Evidence map›Paper›PMID 24043618›Full record

ArticleThe Journal of biological chemistry2013

Analysis of the activities of RAD54, a SWI2/SNF2 protein, using a specific small-molecule inhibitor.

Julianna S Deakyne, Fei Huang, Joseph Negri, Nicola Tolliday, Simon Cocklin, Alexander V Mazin

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

11 citing papers in PubMed, 18 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Julianna S DeakyneFrom the Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, Pennsylvania 19102 and.
Fei Huang
Joseph Negri
Nicola Tolliday
Simon Cocklin
Alexander V Mazin
Drexel University · USBroad Institute · USMassachusetts Institute of Technology · US

Funding

Repair of DNA breaks in human: the role of Rad54 proteinR01CA100839 · NCI · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2003 to 2013
$2.6M
High-throughput Computational Docking Screen for Small-molecule Inhibitors of HIVR21AI087388 · NIAID · DREXEL UNIVERSITY · PI COCKLIN, SIMON · 2010 to 2011
$422k
Repair of DNA breaks in humans: the role of Rad54 proteinR56CA100839 · NCI · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2008 to 2008
$260k
Identification of inhibitors of RAD54, an important DNA repair proteinR03DA033981 · NIDA · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2012 to 2013
$76k
Development of RAD52 inhibitors to induce synthetic lethality of BRCA2-deficientR03MH097512 · NIMH · DREXEL UNIVERSITY · PI MAZIN, ALEXANDER V · 2012 to 2013
$76k
NCI NIH HHS CA100839NCI NIH HHS R01 CA100839NCI NIH HHS R56 CA100839NIAID NIH HHS 1R21AI087388NIAID NIH HHS R21 AI087388NIDA NIH HHS DA033981NIDA NIH HHS R03 DA033981NIMH NIH HHS MH097512NIMH NIH HHS R03 MH097512
6 · The paper itself

Abstract

RAD54, an important homologous recombination protein, is a member of the SWI2/SNF2 family of ATPase-dependent DNA translocases. In vitro, RAD54 stimulates RAD51-mediated DNA strand exchange and promotes branch migration of Holliday junctions. It is thought that an ATPase-dependent DNA translocation is required for both of these RAD54 activities. Here we identified, by high-throughput screening, a specific RAD54 inhibitor, streptonigrin (SN), and used it to investigate the mechanisms of RAD54 activities. We found that SN specifically targets the RAD54 ATPase, but not DNA binding, through direct interaction with RAD54 and generation of reactive oxygen species. Consistent with the dependence of branch migration (BM) on the ATPase-dependent DNA translocation of RAD54, SN inhibited RAD54 BM. Surprisingly, the ability of RAD54 to stimulate RAD51 DNA strand exchange was not significantly affected by SN, indicating a relatively smaller role of RAD54 DNA translocation in this process. Thus, the use of SN enabled us to identify important differences in the effect of the RAD54 ATPase and DNA translocation on two major activities of RAD54, BM of Holliday junctions and stimulation of DNA pairing.

Indexed as

Adenosine TriphosphatasesAntibiotics, AntineoplasticDNA, CruciformDNA, FungalDNA HelicasesDNA Repair EnzymesHomologous RecombinationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStreptonigrinTranscription FactorsAdenosine TriphosphatasesAntibiotics, AntineoplasticDNA, CruciformDNA, FungalDNA HelicasesDNA Repair EnzymesRAD54 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeStreptonigrinTranscription FactorsATPasesDNA Binding ProteinDNA RepairHomologous RecombinationSmall Molecules

Identifiers

PMID24043618
PMCPMC3814753
OpenAlexW2031484121

What OpenQuestion holds

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Read underepoch 390

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.