Evidence map›Paper›PMID 32938550›Full record

ReviewSeminars in cell & developmental biology2021

RAD51: Beyond the break.

Isabel E Wassing, Fumiko Esashi

Open access · hybridAbstract readReview
In one paragraph

Review in Seminars in cell & developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

49 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
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  11. UHRF1 Controls the Timing of RAD51 Removal During DNA Damage Repair Through Suppressing RFWD3.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
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  13. Review
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  17. Review
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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.

Isabel E WassingSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Fumiko EsashiSir William Dunn School of Pathology, University of Oxford, Oxford, UK. Electronic address: fumiko.esashi@path.ox.ac.uk.
University of Oxford · GB

Funding

Medical Research Council 14/15_MSD_439771Wellcome TrustWellcome Trust 101009/Z/13/Z
6 · The paper itself

Abstract

As the primary catalyst of homologous recombination (HR) in vertebrates, RAD51 has been extensively studied in the context of repair of double-stranded DNA breaks (DSBs). With recent advances in the understanding of RAD51 function extending beyond DSBs, the importance of RAD51 throughout DNA metabolism has become increasingly clear. Here we review the suggested roles of RAD51 beyond HR, specifically focusing on their interplay with DNA replication and the maintenance of genomic stability, in which RAD51 function emerges as a double-edged sword.

Indexed as

DNA Breaks, Double-StrandedGenomic InstabilityHumansRad51 RecombinaseRAD51 protein, humanRad51 RecombinaseDouble-stranded DNA breaksFork protectionHomologous recombinationRAD51Replicative stress

Identifiers

PMID32938550
PMCPMC8082279
OpenAlexW3084505752

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.