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Article

Shear-induced unfolding activates von Willebrand factor A2 domain for proteolysis.

Journal of thrombosis and haemostasis : JTH - 1 Dec 2009

Baldauf C, Schneppenheim R, Stacklies W, Obser T, Pieconka A, Schneppenheim S, Budde U, Zhou J, Gräter F

Abstract excerpt

BACKGROUND: To avoid pathological platelet aggregation by von Willebrand factor (VWF), VWF multimers are regulated in size and reactivity for adhesion by ADAMTS13-mediated proteolysis in a shear flow dependent manner. OBJECTIVE AND METHODS: We examined whether tensile stress in VWF under shear flow activates the VWF A2 domain for cleavage by ADAMTS13 using molecular dynamics simulations. We generated a full...

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Share to ADAM Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 19817991
DOI: 10.1111/j.1538-7836.2009.03640.x

Genes

VWF
ADAMTS13

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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