Evidence map›Paper›PMID 19804756›Full record

ArticleCell2009

A supramodular FHA/BRCT-repeat architecture mediates Nbs1 adaptor function in response to DNA damage.

Janette Lloyd, J Ross Chapman, Julie A Clapperton, Lesley F Haire, Edgar Hartsuiker, Jiejin Li, Antony M Carr, Stephen P Jackson, Stephen J Smerdon

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

117 citing papers in PubMed, 174 citations in OpenAlex.

  1. Article
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  5. Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae.Acta crystallographica. Section F, Structural biology communications · 2025
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  17. The dynamic nature of the Mre11-Rad50 DNA break repair complex.Progress in biophysics and molecular biology · 2021
    Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 3 institutions in 1 country.

Janette LloydDivision of Molecular Structure, Medical Research Council National Institute for Medical Research, The Ridgeway, Mill Hill, London, UK.
J Ross Chapman
Julie A Clapperton
Lesley F Haire
Edgar Hartsuiker
Jiejin Li
Antony M Carr
Stephen P Jackson
Stephen J Smerdon
Medical Research Council · GBUniversity of Cambridge · GBUniversity of Sussex · GB

Funding

Cancer Research UK 11224Cancer Research UK A5290Cancer Research UK C20600/A6620Medical Research Council G0001129Medical Research Council G0600233Medical Research Council MC_U117584228Wellcome Trust
6 · The paper itself

Abstract

The Mre11/Rad50/Nbs1 protein complex plays central enzymatic and signaling roles in the DNA-damage response. Nuclease (Mre11) and scaffolding (Rad50) components of MRN have been extensively characterized, but the molecular basis of Nbs1 function has remained elusive. Here, we present a 2.3A crystal structure of the N-terminal region of fission yeast Nbs1, revealing an unusual but conserved architecture in which the FHA- and BRCT-repeat domains structurally coalesce. We demonstrate that diphosphorylated pSer-Asp-pThr-Asp motifs, recently identified as multicopy docking sites within Mdc1, are evolutionarily conserved Nbs1 binding targets. Furthermore, we show that similar phosphomotifs within Ctp1, the fission yeast ortholog of human CtIP, promote interactions with the Nbs1 FHA domain that are necessary for Ctp1-dependent resistance to DNA damage. Finally, we establish that human Nbs1 interactions with Mdc1 occur through both its FHA- and BRCT-repeat domains, suggesting how their structural and functional interdependence underpins Nbs1 adaptor functions in the DNA-damage response.

Indexed as

DNA RepairAmino Acid SequenceCell Cycle ProteinsChromosomal Proteins, Non-HistoneCrystallography, X-RayDNA-Binding ProteinsDNA DamageHumansModels, MolecularMolecular Sequence DataMutationNuclear ProteinsPhosphorylationProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsCell Cycle ProteinsChromosomal Proteins, Non-HistoneCtp1 protein, S pombeDNA-Binding ProteinsNBN protein, humanNbs1 protein, S pombeNuclear ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID19804756
PMCPMC2900601
OpenAlexW2110297856

What OpenQuestion holds

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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.