Evidence map›Paper›PMID 21704205›Full record

ReviewBiochimica et biophysica acta2011

Functions of the Snf2/Swi2 family Rad54 motor protein in homologous recombination.

Shannon J Ceballos, Wolf-Dietrich Heyer

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
5.3field-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

91 citing papers in PubMed, 144 citations in OpenAlex.

  1. Article
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  8. Structural basis for Rad54- and Hed1-mediated regulation of Rad51 during the transition from mitotic to meiotic recombination.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  11. Exploring the Roles of theInternational journal of molecular sciences · 2024
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31 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.

Shannon J CeballosDepartment of Microbiology, University of California, Davis, Davis, CA 95616-8665, USA.
Wolf-Dietrich Heyer
University of California, Davis · US

Funding

UC Davis MCB T32 Administrative Supplement to Recognize Excellence in Diversity, Equity, Inclusion, and Accessibility (DEIA) MentorshipT32GM007377 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEDIN, FREDERIC LOUIS · 1985 to 2023
$9.9M
RECOMBINATIONAL MECHANISMS OF DNA REPAIR IN EUKARYOTESR01GM058015 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI HEYER, WOLF-DIETRICH · 2000 to 2025
$8.8M
Regulation of Recombinational DNA RepairR01CA092276 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI HEYER, WOLF-DIETRICH · 2001 to 2020
$5.2M
NCI NIH HHS CA92276NCI NIH HHS R01 CA092276NIGMS NIH HHS GM58015NIGMS NIH HHS R01 GM058015NIGMS NIH HHS T32 GM007377NIGMS NIH HHS T32GM007377
6 · The paper itself

Abstract

Homologous recombination is a central pathway to maintain genomic stability and is involved in the repair of DNA damage and replication fork support, as well as accurate chromosome segregation during meiosis. Rad54 is a dsDNA-dependent ATPase of the Snf2/Swi2 family of SF2 helicases, although Rad54 lacks classical helicase activity and cannot carry out the strand displacement reactions typical for DNA helicases. Rad54 is a potent and processive motor protein that translocates on dsDNA, potentially executing several functions in recombinational DNA repair. Rad54 acts in concert with Rad51, the central protein of recombination that performs the key reactions of homology search and DNA strand invasion. Here, we will review the role of the Rad54 protein in homologous recombination with an emphasis on mechanistic studies with the yeast and human enzymes. We will discuss how these results relate to in vivo functions of Rad54 during homologous recombination in somatic cells and during meiosis. This article is part of a Special Issue entitled: Snf2/Swi2 ATPase structure and function.

Indexed as

Recombination, GeneticAdenosine TriphosphatasesAnimalsChromatin Assembly and DisassemblyDNA-Binding ProteinsDNA DamageDNA HelicasesDNA RepairDNA Repair EnzymesEndonucleasesHumansNuclear ProteinsRad51 RecombinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranslocation, GeneticAdenosine TriphosphatasesDNA-Binding ProteinsDNA HelicasesDNA Repair EnzymesEndonucleasesMUS81 protein, humanNuclear ProteinsRad51 RecombinaseRAD54L protein, humanRAD54 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID21704205
PMCPMC3171615
OpenAlexW2066883074

What OpenQuestion holds

Textmetadata
LicenceTDM
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.