Evidence map›Paper›PMID 25795425›Full record

ReviewDNA repair2015

The structural basis of XRCC1-mediated DNA repair.

Robert E London

Open access · greenAbstract readReview
In one paragraph

Review in DNA repair, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed, 1 pooled it
5.9field-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

73 citing papers in PubMed, 1 synthesis or guideline pooled it, 138 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. DNA damage and repair in cardiomyopathy: mechanisms and therapeutic opportunities.American journal of physiology. Heart and circulatory physiology · 2026
    Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Genotype and Association of XRCC1 Gene With Liver Disease in Chronic Hcv Patients.Asian Pacific journal of cancer prevention : APJCP · 2025
    Article
  13. Article
  14. Review
  15. Long non-coding RNANon-coding RNA research · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

13 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

1 author at 1 institution in 1 country.

Robert E LondonGenome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, NIH, Research Triangle Park, NC 27709, United States. Electronic address: london@niehs.nih.gov.
National Institute of Environmental Health Sciences · US

Funding

Nmr Studies Of Biomolecular Structure, Function, And DynamicsZIAES050111 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI LONDON, ROBERT E · 2009 to 2020
$11.7M
NMR STUDIES OF BIOMOLECULAR STRUCTURE, FUNCTION, AND DYNAMICSZ01ES050111 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI LONDON, ROBERT E · 1990 to 2008
$1.2M
Intramural NIH HHS Z01 ES050111Intramural NIH HHS ZIA ES050111NIEHS NIH HHS 1ZIA ES050111-26
6 · The paper itself

Abstract

Scaffold proteins play a central role in DNA repair by recruiting and organizing sets of enzymes required to perform multi-step repair processes. X-ray cross complementing group 1 protein (XRCC1) forms enzyme complexes optimized for single-strand break repair, but participates in other repair pathways as well. Available structural data for XRCC1 interactions is summarized and evaluated in terms of its proposed roles in DNA repair. Mutational approaches related to the abrogation of specific XRCC1 interactions are also discussed. Although substantial progress has been made in elucidating the structural basis for XRCC1 function, the molecular mechanisms of XRCC1 recruitment related to several proposed roles of the XRCC1 DNA repair complex remain undetermined.

Indexed as

DNA RepairDNA-Binding ProteinsDNA Polymerase betaDNA Repair EnzymesPhosphotransferases (Alcohol Group Acceptor)Protein BindingProtein Structure, TertiaryX-ray Repair Cross Complementing Protein 1DNA-Binding ProteinsDNA Polymerase betaDNA Repair EnzymesPhosphotransferases (Alcohol Group Acceptor)PNKP protein, humanX-ray Repair Cross Complementing Protein 1XRCC1 protein, humanDNA ligase 3αDNA polymerase betaDNA repairSingle-strand break repairXRCC1

Identifiers

PMID25795425
PMCPMC5580684
OpenAlexW2085585779

What OpenQuestion holds

Textmetadata
LicenceTDM
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.