Evidence map›Paper›PMID 11842112›Full record

ArticleNucleic acids research2002

Interactions involving the Rad51 paralogs Rad51C and XRCC3 in human cells.

Claudia Wiese, David W Collins, Joanna S Albala, Larry H Thompson, Amy Kronenberg, David Schild

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 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

49 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. GermlineJournal of personalized medicine · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. RAD51 paralog function in replicative DNA damage and tolerance.Current opinion in genetics & development · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Novel insights into RAD51 activity and regulation during homologous recombination and DNA replication.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Mediators of homologous DNA pairing.Cold Spring Harbor perspectives in biology · 2014
    Review
  18. Review
  19. Article
  20. Article
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 1 institution in 1 country.

Claudia WieseLife Sciences Division, 1 Cyclotron Road, Mailstop 70A-1118, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
David W Collins
Joanna S Albala
Larry H Thompson
Amy Kronenberg
David Schild
Lawrence Berkeley National Laboratory · US

Funding

A ROLE OF RAD51B IN DNA REPAIR AND BREAST CARCINOGENESISR01CA081019 · NCI · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI ALBALA, JOANNA S · 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
HIGH LET RADIATION &GENOMIC INSTABILITY IN HUMAN CELLSR01CA073966 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KRONENBERG, AMY · 1997 to 2001
$426k
ROLE FOR RAD51B IN DNA REPAIR AND BREAST CARCINOGENESISR55CA081019 · NCI · UNIVERSITY OF CALIF-LAWRNC LVRMR NAT LAB · PI ALBALA, JOANNA S · 1999 to 1999
–
NCI NIH HHS CA73966NCI NIH HHS CA81019NCI NIH HHS R01 CA081019NCI NIH HHS R55 CA081019NIGMS NIH HHS GM30990
6 · The paper itself

Abstract

Homologous recombinational repair of DNA double-strand breaks and crosslinks in human cells is likely to require Rad51 and the five Rad51 paralogs (XRCC2, XRCC3, Rad51B/Rad51L1, Rad51C/Rad51L2 and Rad51D/Rad51L3), as has been shown in chicken and rodent cells. Previously, we reported on the interactions among these proteins using baculovirus and two- and three-hybrid yeast systems. To test for interactions involving XRCC3 and Rad51C, stable human cell lines have been isolated that express (His)6-tagged versions of XRCC3 or Rad51C. Ni2+-binding experiments demonstrate that XRCC3 and Rad51C interact in human cells. In addition, we find that Rad51C, but not XRCC3, interacts directly or indirectly with Rad51B, Rad51D and XRCC2. These results argue that there are at least two complexes of Rad51 paralogs in human cells (Rad51C-XRCC3 and Rad51B-Rad51C-Rad51D-XRCC2), both containing Rad51C. Moreover, Rad51 is not found in these complexes. X-ray treatment did not alter either the level of any Rad51 paralog or the observed interactions between paralogs. However, the endogenous level of Rad51C is moderately elevated in the XRCC3-overexpressing cell line, suggesting that dimerization between these proteins might help stabilize Rad51C.

Indexed as

Avian ProteinsCell DeathCell LineDNA-Binding ProteinsDNA DamageHumansKineticsLymphocytesMacromolecular SubstancesModels, BiologicalPrecipitin TestsRad51 RecombinaseRecombinant Fusion ProteinsTransfectionX-RaysAvian 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, humanNASA Discipline Radiation HealthNon-NASA Center

Identifiers

PMID11842112
PMCPMC100332
OpenAlexW2046032690

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.