Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity.
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The anticoagulant activation of antithrombin by heparinCrystal structure of monomeric native antithrombin reveals a novel reactive center loop conformationAn overview of the serpin superfamilyThe conformational activation of antithrombin. A 2.85-A structure of a fluorescein derivative reveals an electrostatic link between the hinge and heparin binding regionsThe influence of hinge region residue Glu-381 on antithrombin allostery and metastabilityInhibitory properties of the P1 Tyr variant of antithrombin.Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammationRole of P2 glycine in determining the specificity of antithrombin reaction with coagulation proteases.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.The effect of a reducing-end extension on pentasaccharide binding by antithrombin.Inhibitory serpins. New insights into their folding, polymerization, regulation and clearance.The infective polymerization of conformationally unstable antithrombin mutants may play a role in the clinical severity of antithrombin deficiency.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.Effect of citrullination on the function and conformation of antithrombin.Helix D elongation and allosteric activation of antithrombin.Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin.A chemically-modified inactive antithrombin as a potent antagonist of fondaparinux and heparin anticoagulant activity.
P2860
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P2860
Heparin-dependent modification of the reactive center arginine of antithrombin and consequent increase in heparin binding affinity.
description
1997 nî lūn-bûn
@nan
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
1997年论文
@zh
1997年论文
@zh-cn
name
Heparin-dependent modification ...... e in heparin binding affinity.
@en
type
label
Heparin-dependent modification ...... e in heparin binding affinity.
@en
prefLabel
Heparin-dependent modification ...... e in heparin binding affinity.
@en
P2093
P2860
P356
P1476
Heparin-dependent modification ...... e in heparin binding affinity.
@en
P2093
Carrell RW
P2860
P304
19652-19655
P356
10.1074/JBC.272.32.19652
P407
P50
P577
1997-08-01T00:00:00Z