Evidence map›Paper›PMID 22179609›Full record

ArticleThe Journal of biological chemistry2012

Human Ku70/80 protein blocks exonuclease 1-mediated DNA resection in the presence of human Mre11 or Mre11/Rad50 protein complex.

Jingxin Sun, Kyung-Jong Lee, Anthony J Davis, David J Chen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Mechanisms and disease relevance of DNA break repair pathway choice.Nature reviews. Molecular cell biology · 2026
    Review
  2. The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. The Multifaceted Roles of Ku70/80.International journal of molecular sciences · 2021
    Review
  9. The Role of Nitric Oxide in Cancer: Master Regulator or NOt?International journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Alterations in histone acetylation following exposure toRadiation and environmental biophysics · 2018
    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

4 authors at 2 institutions in 1 country.

Jingxin SunDivision of Molecular Radiation Biology, Department of Radiation Oncology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas 75390, USA.
Kyung-Jong Lee
Anthony J Davis
David J Chen
Radiation Oncology Associates · USThe University of Texas Southwestern Medical Center · 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 DNA PK in DNA Double Strand Break RepairR37CA050519 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI CHEN, DAVID J · 2003 to 2011
$3.5M
Pathway Choice of DNA Double-Strand Break RepairR01CA162804 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI DAVIS, ANTHONY J · 2012 to 2021
$3.4M
Functions of WRN in Response to DNA Double-Strand BreaksR01CA134991 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI CHEN, DAVID J · 2009 to 2013
$1.6M
ROLES OF DNA PK IN DNA DOUBLE STRAND BREAK REPAIRR01CA050519 · NCI · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI CHEN, DAVID J · 1989 to 2001
$946k
NCI NIH HHS CA134991NCI NIH HHS CA50519NCI NIH HHS CA92584NCI NIH HHS P01 CA092584NCI NIH HHS R01 CA050519NCI NIH HHS R01 CA134991NCI NIH HHS R01 CA162804NCI NIH HHS R37 CA050519
6 · The paper itself

Abstract

DNA double strand breaks (DSB) are repaired by nonhomologous end-joining (NHEJ) or homologous recombination (HR). Recent genetic data in yeast shows that the choice between these two pathways for the repair of DSBs is via competition between the NHEJ protein, Ku, and the HR protein, Mre11/Rad50/Xrs2 (MRX) complex. To study the interrelationship between human Ku and Mre11 or Mre11/Rad50 (MR), we established an in vitro DNA end resection system using a forked model dsDNA substrate and purified human Ku70/80, Mre11, Mre11/Rad50, and exonuclease 1 (Exo1). Our study shows that the addition of Ku70/80 blocks Exo1-mediated DNA end resection of the forked dsDNA substrate. Although human Mre11 and MR bind to the forked double strand DNA, they could not compete with Ku for DNA ends or actively mediate the displacement of Ku from the DNA end either physically or via its exonuclease or endonuclease activity. Our in vitro studies show that Ku can block DNA resection and suggest that Ku must be actively displaced for DNA end processing to occur and is more complicated than the competition model established in yeast.

Indexed as

Acid Anhydride HydrolasesAntigens, NuclearDNADNA-Binding ProteinsDNA Repair EnzymesExodeoxyribonucleasesHumansKu AutoantigenMRE11 Homologue ProteinMultiprotein ComplexesAcid Anhydride HydrolasesAntigens, NuclearDNADNA-Binding ProteinsDNA Repair EnzymesEXO1 protein, humanExodeoxyribonucleasesKu AutoantigenMRE11 Homologue ProteinMRE11 protein, humanMultiprotein ComplexesRAD50 protein, humanXrcc6 protein, human

Identifiers

PMID22179609
PMCPMC3281638
OpenAlexW2037004712

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.