Evidence map›Paper›PMID 7494304›Full record

ArticleJournal of virology1995

E1A promotes association between p300 and pRB in multimeric complexes required for normal biological activity.

H G Wang, E Moran, P Yaciuk

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1995. 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
4.7field-weighted citation impact, top 5% 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, 63 citations in OpenAlex.

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  10. Structural basis for subversion of cellular control mechanisms by the adenoviral E1A oncoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2009
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  11. Review
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  16. Primary activation of interferon A and interferon B gene transcription by interferon regulatory factor 3.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
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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

3 authors at 1 institution in 1 country.

H G WangFels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
E Moran
P Yaciuk
Temple University · US

Funding

PROTEIN INTERACTIONS AND REPRESSION IN FUNCTION OF THE ER01CA053592 · NCI · TEMPLE UNIVERSITY · PI MORAN, ELIZABETH · 1991 to 2000
$332k
CELL-CYCLE REGULATING ACTIVITIES OF THE ADENOVIRES E1AF32CA009372 · NCI · COLD SPRING HARBOR LABORATORY · PI WANG, HWEI-GENE H · 1992 to 1993
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CELL GROWTH CONTROL FUNCTIONS OF THE E1A ONCOGENER01CA055330 · NCI · TEMPLE UNIVERSITY · PI MORAN, ELIZABETH · 1991 to 1994
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NCI NIH HHS CA-53592NCI NIH HHS CA-55330NCI NIH HHS F32CA09372
6 · The paper itself

Abstract

The oncogenes of the small DNA tumor viruses encode transforming proteins with multiple domains that influence the cell cycle and aspects of the transformed phenotype. Like other gene products of this type, the adenovirus E1A proteins influence the cell by binding to specific cell growth control proteins. These include members of the retinoblastoma gene product (pRB) family, which are bound by the E1A region 2-specific site, and p300, which is bound at the E1A amino terminus. Binding at these two sites is largely independent, and discrete transcription-regulating functions remain intact in E1A products when only one or the other binding site is functional. In this report, immunoprecipitation with p300 antibodies reveals the presence of the pRB family proteins in p300 complexes when E1A is expressed in host cells, indicating that E1A can mediate physical contact between p300 and the pRB-related proteins. The ability of E1A to induce proliferation efficiently in quiescent primary cells correlates closely with the ability to bind p300 and individual members of the pRB family simultaneously in multimeric complexes, even though the E1A active sites can bind their target proteins efficiently when separated on different molecules. Conservation of a spacer region between the two binding sites that is required for simultaneous binding and efficient induction of proliferation supports the concept that the E1A protein structure has evolved to facilitate simultaneous binding. These results indicate that the E1A proteins are designed not merely to sequester these cellular products, but also to bring them into proximal association with each other in biologically significant complexes.

Indexed as

Trans-ActivatorsAdenoviridaeAdenovirus E1A ProteinsAnimalsAntibodies, MonoclonalAntibody SpecificityCell DivisionCell LineCell Transformation, ViralChloramphenicol O-AcetyltransferaseE1A-Associated p300 ProteinHeLa CellsHumansImmunoblottingMacromolecular SubstancesNuclear ProteinsAdenovirus E1A ProteinsAntibodies, MonoclonalChloramphenicol O-AcetyltransferaseE1A-Associated p300 ProteinEp300 protein, ratMacromolecular SubstancesNuclear ProteinsRecombinant ProteinsRetinoblastoma ProteinTrans-ActivatorsTranscription Factors

Identifiers

PMID7494304
PMCPMC189736
OpenAlexW2103182211

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.