Evidence map›Paper›PMID 30551670›Full record

ReviewGenes2018

RAD-ical New Insights into RAD51 Regulation.

Meghan R Sullivan, Kara A Bernstein

Open access · goldAbstract readReview
In one paragraph

Review in Genes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
5.7field-weighted citation impact, top 3% 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

86 citing papers in PubMed, 1 synthesis or guideline pooled it, 130 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Impact of germlineMolecular therapy. Oncology · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. High-throughput mapping of 6,888bioRxiv : the preprint server for biology · 2026
    Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Review
  19. Review
  20. 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

26 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

2 authors at 1 institution in 1 country.

Meghan R SullivanDepartment of Microbiology and Molecular Genetics, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, 5117 Centre Avenue, Pittsburgh, PA 15213, USA. mrs149@pitt.edu.
Kara A BernsteinDepartment of Microbiology and Molecular Genetics, UPMC Hillman Cancer Center, University of Pittsburgh School of Medicine, 5117 Centre Avenue, Pittsburgh, PA 15213, USA. karab@pitt.edu.ORCID 0000-0003-2247-6459
UPMC Hillman Cancer Center · US

Funding

Replication fork dynamics and repair by Rad51 paralogues after DNA alkylationR01ES024872 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BERNSTEIN, KARA A · 2015 to 2019
$2.4M
The interplay between RAD51C sub-complexes during replication fork repairF31ES027321 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SULLIVAN, MEGHAN · 2017 to 2018
$71k
American Cancer Society 129182-RSG-16-043-01-DMCNIEHS NIH HHS R01 ES024872NIH HHS ES024872NIH HHS F31ES027321Stand Up To Cancer SU2C-AACR-IRG-02-16
6 · The paper itself

Abstract

The accurate repair of DNA is critical for genome stability and cancer prevention. DNA double-strand breaks are one of the most toxic lesions; however, they can be repaired using homologous recombination. Homologous recombination is a high-fidelity DNA repair pathway that uses a homologous template for repair. One central HR step is RAD51 nucleoprotein filament formation on the single-stranded DNA ends, which is a step required for the homology search and strand invasion steps of HR. RAD51 filament formation is tightly controlled by many positive and negative regulators, which are collectively termed the RAD51 mediators. The RAD51 mediators function to nucleate, elongate, stabilize, and disassemble RAD51 during repair. In model organisms, RAD51 paralogs are RAD51 mediator proteins that structurally resemble RAD51 and promote its HR activity. New functions for the RAD51 paralogs during replication and in RAD51 filament flexibility have recently been uncovered. Mutations in the human RAD51 paralogs (RAD51B, RAD51C, RAD51D, XRCC2, XRCC3, and SWSAP1) are found in a subset of breast and ovarian cancers. Despite their discovery three decades ago, few advances have been made in understanding the function of the human RAD51 paralogs. Here, we discuss the current perspective on the in vivo and in vitro function of the RAD51 paralogs, and their relationship with cancer in vertebrate models.

Indexed as

BRCA1BRCA2cancerhomologous recombinationRAD51BRAD51CRAD51DRAD51 paralogsShu complexXRCC2XRCC3

Identifiers

PMID30551670
PMCPMC6316741
OpenAlexW2900810167

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.