Evidence map›Paper›PMID 12149653›Full record

ArticleOncogene2002

p53 activation results in rapid dephosphorylation of the eIF4E-binding protein 4E-BP1, inhibition of ribosomal protein S6 kinase and inhibition of translation initiation.

Lynn E Horton, Martin Bushell, Diane Barth-Baus, Vivienne J Tilleray, Michael J Clemens, Jack O Hensold

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed, 1 pooled it
2.1field-weighted citation impact, top 14% 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

46 citing papers in PubMed, 1 synthesis or guideline pooled it, 93 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Regulation of ribosomal protein genes: An ordered anarchy.Wiley interdisciplinary reviews. RNA · 2021
    Review
  9. Article
  10. Oxidative stress-mediated TXNIP loss causes RPE dysfunction.Experimental & molecular medicine · 2019
    Article
  11. Article
  12. Biological Aspects of mTOR in Leukemia.International journal of molecular sciences · 2018
    Review
  13. Review
  14. Translation Control byCancers · 2018
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review
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

6 authors at 4 institutions in 2 countries.

Lynn E HortonThe Department of Medicine, University/Ireland Cancer Center, Case Western Reserve University School of Medicine, 10900 Euclid Ave.-BRB 333, Cleveland, Ohio, OH 44106-4937, USA.
Martin Bushell
Diane Barth-Baus
Vivienne J Tilleray
Michael J Clemens
Jack O Hensold
St George's, University of London · GBCase Western Reserve University · USSt George's Hospital · GBUniversity School · US

Funding

NIDDK NIH HHS DK43414PHITPO CDC HHS HK07147-21A1
6 · The paper itself

Abstract

p53 is an important regulator of cell cycle progression and apoptosis, and inactivation of p53 is associated with tumorigenesis. Although p53 exerts many of its effects through regulation of transcription, this protein is also found in association with ribosomes and several mRNAs have been identified that are translationally controlled in a p53-dependent manner. We have utilized murine erythroleukemic cells that express a temperature-sensitive p53 protein to determine whether p53 also functions at the level of translation. The data presented here demonstrate that p53 causes a rapid decrease in translation initiation. Analysis of several potential mechanisms for regulating protein synthesis shows that p53 has selective effects on the phosphorylation of the eIF4E-binding protein, 4E-BP1, and the activity of the p70 ribosomal protein S6 kinase. These data provide evidence that modulation of translational activity constitutes a further mechanism by which the growth inhibitory effects of p53 may be mediated.

Indexed as

Protein Serine-Threonine KinasesAdaptor Proteins, Signal TransducingAmino AcidsCarrier ProteinsCell Cycle ProteinsCell LineCyclin-Dependent Kinase Inhibitor p21CyclinsDNA-Binding ProteinsErythrocytesEukaryotic Initiation Factor-4EGene Expression RegulationHumansLeukemia, Erythroblastic, AcutePeptide Initiation FactorsPhosphoproteinsAdaptor Proteins, Signal TransducingAmino AcidsCarrier ProteinsCDKN1A protein, humanCell Cycle ProteinsCyclin-Dependent Kinase Inhibitor p21CyclinsDNA-Binding ProteinsEIF4EBP1 protein, humanEukaryotic Initiation Factor-4EMTOR protein, humanPeptide Initiation FactorsPhosphoproteinsProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRepressor ProteinsRibosomal Protein S6 KinasesTOR Serine-Threonine KinasesTranscription FactorsTumor Suppressor Protein p53

Identifiers

PMID12149653
OpenAlexW1997092292

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.