Evidence map›Paper›PMID 19151086›Full record

ArticleNucleic acids research2009

RAD50 and NBS1 form a stable complex functional in DNA binding and tethering.

Eddy van der Linden, Humberto Sanchez, Eri Kinoshita, Roland Kanaar, Claire Wyman

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

33 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
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  5. Review
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  7. Activation of Tel1The Journal of biological chemistry · 2019
    Article
  8. Review
  9. Interdependent and separable functions ofProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. Eukaryotic resectosomes: A single-molecule perspective.Progress in biophysics and molecular biology · 2017
    Review
  12. Article
  13. Article
  14. Eukaryotic Rad50 functions as a rod-shaped dimer.Nature structural & molecular biology · 2017
    Article
  15. Article
  16. Article
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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

5 authors at 2 institutions in 1 country.

Eddy van der LindenDepartment of Cell Biology and Genetics, Cancer Genomics Center, Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands.
Humberto Sanchez
Eri Kinoshita
Roland Kanaar
Claire Wyman
Cancer Genomics Centre · NLErasmus MC · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RAD50/MRE11/NBS1 protein complex (RMN) plays an essential role during the early steps of DNA double-strand break (DSB) repair by homologous recombination. Previous data suggest that one important role for RMN in DSB repair is to provide a link between DNA ends. The striking architecture of the complex, a globular domain from which two extended coiled coils protrude, is essential for this function. Due to its DNA-binding activity, ability to form dimers and interact with both RAD50 and NBS1, MRE11 is considered to be crucial for formation and function of RMN. Here, we show the successful expression and purification of a stable complex containing only RAD50 and NBS1 (RN). The characteristic architecture of the complex was not affected by absence of MRE11. Although MRE11 is a DNA-binding protein it was not required for DNA binding per se or DNA-tethering activity of the complex. The stoichiometry of NBS1 in RMN and RN complexes was estimated by SFM-based volume analysis. These data show that in vitro, R, M and N form a variety of stable complexes with variable subunit composition and stoichiometry, which may be physiologically relevant in different aspects of RMN function.

Indexed as

Acid Anhydride HydrolasesCell Cycle ProteinsDNADNA-Binding ProteinsDNA Repair EnzymesHumansMicroscopy, Atomic ForceMRE11 Homologue ProteinNuclear ProteinsProtein BindingAcid Anhydride HydrolasesCell Cycle ProteinsDNADNA-Binding ProteinsDNA Repair EnzymesMRE11 Homologue ProteinMRE11 protein, humanNBN protein, humanNuclear ProteinsRAD50 protein, human

Identifiers

PMID19151086
PMCPMC2655673
OpenAlexW1995431542

What OpenQuestion holds

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LicenceCC BY-NC
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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.