Evidence map›Paper›PMID 19218448›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation.

Sarah Burge, Daniel P Teufel, Fiona M Townsley, Stefan M V Freund, Mark Bycroft, Alan R Fersht

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Dichotomous transactivation domains contribute to growth inhibitory and promotion functions of TAp73.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Structural diversity of p63 and p73 isoforms.Cell death and differentiation · 2022
    Review
  4. Review
  5. Review
  6. Review
  7. DNA Damaged Induced Cell Death in Oocytes.Molecules (Basel, Switzerland) · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Alterations of p63 and p73 in human cancers.Sub-cellular biochemistry · 2014
    Review
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Sarah BurgeMedical Research Council Centre for Protein Engineering, Hills Road, Cambridge CB2 0QH, United Kingdom.
Daniel P Teufel
Fiona M Townsley
Stefan M V Freund
Mark Bycroft
Alan R Fersht
Medical Research Council · GB

Funding

Medical Research Council MC_U105474168
6 · The paper itself

Abstract

The transcription factor p73 belongs to the p53 family of proteins and can transactivate a number of target genes in common with p53. Here, we characterized the interaction of the p73 N terminus with four domains of the transcriptional coactivator p300 and with the negative regulator Mdm2 by using biophysical and cellular measurements. We found that, like p53, the N terminus of p73 contained two distinct transactivation subdomains, comprising residues 10-30 and residues 46-67. The p73 N terminus bound weakly to the Taz1, Kix, and IBiD domains of p300 but with submicromolar affinity for Taz2, in contrast to previous reports. We found weaker binding of the p73 N terminus to the p300 domains in vitro correlated with a significant decrease in transactivation activity in a cell line for the QS and T14A mutants, and tighter binding of the phosphomimetic T14D in vitro correlated with an increase in vivo. Further, we found that phosphorylation of T14 increased the affinity of the p73 N terminus for Taz2 10-fold. The phosphomimetic p73alpha T14D caused increased levels of transactivation.

Indexed as

Amino Acid Sequencebcl-2-Associated X ProteinCell Line, TumorConserved SequenceDNA-Binding ProteinsE1A-Associated p300 ProteinHumansMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularNuclear ProteinsPhosphorylationProtein BindingSequence AlignmentThermodynamicsTranscriptional Activationbcl-2-Associated X ProteinDNA-Binding ProteinsE1A-Associated p300 ProteinNuclear ProteinsTP73 protein, humanTumor Protein p73Tumor Suppressor Protein p53Tumor Suppressor Proteins

Identifiers

PMID19218448
PMCPMC2651247
OpenAlexW2077477798

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.