Evidence map›Paper›PMID 40820711›Full record

ArticleeLife2025

Structural mechanism of strand exchange by the RAD51 filament.

Luay Joudeh, Robert E Appleby, Joseph D Maman, Luca Pellegrini

Abstract read
In one paragraph

Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
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

17 citing papers in PubMed.

  1. Mechanisms That Govern Recombinase Fidelity Control During Eukaryotic Homologous Recombination.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Review
  3. Article
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  5. Article
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  7. Article
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  11. Article
  12. Review
  13. RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Research Progress of RAD51AP1 in Malignant Tumors of the Female Reproductive System.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  16. Article
  17. Article
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

4 authors.

Luay Joudeh *Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.ORCID https://orcid.org/0000-0001-9338-205X
Robert E Appleby *Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
Joseph D MamanDepartment of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
Luca PellegriniDepartment of Biochemistry, University of Cambridge, Cambridge, United Kingdom.ORCID https://orcid.org/0000-0002-9300-497X

Funding

Biotechnology and Biological Sciences Research Council 2271086Wellcome TrustWellcome Trust 10.35802/221892
6 · The paper itself

Abstract

Homologous recombination (HR) preserves genomic stability by repairing double-strand DNA breaks and ensuring efficient DNA replication. Central to HR is the strand-exchange reaction taking place within the three-stranded synapsis wherein a RAD51 nucleoprotein filament binds to a donor DNA. Here, we present the cryoEM structure of a displacement loop of human RAD51 that captures the synaptic state when the filament has become tightly bound to the donor DNA. The structure elucidates the mechanism of strand exchange by RAD51, including the filament engagement with the donor DNA, the strand invasion and pairing with the complementary sequence of the donor DNA, the capture of the non-complementary strand and the polarity of the strand-exchange reaction. Our findings provide fundamental mechanistic insights into the biochemical reaction of eukaryotic HR.

Indexed as

DNAHomologous RecombinationRad51 RecombinaseCryoelectron MicroscopyHumansModels, MolecularProtein BindingProtein ConformationDNARAD51 protein, humanRad51 RecombinasechromosomescryoEMD-loopDNA repairgene expressionhomologous recombinationhumanmolecular biophysicsRAD51structural biology

Identifiers

PMID40820711
PMCPMC12360782

What OpenQuestion holds

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Registered trials

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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.