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Article

An amino acid polymorphism in von Willebrand factor correlates with increased susceptibility to proteolysis by ADAMTS13.

Blood - 1 Feb 2004

Bowen Derrick John, Collins Peter William

Abstract excerpt

The hypothesis that increased ADAMTS13 (a disintegrin and metalloprotease with thrombospondin repeats) activity or increased susceptibility of von Willebrand factor (VWF) to proteolysis by ADAMTS13 may underlie type I von Willebrand disease (VWD) in some patients was investigated. Plasma from 4 patients with type I VWD was cryoprecipitated. ADAMTS13 activity in the VWF-poor cryodepleted fraction was assessed by...

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Source

Identifiers

PMID: 14525793
DOI: 10.1182/blood-2003-05-1505

Genes

VWF
ADAMTS13

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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An amino acid polymorphism in von Willebrand factor correlates with increased susceptibility to proteolysis by ADAMTS13.PMID 14525793Read ↗

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ADAMTS13 cleavage efficiency is altered by mutagenic and, to a lesser extent, polymorphic sequence changes in the A1 and A2 domains of von Willebrand factor.Semantic proximity Read ↗

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C2362F mutation gives rise to an ADAMTS13-resistant von Willebrand factor.Semantic proximity Read ↗

Founder von Willebrand factor haplotype associated with type 1 von Willebrand disease.Semantic proximity Read ↗

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ADAMTS-13 cysteine-rich/spacer domains are functionally essential for von Willebrand factor cleavage.Semantic proximity Read ↗

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