Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Proceedings of the National Academy of Sciences of the United States of America - 12 Dec 2006

Gao Weiqiang, Anderson Patricia J, Majerus Elaine M, Tuley Elodee A, Sadler J Evan

Abstract excerpt

Von Willebrand factor (VWF) is a multimeric protein that mediates platelet adhesion at sites of vascular injury, and ADAMTS13 (a disintegrin and metalloprotease with thrombospondin)is a multidomain metalloprotease that limits platelet adhesion by a feedback mechanism in which fluid shear stress induces proteolysis of VWF and prevents disseminated microvascular thrombosis. Cleavage of the Tyr(1605)-Met(1606)...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Line
Share to Kinetics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Metalloendopeptidases

Share to Protein Binding

Share to Recombinant Proteins

Share to Substrate Specificity

Share to Thrombosis

Share to von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 17146059
DOI: 10.1073/pnas.0607264104
PMCID: PMC1681350

Genes

ADAMTS13
VWF

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease.PMID 17146059Read ↗

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

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

Shear-induced unfolding activates von Willebrand factor A2 domain for proteolysis.Semantic proximity Read ↗

Mutation G1629E Increases von Willebrand Factor Cleavage via a Cooperative Destabilization Mechanism.Semantic proximity Read ↗

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

Conformational activation of antithrombin by heparin involves an altered exosite interaction with protease.Semantic proximity Read ↗

The various states of von Willebrand factor and their function in physiology and pathophysiology.Semantic proximity Read ↗

The WXXW motif in the TSR1 of ADAMTS13 is important for its secretion and proteolytic activity.Semantic proximity Read ↗

Shear-Induced Unfolding and Enzymatic Cleavage of Full-Length VWF Multimers.Semantic proximity Read ↗

The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity.Semantic proximity Read ↗

ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor.Semantic proximity Read ↗

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 ↗

⌁Select a neighboring publication to make it the new centre.