Evidence map›Paper›PMID 8643650›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

E2F1 and E1A(12S) have a homologous activation domain regulated by RB and CBP.

D Trouche, T Kouzarides

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

42 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
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  3. Exploitation of EP300 and CREBBP Lysine Acetyltransferases by Cancer.Cold Spring Harbor perspectives in medicine · 2017
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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

2 authors at 1 institution in 1 country.

D TroucheWellcome/Cancer Research Campaign Institute, University of Cambridge, United Kingdom.
T Kouzarides
University of Cambridge · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The E2F1 transcription factor has a well-characterized activation domain at its C terminus and the E1A protein has a recently defined activation domain at its N terminus. Here we show that these activation domains are highly related in sequence. The sequence homology reflects, at least partly, the conservation of common binding sites for the RB and CBP/p300 proteins, which are preserved in the same relative order along E2F1 and E1A. Furthermore, the interaction of RB and CBP with these two activation domains results in the same functional consequences: RB represses both activation domains, whereas CBP stimulates them. We conclude that the activation domains of E1A(12s) and E2F1 belong to a novel functional class, characterized by specific protein binding sites. The implication of this conservation with respect to E1A-induced stimulation of E2F activity is discussed.

Indexed as

Carrier ProteinsCell Cycle ProteinsDNA-Binding ProteinsTrans-ActivatorsAdenovirus E1A ProteinsAmino Acid SequenceBinding SitesBone NeoplasmsCREB-Binding ProteinE2F1 Transcription FactorE2F Transcription FactorsHumansMolecular Sequence DataMutagenesis, Site-DirectedNuclear ProteinsOsteosarcomaAdenovirus E1A ProteinsCarrier ProteinsCell Cycle ProteinsCREB-Binding ProteinCREBBP protein, humanDNA-Binding ProteinsE2F1 protein, humanE2F1 Transcription FactorE2F Transcription FactorsNuclear ProteinsRecombinant Fusion ProteinsRetinoblastoma-Binding Protein 1Retinoblastoma ProteinTrans-ActivatorsTranscription Factor DP1Transcription Factors

Identifiers

PMID8643650
PMCPMC39957
OpenAlexW2051060234

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.