Evidence map›Paper›PMID 22705791›Full record

ArticleNature structural & molecular biology2012

Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling.

Christian B Schiller, Katja Lammens, Ilaria Guerini, Britta Coordes, Heidi Feldmann, Florian Schlauderer, Carolin Möckel, Alexandra Schele, Katja Strässer, Stephen P Jackson and 1 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
6.0field-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

81 citing papers in PubMed, 119 citations in OpenAlex.

  1. Article
  2. Review
  3. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  4. Article
  5. NBS1 facilitates preribosomal RNA biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Importance of Germline and Somatic Alterations in HumanInternational journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. A conserved Ctp1/CtIP C-terminal peptide stimulates Mre11 endonuclease activity.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Mechanism and Control of Meiotic DNA Double-Strand Break Formation inFrontiers in cell and developmental biology · 2021
    Review

21 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

11 authors at 4 institutions in 2 countries.

Christian B SchillerGene Center, Ludwig Maximilians University Munich, Munich, Germany.
Katja Lammens
Ilaria Guerini
Britta Coordes
Heidi Feldmann
Florian Schlauderer
Carolin Möckel
Alexandra Schele
Katja Strässer
Stephen P Jackson
Karl-Peter Hopfner
Ludwig-Maximilians-Universität München · DECenter for Integrated Protein Science Munich · DEUniversity of Cambridge · GBWellcome/Cancer Research UK Gurdon Institute · GB

Funding

TRIM mediated host antiviral responses during influenza virus infectionsU19AI083025 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JUNG, JAE U · 2009 to 2013
$10.0M
Cancer Research UK 11224Cancer Research UK A11224Cancer Research UK C6/A11226European Research Council 268536NIAID NIH HHS U19 AI083025NIAID NIH HHS U19AI83025Wellcome Trust 092096
6 · The paper itself

Abstract

The Mre11-Rad50-Nbs1 (MRN) complex tethers, processes and signals DNA double-strand breaks, promoting genomic stability. To understand the functional architecture of MRN, we determined the crystal structures of the Schizosaccharomyces pombe Mre11 dimeric catalytic domain alone and in complex with a fragment of Nbs1. Two Nbs1 subunits stretch around the outside of the nuclease domains of Mre11, with one subunit additionally bridging and locking the Mre11 dimer via a highly conserved asymmetrical binding motif. Our results show that Mre11 forms a flexible dimer and suggest that Nbs1 not only is a checkpoint adaptor but also functionally influences Mre11-Rad50. Clinical mutations in Mre11 are located along the Nbs1-interaction sites and weaken the Mre11-Nbs1 interaction. However, they differentially affect DNA repair and telomere maintenance in Saccharomyces cerevisiae, potentially providing insight into their different human disease pathologies.

Indexed as

DNA DamageMutationSignal TransductionBinding SitesChromosomal Proteins, Non-HistoneDimerizationHumansModels, MolecularProtein ConformationSchizosaccharomyces pombe ProteinsChromosomal Proteins, Non-HistoneNbs1 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID22705791
PMCPMC3392456
OpenAlexW2062136827

What OpenQuestion holds

Textmetadata
LicenceTDM
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.