Evidence map›Paper›PMID 29507080›Full record

ArticleThe EMBO journal2018

Two distinct conformational states define the interaction of human RAD51-ATP with single-stranded DNA.

Ineke Brouwer, Tommaso Moschetti, Andrea Candelli, Edwige B Garcin, Mauro Modesti, Luca Pellegrini, Gijs Jl Wuite, Erwin Jg Peterman

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

53 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Subcellular Stress Markers in Epithelial Ovarian Cancer.International journal of molecular sciences · 2025
    Review
  5. RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. ATP hydrolysis-driven structural transitions within thebioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. Article
  15. Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.bioRxiv : the preprint server for biology · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 3 institutions in 3 countries.

Ineke BrouwerDepartment of Physics and Astronomy and LaserLaB, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands.
Tommaso MoschettiDepartment of Biochemistry, University of Cambridge, Cambridge, UK.
Andrea CandelliDepartment of Physics and Astronomy and LaserLaB, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands.
Edwige B GarcinCancer Research Center of Marseille, CNRS UMR7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université, Marseille, France.
Mauro ModestiCancer Research Center of Marseille, CNRS UMR7258, Inserm U1068, Institut Paoli-Calmettes, Aix-Marseille Université, Marseille, France.
Luca PellegriniDepartment of Biochemistry, University of Cambridge, Cambridge, UK lp212@cam.ac.uk g.j.l.wuite@vu.nl e.j.g.peterman@vu.nl.ORCID 0000-0002-9300-497X
Gijs Jl WuiteDepartment of Physics and Astronomy and LaserLaB, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands lp212@cam.ac.uk g.j.l.wuite@vu.nl e.j.g.peterman@vu.nl.ORCID 0000-0002-5706-043X
Erwin Jg PetermanDepartment of Physics and Astronomy and LaserLaB, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands lp212@cam.ac.uk g.j.l.wuite@vu.nl e.j.g.peterman@vu.nl.ORCID 0000-0003-1058-249X
Vrije Universiteit Amsterdam · NLCentre National de la Recherche Scientifique · FRUniversity of Cambridge · GB

Funding

Wellcome TrustWellcome Trust 104641/Z/14/Z
6 · The paper itself

Abstract

An essential mechanism for repairing DNA double-strand breaks is homologous recombination (HR). One of its core catalysts is human RAD51 (hRAD51), which assembles as a helical nucleoprotein filament on single-stranded DNA, promoting DNA-strand exchange. Here, we study the interaction of hRAD51 with single-stranded DNA using a single-molecule approach. We show that ATP-bound hRAD51 filaments can exist in two different states with different contour lengths and with a free-energy difference of ~4 k

Indexed as

Adenosine TriphosphateCrystallography, X-RayDNADNA-Binding ProteinsDNA Breaks, Double-StrandedDNA RepairDNA ReplicationDNA, Single-StrandedHomologous RecombinationModels, MolecularMolecular ConformationNucleoproteinsRad51 RecombinaseAdenosine TriphosphateDNADNA-Binding ProteinsDNA, Single-StrandedNucleoproteinsRAD51 protein, humanRad51 RecombinaseDNA repairhomologous recombinationRAD51single‐stranded DNA

Identifiers

PMID29507080
PMCPMC5881629
OpenAlexW2793913949

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.