Evidence map›Paper›PMID 10846067›Full record

ArticleJournal of virology2000

AMF-1/Gps2 binds p300 and enhances its interaction with papillomavirus E2 proteins.

Y C Peng, D E Breiding, F Sverdrup, J Richard, E J Androphy

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

53 citing papers in PubMed, 87 citations in OpenAlex.

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  14. CXCL8 histone H3 acetylation is dysfunctional in airway smooth muscle in asthma: regulation by BET.American journal of physiology. Lung cellular and molecular physiology · 2015
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  20. Nuclear receptor corepressor complexes in cancer: mechanism, function and regulation.American journal of clinical and experimental urology · 2014
    Review
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 1 institution in 1 country.

Y C PengDepartment of Dermatology, New England Medical Center, Tufts University School of Medicine, Boston, MA 02111, USA.
D E Breiding
F Sverdrup
J Richard
E J Androphy
Tufts University · US

Funding

CONTROL OF PAPILLOMAVIRUS EXPRESSION AND TRANSFORMATIONR01CA058376 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ANDROPHY, ELLIOT J. · 1993 to 2019
$5.7M
DESIGN OF UMAN PAPILLOMAVIRUS INHIBITORSR01AI038001 · NIAID · TUFTS UNIVERSITY BOSTON · PI BALEJA, JAMES D · 2000 to 2004
$1.8M
DESIGN OF HUMAN PAPILLOMAVIRUS INHIBITORSU01AI038001 · NIAID · TUFTS MEDICAL CENTER · PI ANDROPHY, ELLIOT J · 1995 to 1998
–
NCI NIH HHS CA58376NCI NIH HHS R01 CA058376NIAID NIH HHS AI38001NIAID NIH HHS U01 AI038001
6 · The paper itself

Abstract

The cellular protein AMF-1 (Gps2) positively modulates gene expression by the papillomavirus E2 protein (D. E. Breiding et al., Mol. Cell. Biol. 17:7208-7219, 1997). We show here that AMF-1 also binds the transcriptional coactivator p300 in vitro and in vivo. E2 interacted weakly with p300. These observations led to a model in which AMF-1 recruits p300 into a complex with E2. Cotransfection of AMF-1 or p300 stimulated levels of E2-dependent transcription, while cotransfection of both AMF-1 and p300 showed an additive effect. The functional significance of p300 recruitment for E2 transactivation was evidenced by repression of E2-activated transcription by adenovirus E1A, which inhibits both coactivator and acetylase activities of p300. Antibodies to AMF-1 or E2 immunoprecipitated histone acetylase activity from cell lysates. Western blotting using antibody against acetyl-lysine failed to detect acetylation of AMF-1 or E2 in complex with p300. These results suggest that AMF-1 facilitates the recruitment of p300 and its histone acetylase activity into complexes with E2 and represents a novel mechanism of transcriptional activation.

Indexed as

Bovine papillomavirus 1Repressor ProteinsAcetylationAdenovirus E1A ProteinsAnimalsBinding SitesCattleCell LineChemical PrecipitationDNA-Binding ProteinsFungal ProteinsHistonesHumansIntracellular Signaling Peptides and ProteinsNuclear ProteinsOncogene Proteins, ViralAdenovirus E1A ProteinsDNA-Binding ProteinsE1 protein, Bovine papillomavirusE2 protein, Bovine papillomavirusE2 protein, Human papillomavirus type 16Fungal ProteinsGPS2 protein, humanHistonesIntracellular Signaling Peptides and ProteinsNuclear ProteinsOncogene Proteins, ViralRecombinant Fusion ProteinsRepressor ProteinsTrans-ActivatorsViral Proteins

Identifiers

PMID10846067
PMCPMC112082
OpenAlexW2137478329

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.