Evidence map›Paper›PMID 22362889›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

The p53 cofactor Strap exhibits an unexpected TPR motif and oligonucleotide-binding (OB)-fold structure.

Cassandra J Adams, Ashley C W Pike, Sandra Maniam, Timothy D Sharpe, Amanda S Coutts, Stefan Knapp, Nicholas B La Thangue, Alex N Bullock

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Bi-allelicJournal of medical genetics · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Obesity and p16Molecular and cellular biology · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
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.

Cassandra J AdamsLaboratory of Cancer Biology, Department of Oncology, Medical Sciences Division, University of Oxford, Old Road Campus Research Building, Roosevelt Drive, Oxford, OX3 7DQ, United Kingdom.
Ashley C W Pike
Sandra Maniam
Timothy D Sharpe
Amanda S Coutts
Stefan Knapp
Nicholas B La Thangue
Alex N Bullock
University of Oxford · GBGenomics (United Kingdom) · GB

Funding

Cancer Research UK 13058CIHRMedical Research Council G0500905Medical Research Council G1000807Medical Research Council G9400953Wellcome Trust
6 · The paper itself

Abstract

Activation of p53 target genes for tumor suppression depends on the stress-specific regulation of transcriptional coactivator complexes. Strap (stress-responsive activator of p300) is activated upon DNA damage by ataxia telangiectasia mutated (ATM) and Chk2 kinases and is a key regulator of the p53 response. In addition to antagonizing Mdm2, Strap facilitates the recruitment of p53 coactivators, including JMY and p300. Strap is a predicted TPR-repeat protein, but shows only limited sequence identity with any protein of known structure. To address this and to elucidate the molecular mechanism of Strap activity we determined the crystal structure of the full-length protein at 2.05 Å resolution. The structure of Strap reveals an atypical six tetratricopeptide repeat (TPR) protein that also contains an unexpected oligonucleotide/oligosaccharide-binding (OB)-fold domain. This previously unseen domain organization provides an extended superhelical scaffold allowing for protein-protein as well as protein-DNA interaction. We show that both of the TPR and OB-fold domains localize to the chromatin of p53 target genes and exhibit intrinsic regulatory activity necessary for the Strap-dependent p53 response.

Indexed as

Genes, p53Amino Acid MotifsAnimalsCarrier ProteinsChromatinCrystallography, X-RayDNA DamageE1A-Associated p300 ProteinHumansMiceModels, MolecularNeoplasm ProteinsOligonucleotidesProtein BindingProtein ConformationProtein FoldingCarrier ProteinsChromatinE1A-Associated p300 ProteinEP300 protein, humanNeoplasm ProteinsOligonucleotidesRNA-Binding ProteinsStrap proteinSTRAP protein, humanTumor Suppressor Protein p53

Identifiers

PMID22362889
PMCPMC3309724
OpenAlexW2100816175

What OpenQuestion holds

Textmetadata
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.