ArticleProceedings of the National Academy of Sciences of the United States of America2005
BRCA2 BRC motifs bind RAD51-DNA filaments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
71 citing papers in PubMed, 132 citations in OpenAlex.
- Article
- A guide to heat shock factors as multifunctional transcriptional regulators.The FEBS journal · 2025Review
- In silico structural analysis of Oryza sativa RAD51 reveals key interactions for nucleoprotein filament assembly and regulation.PloS one · 2025Article
- NAE1-mediated neddylation coordinates ubiquitination regulation of meiotic recombination during spermatogenesis.Theranostics · 2025Article
- The human Shu complex promotes RAD51 activity by modulating RPA dynamics on ssDNA.Nature communications · 2024Article
- Natural variation of codon repeats inScience advances · 2023Article
- Dipeptidyl peptidase 9 triggers BRCA2 degradation and promotes DNA damage repair.EMBO reports · 2022Article
- Mechanisms governing the accessibility of DNA damage proteins to constitutive heterochromatin.Frontiers in genetics · 2022Article
- Role of BRCA2 DNA-binding and C-terminal domain in its mobility and conformation in DNA repair.eLife · 2021Article
- Making Choices: DNA Replication Fork Recovery Mechanisms.Seminars in cell & developmental biology · 2021Review
- Clinical use and mechanisms of resistance for PARP inhibitors in homologous recombination-deficient cancers.Translational oncology · 2021Review
- Article
- Single-molecule localization microscopy reveals molecular transactions during RAD51 filament assembly at cellular DNA damage sites.Nucleic acids research · 2018Article
- Observation and Analysis of RAD51 Nucleation Dynamics at Single-Monomer Resolution.Methods in enzymology · 2018Article
- Homologous recombination defects and how they affect replication fork maintenance.AIMS genetics · 2018Review
- Variation in RAD51 details a hub of functions: opportunities to advance cancer diagnosis and therapy.F1000Research · 2018Review
- Defects in recombination activity caused by somatic and germline mutations in the multimerization/BRCA2 binding region of human RAD51 protein.DNA repair · 2017Article
- Mutations in BRCA1, BRCA2 and other breast and ovarian cancer susceptibility genes in Central and South American populations.Biological research · 2017Review
- A phosphorylation-deubiquitination cascade regulates the BRCA2-RAD51 axis in homologous recombination.Genes & development · 2016Article
- High-resolution structure of the presynaptic RAD51 filament on single-stranded DNA by electron cryo-microscopy.Nucleic acids research · 2016Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Germ-line mutations in BRCA2 account for approximately half the cases of autosomal dominant familial breast cancers. BRCA2 has been shown to interact directly with RAD51, an essential component of the cellular machinery for homologous recombination and the maintenance of genome stability. Interactions between BRCA2 and RAD51 take place by means of the conserved BRC repeat regions of BRCA2. Previously, it was shown that peptides corresponding to BRC3 or BRC4 bind RAD51 monomers and block RAD51-DNA filament formation. In this work, we further analyze these interactions and find that at lower molar ratios BRC3 or BRC4 actually bind and form stable complexes with RAD51-DNA nucleoprotein filaments. Only at high concentrations of the BRC repeats are filaments disrupted. The specific protein-protein contacts occur in the RAD51 filament by means of the N-terminal domain of RAD51 for BRC3 and the nucleotide-binding core of RAD51 for BRC4. These observations show that the BRC repeats bind distinct regions of RAD51 and are nonequivalent in their mode of interaction. The results provide insight into why mutation in just one of the eight BRC repeats would affect the way that BRCA2 protein interacts with the RAD51 filament. Disruption of a single RAD51 interaction site, one of several simultaneous interactions occurring throughout the BRC repeat-containing exon 11 of BRCA2, might modulate the ability of RAD51 to promote recombinational repair and lead to an increased risk of breast cancer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.