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Article

Tumor-associated mutations in a conserved structural motif alter physical and biochemical properties of human RAD51 recombinase.

Nucleic acids research - 1 Jan 2015

Chen Jianhong, Morrical Milagros D, Donigan Katherine A, Weidhaas Joanne B, Sweasy Joann B, Averill April M, Tomczak Jennifer A, Morrical Scott W

Abstract excerpt

Human RAD51 protein catalyzes DNA pairing and strand exchange reactions that are central to homologous recombination and homology-directed DNA repair. Successful recombination/repair requires the formation of a presynaptic filament of RAD51 on ssDNA. Mutations in BRCA2 and other proteins that control RAD51 activity are associated with human cancer. Here we describe a set of mutations associated with human breast...

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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: 25539919
DOI: 10.1093/nar/gku1337
PMCID: PMC4333388

Genes

RAD51
BRCA2

Variants

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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Tumor-associated mutations in a conserved structural motif alter physical and biochemical properties of human RAD51 recombinase.PMID 25539919Read ↗

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The translocation activity of Rad54 reduces crossover outcomes during homologous recombination.Semantic proximity Read ↗

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