Evidence map›Paper›PMID 22375013›Full record

ArticleThe Journal of biological chemistry2012

Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair.

Myun Hwa Dunlop, Eloïse Dray, Weixing Zhao, Joseph San Filippo, Miaw-Sheue Tsai, Stanley G Leung, David Schild, Claudia Wiese, Patrick Sung

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. Phosphoregulation of RAD51AP1 function in homology-directed repair.bioRxiv : the preprint server for biology · 2025
    Article
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  5. Review
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  12. Chemical Risk Factors of Primary Liver Cancer: An Update.Hepatic medicine : evidence and research · 2020
    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

9 authors at 2 institutions in 1 country.

Myun Hwa DunlopDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Eloïse Dray
Weixing Zhao
Joseph San Filippo
Miaw-Sheue Tsai
Stanley G Leung
David Schild
Claudia Wiese
Patrick Sung
Yale University · USLawrence Berkeley National Laboratory · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
YEAST DNA REPAIR GENES AND PROTEINS OF THE RAD52 GROUPR01ES007061 · NIEHS · YALE UNIVERSITY · PI Patrick Sung · 1995 to 2026
$9.4M
TUMOR SELECTIVE INACTIVATION OF THE REPAIR PROTEIN AGTP01CA129186 · NCI · YALE UNIVERSITY · PI GLAZER, PETER M · 2007 to 2012
$8.5M
Roles of the RecQ Helicases BLM and RECQ5 in Genome MaintenanceR01ES015632 · NIEHS · YALE UNIVERSITY · PI SUNG, PATRICK · 2007 to 2017
$3.9M
Molecular Basis of BRCA2-mediated DNA Repair and Cancer AvoidanceR01ES015252 · NIEHS · YALE UNIVERSITY · PI SUNG, PATRICK · 2007 to 2016
$3.8M
NUCKS, a novel double-strand break repair gene, implicated in cancer biologyR01ES021454 · NIEHS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI WIESE, CLAUDIA · 2012 to 2016
$1.9M
Determining the role of RAD51AP1: a new gene in DNA repair and genomic stabilityR01CA120315 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI SCHILD, DAVID · 2008 to 2011
$1.6M
NCI NIH HHS P01 CA092584NCI NIH HHS P01CA092584NCI NIH HHS P01 CA129186NCI NIH HHS P01CA129186NCI NIH HHS R01 CA120315NCI NIH HHS R01CA120315NIEHS NIH HHS R01 ES007061NIEHS NIH HHS R01 ES015252NIEHS NIH HHS R01ES015252NIEHS NIH HHS R01 ES015632NIEHS NIH HHS R01ES015632NIEHS NIH HHS R01 ES021454NIEHS NIH HHS R01ES07061
6 · The paper itself

Abstract

Homologous recombination catalyzed by the RAD51 recombinase is essential for maintaining genome integrity upon the induction of DNA double strand breaks and other DNA lesions. By enhancing the recombinase activity of RAD51, RAD51AP1 (RAD51-associated protein 1) serves a key role in homologous recombination-mediated chromosome damage repair. We show here that RAD51AP1 harbors two distinct DNA binding domains that are both needed for maximal protein activity under physiological conditions. We have finely mapped the two DNA binding domains in RAD51AP1 and generated mutant variants that are impaired in either or both of the DNA binding domains. Examination of these mutants reveals that both domains are indispensable for RAD51AP1 function in cells. These and other results illuminate the mechanistic basis of RAD51AP1 action in homologous DNA repair.

Indexed as

DNA RepairAmino Acid SequenceAmino Acid SubstitutionConserved SequenceDNADNA-Binding ProteinsHeLa CellsHumansMutagenesis, Site-DirectedPeptide FragmentsPeptide MappingPhenotypeProtein BindingProtein Structure, TertiaryRecombinant ProteinsRNA-Binding ProteinsDNADNA-Binding ProteinsPeptide FragmentsRAD51AP1 protein, humanRecombinant ProteinsRNA-Binding Proteins

Identifiers

PMID22375013
PMCPMC3320983
OpenAlexW1995437551

What OpenQuestion holds

Textmetadata
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.