PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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 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 9184148-4 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 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 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 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 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 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 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 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. Oligosaccharides 144-160 serpin family C member 1 Homo sapiens 175-187 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 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 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 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 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 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 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 2922702-6 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 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 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 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 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 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 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 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 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 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 6721831-2 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 6721831-3 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 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. Oligosaccharides 106-122 serpin family C member 1 Homo sapiens 127-139 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 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 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 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 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 25145542-0 2014 Antithrombin-binding oligosaccharides: structural diversities in a unique function? Oligosaccharides 21-37 serpin family C member 1 Homo sapiens 0-12 25145542-4 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 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 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 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 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 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 14556453-3 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 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 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 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 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 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 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 10427858-3 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 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