 1976 Heparin is a potent inhibitor of several steps on the intrinsic coagulation pathway through its effect on a plasma cofactor, antithrombin III. Heparin 0-7 serpin family C member 1 Homo sapiens 125-141 1209544-0 1975 Adverse effect of heparin in thrombin-antithrombin III interaction. Heparin 18-25 serpin family C member 1 Homo sapiens 38-54 1209544-8 1975 These results may have some bearings on the approach to heparin therapy in the event when thrombin continuously generates or when a marked deficiency of antithrombin III exists. Heparin 56-63 serpin family C member 1 Homo sapiens 153-169 1247522-8 1976 These occur in position 2 which is occupied by Gly, Arg, and Trp in human, bovine, and horse, respectively; position 6 which has a deletion in human antithrombin III; and position 8 where Ile in human and horse antithrombin III has been replaced by Val in the bovine preparation. Valine 249-252 serpin family C member 1 Homo sapiens 211-227 1194266-7 1975 The addition of heparin dramatically accelerates the rate of this interaction with virtually complete inhibition of Factor IXa occurring within 15 s. Sodium dodecyl sulfate gel electrophoresis of reduced and nonreduced proteins indicates that antithrombin-heparin cofactor functions as a potent inhibitor of Factor IXa by forming an undissociable complex with the enzyme which is stable in the presence of denaturing or reducing agents (or both). Heparin 16-23 serpin family C member 1 Homo sapiens 243-255 1194266-7 1975 The addition of heparin dramatically accelerates the rate of this interaction with virtually complete inhibition of Factor IXa occurring within 15 s. Sodium dodecyl sulfate gel electrophoresis of reduced and nonreduced proteins indicates that antithrombin-heparin cofactor functions as a potent inhibitor of Factor IXa by forming an undissociable complex with the enzyme which is stable in the presence of denaturing or reducing agents (or both). Sodium Dodecyl Sulfate 150-172 serpin family C member 1 Homo sapiens 243-255 52896-0 1975 Effect of anabolic steroids on plasma antithrombin III. Steroids 19-27 serpin family C member 1 Homo sapiens 38-54 1191673-1 1975 It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy. Heparin 27-34 serpin family C member 1 Homo sapiens 223-235 1191673-1 1975 It has been suggested that heparin can affect blood coagulation through thrombin, i.e. the binding of heparin to thrombin induces a conformational change in the enzyme, facilitating a complex formation between thrombin and antithrombin (Machovich, T., Blasko, Gy. Heparin 102-109 serpin family C member 1 Homo sapiens 223-235 53066-1 1975 Human and bovine antithrombin II/III have been isolated by a simple procedure essentially using only affinity chromatography on heparin-agarose and polyethylene glycol precipitation. Heparin 128-135 serpin family C member 1 Homo sapiens 17-36 53066-1 1975 Human and bovine antithrombin II/III have been isolated by a simple procedure essentially using only affinity chromatography on heparin-agarose and polyethylene glycol precipitation. Sepharose 136-143 serpin family C member 1 Homo sapiens 17-36 53066-1 1975 Human and bovine antithrombin II/III have been isolated by a simple procedure essentially using only affinity chromatography on heparin-agarose and polyethylene glycol precipitation. Polyethylene Glycols 148-167 serpin family C member 1 Homo sapiens 17-36 53066-4 1975 End group analysis of human antithrombin II/III shows histidine as the N-terminal amino acid. Histidine 54-63 serpin family C member 1 Homo sapiens 28-47 52896-3 1975 In distinct contrast to the oral contraceptives, five of the six 17-alpha-alkylated anabolic steroids studied produced increased plasma Antithrombin III levels and five produced decreased levels of plasma alpha2-macroglobulin. Steroids 93-101 serpin family C member 1 Homo sapiens 136-152 1188792-0 1975 Proceedings: A method for the quantitative determination of the antithrombin III (AT III) activity in plasma and serum using the complex formation with heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 64-80 1188792-0 1975 Proceedings: A method for the quantitative determination of the antithrombin III (AT III) activity in plasma and serum using the complex formation with heparin. Heparin 152-159 serpin family C member 1 Homo sapiens 82-88 1154312-2 1975 When agarose was applied in the first phase of the crossed immunoelectrophoresis, the normal and the pathological AT-III revealed identical electrophoretic mobility. Sepharose 5-12 serpin family C member 1 Homo sapiens 114-120 1188833-0 1975 Proceedings: Effect of heparin on antithrombin III activity during delivery and early puerperium. Heparin 23-30 serpin family C member 1 Homo sapiens 34-50 1170899-2 1975 Inactivation of Ts-thrombin by antithrombin-III was facilitated with heparin, whereas inactivation of Tp-thrombin was not. Heparin 69-76 serpin family C member 1 Homo sapiens 31-47 1201212-2 1975 Mixing various quantities of heparin with agarose in the first phase of electrophoresis, AT-III from normal human plasma and serum revealed a heterogeneity which depended on the heparin concentration in the agarose gel. Heparin 29-36 serpin family C member 1 Homo sapiens 89-95 1201212-2 1975 Mixing various quantities of heparin with agarose in the first phase of electrophoresis, AT-III from normal human plasma and serum revealed a heterogeneity which depended on the heparin concentration in the agarose gel. Sepharose 42-49 serpin family C member 1 Homo sapiens 89-95 1201212-2 1975 Mixing various quantities of heparin with agarose in the first phase of electrophoresis, AT-III from normal human plasma and serum revealed a heterogeneity which depended on the heparin concentration in the agarose gel. Heparin 178-185 serpin family C member 1 Homo sapiens 89-95 1201212-2 1975 Mixing various quantities of heparin with agarose in the first phase of electrophoresis, AT-III from normal human plasma and serum revealed a heterogeneity which depended on the heparin concentration in the agarose gel. Sepharose 207-214 serpin family C member 1 Homo sapiens 89-95 1201212-3 1975 At heparin concentrations higher than 16 u/ml, AT-III displayed three components with different electrophoretic mobilities. Heparin 3-10 serpin family C member 1 Homo sapiens 47-53 1201212-10 1975 It is concluded that high molecular weight complexes between AT-III and activated coagulation factors may be present in normally circulating blood and that their detection and possibly quantitation can be achieved using the heparin/agarose crossed immunoelectrophoresis system. Heparin 224-231 serpin family C member 1 Homo sapiens 61-67 1201212-10 1975 It is concluded that high molecular weight complexes between AT-III and activated coagulation factors may be present in normally circulating blood and that their detection and possibly quantitation can be achieved using the heparin/agarose crossed immunoelectrophoresis system. Sepharose 232-239 serpin family C member 1 Homo sapiens 61-67 1154312-3 1975 However, when heparin was mixed with agarose in the first phase of electrophoresis, the propositus" plasma displayed a different AT-III pattern from normal plasma. Heparin 14-21 serpin family C member 1 Homo sapiens 129-135 1154312-3 1975 However, when heparin was mixed with agarose in the first phase of electrophoresis, the propositus" plasma displayed a different AT-III pattern from normal plasma. Sepharose 37-44 serpin family C member 1 Homo sapiens 129-135 1090031-0 1975 The effect of major surgery, low doses of heparin and thromboembolism on plasma antithrombin. Heparin 42-49 serpin family C member 1 Homo sapiens 80-92 53064-1 1975 A new rapid method for assaying total antithrombin activity has been developed based on the inactivation of thrombin incorporated into an agarose gel, during the radial diffusion of plasma in the gel. Sepharose 138-145 serpin family C member 1 Homo sapiens 38-50 4450303-0 1974 A simple 2-step isolation procedure for human antithrombin II/III and its biological activity after insolubilization to agarose. Sepharose 120-127 serpin family C member 1 Homo sapiens 46-65 1115795-0 1975 Action of heparin on thrombin-antithrombin reaction. Heparin 10-17 serpin family C member 1 Homo sapiens 30-42 4436339-0 1974 Antithrombin activity of a polyelectrolyte synthesized from cis-1,4-polyisoprene. 1,4-polyisoprene 60-80 serpin family C member 1 Homo sapiens 0-12 47704-14 1975 Ether extraction of plasma reduces antithrombin III activity. Ether 0-5 serpin family C member 1 Homo sapiens 35-51 47704-18 1975 Antithrombin III neutralizes the activity of prethrombin-E and thrombin-E; consequently, an active histidine center found in the B1 chain of thrombin is not essential for the binding of antithrombin. Histidine 99-108 serpin family C member 1 Homo sapiens 0-16 4423843-0 1974 The rivanol method for the quantitative determination of antithrombin III in plasma. Ethacridine 4-11 serpin family C member 1 Homo sapiens 57-73 4790174-0 1973 [Experimental fibrinogenopathy after reaction of human fibrinogen with beta propiolactone: antithrombin activity, effect on platelet aggregation and function and on fibrin stabilization phase]. Propiolactone 71-89 serpin family C member 1 Homo sapiens 91-103 4633781-0 1973 [Behavior of the progessive antithrombin during long-term anticoagulant therapy (Vitamin K antagonists)]. Vitamin K 81-90 serpin family C member 1 Homo sapiens 28-40 4631013-0 1972 Inactivation of antithrombin 3 by fatty acids. Fatty Acids 34-45 serpin family C member 1 Homo sapiens 16-28 6035543-0 1967 Heparin cofactor and plasma antithrombin in relation to the mechanism of inactivation of thrombin by heparin. Heparin 101-108 serpin family C member 1 Homo sapiens 28-40 5019894-0 1972 [Blood antithrombin activity in intact and adrenalectomized animals during administration of catecholamines and corticosteroids]. Catecholamines 93-107 serpin family C member 1 Homo sapiens 7-19 5643308-0 1968 Protamine, polybrene and the antithrombin action of heparin. Heparin 52-59 serpin family C member 1 Homo sapiens 29-41 5637480-0 1968 Highly purified antithrombin 3 with heparin cofactor activity prepared by disc electrophoresis. Heparin 36-43 serpin family C member 1 Homo sapiens 16-28 14347404-0 1965 [ELEVATION OF THE ANTITHROMBIN CONTENT OF THE BLOOD DURING COUMARIN THERAPY]. coumarin 59-67 serpin family C member 1 Homo sapiens 18-30 5944879-0 1966 The influence of calcium on the binding of antithrombin by antithrombin inhibitor. Calcium 17-24 serpin family C member 1 Homo sapiens 43-55 5944879-0 1966 The influence of calcium on the binding of antithrombin by antithrombin inhibitor. Calcium 17-24 serpin family C member 1 Homo sapiens 59-71 5857034-1 1965 Some preliminary findings on antithrombin mechanisms under the influence of methylene blue]. Methylene Blue 76-90 serpin family C member 1 Homo sapiens 29-41 4166629-0 1967 Interaction of heparin with the plasma proteins in relation to its antithrombin activity. Heparin 15-22 serpin family C member 1 Homo sapiens 67-79 5865614-0 1965 [On the increase of antithrombin levels during coumarin therapy]. coumarin 47-55 serpin family C member 1 Homo sapiens 20-32 13648508-0 1959 [Antithrombin effect of heparin under the influence of activating and inhibitory factors]. Heparin 24-31 serpin family C member 1 Homo sapiens 1-13 5844087-0 1965 Rise of blood antithrombin level during coumarin therapy. coumarin 40-48 serpin family C member 1 Homo sapiens 14-26 14258688-2 1964 ACTION OF BLOOD PLATELETS AND THEIR PHOSPHOLIPID SUBSTITUTES ON THE ANTITHROMBIN ACTIVITY OF HEPARIN]. Phospholipids 36-48 serpin family C member 1 Homo sapiens 68-80 14258688-2 1964 ACTION OF BLOOD PLATELETS AND THEIR PHOSPHOLIPID SUBSTITUTES ON THE ANTITHROMBIN ACTIVITY OF HEPARIN]. Heparin 93-100 serpin family C member 1 Homo sapiens 68-80 13888345-0 1962 [Relation between variations of plasmatic clearing and antithrombin power after heparin and fatty meal]. Heparin 80-87 serpin family C member 1 Homo sapiens 55-67 14458319-0 1961 The antithrombin activity of glucuronic esters of bilirubin. glucuronic 29-39 serpin family C member 1 Homo sapiens 4-16 14458319-0 1961 The antithrombin activity of glucuronic esters of bilirubin. Esters 40-46 serpin family C member 1 Homo sapiens 4-16 14458319-0 1961 The antithrombin activity of glucuronic esters of bilirubin. Bilirubin 50-59 serpin family C member 1 Homo sapiens 4-16 14390722-0 1955 Studies on the antithrombin and heparin cofactor activities of a fraction adsorbed from plasma by aluminum hydroxide. Aluminum Hydroxide 98-116 serpin family C member 1 Homo sapiens 15-27 13341284-0 1956 [Plasmatic cofactor of heparin and its relations with antithrombin]. Heparin 23-30 serpin family C member 1 Homo sapiens 54-66 13417492-0 1957 [Mechanism of action of heparin as antithrombin and dynamics of fibrin formation]. Heparin 24-31 serpin family C member 1 Homo sapiens 35-47 14945138-0 1952 [The antithrombin effect of heparin. Heparin 28-35 serpin family C member 1 Homo sapiens 5-17 13243272-0 1955 [Thrombin time and antithrombin power of human plasma in the presence of heparin and some synthetic heparinoids]. Heparin 73-80 serpin family C member 1 Homo sapiens 19-31 13243272-0 1955 [Thrombin time and antithrombin power of human plasma in the presence of heparin and some synthetic heparinoids]. Heparinoids 100-111 serpin family C member 1 Homo sapiens 19-31 13135008-0 1953 [Antithrombin action of heparin; role of fibrinogen and of heparin concentration]. Heparin 24-31 serpin family C member 1 Homo sapiens 1-13 13122496-2 1953 An evaluation of true plasma antithrombin titers with particular reference to the Kay test and alpha-tocopherol-calcium gluconate prophylaxis. alpha-Tocopherol 95-111 serpin family C member 1 Homo sapiens 29-41 13198841-0 1954 The antithrombin activity of heparin. Heparin 29-36 serpin family C member 1 Homo sapiens 4-16 13060907-0 1953 [Plasma content of accelerator and antithrombin active substance in dicumarol induced prothrombinemia]. Dicumarol 68-77 serpin family C member 1 Homo sapiens 35-47 34017838-3 2021 The experimental results showed that PLA-combined Fe3O4-GO-ASA nanobubbles could effectively improve the antithrombin parameters of PT, TT, APTT, and INR, and significantly inhibit thrombosis when the composite nanobubbles with a concentration of 80 mg mL-1 interacted with the rabbit blood. fe3o4-go-asa 50-62 serpin family C member 1 Homo sapiens 105-117 15391885-0 1949 Effect of ultrafiltration and carbon dioxide on antithrombin activity of fresh and stored human plasma. Carbon Dioxide 30-44 serpin family C member 1 Homo sapiens 48-60 20265749-0 1947 Variations in prothrombin and antithrombin following the administration of dicumarol. Dicumarol 75-84 serpin family C member 1 Homo sapiens 30-42 14782864-0 1950 Determination of serum prothrombin with a two-stage method, using alcohol to block antithrombin activity. Alcohols 66-73 serpin family C member 1 Homo sapiens 83-95 33601159-1 2021 The highly anionic synthetic pentasaccharide fondaparinux (FDPX) - representing the antithrombin binding sequence of heparin - is in clinical use as a potent anticoagulant. pentasaccharide 29-44 serpin family C member 1 Homo sapiens 84-96 32040256-0 2021 Antithrombin III as predictive indicator of survival in IPF patients treated with Nintedanib: a preliminary study. nintedanib 82-92 serpin family C member 1 Homo sapiens 0-16 32040256-3 2021 A previous proteomic analysis of serum of IPF patients before and after one year of Nintedanib treatment showed differential protein expression of antithrombin III. nintedanib 84-94 serpin family C member 1 Homo sapiens 147-163 32040256-5 2021 METHODS: Serum levels of ATIII were measured by ELISA in 14 IPF patients before and after one year of Nintedanib treatment. nintedanib 102-112 serpin family C member 1 Homo sapiens 25-30 32040256-10 2021 The results of this preliminary study suggest, that ATIII has potential as a biomarker of IPF severity and in predicting answer to Nintedanib therapy. nintedanib 131-141 serpin family C member 1 Homo sapiens 52-57 33929278-8 2021 Heparin potentiates antithrombin and hirudin binds to active thrombin, inactivating the thrombin irreversibly. Heparin 0-7 serpin family C member 1 Homo sapiens 20-32 33924175-1 2021 Antithrombin (AT) is a natural anticoagulant that interacts with activated proteases of the coagulation system and with heparan sulfate proteoglycans (HSPG) on the surface of cells. Heparitin Sulfate 120-135 serpin family C member 1 Homo sapiens 0-12 33601159-1 2021 The highly anionic synthetic pentasaccharide fondaparinux (FDPX) - representing the antithrombin binding sequence of heparin - is in clinical use as a potent anticoagulant. Fondaparinux 45-57 serpin family C member 1 Homo sapiens 84-96 33601159-1 2021 The highly anionic synthetic pentasaccharide fondaparinux (FDPX) - representing the antithrombin binding sequence of heparin - is in clinical use as a potent anticoagulant. Fondaparinux 59-63 serpin family C member 1 Homo sapiens 84-96 33601159-1 2021 The highly anionic synthetic pentasaccharide fondaparinux (FDPX) - representing the antithrombin binding sequence of heparin - is in clinical use as a potent anticoagulant. Heparin 117-124 serpin family C member 1 Homo sapiens 84-96 33917853-0 2021 Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods. Heparin 52-59 serpin family C member 1 Homo sapiens 36-48 33756075-4 2021 We found that substitutions with hydrophobic amino acids in the loop region possessed significantly enhanced antithrombin activity, up to 3-fold higher than the native TBA. tba 168-171 serpin family C member 1 Homo sapiens 109-121 33917853-1 2021 Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Serine 23-29 serpin family C member 1 Homo sapiens 0-12 33917853-1 2021 Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Heparin 88-95 serpin family C member 1 Homo sapiens 0-12 32536326-12 2021 Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003). Heparin 99-106 serpin family C member 1 Homo sapiens 0-12 33187852-0 2021 Successful Antithrombin Administration in Andexanet Alfa-Associated Heparin Resistance. Heparin 68-75 serpin family C member 1 Homo sapiens 11-23 33860518-4 2021 Thus, by activating antithrombin, heparin mainly inhibits factor Xa and thrombin, whereas VKAs lower the levels of the vitamin K-dependent clotting factors. Heparin 34-41 serpin family C member 1 Homo sapiens 20-32 33860518-4 2021 Thus, by activating antithrombin, heparin mainly inhibits factor Xa and thrombin, whereas VKAs lower the levels of the vitamin K-dependent clotting factors. Vitamin K 119-128 serpin family C member 1 Homo sapiens 20-32 32536326-0 2021 Application of goal-directed therapy for the use of concentrated antithrombin for heparin resistance during cardiac surgery. Heparin 82-89 serpin family C member 1 Homo sapiens 65-77 32536326-3 2021 The purpose of this study was to evaluate a goal-directed approach for the use of antithrombin in patients who were resistant to heparin. Heparin 129-136 serpin family C member 1 Homo sapiens 82-94 32536326-5 2021 A goal-directed protocol for antithrombin was established based upon heparin dosing (400 IU kg-1 body weight) and achieving an activated clotting time of >=500 seconds prior to cardiopulmonary bypass. Heparin 69-76 serpin family C member 1 Homo sapiens 29-41 32536326-10 2021 Patients in the antithrombin group were on preoperative heparin therapy (80.0% vs. 24.6%, p = 0.001). Heparin 56-63 serpin family C member 1 Homo sapiens 16-28 32536326-12 2021 Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003). Heparin 34-41 serpin family C member 1 Homo sapiens 0-12 32536326-12 2021 Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003). Heparin 99-106 serpin family C member 1 Homo sapiens 0-12 32536326-12 2021 Antithrombin patients had a lower heparin sensitivity index (0.55 +- 0.17 vs. 1.05 +- 0.44 seconds heparin-1 IU kg-1, p = 0.001), received more total heparin (961.3 +- 158.5 IU kg-1 vs. 677.5 +- 199.0 IU kg-1, p = 0.001), more cardiopulmonary bypass heparin (22,500 +- 10,300 IU vs. 12,100 +- 13,200 IU, p = 0.016), and more protamine (5.4 +- 1.2 vs. 4.1 +- 1.1 mg kg-1, p = 0.003). Heparin 99-106 serpin family C member 1 Homo sapiens 0-12 32536326-14 2021 Utilization of a goal-directed algorithm for the administration of antithrombin for the treatment of heparin resistance is effective in patients undergoing cardiac surgery. Heparin 101-108 serpin family C member 1 Homo sapiens 67-79 32650697-3 2021 Antithrombin is administered to potentiate heparin"s effects. Heparin 43-50 serpin family C member 1 Homo sapiens 0-12 33176060-9 2021 In addition to the chain length, the type and extent of sulfation of glycosaminoglycans influenced the ability of skeletal muscle myosin to neutralize the polysaccharide"s ability to enhance antithrombin"s activity. Polysaccharides 155-169 serpin family C member 1 Homo sapiens 191-203 33169829-6 2021 Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds. Disulfides 13-22 serpin family C member 1 Homo sapiens 84-92 33169829-6 2021 Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds. Disulfides 13-22 serpin family C member 1 Homo sapiens 145-153 33169829-6 2021 Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds. Disulfides 185-194 serpin family C member 1 Homo sapiens 145-153 33169829-6 2021 Knockdown of disulfide-isomerase PDIA4, a measured interactor with significance for SERPINC1 but not SERPINA1, led to the decreased secretion of SERPINC1, which relies on its extensive disulfide bonds, compared to SERPINA1, which has no disulfide bonds. Disulfides 185-194 serpin family C member 1 Homo sapiens 145-153 33176060-0 2021 Skeletal muscle myosin and cardiac myosin attenuate heparin"s antithrombin-dependent anticoagulant activity. Heparin 52-59 serpin family C member 1 Homo sapiens 62-74 33176060-1 2021 BACKGROUND: Heparin enhances the ability of the plasma protease inhibitor, antithrombin, to neutralize coagulation factor Xa and thrombin. Heparin 12-19 serpin family C member 1 Homo sapiens 75-87 33387876-0 2021 SERPINC1 novel mutation (c.637C > T p. Gln213Ter) in a cerebral venous sinus thrombosis case and treatment with agatroban. agatroban 112-121 serpin family C member 1 Homo sapiens 0-8 33176060-3 2021 OBJECTIVES: The aim of this study was to investigate the influence of myosin binding to heparin on antithrombin"s anticoagulant activity. Heparin 88-95 serpin family C member 1 Homo sapiens 99-111 33367661-0 2021 The Effect of Direct Oral Anticoagulants on Antithrombin Activity Testing Is Abolished by DOAC-Stop in Venous Thromboembolism Patients. 1-(4-acetyl-2,5-dimethoxyphenyl)-2-aminopropane 90-94 serpin family C member 1 Homo sapiens 44-56 33176060-4 2021 METHODS: Inhibition of factor Xa and thrombin by antithrombin in the presence of different heparins and skeletal muscle myosin or cardiac myosin was studied by measuring inhibition of each enzyme"s chromogenic substrate hydrolysis. Heparin 91-99 serpin family C member 1 Homo sapiens 49-61 33176060-5 2021 RESULTS AND CONCLUSIONS: Skeletal muscle myosin and cardiac myosin neutralized unfractionated heparin"s enhancement of antithrombin"s inhibition of purified factor Xa and thrombin. Heparin 94-101 serpin family C member 1 Homo sapiens 119-131 33176060-6 2021 Skeletal muscle myosin also reduced the inhibition of factor Xa and thrombin by antithrombin in the presence of heparan sulfate. Heparitin Sulfate 112-127 serpin family C member 1 Homo sapiens 80-92 33176060-9 2021 In addition to the chain length, the type and extent of sulfation of glycosaminoglycans influenced the ability of skeletal muscle myosin to neutralize the polysaccharide"s ability to enhance antithrombin"s activity. Glycosaminoglycans 69-87 serpin family C member 1 Homo sapiens 191-203 33528157-2 2021 Unfractionated heparin (UFH) is commonly used, which depends on native antithrombin (AT) function to exert anticoagulant effects. Heparin 15-22 serpin family C member 1 Homo sapiens 71-83 33528157-2 2021 Unfractionated heparin (UFH) is commonly used, which depends on native antithrombin (AT) function to exert anticoagulant effects. Heparin 24-27 serpin family C member 1 Homo sapiens 71-83 33419227-0 2021 N-Glycosylation as a Tool to Study Antithrombin Secretion, Conformation, and Function. Nitrogen 0-1 serpin family C member 1 Homo sapiens 35-47 33419227-3 2021 Antithrombin, a serpin with four potential N-glycosylation sites, plays a pivotal role in hemostasis, wherein its deficiency significantly increases thrombotic risk. Nitrogen 43-44 serpin family C member 1 Homo sapiens 0-12 32920809-13 2021 On crossed immunoelectrophoresis, an increase of antithrombin fractions with reduced heparin affinity was observed under high ionic strength conditions but not under physiological conditions. Heparin 85-92 serpin family C member 1 Homo sapiens 49-61 32920809-17 2021 CONCLUSION: Antithrombin p.Thr147Ala, responsible for antithrombin type II heparin binding site deficiency, is the first founder mutation reported in people of African ancestry. Heparin 76-83 serpin family C member 1 Homo sapiens 13-25 32920809-17 2021 CONCLUSION: Antithrombin p.Thr147Ala, responsible for antithrombin type II heparin binding site deficiency, is the first founder mutation reported in people of African ancestry. Heparin 76-83 serpin family C member 1 Homo sapiens 55-67 33105321-0 2021 Chronic application of low-dose aspirin affects multiple parameters of three blood cellular types and antithrombin activity: A 1: 1: 1 Propensity Score Matching Analysis. Aspirin 32-39 serpin family C member 1 Homo sapiens 102-114 32829961-4 2021 Reductions in circulating levels of Antithrombin III (AT), the primary mediator of heparin"s action, is present in cases of coronavirus related critical illness. Heparin 83-90 serpin family C member 1 Homo sapiens 36-52 33157292-1 2021 Nafamostat, a serine proteinase inhibitor with various actions including antithrombin, antiplasmin, and antitrypsin effects, has been used in clinical practice to treat disseminated intravascular coagulation (DIC) and pancreatitis. nafamostat 0-10 serpin family C member 1 Homo sapiens 73-85 33105321-6 2021 A dose-dependent relationship was observed between aspirin and decreased HPR incidence (PAA < 0.001, PADP < 0.01, respectively), decreased monocyte ratio (P = 0.052), increased antithrombin activity (P < 0.001), and increased platelet distribution width (P < 0.05). Aspirin 51-58 serpin family C member 1 Homo sapiens 177-189 33105321-8 2021 Our finding demonstrated that aspirin exerts its antithrombotic effects at least by antiplatelet function, enhancing antithrombin activity and suppressing monocytes in vivo. Aspirin 30-37 serpin family C member 1 Homo sapiens 117-129 33343739-6 2021 Experience with low serum albumin levels and antithrombin III activity in nephrotic patients helps to point out the decreasing effects of loop diuretics and heparin to other specialist disciplines. Heparin 157-164 serpin family C member 1 Homo sapiens 45-61 33738401-2 2021 Although conservative treatment options for hereditary AT deficiency-associated VTE such as anticoagulation (warfarin, direct oral anticoagulant, or heparin), intravenous thrombolysis, and recombinant AT are well known, interventional treatment options have not been reported so far. Warfarin 109-117 serpin family C member 1 Homo sapiens 55-57 33738401-2 2021 Although conservative treatment options for hereditary AT deficiency-associated VTE such as anticoagulation (warfarin, direct oral anticoagulant, or heparin), intravenous thrombolysis, and recombinant AT are well known, interventional treatment options have not been reported so far. Heparin 149-156 serpin family C member 1 Homo sapiens 55-57 33390937-11 2020 This study is the first report of administering argatroban and titrating to its appropriate dose in the patient with valve thrombosis, antithrombin deficiency, and HT after mechanical thrombectomy for acute ischemic stroke. argatroban 48-58 serpin family C member 1 Homo sapiens 135-147 33146178-0 2020 Visualizing antithrombin-binding 3-O-sulfated heparan sulfate motifs on cell surfaces. Heparitin Sulfate 46-61 serpin family C member 1 Homo sapiens 12-24 33312433-10 2020 The activity of AT III and PC differed significantly between the two groups from postoperative day 1 to postoperative day 5 (P < 0.05), showing a moderate drop in activity of AT III and PC in the desflurane treatment group and a dramatic drop in the control group. Desflurane 196-206 serpin family C member 1 Homo sapiens 16-22 33312433-10 2020 The activity of AT III and PC differed significantly between the two groups from postoperative day 1 to postoperative day 5 (P < 0.05), showing a moderate drop in activity of AT III and PC in the desflurane treatment group and a dramatic drop in the control group. Desflurane 196-206 serpin family C member 1 Homo sapiens 175-181 33237165-9 2020 The stages of NHL were: I (21%), II (18,4%), III (26,3%), and IV (34,2%), but KS were found only at III (40%) and IV (60%) stages. Potassium 78-80 serpin family C member 1 Homo sapiens 97-103 33305345-6 2020 We administered antithrombin III concentrate with heparin for 5 days; thereafter, we switched to 60 mg edoxaban. Heparin 50-57 serpin family C member 1 Homo sapiens 16-32 32799002-5 2020 Because heparin relies on AT to augment its physiologic function, patients with ATD often exhibit profound heparin resistance. Heparin 8-15 serpin family C member 1 Homo sapiens 26-28 32799002-5 2020 Because heparin relies on AT to augment its physiologic function, patients with ATD often exhibit profound heparin resistance. Heparin 107-114 serpin family C member 1 Homo sapiens 26-28 33146178-1 2020 To map the cellular topography of the rare 3-O-sulfated structural motif of heparan sulfate (HS), we constructed quantum dot-based probes for antithrombin and FGF2, which reveal widely different distribution of the targeted HS motifs. Heparitin Sulfate 93-95 serpin family C member 1 Homo sapiens 142-154 32761495-6 2020 The level of ATIII was significantly negatively correlated with the levels of neutrophils, ferritin, LDH, total bilirubin, IL2R, IL6 and IL8 (p < 0.05). Bilirubin 112-121 serpin family C member 1 Homo sapiens 13-18 33196311-4 2020 We give illustrative examples of benefit-risk evaluations using 4 treatment interventions including sodium glucose cotransporter 2 inhibitors in patients with type 2 diabetes; a direct antithrombin agent, dabigatran, for reducing stroke and systemic embolism in patients with nonvalvular atrial fibrillation; transcatheter aortic valve replacement in patients with symptomatic severe aortic valve stenosis; and antiplatelet agents vorapaxar and prasugrel for reducing cardiovascular events in patients at high cardiovascular risk. Dabigatran 205-215 serpin family C member 1 Homo sapiens 185-197 32945907-1 2020 The 3-O sulfate-modified -GlcNS3S6S- monosaccharide in heparin and heparan sulfate glycosaminoglycans (HSGAGs) is a relatively rare yet important modification that facilitates HSGAG-antithrombin binding and subsequent anticoagulant activity. 3-o sulfate 4-15 serpin family C member 1 Homo sapiens 182-194 32945907-1 2020 The 3-O sulfate-modified -GlcNS3S6S- monosaccharide in heparin and heparan sulfate glycosaminoglycans (HSGAGs) is a relatively rare yet important modification that facilitates HSGAG-antithrombin binding and subsequent anticoagulant activity. -glcns3s6s- monosaccharide 25-51 serpin family C member 1 Homo sapiens 182-194 32945907-1 2020 The 3-O sulfate-modified -GlcNS3S6S- monosaccharide in heparin and heparan sulfate glycosaminoglycans (HSGAGs) is a relatively rare yet important modification that facilitates HSGAG-antithrombin binding and subsequent anticoagulant activity. Heparin 55-62 serpin family C member 1 Homo sapiens 182-194 32945907-1 2020 The 3-O sulfate-modified -GlcNS3S6S- monosaccharide in heparin and heparan sulfate glycosaminoglycans (HSGAGs) is a relatively rare yet important modification that facilitates HSGAG-antithrombin binding and subsequent anticoagulant activity. heparan sulfate glycosaminoglycans 67-101 serpin family C member 1 Homo sapiens 182-194 32745482-0 2020 Novel SERPINC1 missense mutation (Cys462Tyr) causes disruption of the 279Cys-462Cys disulfide bond and leads to type I hereditary antithrombin deficiency. 279cys 70-76 serpin family C member 1 Homo sapiens 6-14 32745482-0 2020 Novel SERPINC1 missense mutation (Cys462Tyr) causes disruption of the 279Cys-462Cys disulfide bond and leads to type I hereditary antithrombin deficiency. Disulfides 84-93 serpin family C member 1 Homo sapiens 6-14 32745482-10 2020 CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family. 279cys 75-81 serpin family C member 1 Homo sapiens 14-22 32745482-10 2020 CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family. 279cys 75-81 serpin family C member 1 Homo sapiens 111-113 32745482-10 2020 CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family. Disulfides 89-98 serpin family C member 1 Homo sapiens 14-22 32745482-10 2020 CONCLUSION: A SERPINC1 missense mutation (Cys462Tyr) causing damage to the 279Cys-462Cys disulfide bond of the AT protein appears to be the cause of Type I AT deficiency in this family. Disulfides 89-98 serpin family C member 1 Homo sapiens 111-113 32947474-1 2020 OBJECTIVES: Supplementation of antithrombin might decrease the amount of heparin needed to achieve a given anticoagulation target during extracorporeal membrane oxygenation. Heparin 73-80 serpin family C member 1 Homo sapiens 31-43 32947474-3 2020 We conceived a study to evaluate the effect of antithrombin supplementation in adult patients requiring venovenous extracorporeal membrane oxygenation for respiratory failure on heparin dose, adequacy of anticoagulation, and safety. Heparin 178-185 serpin family C member 1 Homo sapiens 47-59 32841498-0 2020 Impact of exogenous antithrombin on low molecular weight heparin anti-Xa activity assays in a pediatric and young adult leukemia and lymphoma cohort with variable antithrombin levels. Heparin, Low-Molecular-Weight 36-64 serpin family C member 1 Homo sapiens 20-32 32718661-4 2020 The prototypical heparin-binding protein is antithrombin III (AT), responsible for heparin"s anticoagulant/antithrombotic activity. Heparin 17-24 serpin family C member 1 Homo sapiens 44-60 32907762-3 2020 Clinical efficacy of heparin is due to its interaction with antithrombin (AT) that may be decreased in COVID-19. Heparin 21-28 serpin family C member 1 Homo sapiens 60-72 32791278-0 2020 Antithrombin III-mediated blood coagulation inhibitory activity of chitosan sulfate derivatized with different functional groups. chitosan sulfate 67-83 serpin family C member 1 Homo sapiens 0-16 32791278-2 2020 The beneficial structural properties and high availability of the sulfate group in ChS1 led to greater anticoagulant activity through both the intrinsic and common pathways with antithrombin III (AT III)-mediated inhibition, particularly involving coagulation factors FXa and FIIa. Sulfates 66-73 serpin family C member 1 Homo sapiens 178-194 32791278-2 2020 The beneficial structural properties and high availability of the sulfate group in ChS1 led to greater anticoagulant activity through both the intrinsic and common pathways with antithrombin III (AT III)-mediated inhibition, particularly involving coagulation factors FXa and FIIa. Sulfates 66-73 serpin family C member 1 Homo sapiens 196-202 33083465-9 2020 Antithrombin III activity and body temperature 10 minutes after tourniquet release were significantly lower in the DEX group than in the CON group. Dexmedetomidine 115-118 serpin family C member 1 Homo sapiens 0-16 32404633-14 2020 Comprehensive cost analysis that includes anticoagulant, laboratories, and antithrombin III cost, showed that heparin anticoagulation therapy total cost was significantly higher than bivalirudin (1,184 dollars per day in heparin group vs 494 dollars per day in bivalirudin group; p = 0.03). Heparin 110-117 serpin family C member 1 Homo sapiens 75-91 32515841-0 2020 Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid. Heparin 51-58 serpin family C member 1 Homo sapiens 18-30 32515841-0 2020 Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid. Iduronic Acid 73-86 serpin family C member 1 Homo sapiens 18-30 32515841-0 2020 Degeneracy of the antithrombin binding sequence in heparin: 2-O-sulfated Iduronic acid can replace the critical glucuronic acid. Glucuronic Acid 112-127 serpin family C member 1 Homo sapiens 18-30 32515841-1 2020 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Heparin 0-7 serpin family C member 1 Homo sapiens 31-43 32515841-1 2020 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. pentasaccharide 68-83 serpin family C member 1 Homo sapiens 31-43 32515841-1 2020 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Trisaccharides 104-117 serpin family C member 1 Homo sapiens 31-43 32515841-1 2020 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Glucuronic Acid 138-153 serpin family C member 1 Homo sapiens 31-43 32515841-1 2020 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Glucuronic Acid 155-159 serpin family C member 1 Homo sapiens 31-43 32515841-1 2020 Heparin binds to and activates antithrombin (AT) through a specific pentasaccharide sequence in which a trisaccharide subsite, containing glucuronic acid (GlcA), has been considered as the initiator in the recognition of the polysaccharide by the protein. Polysaccharides 225-239 serpin family C member 1 Homo sapiens 31-43 32515841-3 2020 Indeed, a heparin octasaccharidic sequence obtained by chemoenzymatic synthesis, in which GlcA is replaced by IdoA2S has been found to similarly bind to and activate antithrombin. Heparin 10-17 serpin family C member 1 Homo sapiens 166-178 32515841-3 2020 Indeed, a heparin octasaccharidic sequence obtained by chemoenzymatic synthesis, in which GlcA is replaced by IdoA2S has been found to similarly bind to and activate antithrombin. Glucuronic Acid 90-94 serpin family C member 1 Homo sapiens 166-178 32515841-3 2020 Indeed, a heparin octasaccharidic sequence obtained by chemoenzymatic synthesis, in which GlcA is replaced by IdoA2S has been found to similarly bind to and activate antithrombin. idoa2s 110-116 serpin family C member 1 Homo sapiens 166-178 32515841-5 2020 Interestingly, two IdoA2S units, both present in a 1C4 - 2S0 equilibrium in the unbound saccharide, respectively shift to full 2S0 and full 1C4 upon binding to antithrombin, providing the best illustration of the critical role of iduronic acid conformational flexibility in biological systems. Iduronic Acid 230-243 serpin family C member 1 Homo sapiens 160-172 31686597-1 2020 The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa. Heparin 79-86 serpin family C member 1 Homo sapiens 16-28 31686597-1 2020 The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa. Heparin 79-86 serpin family C member 1 Homo sapiens 30-32 31686597-1 2020 The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa. Heparin 91-98 serpin family C member 1 Homo sapiens 16-28 31686597-1 2020 The activity of antithrombin (AT), a serpin protease inhibitor, is enhanced by heparin and heparin analogs against its target proteases, mainly thrombin, factors Xa and IXa. Heparin 91-98 serpin family C member 1 Homo sapiens 30-32 31686597-8 2020 We could also confirm the high stability of helix P in non-activated AT conformations, such states might play an important role in heparin binding. Heparin 131-138 serpin family C member 1 Homo sapiens 69-71 32020514-7 2020 In vitro purification and characterization of variant AT showed significant decrease in fluorescence emission intensity, decreased bis-ANS fluorescence emission, changes in secondary structure and presence of polymerized AT in patient"s plasma as assessed by fluorescence, circular dichroism and transmission electron microscopy respectively. 5,5'-bis(8-(phenylamino)-1-naphthalenesulfonate) 131-138 serpin family C member 1 Homo sapiens 54-56 31977357-5 2020 The UFH rate decreased after the administration of both types of ATIII. Heparin 4-7 serpin family C member 1 Homo sapiens 65-70 32228213-2 2020 Unfractionated heparin, a glycosaminoglycan that must bind to antithrombin as a cofactor, is currently the standard anticoagulant adopted during extracorporeal membrane oxygenation. Heparin 15-22 serpin family C member 1 Homo sapiens 62-74 32228213-8 2020 Consistently, antithrombin is considered able to achieve better anticoagulation targets in or not in the presence of heparin resistance. Heparin 117-124 serpin family C member 1 Homo sapiens 14-26 32905087-1 2020 Mannose phosphate isomerase deficiency-congenital disorder of glycosylation (MPI-CDG; formerly named CDG type 1b) is characterized by the clinical triad of hepatopathy, protein-losing enteropathy, and hyperinsulinemic hypoglycemia in combination with coagulation disorder (thrombophilia, depletion of antithrombin, proteins C and S, factor XI). Mannosephosphates 0-17 serpin family C member 1 Homo sapiens 301-313 33134780-6 2020 Results: TM-alpha administration did not prolong activated partial thromboplastin time but significantly decreased thrombin-antithrombin complex levels compared with heparin treatment. tm-alpha 9-17 serpin family C member 1 Homo sapiens 124-136 33134780-7 2020 TM-alpha administration reduced consumption of endogenous anticoagulants such as antithrombin and protein C by DIC, compared with the heparin group. tm-alpha 0-8 serpin family C member 1 Homo sapiens 81-93 32905087-1 2020 Mannose phosphate isomerase deficiency-congenital disorder of glycosylation (MPI-CDG; formerly named CDG type 1b) is characterized by the clinical triad of hepatopathy, protein-losing enteropathy, and hyperinsulinemic hypoglycemia in combination with coagulation disorder (thrombophilia, depletion of antithrombin, proteins C and S, factor XI). mpi-cdg 77-84 serpin family C member 1 Homo sapiens 301-313 32347711-5 2020 When applied to a paradigmatic heparin/antithrombin system, the new method generates a series of oligomers with surprisingly distinct sulfation levels. Heparin 31-38 serpin family C member 1 Homo sapiens 39-51 32452976-1 2020 OBJECTIVES: Antithrombin is a cofactor in the coagulation cascade with mild anticoagulant activity and facilitates the action of heparin as an anticoagulant. Heparin 129-136 serpin family C member 1 Homo sapiens 12-24 32452976-15 2020 Age, disease state, and extracorporeal life support should be taken into consideration when administering antithrombin concentrate. concentrate 119-130 serpin family C member 1 Homo sapiens 106-118 32388896-2 2020 Because these tetrasaccharides are derived from antithrombin III-binding sites of heparin, we examined whether this method could be applied to estimate the anticoagulant activity of heparin. Heparin 82-89 serpin family C member 1 Homo sapiens 48-64 32380829-9 2020 We expect that the tuning of plasmonic coupling at 3D level can open up new routes to design high performance SERS substrates for wide applications. sers 110-114 serpin family C member 1 Homo sapiens 48-53 32422680-1 2020 Antithrombin (AT) is a serine protease inhibitor that regulates the activity of coagulation proteases of both intrinsic and extrinsic pathways. Serine 23-29 serpin family C member 1 Homo sapiens 0-12 32523095-8 2020 When the targets of nintedanib (VEGFR, FGFR and PDGFR) were added, enrichment analysis extracted molecular pathways and process networks involved in cell differentiation (haptoglobin and albumin), coagulation (antithrombin III), epithelial mesenchymal transition, cell proliferation and transmigration. nintedanib 20-30 serpin family C member 1 Homo sapiens 210-226 32347711-6 2020 The extent of sulfation of the minimal-length binder (hexamer) is relatively modest yet persistent, consistent with the notion of six sulfate groups being both essential and sufficient for antithrombin binding. Sulfates 134-141 serpin family C member 1 Homo sapiens 189-201 32347711-8 2020 Molecular dynamics simulations confirm the existence of favorable electrostatic interactions between the high charge-density saccharide residues flanking the "canonical" antithrombin-binding hexasaccharide and the positive patch on the surface of the overall negatively charged protein. Carbohydrates 125-135 serpin family C member 1 Homo sapiens 170-182 32347711-8 2020 Molecular dynamics simulations confirm the existence of favorable electrostatic interactions between the high charge-density saccharide residues flanking the "canonical" antithrombin-binding hexasaccharide and the positive patch on the surface of the overall negatively charged protein. hexasaccharide 191-205 serpin family C member 1 Homo sapiens 170-182 31750755-1 2020 BACKGROUND: Antithrombin III deficiency can occur with heparin anticoagulation during extracorporeal membrane oxygenation leading to heparin resistance. Heparin 55-62 serpin family C member 1 Homo sapiens 12-28 32194043-0 2020 Structural alteration in hypochlorous acid modified antithrombin indicates generation of neo-epitopes. Hypochlorous Acid 25-42 serpin family C member 1 Homo sapiens 52-64 32469847-1 2020 BACKGROUND Heparin, often used as an anticoagulant, acts by binding to antithrombin III. Heparin 11-18 serpin family C member 1 Homo sapiens 71-87 32469847-2 2020 Indeed, heparin binds to a variety of proteins other than antithrombin III. Heparin 8-15 serpin family C member 1 Homo sapiens 58-74 31750755-1 2020 BACKGROUND: Antithrombin III deficiency can occur with heparin anticoagulation during extracorporeal membrane oxygenation leading to heparin resistance. Heparin 133-140 serpin family C member 1 Homo sapiens 12-28 31750755-4 2020 METHODS: We conducted a retrospective cohort study using electronic medical records of patients who received >=1 dose of antithrombin III during extracorporeal membrane oxygenation while on continuous heparin. Heparin 201-208 serpin family C member 1 Homo sapiens 121-137 31750755-9 2020 Mean (standard deviation) heparin rates at 6 versus 12 h after antithrombin III for pediatrics were 23.6 (6) versus 23.5 (6.5) units/kg/h (p-value: 0.728), and 15.3 (6.6) versus 13.5 (8) units/kg/h (p-value: 0.188) for adults. Heparin 26-33 serpin family C member 1 Homo sapiens 63-79 31750755-11 2020 Our findings suggest that the use of antithrombin III restores heparin responsiveness in patients with low antithrombin III activity and low anti-Xa activity. Heparin 63-70 serpin family C member 1 Homo sapiens 37-53 31750755-11 2020 Our findings suggest that the use of antithrombin III restores heparin responsiveness in patients with low antithrombin III activity and low anti-Xa activity. Heparin 63-70 serpin family C member 1 Homo sapiens 107-123 32402428-1 2020 The recognized therapeutic effect of heparins is an anticoagulant activity (anti-Xa and anti-IIa) acting in an indirect manner (cofactor of antithrombin) but which is carried by only 20% at best of the glycan chains composing any commercial preparation of heparin, whether unfractionated or low molecular weight. Heparin 37-45 serpin family C member 1 Homo sapiens 140-152 32402428-1 2020 The recognized therapeutic effect of heparins is an anticoagulant activity (anti-Xa and anti-IIa) acting in an indirect manner (cofactor of antithrombin) but which is carried by only 20% at best of the glycan chains composing any commercial preparation of heparin, whether unfractionated or low molecular weight. Heparin 37-44 serpin family C member 1 Homo sapiens 140-152 32402428-10 2020 This also has clinical implications: in the era of generics and biosimilars where biosimilar heparins begin to appear, it is important to know that accordingly to FDA and EMEA rules: their biosimilarity is judged only on the "classical" anticoagulation effect cofactor of antithrombin (anti-IIa/anti-Xa) but that all glycan effects that are potentially beneficial or potentially deleterious are not taken into consideration in their assessment. Heparin 93-101 serpin family C member 1 Homo sapiens 272-284 32397894-3 2020 In the manufacturing process of fractionated antithrombin from plasma, heat treatment, citrate, and freeze drying speed up the transformation of native antithrombin to latent antithrombin. Citric Acid 87-94 serpin family C member 1 Homo sapiens 45-57 31885188-3 2020 Although transitory AT deficiencies and congenital disorders of the N-glycosylation pathways (CDG) have been recently reported as causes of AT deficiency, the current AT clinical screening still only includes anti-FXa activity. Nitrogen 68-69 serpin family C member 1 Homo sapiens 140-142 32397894-3 2020 In the manufacturing process of fractionated antithrombin from plasma, heat treatment, citrate, and freeze drying speed up the transformation of native antithrombin to latent antithrombin. Citric Acid 87-94 serpin family C member 1 Homo sapiens 152-164 32397894-3 2020 In the manufacturing process of fractionated antithrombin from plasma, heat treatment, citrate, and freeze drying speed up the transformation of native antithrombin to latent antithrombin. Citric Acid 87-94 serpin family C member 1 Homo sapiens 152-164 32397894-6 2020 The aims of this work were (1) to convey increased awareness to clinicians who may experience defaulted, expected effect after antithrombin supplementation in, for example, heparin anticoagulation during extracorporeal life support and (2) to urge manufacturers to assess and disclose latent antithrombin content in their products. Heparin 173-180 serpin family C member 1 Homo sapiens 127-139 32397894-6 2020 The aims of this work were (1) to convey increased awareness to clinicians who may experience defaulted, expected effect after antithrombin supplementation in, for example, heparin anticoagulation during extracorporeal life support and (2) to urge manufacturers to assess and disclose latent antithrombin content in their products. Heparin 173-180 serpin family C member 1 Homo sapiens 292-304 32039550-6 2020 RESULTS: Our data confirmed the overestimation of apixaban and rivaroxaban levels by the antithrombin-supplemented anti-Xa method (Berichrom). apixaban 50-58 serpin family C member 1 Homo sapiens 89-101 31950133-10 2020 These data suggest that the antithrombin-binding regions of low molecular weight heparin is required to confer its protective effects on fetal growth and placental development. Heparin 81-88 serpin family C member 1 Homo sapiens 28-40 32300539-1 2020 We report the case of a 35-year-old pregnant woman (gravida 3, para 1) with antithrombin deficiency who was successfully treated with apixaban. apixaban 134-142 serpin family C member 1 Homo sapiens 76-88 32039550-6 2020 RESULTS: Our data confirmed the overestimation of apixaban and rivaroxaban levels by the antithrombin-supplemented anti-Xa method (Berichrom). Rivaroxaban 63-74 serpin family C member 1 Homo sapiens 89-101 31895135-14 2020 The AT-III mRNA levels increased from groups A to C and was positively associated with heparin sensitivity; the factor X mRNA levels changed in the opposite direction; a significant difference was observed between groups A and C (P < 0.05). Heparin 87-94 serpin family C member 1 Homo sapiens 4-10 32048330-2 2020 Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions. Heparin 0-22 serpin family C member 1 Homo sapiens 83-99 32048330-2 2020 Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions. Heparin 0-22 serpin family C member 1 Homo sapiens 101-107 32048330-2 2020 Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions. Heparin 24-27 serpin family C member 1 Homo sapiens 83-99 32048330-2 2020 Unfractionated heparin (UFH) is the mainstay antithrombotic in ECMO and depends on antithrombin III (AT III) to exhibit its actions. Heparin 24-27 serpin family C member 1 Homo sapiens 101-107 32194638-10 2020 This novel mutation resulted in a substitution of arginine by tryptophan, leading to antithrombin resistance (ATR). Arginine 50-58 serpin family C member 1 Homo sapiens 85-97 32194638-10 2020 This novel mutation resulted in a substitution of arginine by tryptophan, leading to antithrombin resistance (ATR). Tryptophan 62-72 serpin family C member 1 Homo sapiens 85-97 31895135-18 2020 Individual variation in heparin sensitivity is related to the mRNA and plasma levels of AT-III and factor X. Heparin 24-31 serpin family C member 1 Homo sapiens 88-94 31959232-5 2020 One aspect of anticoagulation therapy that is particularly challenging is the use of antithrombin (AT) supplementation for heparin resistance. Heparin 123-130 serpin family C member 1 Homo sapiens 85-97 31986476-0 2020 Supplementation with antithrombin III ex vivo optimizes enoxaparin responses in critically injured patients. Enoxaparin 56-66 serpin family C member 1 Homo sapiens 21-37 30913107-3 2020 aXa correlated with heparin (r = 0.97) and antithrombin (r = 0.98) but was unaffected by other parameters. axa 0-3 serpin family C member 1 Homo sapiens 43-55 32010265-7 2020 ATIII expression was a predictor of AKI nondevelopment [Area under the curve (AUC)-Receiving operator characteristic (ROC)=0.729; sensitivity, 0.700; specificity, 0.714], and the ATIII/Creatine ratio was also a predictor of AKI nondevelopment (AUC-ROC=0.971; sensitivity, 0.900; specificity, 1). Creatine 185-193 serpin family C member 1 Homo sapiens 0-5 33214783-0 2020 Evaluation of Heparin Anti-Factor Xa Levels Following Antithrombin Supplementation in Pediatric Patients Supported With Extracorporeal Membrane Oxygenation. Heparin 14-21 serpin family C member 1 Homo sapiens 54-66 31850760-8 2020 Moreover, molecular docking illustrates the mechanism for the antithrombin activity of PfCN. pfcn 87-91 serpin family C member 1 Homo sapiens 62-74 31766871-5 2020 Approach and Results: We observed that ellagic acid and long-chain polyphosphates activated the coagulation system in FXI-deficient plasma, as could be demonstrated by measurement of thrombin generation, FIXa-AT (antithrombin), and FXa-AT complex levels, suggesting an FXI bypass route of FIX activation. Ellagic Acid 39-51 serpin family C member 1 Homo sapiens 213-225 31766871-5 2020 Approach and Results: We observed that ellagic acid and long-chain polyphosphates activated the coagulation system in FXI-deficient plasma, as could be demonstrated by measurement of thrombin generation, FIXa-AT (antithrombin), and FXa-AT complex levels, suggesting an FXI bypass route of FIX activation. Polyphosphates 67-81 serpin family C member 1 Homo sapiens 213-225 31471127-2 2020 Soon it was found that: 1) thrombin inactivation by UFH was associated with the formation of molecular complexes between antithrombin and the activated forms of factor X (FXa) and thrombin, 2) low-molecular-weight fractions of UFH lose their antithrombin activity while still interacting with FXa, 3) a pentasaccharide sequence of UHF increases FXa (but not thrombin) inactivation by antithrombin. pentasaccharide 303-318 serpin family C member 1 Homo sapiens 121-133 33214783-2 2020 Heparin works by potentiating the effects of antithrombin (AT), which may be deficient in critically ill patients and can be replaced. Heparin 0-7 serpin family C member 1 Homo sapiens 45-57 32002903-5 2020 In addition, many plasma proteins such as antithrombin III, superoxide dismutase, C1 inhibitor, and growth factors and cytokines bind to heparan sulfate and by this scenario contribute to the establishment of an anticoagulant and anti-inflammatory endothelial surface. Heparitin Sulfate 137-152 serpin family C member 1 Homo sapiens 42-58 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). Heparin 359-366 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). argatroban 470-480 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). bivalirudin 482-493 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). dabigatran 495-505 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). rivaroxaban 534-545 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). apixaban 547-555 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). edoxaban 557-565 serpin family C member 1 Homo sapiens 44-56 31894660-2 2020 Guidance for laboratory testing to diagnose antithrombin deficiency include the use of an activity assay for initial testing, performing an antigen test and activity-to-antigen ratio when the activity level is low, using pediatric reference ranges until the age of 6 months, excluding acquired causes of low antithrombin (e.g. liver dysfunction, proteinuria, heparin, disseminated intravascular coagulation, thrombosis, surgery) or falsely normal/elevated results (e.g. argatroban, bivalirudin, dabigatran in factor IIa-based assays; rivaroxaban, apixaban, edoxaban, but not betrixaban in Xa-based assays). betrixaban 575-585 serpin family C member 1 Homo sapiens 44-56 32152974-0 2020 Formulation and Characterization of Antithrombin Perfluorocarbon Nanoparticles. Fluorocarbons 49-64 serpin family C member 1 Homo sapiens 36-48 32128502-9 2020 Discussion : Patients with AT III deficiency are likely to be heparin-resistant and will require higher heparin doses or the administration of AT III replacement therapy for the treatment of thrombosis, both of which are associated with an increased risk for haemorrhagic complications. Heparin 62-69 serpin family C member 1 Homo sapiens 27-33 32835836-9 2020 Multiple regression analysis adjusted for age, body-mass index, and fibrinogen levels showed that anti-FXa activity, antithrombin activity, and FVIII activity determined Ks, while anti-FXa activity, plasminogen activator inhibitor-1 level, and presence of right ventricular dysfunction determined CLT. Potassium 170-172 serpin family C member 1 Homo sapiens 117-129 32128502-9 2020 Discussion : Patients with AT III deficiency are likely to be heparin-resistant and will require higher heparin doses or the administration of AT III replacement therapy for the treatment of thrombosis, both of which are associated with an increased risk for haemorrhagic complications. Heparin 104-111 serpin family C member 1 Homo sapiens 27-33 31747245-4 2019 Constructing an array with TAMRA-modified DNA aptamers that bind to different sites of human thrombin provides fluorescence fingerprints that reflect a reduction of the exposed surface area of thrombin upon complexation with antithrombin III, even in the presence of human serum. tamra 27-32 serpin family C member 1 Homo sapiens 225-241 31861225-2 2019 Various biological activities of heparin/HS are attributed to their specific interaction and regulation with various heparin-binding cytokines, antithrombin (AT), and extracellular matrix (ECM) biomolecules. Heparin 33-40 serpin family C member 1 Homo sapiens 144-156 31797980-1 2019 Heparin is a widely used anticoagulant which inhibits factor Xa and thrombin through potentiation of antithrombin. Heparin 0-7 serpin family C member 1 Homo sapiens 101-113 31423004-0 2019 A Comparison of the Oligosaccharide Structures of Antithrombin Derived from Plasma and Recombinant Using POTELLIGENT Technology. Oligosaccharides 20-35 serpin family C member 1 Homo sapiens 50-62 31423004-1 2019 Human antithrombin (AT) has two isoforms of which the predominant alpha-form is glycosylated on all four possible glycosylation sites and the lower abundant beta-isoform lacks the oligosaccharide on Asn135. Oligosaccharides 180-195 serpin family C member 1 Homo sapiens 6-18 31662433-5 2019 Although ATIII has N-glycans and a hydrophobic core, we found that its quality control depended solely on free thiol content. Sulfhydryl Compounds 111-116 serpin family C member 1 Homo sapiens 9-14 31662433-6 2019 Mutagenesis of all six Cys residues in ATIII to Ala resulted in its efficient secretion even though the product was not natively folded. cysteinylcysteine 23-26 serpin family C member 1 Homo sapiens 39-44 31662433-6 2019 Mutagenesis of all six Cys residues in ATIII to Ala resulted in its efficient secretion even though the product was not natively folded. alanyl-alanyl-alanyl-alanine 48-51 serpin family C member 1 Homo sapiens 39-44 31662433-7 2019 ATIII variants with free thiols were retained in the ER but not degraded. Sulfhydryl Compounds 25-31 serpin family C member 1 Homo sapiens 0-5 31279893-2 2019 The anticoagulant process is mainly mediated by the interaction of heparin with antithrombin followed by inhibition of clotting factors IIa (FIIa) and Xa (FXa). Heparin 67-74 serpin family C member 1 Homo sapiens 80-92 31232851-14 2019 Unfractionated heparin dose and baseline antithrombin activity level should be considered when dosing antithrombin in pediatric ventricular assist device patients. Heparin 15-22 serpin family C member 1 Homo sapiens 102-114 31803745-4 2019 Consequently, the therapeutic potency of a heparin is determined by its aIIa activity, i.e., the concentration of a domain in which 12 sugar flank the high affinity antithrombin-binding pentasaccharide (HA5) at one side. Heparin 43-50 serpin family C member 1 Homo sapiens 165-177 31803745-4 2019 Consequently, the therapeutic potency of a heparin is determined by its aIIa activity, i.e., the concentration of a domain in which 12 sugar flank the high affinity antithrombin-binding pentasaccharide (HA5) at one side. Carbohydrates 135-140 serpin family C member 1 Homo sapiens 165-177 31634932-0 2019 Use of Antithrombin Concentrate for Acquired Antithrombin Deficiency in Acutely Unwell Children Receiving Unfractionated Heparin. Heparin 121-128 serpin family C member 1 Homo sapiens 7-19 31283067-13 2019 TEG combined with detection of AT-III and D-Dimer levels can distinguish patient with RSA from those with normal fertility and highly possibly predict the occurrence of RSA. rabbit sperm membrane autoantigen 86-89 serpin family C member 1 Homo sapiens 31-37 31162225-0 2019 Non-Antithrombin-Mediated Heparin Resistance During Cardiac Surgery: Two Case Reports. Heparin 26-33 serpin family C member 1 Homo sapiens 4-16 31162225-1 2019 It is well known that antithrombin (AT) deficiency results in decreased heparin sensitivity, also known as "heparin resistance." Heparin 72-79 serpin family C member 1 Homo sapiens 22-34 31162225-1 2019 It is well known that antithrombin (AT) deficiency results in decreased heparin sensitivity, also known as "heparin resistance." Heparin 108-115 serpin family C member 1 Homo sapiens 22-34 31572449-3 2019 Hence, in the present study, we conducted a case-control study to further evaluate the association between the variant rs2227589 with antithrombin deficiency in pulmonary embolism (PTE). poly(thienyl ethylene oxide butyl sulfonate) 181-184 serpin family C member 1 Homo sapiens 134-146 30540616-4 2019 When heparin resistance was encountered, 54.2% of respondents (95% CI, 50.0%-58.4%) administered antithrombin concentrates as a first-line therapy. Heparin 5-12 serpin family C member 1 Homo sapiens 97-109