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Article

Shear-Induced Unfolding and Enzymatic Cleavage of Full-Length VWF Multimers.

Biophysical journal - 2 Feb 2016

Lippok Svenja, Radtke Matthias, Obser Tobias, Kleemeier Lars, Schneppenheim Reinhard, Budde Ulrich, Netz Roland R, Rädler Joachim O

Abstract excerpt

Proteolysis of the multimeric blood coagulation protein von Willebrand Factor (VWF) by ADAMTS13 is crucial for prevention of microvascular thrombosis. ADAMTS13 cleaves VWF within the mechanosensitive A2 domain, which is believed to open under shear flow. In this study, we combine fluorescence correlation spectroscopy (FCS) and a microfluidic shear cell to monitor real-time kinetics of full-length VWF proteolysis...

Topics

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ADAM Proteins
ADAMTS13 gene
VWF gene
Mutation
Protein Multimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Unfolding

von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 26840720
DOI: 10.1016/j.bpj.2015.12.023
PMCID: PMC4744175

Genes

VWF
ADAMTS13

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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Shear-Induced Unfolding and Enzymatic Cleavage of Full-Length VWF Multimers.PMID 26840720Read ↗

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