Evidence map›Paper›PMID 10698955›Full record

ArticleThe EMBO journal2000

Tailed duplex DNA is the preferred substrate for Rad51 protein-mediated homologous pairing.

A V Mazin, E Zaitseva, P Sung, S C Kowalczykowski

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

64 citing papers in PubMed, 150 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Rad54 and Rdh54 prevent Srs2-mediated disruption of Rad51 presynaptic filaments.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. The Post-Synaptic Function of Brca2.Scientific reports · 2019
    Article
  13. Frontiers in microbiology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

4 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

4 authors at 2 institutions in 1 country.

A V MazinDivision of Biological Sciences, Sections of Microbiology, University of California, Davis, CA 95616-8665, USA.
E Zaitseva
P Sung
S C Kowalczykowski
University of California, Davis · USThe University of Texas Health Science Center at San Antonio · US

Funding

Mechanistic Studies of Genetic RecombinationR01GM062653 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 2010 to 2018
$4.4M
MECHANISTIC STUDIES OF GENETIC RECOMBINATIONR01AI018987 · NIAID · UNIVERSITY OF CALIFORNIA DAVIS · PI KOWALCZYKOWSKI, STEPHEN CHARLES · 1985 to 1999
–
NIAID NIH HHS AI-18987NIGMS NIH HHS R01 GM062653
6 · The paper itself

Abstract

The repair of potentially lethal DNA double-stranded breaks (DSBs) by homologous recombination requires processing of the broken DNA into a resected DNA duplex with a protruding 3'-single-stranded DNA (ssDNA) tail. Accordingly, the canonical models for DSB repair require invasion of an intact homologous DNA template by the 3'-end of the ssDNA, a characteristic that the bacterial pairing protein RecA possesses. Unexpectedly, we find that for the eukaryotic homolog, Rad51 protein, the 5'-end of ssDNA is more invasive than the 3'-end. This pairing bias is unaffected by Rad52, Rad54 or Rad55-57 proteins. However, further investigation reveals that, in contrast to RecA protein, the preferred DNA substrate for Rad51 protein is not ssDNA but rather dsDNA with ssDNA tails. This important distinction permits the Rad51 proteins to promote DNA strand invasion using either 3'- or 5'-ends with similar efficiency.

Indexed as

Base PairingRecombination, GeneticDNADNA-Binding ProteinsDNA RepairEscherichia coliHumansRad51 RecombinaseSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNADNA-Binding ProteinsRAD51 protein, humanRAD51 protein, S cerevisiaeRad51 RecombinaseSaccharomyces cerevisiae Proteins

Identifiers

PMID10698955
PMCPMC305653
OpenAlexW2130586544

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.