Evidence map›Paper›PMID 19740981›Full record

ArticleJournal of virology2009

Histone deacetylases 1 and 2 are phosphorylated at novel sites during varicella-zoster virus infection.

Matthew S Walters, Angela Erazo, Paul R Kinchington, Saul Silverstein

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

26 citing papers in PubMed, 37 citations in OpenAlex.

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  18. Viral serine/threonine protein kinases.Journal of virology · 2011
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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

4 authors at 2 institutions in 1 country.

Matthew S WaltersDepartment of Microbiology, College of Physicians and Surgeons, Columbia University, 701 W. 168th St., New York, NY 10032, USA.
Angela Erazo
Paul R Kinchington
Saul Silverstein
Columbia University · USUniversity of Pittsburgh · US

Funding

Virus Production and Manipulation of Protein/Gene Expression ModuleP30EY008098 · NEI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Ethan A Rossi · 1989 to 2026
$17.8M
Immunology of Infectious DiseaseT32AI060525 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI JoAnne L. Flynn · 2005 to 2026
$5.3M
Varicella zoster virus-Induced Pain in a Rat Model of Post-Herpetic NeuralgiaR01NS064022 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KINCHINGTON, PAUL R. · 2009 to 2019
$3.6M
VZ VIRUS: CLINICAL IMPLICATIONS OF IMMUNITYR01AI024021 · NIAID · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI SILVERSTEIN, SAUL J · 1986 to 2008
$3.0M
Varicella zoster virus-Induced Pain in a Rat Model of Post-Herpetic NeuralgiaR56NS064022 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KINCHINGTON, PAUL R. · 2015 to 2015
$532k
Varicella Zoster Virus:Clinical Implications of ImmunityR21AI024021 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI SILVERSTEIN, SAUL J · 2003 to 2003
$363k
NEI NIH HHS EY08098NEI NIH HHS P30 EY008098NIAID NIH HHS AI-024021NIAID NIH HHS AI060525NIAID NIH HHS R01 AI024021NIAID NIH HHS R21 AI024021NIAID NIH HHS T32 AI060525NINDS NIH HHS NS064022NINDS NIH HHS R01 NS064022NINDS NIH HHS R56 NS064022
6 · The paper itself

Abstract

ORF66p, a virion-associated varicella-zoster virus (VZV) protein, is a member of a conserved Alphaherpesvirinae kinase family with homology to herpes simplex virus US3 kinase. Expression of ORF66p in cells infected with VZV or an adenovirus expressing only ORF66p results in hyperphosphorylation of histone deacetylase 1 (HDAC1) and HDAC2. Mapping studies reveal that phosphorylation is at a unique conserved Ser residue in the C terminus of both HDACs. This modification requires an active kinase domain in ORF66p, as neither protein is phosphorylated in cells infected with VZV lacking kinase activity. However, hyperphosphorylation appears to occur indirectly, as within the context of in vitro kinase reactions, purified ORF66p phosphorylates a peptide derived from ORF62p, a known substrate, but does not phosphorylate HDAC. These results support a model where ORF66p is necessary but not sufficient to effect hyperphosphorylation of HDAC1 and HDAC2.

Indexed as

Cell LineCell Line, TumorGenetic VectorsHerpesvirus 3, HumanHerpes ZosterHistone Deacetylase 1Histone Deacetylase 2HumansPhosphorylationProtein KinasesViral ProteinsHDAC1 protein, humanHistone Deacetylase 1Histone Deacetylase 2Protein KinasesViral Proteins

Identifiers

PMID19740981
PMCPMC2772673
OpenAlexW2115151554

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.