Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib - Wikidata - awgldk - TriplyDB

Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

http://www.wikidata.org/entity/Q27681197

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Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.Data on the purification and crystallization of the loss-of-function von Willebrand disease variant (p.Gly1324Ser) of the von Willebrand factor A1 domain.Enhanced Local Disorder in a Clinically Elusive von Willebrand Factor Provokes High-Affinity Platelet Clumping.von Willebrand factor, Jedi knight of the bloodstream Exploiting the kinetic interplay between GPIbα-VWF binding interfaces to regulate hemostasis and thrombosis Identification of a juxtamembrane mechanosensitive domain in the platelet mechanosensor glycoprotein Ib-IX complex.Force-induced on-rate switching and modulation by mutations in gain-of-function von Willebrand diseases.Structural origins of misfolding propensity in the platelet adhesive von Willebrand factor A1 domain.Force-Induced Unfolding of Leucine-Rich Repeats of Glycoprotein Ibα Strengthens Ligand Interaction Platelet clearance via shear-induced unfolding of a membrane mechanoreceptor.Primary haemostasis: newer insights.Spectrum of the mutations in Bernard-Soulier syndrome.A biophysical view on von Willebrand factor activation.N-linked glycan stabilization of the VWF A2 domain Force-sensitive autoinhibition of the von Willebrand factor is mediated by interdomain interactions Flow-induced elongation of von Willebrand factor precedes tension-dependent activation.A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct.Refrigeration-Induced Binding of von Willebrand Factor Facilitates Fast Clearance of Refrigerated Platelets.A discontinuous autoinhibitory module masks the A1 domain of von Willebrand factor.Qualitative and quantitative modifications of von Willebrand factor in patients with essential thrombocythemia and controlled platelet count.

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

http://www.wikidata.org/entity/Q27681197

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2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2014 թվականի փետրվարին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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JBC.M113.511220

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Journal of Biological Chemistry

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Structural Basis of Regulation of von Willebrand Factor Binding to Glycoprotein Ib

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Mark A Blenner

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

Timothy A Springer

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

Xianchi Dong

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P2860

Biochemistry and genetics of von Willebrand factor

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain

Modulation of alpha-thrombin function by distinct interactions with platelet glycoprotein Ibalpha

Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor

Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations

A pH-regulated dimeric bouquet in the structure of von Willebrand factor

Electrostatics of nanosystems: application to microtubules and the ribosome

PHENIX: a comprehensive Python-based system for macromolecular structure solution

MolProbity: all-atom contacts and structure validation for proteins and nucleic acids

von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule

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5565-79

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scholarly article

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3328954

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10.1074/JBC.M113.511220

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9

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289

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2014-02-28T00:00:00Z

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