Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa - Wikidata - awgldk - TriplyDB

Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa

Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa

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Future prospects for contact factors as therapeutic targets Factor XI as a target for antithrombotic therapy Factor XI Deficiency Alters the Cytokine Response and Activation of Contact Proteases during Polymicrobial Sepsis in Mice The mechanism underlying activation of factor IX by factor XIa.Allosteric inhibition of human factor XIa: discovery of monosulfated benzofurans as a class of promising inhibitors Why factor XI deficiency is a clinical concern.Evidence for factor IX-independent roles for factor XIa in blood coagulation.An update on factor XI structure and function.Generation and characterization of aptamers targeting factor XIa.

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P2860

Analysis of the factor XI variant Arg184Gly suggests a structural basis for factor IX binding to factor XIa

http://www.wikidata.org/entity/Q34153581

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2013 nî lūn-bûn

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2013 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2013 թվականի հուլիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Analysis of the factor XI vari ...... actor IX binding to factor XIa

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Analysis of the factor XI vari ...... actor IX binding to factor XIa

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Analysis of the factor XI vari ...... actor IX binding to factor XIa

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type

label

Analysis of the factor XI vari ...... actor IX binding to factor XIa

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Analysis of the factor XI vari ...... actor IX binding to factor XIa

@en

Analysis of the factor XI vari ...... actor IX binding to factor XIa

@nl

prefLabel

Analysis of the factor XI vari ...... actor IX binding to factor XIa

@ast

Analysis of the factor XI vari ...... actor IX binding to factor XIa

@en

Analysis of the factor XI vari ...... actor IX binding to factor XIa

@nl

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Journal of Thrombosis and Haemostasis

P1476

Analysis of the factor XI vari ...... actor IX binding to factor XIa

@en

P2093

D Gailani

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

I M Verhamme

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

J Emsley

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M F Sun

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S P Bajaj

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

Y Geng

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

P2860

Crystal structure of the calcium-stabilized human factor IX Gla domain bound to a conformation-specific anti-factor IX antibody

Molecular modeling of the prekallikrein structure provides insights into high-molecular-weight kininogen binding and zymogen activation

Structural and mutational analyses of the molecular interactions between the catalytic domain of factor XIa and the Kunitz protease inhibitor domain of protease nexin 2

Exosite-driven substrate specificity and function in coagulation

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

Global kinetic explorer: a new computer program for dynamic simulation and fitting of kinetic data.

Structure and function of factor XI

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

Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule.

Polyphosphate is a cofactor for the activation of factor XI by thrombin.

P304

1374-1384

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scholarly article

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10.1111/JTH.12275

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7

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11

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4158700

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