Evidence map›Paper›PMID 22492707›Full record

ArticleNucleic acids research2012

Rad51 presynaptic filament stabilization function of the mouse Swi5-Sfr1 heterodimeric complex.

Shang-Pu Tsai, Guan-Chin Su, Sheng-Wei Lin, Chan-I Chung, Xiaoyu Xue, Myun Hwa Dunlop, Yufuko Akamatsu, Maria Jasin, Patrick Sung, Peter Chi

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

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  12. Rad51 facilitates filament assembly of meiosis-specific Dmc1 recombinase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  13. Article
  14. Article
  15. Swi5-Sfr1 stimulates Rad51 recombinase filament assembly by modulating Rad51 dissociation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Review
  17. 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

10 authors at 3 institutions in 2 countries.

Shang-Pu TsaiInstitute of Biochemical Sciences, National Taiwan University, No. 1, Section 4, Roosevelt Road, Taipei, 10617, Taiwan.
Guan-Chin Su
Sheng-Wei Lin
Chan-I Chung
Xiaoyu Xue
Myun Hwa Dunlop
Yufuko Akamatsu
Maria Jasin
Patrick Sung
Peter Chi
Institute of Biological Chemistry, Academia Sinica · TWMemorial Sloan Kettering Cancer Center · USNational Taiwan University · TW

Funding

RADIATION RESISTANT AND SENSITIVE CELLS DNA BREAK REPAIRR01GM054668 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI JASIN, MARIA · 1998 to 2015
$5.3M
Molecular Basis of BRCA2-mediated DNA Repair and Cancer AvoidanceR01ES015252 · NIEHS · YALE UNIVERSITY · PI SUNG, PATRICK · 2007 to 2016
$3.8M
NIEHS NIH HHS R01 ES015252NIGMS NIH HHS R01 GM54668
6 · The paper itself

Abstract

Homologous recombination (HR) represents a major error-free pathway to eliminate pre-carcinogenic chromosomal lesions. The DNA strand invasion reaction in HR is mediated by a helical filament of the Rad51 recombinase assembled on single-stranded DNA that is derived from the nucleolytic processing of the primary lesion. Recent studies have found that the human and mouse Swi5 and Sfr1 proteins form a complex that influences Rad51-mediated HR in cells. Here, we provide biophysical evidence that the mouse Swi5-Sfr1 complex has a 1:1 stoichiometry. Importantly, the Swi5-Sfr1 complex, but neither Swi5 nor Sfr1 alone, physically interacts with Rad51 and stimulates Rad51-mediated homologous DNA pairing. This stimulatory effect stems from the stabilization of the Rad51-ssDNA presynaptic filament. Moreover, we provide evidence that the RSfp (rodent Sfr1 proline rich) motif in Sfr1 serves as a negative regulatory element. These results thus reveal an evolutionarily conserved function in the Swi5-Sfr1 complex and furnish valuable information as to the regulatory role of the RSfp motif that is specific to the mammalian Sfr1 orthologs.

Indexed as

Amino Acid MotifsAnimalsDimerizationMiceNuclear ProteinsProtein MultimerizationRad51 RecombinaseNuclear ProteinsRad51 RecombinaseSfr1 protein, mouseSwi5 protein, mouse

Identifiers

PMID22492707
PMCPMC3413116
OpenAlexW2000373893

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.