Evidence map›Paper›PMID 22787207›Full record

ArticleJournal of virology2012

Phosphorylation regulates binding of the human papillomavirus type 8 E2 protein to host chromosomes.

Vandana Sekhar, Alison A McBride

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 31 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Vandana SekharLaboratory of Viral Diseases, NIAID, NIH, Bethesda, Maryland, USA.
Alison A McBride
National Institute of Allergy and Infectious Diseases · US

Funding

Genome Replication and Partitioning of Beta PapillomavirusesZIAAI001072 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MCBRIDE, ALISON · 2009 to 2016
$1.4M
Intramural NIH HHS
6 · The paper itself

Abstract

The papillomavirus E2 proteins are indispensable for the viral life cycle, and their functions are subject to tight regulation. The E2 proteins undergo posttranslational modifications that regulate their properties and roles in viral transcription, replication, and genome maintenance. During persistent infection, the E2 proteins from many papillomaviruses act as molecular bridges that tether the viral genomes to host chromosomes to retain them within the host nucleus and to partition them to daughter cells. The betapapillomavirus E2 proteins bind to pericentromeric regions of host mitotic chromosomes, including the ribosomal DNA loci. We recently reported that two residues (arginine 250 and serine 253) within the chromosome binding region of the human papillomavirus type 8 (HPV8) E2 protein are required for this binding. In this study, we show that serine 253 is phosphorylated, most likely by protein kinase A, and this modulates the interaction of the E2 protein with cellular chromatin. Furthermore, we show that this phosphorylation occurs in S phase, increases the half-life of the E2 protein, and promotes chromatin binding from S phase through mitosis.

Indexed as

AnimalsBetapapillomavirusBinding SitesCell LineChlorocebus aethiopsChromosomesCyclic AMP-Dependent Protein KinasesGenome, ViralHalf-LifeHost-Pathogen InteractionsHumansOncogene Proteins, ViralPhosphorylationProtein BindingRecombinant ProteinsSerineCyclic AMP-Dependent Protein Kinasesoncogene protein E2, Human papillomavirus type 8Oncogene Proteins, ViralRecombinant ProteinsSerineTrans-Activators

Identifiers

PMID22787207
PMCPMC3446558
OpenAlexW2108686054

What Socratic 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 Socratic graph.