Evidence map›Paper›PMID 20385586›Full record

ArticleNucleic acids research2010

Functional capacity of XRCC1 protein variants identified in DNA repair-deficient Chinese hamster ovary cell lines and the human population.

Brian R Berquist, Dharmendra Kumar Singh, Jinshui Fan, Daemyung Kim, Elizabeth Gillenwater, Avanti Kulkarni, Vilhelm A Bohr, Eric J Ackerman, Alan E Tomkinson, David M Wilson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.

  1. X-ray repair cross-complementing group 1 Arg194Trp polymorphism is associated with increased risk of lung cancer in Chinese Han population.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013
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  18. Enhancement of silencing DNA polymerase β on the radiotherapeutic sensitivity of human esophageal carcinoma cell lines.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
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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

10 authors at 4 institutions in 2 countries.

Brian R BerquistLaboratory of Molecular Gerontology, National Institute on Aging, NIH, Baltimore, MD 21224, USA.
Dharmendra Kumar Singh
Jinshui Fan
Daemyung Kim
Elizabeth Gillenwater
Avanti Kulkarni
Vilhelm A Bohr
Eric J Ackerman
Alan E Tomkinson
David M Wilson
University of Maryland, Baltimore · USUniversity of Baltimore · USNational Institute on Aging · USSandia National Laboratories California · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Oxidative DNA Damage And Its ProcessingZIAAG000727 · NIA · NATIONAL INSTITUTE ON AGING · PI FERRUCCI, LUIGI · 2009 to 2022
$8.4M
Roles of LIG3 and XRCC1 genes in genome stability.R01ES012512 · NIEHS · UNIVERSITY OF NEW MEXICO HEALTH SCIS CTR · PI Alan E Tomkinson · 2004 to 2026
$6.3M
Base Excision DNA Repair in Disease Susceptibility and TreatmentZIAAG000750 · NIA · NATIONAL INSTITUTE ON AGING · PI BOHR, VILHELM A · 2009 to 2019
$5.4M
Intramural NIH HHSNCI NIH HHS CA92584NCI NIH HHS P01 CA092584NIEHS NIH HHS ES12512NIEHS NIH HHS R01 ES012512
6 · The paper itself

Abstract

XRCC1 operates as a scaffold protein in base excision repair, a pathway that copes with base and sugar damage in DNA. Studies using recombinant XRCC1 proteins revealed that: a C389Y substitution, responsible for the repair defects of the EM-C11 CHO cell line, caused protein instability; a V86R mutation abolished the interaction with POLbeta, but did not disrupt the interactions with PARP-1, LIG3alpha and PCNA; and an E98K substitution, identified in EM-C12, reduced protein integrity, marginally destabilized the POLbeta interaction, and slightly enhanced DNA binding. Two rare (P161L and Y576S) and two frequent (R194W and R399Q) amino acid population variants had little or no effect on XRCC1 protein stability or the interactions with POLbeta, PARP-1, LIG3alpha, PCNA or DNA. One common population variant (R280H) had no pronounced effect on the interactions with POLbeta, PARP-1, LIG3alpha and PCNA, but did reduce DNA-binding ability. When expressed in HeLa cells, the XRCC1 variants-excluding E98K, which was largely nucleolar, and C389Y, which exhibited reduced expression-exhibited normal nuclear distribution. Most of the protein variants, including the V86R POLbeta-interaction mutant, displayed normal relocalization kinetics to/from sites of laser-induced DNA damage: except for E98K and C389Y, and the polymorphic variant R280H, which exhibited a slightly shorter retention time at DNA breaks.

Indexed as

Amino Acid SubstitutionAnimalsCHO CellsCricetinaeCricetulusDNADNA-Binding ProteinsDNA RepairHumansX-ray Repair Cross Complementing Protein 1DNADNA-Binding ProteinsX-ray Repair Cross Complementing Protein 1XRCC1 protein, human

Identifiers

PMID20385586
PMCPMC2926592
OpenAlexW2089694648

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.