Evidence map›Paper›PMID 15141025›Full record

ArticleNucleic acids research2004

Preferential binding to branched DNA strands and strand-annealing activity of the human Rad51B, Rad51C, Rad51D and Xrcc2 protein complex.

Hiroshi Yokoyama, Naoyuki Sarai, Wataru Kagawa, Rima Enomoto, Takehiko Shibata, Hitoshi Kurumizaka, Shigeyuki Yokoyama

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

46 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Structural basis of homologous recombination.Cellular and molecular life sciences : CMLS · 2020
    Review
  10. Article
  11. XRCC2 (X-ray repair cross complementing 2).Atlas of genetics and cytogenetics in oncology and haematology · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Novel insights into RAD51 activity and regulation during homologous recombination and DNA replication.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

7 authors at 1 institution in 1 country.

Hiroshi YokoyamaRIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan.
Naoyuki Sarai
Wataru Kagawa
Rima Enomoto
Takehiko Shibata
Hitoshi Kurumizaka
Shigeyuki Yokoyama
National Agriculture and Food Research Organization · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rad51B, Rad51C, Rad51D and Xrcc2 proteins are Rad51 paralogs, and form a complex (BCDX2 complex) in mammalian cells. Mutant cells defective in any one of the Rad51-paralog genes exhibit spontaneous genomic instability and extreme sensitivity to DNA-damaging agents, due to inefficient recombinational repair. Therefore, the Rad51 paralogs play important roles in the maintenance of genomic integrity through recombinational repair. In the present study, we examined the DNA-binding preference of the human BCDX2 complex. Competitive DNA-binding assays using seven types of DNA substrates, single-stranded DNA (ssDNA), double-stranded DNA, 5'- and 3'-tailed duplexes, nicked duplex DNA, Y-shaped DNA and a synthetic Holliday junction, revealed that the BCDX2 complex preferentially bound to the two DNA substrates with branched structures (the Y-shaped DNA and the synthetic Holliday junction). Furthermore, the BCDX2 complex catalyzed the strand-annealing reaction between a long linear ssDNA (1.2 kb in length) and its complementary circular ssDNA. These properties of the BCDX2 complex may be important for its roles in the maintenance of chromosomal integrity.

Indexed as

Adenosine TriphosphatasesBinding SitesDNADNA-Binding ProteinsDNA, CruciformDNA, Single-StrandedMacromolecular SubstancesNucleic Acid ConformationAdenosine TriphosphatasesDNADNA-Binding ProteinsDNA, CruciformDNA, Single-StrandedMacromolecular SubstancesRAD51B protein, humanRAD51C protein, humanRAD51D protein, humanXRCC2 protein, human

Identifiers

PMID15141025
PMCPMC419466
OpenAlexW2071322868

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.