Evidence map›Paper›PMID 11842113›Full record

ArticleNucleic acids research2002

Involvement of Rad51C in two distinct protein complexes of Rad51 paralogs in human cells.

Nan Liu, David Schild, Michael P Thelen, Larry H Thompson

Open access · greenAbstract read
In one paragraph

Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
6.2field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 127 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. GermlineJournal of personalized medicine · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. XRCC2 (X-ray repair cross complementing 2).Atlas of genetics and cytogenetics in oncology and haematology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Mediators of homologous DNA pairing.Cold Spring Harbor perspectives in biology · 2014
    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

4 authors at 1 institution in 1 country.

Nan LiuBiology and Biotechnology Research Program, L441, Lawrence Livermore National Laboratory, PO Box 808, Livermore, CA 94551-0808, USA. liu3@llnl.gov
David Schild
Michael P Thelen
Larry H Thompson
Lawrence Livermore National Laboratory · US

Funding

BIOLOGICAL FUNCTION OF XRCC2 IN RECOMBINATIONAL REPAIRR01CA084407 · NCI · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI LIU, NAN · 2000 to 2003
$1.2M
YEAST RAD GENES IN REPAIR, RECOMBINATION, AND MEIOSISR01GM030990 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SCHILD, DAVID · 1985 to 2001
$718k
NCI NIH HHS CA84407-01NCI NIH HHS R01 CA084407NIGMS NIH HHS GM30990
6 · The paper itself

Abstract

Genetic studies in rodent and chicken mutant cell lines have suggested that Rad51 paralogs (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2 and Rad51D/Rad51L3) play important roles in homologous recombinational repair of DNA double-strand breaks and in maintaining chromosome stability. Previous studies using yeast two- and three-hybrid systems have shown interactions among these proteins, but it is not clear whether these interactions occur simultaneously or sequentially in vivo. By utilizing immunoprecipitation with extracts of human cells expressing epitope-tagged Rad51 paralogs, we demonstrate that XRCC2 and Rad51D, while stably interacting with each other, co-precipitate with Rad51C but not with XRCC3. In contrast, Rad51C is pulled down with XRCC3, whereas XRCC2 and Rad51D are not. In addition, Rad51B could be pulled down with Rad51C and Rad51D, but not with XRCC3. These results suggest that Rad51C is involved in two distinct in vivo complexes: Rad51B-Rad51C-Rad51D-XRCC2 and Rad51C-XRCC3. In addition, we demonstrate that Rad51 co-precipitates with XRCC3 but not with XRCC2 or Rad51D, suggesting that Rad51 can be present in an XRCC3-Rad51C-Rad51 complex. These complexes may act as functional units and serve accessory roles for Rad51 in the presynapsis stage of homologous recombinational repair.

Indexed as

AnimalsAvian ProteinsCell LineCricetinaeDNA-Binding ProteinsGamma RaysHeLa CellsHumansMacromolecular SubstancesMicroscopy, FluorescenceModels, BiologicalPrecipitin TestsRad51 RecombinaseRecombinant Fusion ProteinsTransfectionAvian ProteinsDNA-Binding ProteinsMacromolecular SubstancesRAD51B protein, humanRAD51C protein, humanRAD51D protein, humanRAD51 protein, Gallus gallusRAD51 protein, humanRad51 RecombinaseRecombinant Fusion ProteinsX-ray repair cross complementing protein 3XRCC2 protein, human

Identifiers

PMID11842113
PMCPMC100342
OpenAlexW1989613054

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.