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Article

Massively parallel enzyme kinetics reveals the substrate recognition landscape of the metalloprotease ADAMTS13.

Proceedings of the National Academy of Sciences of the United States of America - 28 Jul 2015

Kretz Colin A, Dai Manhong, Soylemez Onuralp, Yee Andrew, Desch Karl C, Siemieniak David, Tomberg Kärt, Kondrashov Fyodor A, Meng Fan, Ginsburg David

Abstract excerpt

Proteases play important roles in many biologic processes and are key mediators of cancer, inflammation, and thrombosis. However, comprehensive and quantitative techniques to define the substrate specificity profile of proteases are lacking. The metalloprotease ADAMTS13 regulates blood coagulation by cleaving von Willebrand factor (VWF), reducing its procoagulant activity. A mutagenized substrate phage display...

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Topics

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Share to ADAM Proteins
Share to ADAMTS13 Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Epistasis, Genetic

Share to Peptide Library

Share to Proteolysis

Share to Substrate Specificity

Share to von Willebrand Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 26170332
DOI: 10.1073/pnas.1511328112
PMCID: PMC4522773

Genes

ADAMTS13
VWF

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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