Evidence map›Paper›PMID 10330164›Full record

ArticleMolecular and cellular biology1999

Specificity of cyclin E-Cdk2, TFIIB, and E1A interactions with a common domain of the p300 coactivator.

L K Felzien, S Farrell, J C Betts, R Mosavin, G J Nabel

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

25 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
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  9. Review
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  11. Cell-type-specific binding of the transcription factor CREB to the cAMP-response element.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  12. Article
  13. Article
  14. Fine tuning the transcriptional regulation of the CXCL1 chemokine.Progress in nucleic acid research and molecular biology · 2003
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Acetylation of adenovirus E1A regulates binding of the transcriptional corepressor CtBP.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  20. Regulation of beta -catenin transformation by the p300 transcriptional coactivator.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

5 authors at 2 institutions in 1 country.

L K FelzienHoward Hughes Medical Institute, University of Michigan Medical Center, Departments of Internal Medicine and Biological Chemistry, Ann Arbor, Michigan 48109-0650, USA.
S Farrell
J C Betts
R Mosavin
G J Nabel
Howard Hughes Medical Institute · USUniversity of Michigan–Ann Arbor · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The p300 and CREB binding protein (CBP) transcriptional coactivators interact with a variety of transcription factors and regulate their activity. Among the interactions that have been described, the COOH-terminal region of p300 binds to cyclin E-cyclin-dependent kinase 2 (cyclin E-Cdk2) and TFIIB, as well as to the E1A gene products of adenovirus. Inhibition of Cdk activity by Cdk inhibitors, such as p21 or p27, potentiates NF-kappaB activity and provides a mechanism to coordinate cell cycle progression with the transcription of genes expressed during growth arrest. In this report, we analyze the specific domains of p300 required for the binding of p300 to cyclin E-Cdk2, TFIIB, and E1A and the ability of these proteins to interact with p300, alone or in combination. 12S E1A, an inhibitor of p300-dependent transcription, reduces the binding of TFIIB, but not that of cyclin E-Cdk2, to p300. In contrast, 13S E1A, a pleiotropic transcriptional activator, does not inhibit TFIIB binding to p300, although it enhances the interaction of cyclin E-Cdk2 with p300. Modification of cyclin E-Cdk2 is most likely required for association with p300 since the interaction is observed only with cyclin E-Cdk2 purified from mammalian cells. Domain swap studies show that the cyclin homology domain of TFIIB is involved in interactions with p300, although the homologous region from cyclin E does not mediate this interaction. These findings suggest that p300 or CBP function is regulated by interactions of various proteins with a common coactivator domain.

Indexed as

CDC2-CDC28 KinasesAdenovirus E1A ProteinsBlotting, WesternCyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclin EHumansJurkat CellsModels, GeneticNuclear ProteinsPrecipitin TestsProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryReverse Transcriptase Polymerase Chain ReactionTrans-ActivatorsAdenovirus E1A ProteinsCDC2-CDC28 KinasesCDK2 protein, humanCyclin-Dependent Kinase 2Cyclin-Dependent KinasesCyclin ENuclear ProteinsProtein Serine-Threonine KinasesTrans-ActivatorsTranscription FactorsTranscription Factor TFIIB

Identifiers

PMID10330164
PMCPMC104383
OpenAlexW2105378410

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.