The role of high molecular weight kininogen and prothrombin as cofactors in the binding of factor XI A3 domain to the platelet surface
about
Domain V of beta2-glycoprotein I binds factor XI/XIa and is cleaved at Lys317-Thr318Structure and function of factor XISurvey of the year 2000 commercial optical biosensor literature.Assembly, activation, and physiologic influence of the plasma kallikrein/kinin system.The dimeric structure of factor XI and zymogen activationA catalytic domain exosite (Cys527-Cys542) in factor XIa mediates binding to a site on activated platelets.Characterization of Novel Forms of Coagulation Factor XIa: independence of factor XIa subunits in factor IX activation.Microneme proteins in apicomplexans.Identification of coagulation factor XI as a ligand for platelet apolipoprotein E receptor 2 (ApoER2).Molecular characterization of FXI deficiency.The many faces of the contact pathway and their role in thrombosis.The glycoprotein Ib-IX-V complex mediates localization of factor XI to lipid rafts on the platelet membrane.Characterization of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein.The factor IX gamma-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa.Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors.The relative priority of prekallikrein and factors XI/XIa assembly on cultured endothelial cells.Factor XI apple domains and protein dimerization.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.Structural interpretation of 42 mutations causing factor XI deficiency using homology modeling.Factor XI binding to the platelet glycoprotein Ib-IX-V complex promotes factor XI activation by thrombin.Factor XI, but not prekallikrein, blocks high molecular weight kininogen binding to human umbilical vein endothelial cells.Identification of a Binding Site for Glycoprotein Ibα in the Apple 3 Domain of Factor XI
P2860
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P2860
The role of high molecular weight kininogen and prothrombin as cofactors in the binding of factor XI A3 domain to the platelet surface
description
2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2000
@ast
im August 2000 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/08/18)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/08/18)
@nl
наукова стаття, опублікована в серпні 2000
@uk
name
The role of high molecular wei ...... domain to the platelet surface
@ast
The role of high molecular wei ...... domain to the platelet surface
@en
The role of high molecular wei ...... domain to the platelet surface
@nl
type
label
The role of high molecular wei ...... domain to the platelet surface
@ast
The role of high molecular wei ...... domain to the platelet surface
@en
The role of high molecular wei ...... domain to the platelet surface
@nl
prefLabel
The role of high molecular wei ...... domain to the platelet surface
@ast
The role of high molecular wei ...... domain to the platelet surface
@en
The role of high molecular wei ...... domain to the platelet surface
@nl
P2093
P2860
P356
P1476
The role of high molecular wei ...... domain to the platelet surface
@en
P2093
D. Gailani
F. A. Baglia
K. Badellino
M. M. Zhao
P. N. Walsh
P2860
P304
25139–25145
P356
10.1074/JBC.M001890200
P407
P577
2000-08-18T00:00:00Z