Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin.
about
Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activationEngineering the substrate and inhibitor specificities of human coagulation Factor VIIaMolecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complexStructure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin.Allosteric activation of antithrombin critically depends upon hinge region extension.Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Structural and functional characterization of cleavage and inactivation of human serine protease inhibitors by the bacterial SPATE protease EspPα from enterohemorrhagic E. coli.Specificity and selectivity profile of EP217609: a new neutralizable dual-action anticoagulant that targets thrombin and factor XaSaturation Mutagenesis of the Antithrombin Reactive Center Loop P14 Residue Supports a Three-step Mechanism of Heparin Allosteric Activation Involving Intermediate and Fully Activated StatesSerpins in thrombosis, hemostasis and fibrinolysisThe 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.Exosite determinants of serpin specificity.The signature 3-O-sulfo group of the anticoagulant heparin sequence is critical for heparin binding to antithrombin but is not required for allosteric activation.Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors.Limitations of conventional anticoagulant therapy and the promises of non-heparin based conformational activators of antithrombin.Kinetic evidence that allosteric activation of antithrombin by heparin is mediated by two sequential conformational changes.Characterization of the conformational alterations, reduced anticoagulant activity, and enhanced antiangiogenic activity of prelatent antithrombinInhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Engineering functional antithrombin exosites in alpha1-proteinase inhibitor that specifically promote the inhibition of factor Xa and factor IXa.Activation of antithrombin as a factor IXa and Xa inhibitor involves mitigation of repression rather than positive enhancement.Ixolaris: a factor Xa heparin-binding exosite inhibitorDisease-causing mutations in the serpin antithrombin reveal a key domain critical for inhibiting protease activities.Kinetic characterization of the protein Z-dependent protease inhibitor reaction with blood coagulation factor Xa.Residues Tyr253 and Glu255 in strand 3 of beta-sheet C of antithrombin are key determinants of an exosite made accessible by heparin activation to promote rapid inhibition of factors Xa and IXa.
P2860
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P2860
Localization of an antithrombin exosite that promotes rapid inhibition of factors Xa and IXa dependent on heparin activation of the serpin.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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2003年学术文章
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name
Localization of an antithrombi ...... arin activation of the serpin.
@en
Localization of an antithrombi ...... arin activation of the serpin.
@nl
type
label
Localization of an antithrombi ...... arin activation of the serpin.
@en
Localization of an antithrombi ...... arin activation of the serpin.
@nl
prefLabel
Localization of an antithrombi ...... arin activation of the serpin.
@en
Localization of an antithrombi ...... arin activation of the serpin.
@nl
P2093
P2860
P356
P1476
Localization of an antithrombi ...... arin activation of the serpin.
@en
P2093
Gonzalo Izaguirre
Richard Swanson
Steven T Olson
Tina Bedsted
Weiqing Zhang
P2860
P304
51433-51440
P356
10.1074/JBC.M309266200
P407
P577
2003-10-07T00:00:00Z