Evidence map›Paper›PMID 25282148›Full record

ArticleNature structural & molecular biology2014

Structure and mechanism of action of the BRCA2 breast cancer tumor suppressor.

Taha Shahid, Joanna Soroka, Eric Kong, Laurent Malivert, Michael J McIlwraith, Tillman Pape, Stephen C West, Xiaodong Zhang

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Complex Interplay Between Obesity and BRCA1/2-Associated Breast Cancer: An Overview.Obesity reviews : an official journal of the International Association for the Study of Obesity · 2025
    Review
  5. Identification and Computational Analysis ofMedical sciences (Basel, Switzerland) · 2025
    Article
  6. International journal of molecular sciences · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Article
  16. Structure of RADX and mechanism for regulation of RAD51 nucleofilaments.bioRxiv : the preprint server for biology · 2023
    Article
  17. Article
  18. Article
  19. BRCA2 chaperones RAD51 to single molecules of RPA-coated ssDNA.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. Article

5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Taha Shahid *Centre for Structural Biology, Imperial College, London, U.K.
Joanna Soroka *London Research Institute, Clare Hall Laboratories, South Mimms, U.K.
Eric Kong *Centre for Structural Biology, Imperial College, London, U.K.
Laurent MalivertLondon Research Institute, Clare Hall Laboratories, South Mimms, U.K.
Michael J McIlwraithLondon Research Institute, Clare Hall Laboratories, South Mimms, U.K.
Tillman PapeCentre for Structural Biology, Imperial College, London, U.K.
Stephen C WestLondon Research Institute, Clare Hall Laboratories, South Mimms, U.K.
Xiaodong ZhangCentre for Structural Biology, Imperial College, London, U.K.
Imperial College London · GBInstitute of Structural and Molecular Biology · GB

Funding

Breast Cancer Now 2009MAYPR01Cancer Research UK 11582Medical Research Council MR/J001201/1Wellcome Trust 098412
6 · The paper itself

Abstract

Mutations in BRCA2 increase susceptibility to breast, ovarian and prostate cancers. The product of human BRCA2, BRCA2 protein, has a key role in the repair of DNA double-strand breaks and interstrand cross-links by RAD51-mediated homologous recombination. Here, we present a biochemical and structural characterization of full-length (3,418 amino acid) BRCA2, alone and in complex with RAD51. We show that BRCA2 facilitates nucleation of RAD51 filaments at multiple sites on single-stranded DNA. Three-dimensional EM reconstructions revealed that BRCA2 exists as a dimer and that two oppositely oriented sets of RAD51 molecules bind the dimer. Single-stranded DNA binds along the long axis of BRCA2, such that only one set of RAD51 monomers can form a productive complex with DNA and establish filament formation. Our data define the molecular mechanism by which this tumor suppressor facilitates RAD51-mediated homologous-recombinational repair.

Indexed as

DNA RepairBRCA2 ProteinDNA Breaks, Double-StrandedDNA, Single-StrandedGene ExpressionHeLa CellsHomologous RecombinationHumansModels, MolecularProtein ConformationProtein MultimerizationRad51 RecombinaseRecombinant ProteinsBRCA2 ProteinBRCA2 protein, humanDNA, Single-StrandedRAD51 protein, humanRad51 RecombinaseRecombinant Proteins

Identifiers

PMID25282148
PMCPMC4222816
OpenAlexW2026327099

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.