Evidence map›Paper›PMID 7853498›Full record

ArticleJournal of virology1995

Adenovirus E1A proteins interact with the cellular YY1 transcription factor.

B A Lewis, G Tullis, E Seto, N Horikoshi, R Weinmann, T Shenk

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 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
9.0field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 99 citations in OpenAlex.

  1. Review
  2. The YYR (YY1- RKIP) Regulatory Axis in the pathogenesis of Cancer and Immune Evasion.Journal of experimental & clinical cancer research : CR · 2025
    Review
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  6. Mechanisms of Enhancer-Promoter Interactions in Higher Eukaryotes.International journal of molecular sciences · 2021
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  7. Article
  8. Yin Yang 1 promotes mTORC2-mediated AKT phosphorylation.Journal of molecular cell biology · 2016
    Article
  9. Article
  10. Review
  11. Review
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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

6 authors at 1 institution in 1 country.

B A LewisDepartment of Molecular Biology, Howard Hughes Medical Institute, Princeton University, New Jersey 08544-1014.
G Tullis
E Seto
N Horikoshi
R Weinmann
T Shenk
Howard Hughes Medical Institute · US

Funding

STRUCTURE &FUNCTION OF DNA TUMOR VIRUS GENOMESR37CA038965 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 1987 to 2002
$1.1M
STRUCTURE AND FUNCTION OF DNA TUMOR VIRUS GENOMESR01CA038965 · NCI · PRINCETON UNIVERSITY · PI SHENK, THOMAS E · 1985 to 1986
–
ONCOGENE E1A INDUCED TRANSACTIVATIONR01CA044466 · NCI · WISTAR INSTITUTE · PI WEINMANN, ROBERTO · 1988 to 1997
–
NCI NIH HHS CA38965NCI NIH HHS CA44466
6 · The paper itself

Abstract

The adenovirus 12S and 13S E1A proteins have been shown to relieve repression mediated by the cellular transcription factor YY1. The 13S E1A protein not only relieves repression but also activates transcription through YY1 binding sites. In this study, using a variety of in vivo and in vitro assays, we demonstrate that both E1A proteins can bind to YY1, although the 13S E1A protein binds more efficiently than the 12S E1A protein. Two domains on the E1A proteins interact with YY1: an amino-terminal sequence (residues 15 to 35) that is present in both E1A proteins and a domain that includes at least a portion of conserved region 3 (residues 140 to 188) that is present in the 13S but not the 12S E1A protein. Two domains on YY1 interact with E1A proteins: one is contained within residues 54 to 260, and the other is contained within the carboxy-terminal domain of YY1 (residues 332 to 414). Cotransfection of a plasmid expressing carboxy-terminal amino acids 332 to 414 of YY1 fused to the GAL4 DNA-binding domain can inhibit expression from a reporter construct with GAL4 DNA binding sites in its promoter, and inclusion of a third plasmid expressing E1A proteins can relieve the repression. Thus, we find a correlation between the ability of E1A to interact with the carboxy-terminal domain of YY1 and its ability to relieve repression caused by the carboxy-terminal domain of YY1. We propose that E1A proteins normally relieve YY1-mediated transcriptional repression by binding directly to the cellular transcription factor.

Indexed as

Adenovirus E1A ProteinsDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsGene Expression Regulation, ViralHeLa CellsHumansIn Vitro TechniquesProtein BindingRecombinant Fusion ProteinsRNA, MessengerStructure-Activity RelationshipTranscription FactorsYY1 Transcription FactorAdenovirus E1A ProteinsDNA-Binding ProteinsErythroid-Specific DNA-Binding FactorsRecombinant Fusion ProteinsRNA, MessengerTranscription FactorsYY1 protein, humanYY1 Transcription Factor

Identifiers

PMID7853498
PMCPMC188760
OpenAlexW2159299465

What OpenQuestion holds

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Registered trials

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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.