Evidence map›Paper›PMID 26384422›Full record

ArticleNucleic acids research2015

Integrating multi-scale data on homologous recombination into a new recognition mechanism based on simulations of the RecA-ssDNA/dsDNA structure.

Darren Yang, Benjamin Boyer, Chantal Prévost, Claudia Danilowicz, Mara Prentiss

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.4field-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

32 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
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  7. Review
  8. Article
  9. CRISPR-Cas9 bends and twists DNA to read its sequence.Nature structural & molecular biology · 2022
    Article
  10. Article
  11. Article
  12. How strand exchange protein function benefits from ATP hydrolysis.Current opinion in genetics & development · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Mismatch sensing by nucleofilament deciphers mechanism of RecA-mediated homologous recombination.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

5 authors at 3 institutions in 2 countries.

Darren YangSchool of Engineering and Applied Sciences, Harvard University, Cambridge, MA 02138, USA.
Benjamin BoyerLaboratoire de Biochimie Théorique, CNRS UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, IBPC, Paris, France.
Chantal PrévostLaboratoire de Biochimie Théorique, CNRS UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, IBPC, Paris, France.
Claudia DanilowiczDepartment of Physics, Harvard University, Cambridge, MA 02138, USA.
Mara PrentissDepartment of Physics, Harvard University, Cambridge, MA 02138, USA prentiss@fas.harvard.edu.
Harvard University · USSorbonne Paris Cité · FRUniversité Paris Cité · FR

Funding

ILLEGITIMATE RECOMBINATION BY DRUG RESISTANCE ELEMENTSR01GM025326 · NIGMS · HARVARD UNIVERSITY · PI KLECKNER, NANCY E · 1985 to 2019
$12.5M
NIGMS NIH HHS R01 GM025326NIGMS NIH HHS R01-GM025326
6 · The paper itself

Abstract

RecA protein is the prototypical recombinase. Members of the recombinase family can accurately repair double strand breaks in DNA. They also provide crucial links between pairs of sister chromatids in eukaryotic meiosis. A very broad outline of how these proteins align homologous sequences and promote DNA strand exchange has long been known, as are the crystal structures of the RecA-DNA pre- and postsynaptic complexes; however, little is known about the homology searching conformations and the details of how DNA in bacterial genomes is rapidly searched until homologous alignment is achieved. By integrating a physical model of recognition to new modeling work based on docking exploration and molecular dynamics simulation, we present a detailed structure/function model of homology recognition that reconciles extremely quick searching with the efficient and stringent formation of stable strand exchange products and which is consistent with a vast body of previously unexplained experimental results.

Indexed as

Homologous RecombinationBase PairingDNA, B-FormDNA, Single-StrandedMolecular Dynamics SimulationProtein BindingRec A RecombinasesDNA, B-FormDNA, Single-StrandedRec A Recombinases

Identifiers

PMID26384422
PMCPMC4666392
OpenAlexW1443844529

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.