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Article

Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays.

The Biochemical journal - 28 Apr 2009

Maretzky Thorsten, Yang Guangli, Ouerfelli Ouathek, Overall Christopher M, Worpenberg Susanne, Hassiepen Ulrich, Eder Joerg, Blobel Carl P

Abstract excerpt

ADAM15 (a disintegrin and metalloproteinase 15) is a membrane-anchored metalloproteinase, which is overexpressed in several human cancers and has been implicated in pathological neovascularization and prostate cancer metastasis. Yet, little is known about the catalytic properties of ADAM15. Here, we purified soluble recombinant ADAM15 to test for its ability to cleave a library of peptide substrates. However, we...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 19207106
DOI: 10.1042/BJ20082127

Genes

ADAM15

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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Characterization of the catalytic activity of the membrane-anchored metalloproteinase ADAM15 in cell-based assays.PMID 19207106Read ↗

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