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Article

Essential domains of a disintegrin and metalloprotease with thrombospondin type 1 repeats-13 metalloprotease required for modulation of arterial thrombosis.

Arteriosclerosis, thrombosis, and vascular biology - 1 Oct 2011

Xiao Juan, Jin Sheng-Yu, Xue Jing, Sorvillo Nicoletta, Voorberg Jan, Zheng X Long

Abstract excerpt

OBJECTIVE: A disintegrin and metalloprotease with thrombospondin type 1 repeats-13 (ADAMTS13) inhibits platelet aggregation and arterial thrombosis by cleavage of von Willebrand factor. However, the structural components of ADAMTS13 required for inhibition of arterial thrombosis are not fully defined. METHODS AND RESULTS: Using recombinant proteins and a murine model, we demonstrated that an ADAMTS13 variant...

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Identifiers

PMID: 21799176
DOI: 10.1161/ATVBAHA.111.229609
PMCID: PMC3174348

Genes

ADAMTS13

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Essential domains of a disintegrin and metalloprotease with thrombospondin type 1 repeats-13 metalloprotease required for modulation of arterial thrombosis.PMID 21799176Read ↗

The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formationSemantic proximity Read ↗

Essential role of the disintegrin-like domain in ADAMTS13 function.Semantic proximity Read ↗

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

The distal carboxyterminal domains of murine ADAMTS13 influence proteolysis of platelet-decorated VWF strings in vivo.Semantic proximity Read ↗

Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease.Semantic proximity Read ↗

Mutations and Common Polymorphisms in ADAMTS13 and vWF Genes Responsible for Increasing Risk of Thrombosis.Semantic proximity Read ↗

Expression of a structurally constrained von Willebrand factor variant triggers acute thrombotic thrombocytopenic purpura in mice.Semantic proximity Read ↗

ADAMTS proteases in cardiovascular physiology and diseaseSemantic proximity Read ↗

Gain-of-function ADAMTS13 variants that are resistant to autoantibodies against ADAMTS13 in patients with acquired thrombotic thrombocytopenic purpura.Semantic proximity Read ↗

Expression and functional characterization of two natural heparin-binding site variants of antithrombin.Semantic proximity Read ↗

Use of a mouse model to elucidate the phenotypic effects of the von Willebrand factor cleavage mutants, Y1605A/M1606A and R1597W.Semantic proximity Read ↗

Complete deficiency in ADAMTS13 is prothrombotic, but it alone is not sufficient to cause thrombotic thrombocytopenic purpura.Semantic proximity Read ↗

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