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Article

Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbalpha.

Biophysical journal - 22 Jul 2009

Auton Matthew, Sedlák Erik, Marek Jozef, Wu Tao, Zhu Cheng, Cruz Miguel A

Abstract excerpt

In circulation, plasma glycoprotein von Willebrand Factor plays an important role in hemostasis and in pathological thrombosis under hydrodynamic forces. Mutations in the A1 domain of von Willebrand factor cause the hereditary types 2B and 2M von Willebrand disease that either enhance (2B) or inh...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 19619477
DOI: 10.1016/j.bpj.2009.05.009
PMCID: PMC2711320

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19619477-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbalpha.PMID 19619477Read ↗

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

Misfolding of vWF to pathologically disordered conformations impacts the severity of von Willebrand disease.Semantic proximity Read ↗

Type 2B von Willebrand disease mutations differentially perturb autoinhibition of the A1 domain.Semantic proximity Read ↗

Thermodynamic stabilization of the von Willebrand Factor A1 domain due to loss-of-function disease-related mutationsSemantic proximity Read ↗

Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain.Semantic proximity Read ↗

Structural basis of regulation of von Willebrand factor binding to glycoprotein Ib.Semantic proximity Read ↗

GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease.Semantic proximity Read ↗

Structure-resolved dynamics of type 2M von Willebrand disease.Semantic proximity Read ↗

Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF.Semantic proximity Read ↗

A mechanism for localized dynamics-driven affinity regulation of the binding of von Willebrand factor to platelet glycoprotein Ibα.Semantic proximity Read ↗

Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibalpha and platelet activation under shear stress.Semantic proximity Read ↗

Force-induced on-rate switching and modulation by mutations in gain-of-function von Willebrand diseases.Semantic proximity Read ↗

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