PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10201371-6 1999 To obtain more potent and well-tolerated antithrombotic drugs, we wished to synthesize heparin mimetics able to inhibit thrombin, that is, longer oligosaccharides. Oligosaccharides 146-162 coagulation factor II, thrombin Homo sapiens 120-128 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 coagulation factor II, thrombin Homo sapiens 66-74 10328304-2 1999 The pentadecasaccharide is the shortest oligosaccharide able to catalyse thrombin inhibition by AT III. Oligosaccharides 40-55 coagulation factor II, thrombin Homo sapiens 73-81 3782075-6 1986 Moreover, similar binary complexes with 3H-labeled octadecasaccharide or larger chains, but not with smaller oligosaccharides, were capable of binding to matrix-linked inactivated thrombin. Oligosaccharides 109-125 coagulation factor II, thrombin Homo sapiens 180-188 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 coagulation factor II, thrombin Homo sapiens 36-44 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 coagulation factor II, thrombin Homo sapiens 60-68 3218731-7 1988 However, results obtained with heparan sulfate preparations did not indicate any clear relationship between either molecular weight or sulfate content and thrombin binding, but suggested that there may be an oligosaccharide sequence containing N-sulfate residues which confers high affinity for thrombin. Oligosaccharides 208-223 coagulation factor II, thrombin Homo sapiens 295-303 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 coagulation factor II, thrombin Homo sapiens 136-144 6721831-8 1984 The anti-thrombin activities of the octadecasaccharide and larger oligosaccharides were more readily neutralized by platelet factor 4 than were their anti-Factor Xa activities. Oligosaccharides 66-82 coagulation factor II, thrombin Homo sapiens 9-17 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 coagulation factor II, thrombin Homo sapiens 106-114 28755259-3 2017 Accurate mass measurements revealed that the predominant form of native human alpha-thrombin contains a glycosylation mass of 2205 Da, corresponding to a sialylated symmetric biantennary oligosaccharide structure without fucosylation. Oligosaccharides 187-202 coagulation factor II, thrombin Homo sapiens 84-92 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 coagulation factor II, thrombin Homo sapiens 118-126 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 coagulation factor II, thrombin Homo sapiens 122-130 6317088-0 1984 The oligosaccharide of human thrombin: investigations of functional significance. Oligosaccharides 4-19 coagulation factor II, thrombin Homo sapiens 29-37 6317088-1 1984 Functional properties of the carbohydrate chain of human thrombin were examined by quantitating the activity of the enzyme before and after partial removal of its oligosaccharide by exoglycosidases. Oligosaccharides 163-178 coagulation factor II, thrombin Homo sapiens 57-65 6317088-5 1984 It is concluded, therefore, that the oligosaccharide of human thrombin is located outside the major protein and platelet-binding regions of the molecule. Oligosaccharides 37-52 coagulation factor II, thrombin Homo sapiens 62-70 6870248-0 1983 The carbohydrate of human thrombin: structural analysis of glycoprotein oligosaccharides by mass spectrometry. Oligosaccharides 72-88 coagulation factor II, thrombin Homo sapiens 26-34 6870248-1 1983 The carbohydrate structure of human thrombin has been determined by direct probe mass spectrometry of the oligosaccharides released by trifluoroacetolysis from the asialo glycoprotein. Oligosaccharides 106-122 coagulation factor II, thrombin Homo sapiens 36-44 6847629-4 1983 An anti-thrombin III-binding oligosaccharide preparation (containing predominantly eight to ten saccharide units), prepared by degradation of heparin with HNO2 had high (800 units/mg) anti-Factor Xa, but negligible anti-thrombin, specific activity. Oligosaccharides 29-44 coagulation factor II, thrombin Homo sapiens 8-16