Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively. - Wikidata - awgldk - TriplyDB

Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively.

Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively.

http://www.wikidata.org/entity/Q45063820

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Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa Structural basis of Na+ activation mimicry in murine thrombin Na+ binding to meizothrombin desF1 Mutant N143P Reveals How Na+ Activates Thrombin Rigidification of the autolysis loop enhances Na+ binding to thrombin Molecular mapping of the thrombin-heparin cofactor II complex Molecular recognition mechanisms of thrombin.Thrombin hydrolysis of human osteopontin is dependent on thrombin anion-binding exosites.How Na+ activates thrombin--a review of the functional and structural data.Biophysical investigation of GpIbalpha binding to thrombin anion binding exosite II.Structure-based predictive models for allosteric hot spots.Structure and function of factor XI Evidence of the E*-E equilibrium from rapid kinetics of Na+ binding to activated protein C and factor Xa.Activation of factor XI by products of prothrombin activation Site-specific N-glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite.Thromboelastography as a better indicator of hypercoagulable state after injury than prothrombin time or activated partial thromboplastin time Receptors, rafts, and microvesicles in thrombosis and inflammation.Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system.Role of Na+ and K+ in enzyme function.Thrombin.Exosites in the substrate specificity of blood coagulation reactions.New Tools to Study Contact Activation.Polyphosphate binds with high affinity to exosite II of thrombin.Crystal structure of the factor XI zymogen reveals a pathway for transactivation.Factor XI interacts with the leucine-rich repeats of glycoprotein Ibalpha on the activated platelet.A novel factor XI missense mutation (Val371Ile) in the activation loop is responsible for a case of mild type II factor XI deficiency.Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

P2860

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P2860

Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively.

http://www.wikidata.org/entity/Q45063820

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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2003年学术文章

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2003年學術文章

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2003年學術文章

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name

Thrombin activation of factor ...... osites I and II, respectively.

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Thrombin activation of factor ...... osites I and II, respectively.

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type

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Thrombin activation of factor ...... osites I and II, respectively.

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Thrombin activation of factor ...... osites I and II, respectively.

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Thrombin activation of factor ...... osites I and II, respectively.

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Thrombin activation of factor ...... osites I and II, respectively.

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P2860

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P1433

Journal of Biological Chemistry

P1476

Thrombin activation of factor ...... osites I and II, respectively.

@en

P2093

Duraiswamy Navaneetham

http://www.w3.org/2001/XMLSchema#string

Frank A Baglia

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José A López

http://www.w3.org/2001/XMLSchema#string

Lawrence L K Leung

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Peter N Walsh

http://www.w3.org/2001/XMLSchema#string

Thomas H Yun

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Timothy Myles

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P2860

Crystal structure of the human alpha-thrombin-haemadin complex: an exosite II-binding inhibitor

The molecular basis of thrombin allostery revealed by a 1.8 A structure of the "slow" form

The refined 1.9-Å X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships

The structure of a complex of recombinant hirudin and human alpha-thrombin

The role of high molecular weight kininogen and prothrombin as cofactors in the binding of factor XI A3 domain to the platelet surface

Vitamin K-dependent carboxylase

Model for a factor IX activation complex on blood platelets: dimeric conformation of factor XIa is essential

Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains

Binding of coagulation factor XI to washed human platelets

A thrombin receptor function for platelet glycoprotein Ib-IX unmasked by cleavage of glycoprotein V.

P304

48112-48119

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P31

scholarly article

P356

10.1074/JBC.M306925200

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P433

48

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P478

278

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2003-09-10T00:00:00Z

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12968031

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