Evidence map›Paper›PMID 28867292›Full record

ArticleMolecular cell2017

Single-Molecule Imaging Reveals How Mre11-Rad50-Nbs1 Initiates DNA Break Repair.

Logan R Myler, Ignacio F Gallardo, Michael M Soniat, Rajashree A Deshpande, Xenia B Gonzalez, Yoori Kim, Tanya T Paull, Ilya J Finkelstein

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
10.2field-weighted citation impact, top 1% 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

121 citing papers in PubMed, 195 citations in OpenAlex.

  1. DNA Repair Mechanisms.Methods in molecular biology (Clifton, N.J.) · 2027
    Review
  2. Article
  3. Mechanisms and disease relevance of DNA break repair pathway choice.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. DNA Damage and Replication Stress Checkpoints.Annual review of biochemistry · 2025
    Review
  11. Review
  12. Article
  13. Review
  14. ATM priming and end resection-coupled phosphorylation of MRE11 is important for fork protection and replication restart.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

61 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

8 authors at 2 institutions in 1 country.

Logan R MylerDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Howard Hughes Medical Institute, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Ignacio F GallardoDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Michael M SoniatDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Rajashree A DeshpandeDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Howard Hughes Medical Institute, The University of Texas at Austin, Austin, TX 78712, USA.
Xenia B GonzalezDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Yoori KimDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA.
Tanya T PaullDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Howard Hughes Medical Institute, The University of Texas at Austin, Austin, TX 78712, USA.
Ilya J FinkelsteinDepartment of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712, USA; Center for Systems and Synthetic Biology, The University of Texas at Austin, Austin, TX 78712, USA. Electronic address: ifinkelstein@cm.utexas.edu.
The University of Texas at Austin · USHoward Hughes Medical Institute · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Mechanistic Characterization of the First Steps of Human DNA Break RepairR01GM120554 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI FINKELSTEIN, ILYA J · 2016 to 2020
$1.5M
Mechanisms of chromatin remodeling and roadblock clearance by DNA motor proteinsR00GM097177 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI FINKELSTEIN, ILYA J · 2013 to 2015
$747k
Single-Molecule Studies of Human DNA Double Strand Break RepairK00CA212452 · NCI · ROCKEFELLER UNIVERSITY · PI MYLER, LOGAN ROSS · 2018 to 2021
$376k
Single-Molecule Studies of Human DNA Double Strand Break RepairF99CA212452 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MYLER, LOGAN ROSS · 2016 to 2017
$69k
NCI NIH HHS F99 CA212452NCI NIH HHS K00 CA212452NCI NIH HHS P01 CA092584NIGMS NIH HHS R00 GM097177NIGMS NIH HHS R01 GM120554
6 · The paper itself

Abstract

DNA double-strand break (DSB) repair is essential for maintaining our genomes. Mre11-Rad50-Nbs1 (MRN) and Ku70-Ku80 (Ku) direct distinct DSB repair pathways, but the interplay between these complexes at a DSB remains unclear. Here, we use high-throughput single-molecule microscopy to show that MRN searches for free DNA ends by one-dimensional facilitated diffusion, even on nucleosome-coated DNA. Rad50 binds homoduplex DNA and promotes facilitated diffusion, whereas Mre11 is required for DNA end recognition and nuclease activities. MRN gains access to occluded DNA ends by removing Ku or other DNA adducts via an Mre11-dependent nucleolytic reaction. Next, MRN loads exonuclease 1 (Exo1) onto the free DNA ends to initiate DNA resection. In the presence of replication protein A (RPA), MRN acts as a processivity factor for Exo1, retaining the exonuclease on DNA for long-range resection. Our results provide a mechanism for how MRN promotes homologous recombination on nucleosome-coated DNA.

Indexed as

DNA Breaks, Double-StrandedRecombinational DNA RepairSingle Molecule ImagingAcid Anhydride HydrolasesCell Cycle ProteinsDiffusionDNA AdductsDNA-Binding ProteinsDNA Repair EnzymesExodeoxyribonucleasesHumansKu AutoantigenMicroscopy, FluorescenceMRE11 Homologue ProteinNuclear ProteinsNucleosomesAcid Anhydride HydrolasesCell Cycle ProteinsDNA AdductsDNA-Binding ProteinsDNA Repair EnzymesEXO1 protein, humanExodeoxyribonucleasesKu AutoantigenMRE11 Homologue ProteinMRE11 protein, humanNBN protein, humanNuclear ProteinsNucleosomesRAD50 protein, humanXRCC5 protein, humanXrcc6 protein, humanDNA repairdouble-strand breakKuMRNresectionresectosomesingle-molecule

Identifiers

PMID28867292
PMCPMC5609712
OpenAlexW2753229012

What OpenQuestion holds

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Registered trials

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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.