Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor. - Wikidata - wikimedia - TriplyDB

Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.

Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.

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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.A biophysical view on von Willebrand factor activation.Clinical and laboratory phenotype variability in type 2M von Willebrand disease.The physical spacing between the von willebrand factor d'd3- and a1- domains regulates platelet adhesion in vitro and in vivo.A discontinuous autoinhibitory module masks the A1 domain of von Willebrand factor.The Von Willebrand Factor A1-Collagen III Interaction Is Independent of Conformation and Type 2 Von Willebrand Disease Phenotype.

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Mutational Constraints on Local Unfolding Inhibit the Rheological Adaptation of von Willebrand Factor.

http://www.wikidata.org/entity/Q30382597

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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Mutational Constraints on Loca ...... tion of von Willebrand Factor.

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Mutational Constraints on Loca ...... tion of von Willebrand Factor.

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Mutational Constraints on Loca ...... tion of von Willebrand Factor.

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Mutational Constraints on Loca ...... tion of von Willebrand Factor.

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Mutational Constraints on Loca ...... tion of von Willebrand Factor.

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JBC.M115.703850

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Journal of Biological Chemistry

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Mutational Constraints on Loca ...... ation of von Willebrand Factor

@en

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Alexander Tischer

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

Banumathi Sankaran

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Choel Kim

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James C Campbell

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Laurie Moon-Tasson

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Linda M Benson

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

Venkata R Machha

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P2860

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

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

Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins

Von Willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kinetics

Structural basis of von Willebrand factor activation by the snake toxin botrocetin

Crystal structure of von Willebrand factor A1 domain complexed with snake venom, bitiscetin: insight into glycoprotein Ibalpha binding mechanism induced by snake venom proteins

A Structural Explanation for the Antithrombotic Activity of ARC1172, a DNA Aptamer that Binds von Willebrand Factor Domain A1

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

Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab

Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib

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3848-3859

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