The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site
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Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidisThe anticoagulant activation of antithrombin by heparinAn overview of the serpin superfamilyInhibition of antithrombin by hyaluronic acid may be involved in the pathogenesis of rheumatoid arthritis.The conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regionsTopography of a 2.0 Å structure of α1-antitrypsin reveals targets for rational drug design to prevent conformational diseaseC1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational diseaseContribution of basic residues of the A helix of heparin cofactor II to heparin- or dermatan sulfate-mediated thrombin inhibitionStructure of a serpin-enzyme complex probed by cysteine substitutions and fluorescence spectroscopy.The role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsinStructure of heparin-derived tetrasaccharide complexed to the plasma protein antithrombin derived from NOEs, J-couplings and chemical shifts.Cloning of the full-length cDNA of porcine antithrombin III and comparison with its human homolog.From natural to synthetic multisite thrombin inhibitors.Hydration effects of heparin on antithrombin probed by osmotic stress.Latent antithrombin and its detection, formation and turnover in the circulation.Anti-thrombin is expressed in the benign prostatic epithelium and in prostate cancer and is capable of forming complexes with prostate-specific antigen and human glandular kallikrein 2.Heparin-binding domains in vascular biology.Serpins in T cell immunity.Smoothing a rugged protein folding landscape by sequence-based redesign.Mutagenesis studies toward understanding the intracellular signaling mechanism of antithrombin.A computational modeling and molecular dynamics study of the Michaelis complex of human protein Z-dependent protease inhibitor (ZPI) and factor Xa (FXa).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.Lysine 114 of antithrombin is of crucial importance for the affinity and kinetics of heparin pentasaccharide binding.Conformational transitions induced in heparin octasaccharides by binding with antithrombin III.Critical role of the linker region between helix D and strand 2A in heparin activation of antithrombin.Effects of glycosylation on heparin binding and antithrombin activation by heparin.The ternary complex of antithrombin-anhydrothrombin-heparin reveals the basis of inhibitor specificity.The N-terminal segment of antithrombin acts as a steric gate for the binding of heparin.Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity.Characterization of the conformational alterations, reduced anticoagulant activity, and enhanced antiangiogenic activity of prelatent antithrombinStructural differences between active forms of plasminogen activator inhibitor type 1 revealed by conformationally sensitive ligands.Elimination of P1 arginine 393 interaction with underlying glutamic acid 255 partially activates antithrombin III for thrombin inhibition but not factor Xa inhibition.Molecular determinants of the mechanism underlying acceleration of the interaction between antithrombin and factor Xa by heparin pentasaccharide.Partial activation of antithrombin without heparin through deletion of a unique sequence on the reactive site loop of the serpin.The heparin-binding site of antithrombin is crucial for antiangiogenic activityIntrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition.Regulation of glycosaminoglycan function by osmotic potentials. Measurement of water transfer during antithrombin activation by heparin.Helix D elongation and allosteric activation of antithrombin.Intracellular accumulation of antithrombin Morioka (C95R), a novel mutation causing type I antithrombin deficiency.Characterization of the necrotic protein that regulates the Toll-mediated immune response in Drosophila.
P2860
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P2860
The 2.6 A structure of antithrombin indicates a conformational change at the heparin binding site
description
1997 nî lūn-bûn
@nan
1997 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The 2.6 A structure of antithr ...... ge at the heparin binding site
@ast
The 2.6 A structure of antithr ...... ge at the heparin binding site
@en
The 2.6 A structure of antithr ...... ge at the heparin binding site
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type
label
The 2.6 A structure of antithr ...... ge at the heparin binding site
@ast
The 2.6 A structure of antithr ...... ge at the heparin binding site
@en
The 2.6 A structure of antithr ...... ge at the heparin binding site
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prefLabel
The 2.6 A structure of antithr ...... ge at the heparin binding site
@ast
The 2.6 A structure of antithr ...... ge at the heparin binding site
@en
The 2.6 A structure of antithr ...... ge at the heparin binding site
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P2093
P50
P3181
P356
P1476
The 2.6 A structure of antithr ...... ge at the heparin binding site
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P2093
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P3181
P356
10.1006/JMBI.1996.0798
P407
P577
1997-02-01T00:00:00Z