Evidence map›Paper›PMID 14704354›Full record

ArticleNucleic acids research2004

Domain mapping of the Rad51 paralog protein complexes.

Kristi A Miller, Dorota Sawicka, Daniel Barsky, Joanna S Albala

Open access · bronzeAbstract readComparative Study
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 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

47 citing papers in PubMed, 85 citations in OpenAlex.

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  9. Epithelial Ovarian Cancer: Providing Evidence of Predisposition Genes.International journal of environmental research and public health · 2022
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  18. XRCC2 (X-ray repair cross complementing 2).Atlas of genetics and cytogenetics in oncology and haematology · 2019
    Article
  19. 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

4 authors at 1 institution in 1 country.

Kristi A MillerBiology and Biotechnology Research Program, Lawrence Livermore National Laboratory, 7000 East Avenue, L-448, Livermore, CA 94550, USA.
Dorota Sawicka
Daniel Barsky
Joanna S Albala
Lawrence Livermore 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
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 CA-81019-02NCI NIH HHS R01 CA081019NCI NIH HHS R55 CA081019
6 · The paper itself

Abstract

The five human Rad51 paralogs are suggested to play an important role in the maintenance of genome stability through their function in DNA double-strand break repair. These proteins have been found to form two distinct complexes in vivo, Rad51B-Rad51C-Rad51D-Xrcc2 (BCDX2) and Rad51C-Xrcc3 (CX3). Based on the recent Pyrococcus furiosus Rad51 structure, we have used homology modeling to design deletion mutants of the Rad51 paralogs. The models of the human Rad51B, Rad51C, Xrcc3 and murine Rad51D (mRad51D) proteins reveal distinct N-terminal and C-terminal domains connected by a linker region. Using yeast two-hybrid and co-immunoprecipitation techniques, we have demonstrated that a fragment of Rad51B containing amino acid residues 1-75 interacts with the C-terminus and linker of Rad51C, residues 79-376, and this region of Rad51C also interacts with mRad51D and Xrcc3. We have also determined that the N-terminal domain of mRad51D, residues 4-77, binds to Xrcc2 while the C-terminal domain of mRad51D, residues 77-328, binds Rad51C. By this, we have identified the binding domains of the BCDX2 and CX3 complexes to further characterize the interaction of these proteins and propose a scheme for the three-dimensional architecture of the BCDX2 and CX3 paralog complexes.

Indexed as

Amino Acid SequenceAnimalsBinding SitesComputational BiologyDNA-Binding ProteinsHumansMacromolecular SubstancesMiceModels, MolecularMolecular Sequence DataPrecipitin TestsProtein BindingProtein Structure, TertiaryPyrococcus furiosusRad51 RecombinaseSequence AlignmentDNA-Binding ProteinsMacromolecular SubstancesRAD51B protein, humanRAD51C protein, humanRAD51D protein, humanRad51d protein, mouseRAD51 protein, humanRad51 protein, mouseRad51 RecombinaseXRCC2 protein, humanXrcc2 protein, mouse

Identifiers

PMID14704354
PMCPMC373258
OpenAlexW2017282110

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.