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Article

Functional analysis of a breast cancer-associated mutation in the intracellular domain of the metalloprotease ADAM12.

PloS one - 1 Jan 2012

Stautz Dorte, Wewer Ulla M, Kveiborg Marie

Abstract excerpt

A recently identified breast cancer-associated mutation in the metalloprotease ADAM12 alters a potential dileucine trafficking signal, which could affect protein processing and cellular localization. ADAM12 belongs to the group of A Disintegrin And Metalloproteases (ADAMs), which are typically membrane-associated proteins involved in ectodomain shedding, cell-adhesion, and signaling. ADAM12 as well as several...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 22662180
DOI: 10.1371/journal.pone.0037628
PMCID: PMC3360752

Genes

ADAM12
EGF

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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Functional analysis of a breast cancer-associated mutation in the intracellular domain of the metalloprotease ADAM12.PMID 22662180Read ↗

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