Evidence map›Paper›PMID 21816818›Full record

ArticleThe Journal of biological chemistry2011

Human Mre11/human Rad50/Nbs1 and DNA ligase IIIalpha/XRCC1 protein complexes act together in an alternative nonhomologous end joining pathway.

Julie Della-Maria, Yi Zhou, Miaw-Sheue Tsai, Jeff Kuhnlein, James P Carney, Tanya T Paull, Alan E Tomkinson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
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

89 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
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  6. Disruption of Microhomology-mediated End-joining in Ewing Sarcoma.bioRxiv : the preprint server for biology · 2025
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29 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

7 authors at 4 institutions in 1 country.

Julie Della-MariaRadiation Oncology Research Laboratory, Department of Radiation Oncology and The Marlene and Stewart Greenebaum Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.
Yi Zhou
Miaw-Sheue Tsai
Jeff Kuhnlein
James P Carney
Tanya T Paull
Alan E Tomkinson
Howard Hughes Medical Institute · USUniversity of New Mexico · USLawrence Berkeley National Laboratory · USThe University of Texas at Austin · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
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
Mrell/Rad50/Nbs1 and DNA double strand break repairR01CA094008 · NCI · UNIVERSITY OF TEXAS AUSTIN · PI PAULL, TANYA T · 2002 to 2011
$2.8M
Howard Hughes Medical InstituteNCI NIH HHS CA094008NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA094008NIEHS NIH HHS ES012512NIEHS NIH HHS R01 ES012512
6 · The paper itself

Abstract

Recent studies have implicated a poorly defined alternative pathway of nonhomologous end joining (alt-NHEJ) in the generation of large deletions and chromosomal translocations that are frequently observed in cancer cells. Here, we describe an interaction between two factors, hMre11/hRad50/Nbs1 (MRN) and DNA ligase IIIα/XRCC1, that have been linked with alt-NHEJ. Expression of DNA ligase IIIα and the association between MRN and DNA ligase IIIα/XRCC1 are altered in cell lines defective in the major NHEJ pathway. Most notably, DNA damage induced the association of these factors in DNA ligase IV-deficient cells. MRN interacts with DNA ligase IIIα/XRCC1, stimulating intermolecular ligation, and together these proteins join incompatible DNA ends in a reaction that mimics alt-NHEJ. Thus, our results provide novel mechanistic insights into the alt-NHEJ pathway that not only contributes to genome instability in cancer cells but may also be a therapeutic target.

Indexed as

Acid Anhydride HydrolasesCell Cycle ProteinsCell Line, TumorDNA-Binding ProteinsDNA DamageDNA Ligase ATPDNA LigasesDNA RepairDNA Repair EnzymesGenomic InstabilityHumansMRE11 Homologue ProteinMultiprotein ComplexesNuclear ProteinsPoly-ADP-Ribose Binding ProteinsXenopus ProteinsAcid Anhydride HydrolasesCell Cycle ProteinsDNA-Binding ProteinsDNA Ligase ATPDNA ligase III alpha protein, XenopusDNA LigasesDNA Repair EnzymesMRE11 Homologue ProteinMRE11 protein, humanMultiprotein ComplexesNBN protein, humanNuclear ProteinsPoly-ADP-Ribose Binding ProteinsRAD50 protein, humanXenopus ProteinsX-ray Repair Cross Complementing Protein 1XRCC1 protein, human

Identifiers

PMID21816818
PMCPMC3190819
OpenAlexW2016999017

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.