Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI - Wikidata - awgldk - TriplyDB

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

http://www.wikidata.org/entity/Q57372279

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Crystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactions A role for factor XIIa-mediated factor XI activation in thrombus formation in vivo Structure of AMA1 from Plasmodium falciparum reveals a clustering of polymorphisms that surround a conserved hydrophobic pocket.Structure and function of factor XI Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa Sulfated pentagalloylglucoside is a potent, allosteric, and selective inhibitor of factor XIa Activated factor XI increases the procoagulant activity of the extrinsic pathway by inactivating tissue factor pathway inhibitor Site-specific N-glycosylation analysis of human factor XI: Identification of a noncanonical NXC glycosite.Allosteric inhibition of factor XIa. Sulfated non-saccharide glycosaminoglycan mimetics as promising anticoagulants.Platelet-Derived Short-Chain Polyphosphates Enhance the Inactivation of Tissue Factor Pathway Inhibitor by Activated Coagulation Factor XI.Characterization of Novel Forms of Coagulation Factor XIa: independence of factor XIa subunits in factor IX activation.Factor XI contributes to thrombin generation in the absence of factor XII Update on the physiology and pathology of factor IX activation by factor XIa.Identification of coagulation factor XI as a ligand for platelet apolipoprotein E receptor 2 (ApoER2).Structural and functional features of factor XI.The many faces of the contact pathway and their role in thrombosis.Crystal structure of the factor XI zymogen reveals a pathway for transactivation.An update on factor XI structure and function.Unravelling the mechanism and significance of thrombin binding to platelet glycoprotein Ib.Cell Receptor and Cofactor Interactions of the Contact Activation System and Factor XI.

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P2860

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

http://www.wikidata.org/entity/Q57372279

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im August 2004 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2004

@uk

name

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@en

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@nl

type

label

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@en

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@nl

prefLabel

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@en

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@nl

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Journal of Biological Chemistry

P1476

Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI

@en

P2093

David Gailani

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

Frank A. Baglia

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

José A. López

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

Peter N. Walsh

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

P2860

Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain

Crystal structure of the platelet glycoprotein Ib(alpha) N-terminal domain reveals an unmasking mechanism for receptor activation

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

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

Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein.

Factor XI activation in a revised model of blood coagulation.

The glycoprotein Ib-IX-V complex mediates localization of factor XI to lipid rafts on the platelet membrane.

Factor XI activation by thrombin and factor XIa.

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45470-45476

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scholarly article

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10.1074/JBC.M406727200

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44

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279

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2004-08-17T00:00:00Z

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P698

15317813

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