PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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