Evidence map›Paper›PMID 22172279›Full record

ArticleFEBS letters2012

HPV E7 viral oncoprotein disrupts transcriptional regulation of L1Md retrotransposon.

Diego E Montoya-Durango, Kenneth S Ramos

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 89% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

2 authors at 1 institution in 1 country.

Diego E Montoya-DurangoDepartment of Biochemistry and Molecular Biology and Center for Genetics and Molecular Medicine, School of Medicine, University of Louisville, Louisville, KY 40202, USA.
Kenneth S Ramos
University of Louisville · US

Funding

Strategic Vision & Impact on Environmental HealthP30ES014443 · NIEHS · UNIVERSITY OF LOUISVILLE · PI PROUGH, RUSSELL ALLEN · 2007 to 2010
$4.4M
MOLECULAR MECHANISMS OF VASCULAR TOXICITYR01ES004849 · NIEHS · UNIVERSITY OF LOUISVILLE · PI RAMOS, KENNETH S · 1988 to 2005
$1.3M
NIEHS NIH HHS 5R01 ES004849NIEHS NIH HHS P30 ES014443NIEHS NIH HHS R01 ES004849
6 · The paper itself

Abstract

Murine L1Md-A5 retrotransposon is a redox-inducible element regulated by Nrf-2/JunD and E2F/Rb-binding sites within its promoter (5'-UTR). Because the human papillomavirus (HPV) oncoprotein E7 interacts with retinoblastoma (pRb) and members of the AP1 family, studies were conducted to examine functional interactions between HPV E7, pRb, and histone deacetylase 2 (HDAC2) in the regulation of L1Md-A5. Using a transient heterologous transcription system we found that HPV E7 alone, or in combination with HDAC2, disrupted pRb-mediated L1MdA-5 transactivation. HPV E7 also ablated the transcriptional response of L1Md-A5 to genotoxic stress, but did not interfere with basal activity. We conclude that HPV E7 associates with proteins involved in the assembly of macromolecular complexes that regulate antioxidant and E2F/Rb sites within L1MdA-5 to regulate biological activity.

Indexed as

RetroelementsAlphapapillomavirusAnimalsBenzo(a)pyreneCarcinogensE2F Transcription FactorsGene Expression RegulationGenes, ReporterHeLa CellsHistone Deacetylase 2HumansLong Interspersed Nucleotide ElementsLuciferasesMiceOncogene Proteins, ViralPromoter Regions, GeneticBenzo(a)pyreneCarcinogensE2F Transcription FactorsHistone Deacetylase 2LuciferasesOncogene Proteins, ViralRetinoblastoma ProteinRetroelements

Identifiers

PMID22172279
PMCPMC3263525
OpenAlexW2002964082

What OpenQuestion holds

Textmetadata
LicenceTDM
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.