Evidence map›Paper›PMID 32493825›Full record

ArticleJournal of virology2020

Human Papillomavirus 31 Tyrosine 102 Regulates Interaction with E2 Binding Partners and Episomal Maintenance.

Timra Gilson, Sara Culleton, Fang Xie, Marsha DeSmet, Elliot J Androphy

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 28% 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

6 citing papers in PubMed, 8 citations in OpenAlex.

  1. E2 Tyrosine 102 Regulates MmuPV1 Pathogenesis In Vivo.Pathogens (Basel, Switzerland) · 2025
    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

5 authors at 2 institutions in 2 countries.

Timra GilsonDepartment of Dermatology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Sara CulletonDepartment of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Fang XieDepartment of Dermatology, Chinese People's Liberation Army General Hospital, Beijing, China.
Marsha DeSmetDepartment of Dermatology, Indiana University School of Medicine, Indianapolis, Indiana, USA.
Elliot J AndrophyDepartment of Dermatology, Indiana University School of Medicine, Indianapolis, Indiana, USA eandro@iu.edu.ORCID 0000-0002-8104-0703
Indiana University School of MedicineChinese People's Liberation Army · CN

Funding

Immunology and Infectious Diseases Training ProgramT32AI060519 · NIAID · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI MARK H KAPLAN · 2004 to 2026
$6.0M
CONTROL OF PAPILLOMAVIRUS EXPRESSION AND TRANSFORMATIONR01CA058376 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI ANDROPHY, ELLIOT J. · 1993 to 2019
$5.7M
Training in STIs and infections of global health significanceT32AI007637 · NIAID · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI WOOLS-KALOUSTIAN, KARA KAY · 2001 to 2020
$3.4M
The Indiana Cutaneous Biological Research Training ProgramT32AR062495 · NIAMS · INDIANA UNIVERSITY INDIANAPOLIS · PI ANDROPHY, ELLIOT J. · 2013 to 2017
$649k
Host Control of Viral Protein Function: Phosphorylation in the Papillomavirus E2F30AI114284 · NIAID · INDIANA UNIVERSITY INDIANAPOLIS · PI CULLETON, SARA POIRIER · 2014 to 2016
$120k
NCI NIH HHS R01 CA058376NIAID NIH HHS F30 AI114284NIAID NIH HHS T32 AI007637NIAID NIH HHS T32 AI060519NIAMS NIH HHS T32 AR062495
6 · The paper itself

Abstract

Several serine and threonine residues of the papillomavirus early E2 protein have been found to be phosphorylated. In contrast, only one E2 tyrosine phosphorylation site in BPV-1 (tyrosine 102) and one in HPV-16/31 (tyrosine 138) site have been characterized. Between BPV-1 and HPV-31 E2, 8 of the 11 tyrosines are conserved in the N-terminal domain, suggesting that phosphorylation of tyrosines has an essential role in E2 biology. In this study, we examine the effect of Y102 phosphorylation on HPV-31 E2 biology. Y102 proteins mutated either to the potential phospho-mimetic glutamic acid (Y102E) or to the nonphosphorylated homologue phenylalanine (Y102F) remain nuclear; however, Y102E is more associated with the nuclear matrix fraction. This is consistent with the inability of Y102E to bind TopBP1. Both BPV-1 and HPV-31 Y102E are similar in that neither binds the C terminus of Brd4, but in all other aspects the mutant behaves differently between the two families of papillomaviruses. BPV-1 Y102E was unable to bind E1 and did not replicate in a transient

Indexed as

Cell LineDNA-Binding ProteinsDNA HelicasesDNA ReplicationGenome, ViralHEK293 CellsHuman papillomavirus 31HumansNuclear ProteinsPhosphorylationPlasmidsTranscription FactorsTyrosineViral ProteinsVirus ReplicationDNA-Binding ProteinsDNA HelicasesE2 protein, Human papillomavirus type 31Nuclear ProteinsTranscription FactorsTyrosineViral ProteinsE2HPVtyrosine phosphorylationviral replication

Identifiers

PMID32493825
PMCPMC7394896
OpenAlexW3029894930

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.