Evidence map›Paper›PMID 29321177›Full record

ArticleGenes & development2017

Plasticity of the Mre11-Rad50-Xrs2-Sae2 nuclease ensemble in the processing of DNA-bound obstacles.

Weibin Wang, James M Daley, Youngho Kwon, Danielle S Krasner, Patrick Sung

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
–field-weighted citation impact
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

84 citing papers in PubMed, 121 citations in OpenAlex.

  1. Taming Mre11-Rad50 at Telomeres: Convergent Strategies for Chromosome-End Protection Across Evolution.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Rap1-mediated steric hindrance protects telomeres from MRX sensing.Nature structural & molecular biology · 2026
    Article
  3. Article
  4. Article
  5. Asymmetrical recognition and processing of double-strand breaks formed during DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  12. Article
  13. Article
  14. A comparative evaluation of CRISPR-Cas9 allele editing systems inbioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

24 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Weibin WangDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
James M DaleyDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Youngho KwonDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Danielle S KrasnerDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Patrick SungDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
Yale University · US

Funding

YEAST DNA REPAIR GENES AND PROTEINS OF THE RAD52 GROUPR01ES007061 · NIEHS · YALE UNIVERSITY · PI Patrick Sung · 1995 to 2026
$9.4M
Roles of the RecQ Helicases BLM and RECQ5 in Genome MaintenanceR01ES015632 · NIEHS · YALE UNIVERSITY · PI SUNG, PATRICK · 2007 to 2017
$3.9M
NIEHS NIH HHS R01 ES007061NIEHS NIH HHS R01 ES015632
6 · The paper itself

Abstract

The budding yeast Mre11-Rad50-Xrs2 (MRX) complex and Sae2 function together in DNA end resection during homologous recombination. Here we show that the Ku complex shields DNA ends from exonucleolytic digestion but facilitates endonucleolytic scission by MRX with a dependence on ATP and Sae2. The incision site is enlarged into a DNA gap via the exonuclease activity of MRX, which is stimulated by Sae2 without ATP being present. RPA renders a partially resected or palindromic DNA structure susceptible to MRX-Sae2, and internal protein blocks also trigger DNA cleavage. We present models for how MRX-Sae2 creates entry sites for the long-range resection machinery.

Indexed as

DNA End-Joining RepairDNA-Binding ProteinsDNA CleavageDNA RepairEndodeoxyribonucleasesEndonucleasesEnzyme ActivationExodeoxyribonucleasesExonucleasesMultienzyme ComplexesMultiprotein ComplexesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsEndodeoxyribonucleasesEndonucleasesexodeoxyribonuclease IExodeoxyribonucleasesExonucleaseshigh affinity DNA-binding factor, S cerevisiaeMRE11 protein, S cerevisiaeMultienzyme ComplexesMultiprotein ComplexesRAD50 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSAE2 protein, S cerevisiaeXRS2 protein, S cerevisiaeDNA end resectionKu70–Ku80MRX–Sae2nucleasenucleosomeRPA

Identifiers

PMID29321177
PMCPMC5795780
OpenAlexW2783514031

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.