| pubmed-article:20660201 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20660201 | lifeskim:mentions | umls-concept:C0682451 | lld:lifeskim |
| pubmed-article:20660201 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:20660201 | lifeskim:mentions | umls-concept:C0768528 | lld:lifeskim |
| pubmed-article:20660201 | pubmed:issue | 19 | lld:pubmed |
| pubmed-article:20660201 | pubmed:dateCreated | 2010-9-8 | lld:pubmed |
| pubmed-article:20660201 | pubmed:abstractText | A serine/threonine (S/T) kinase encoded by the US3 gene of herpes simplex virus type 1 (HSV-1) is conserved in varicella-zoster virus (VZV) and pseudorabies virus (PRV). Expression of US3 kinase in cells transformed with US3 expression plasmids or infected with each virus results in hyperphosphorylation of histone deacetylase 2 (HDAC2). Mapping studies revealed that each US3 kinase phosphorylates HDAC2 at the same unique conserved Ser residue in its C terminus. HDAC2 was also hyperphosphorylated in cells infected with PRV lacking US3 kinase, indicating that hyperphosphorylation of HDAC2 by PRV occurs in a US3-independent manner. Specific chemical inhibition of class I HDAC activity increases the plaquing efficiency of VZV and PRV lacking US3 or its enzymatic activity, whereas only minimal effects are observed with wild-type viruses, suggesting that VZV and PRV US3 kinase activities target HDACs to reduce viral genome silencing and allow efficient viral replication. However, no effect was observed for wild-type or US3 null HSV-1. Thus, we have demonstrated that while HDAC2 is a conserved target of alphaherpesvirus US3 kinases, the functional significance of these events is virus specific. | lld:pubmed |
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| pubmed-article:20660201 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20660201 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20660201 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:20660201 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20660201 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:20660201 | pubmed:issn | 1098-5514 | lld:pubmed |
| pubmed-article:20660201 | pubmed:author | pubmed-author:BanfieldBruce... | lld:pubmed |
| pubmed-article:20660201 | pubmed:author | pubmed-author:KinchingtonPa... | lld:pubmed |
| pubmed-article:20660201 | pubmed:author | pubmed-author:WaltersMatthe... | lld:pubmed |
| pubmed-article:20660201 | pubmed:author | pubmed-author:SilversteinSa... | lld:pubmed |
| pubmed-article:20660201 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20660201 | pubmed:volume | 84 | lld:pubmed |
| pubmed-article:20660201 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20660201 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20660201 | pubmed:pagination | 9666-76 | lld:pubmed |
| pubmed-article:20660201 | pubmed:dateRevised | 2011-7-27 | lld:pubmed |
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