ArticleJournal of virology2005
Herpes simplex virus 1 ICP22 regulates the accumulation of a shorter mRNA and of a truncated US3 protein kinase that exhibits altered functions.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 37 citations in OpenAlex.
- Impaired endocytosis and accumulation in early endosomal compartments defines herpes simplex virus-mediated disruption of the nonclassical MHC class I-related molecule MR1.The Journal of biological chemistry · 2024Article
- "Non-Essential" Proteins of HSV-1 with Essential Roles In Vivo: A Comprehensive Review.Viruses · 2020Review
- Roles of the Different Isoforms of the Pseudorabies Virus Protein Kinase pUS3 in Nuclear Egress.Journal of virology · 2020Article
- Sequence variation in the herpes simplex virus U(S)1 ocular virulence determinant.Investigative ophthalmology & visual science · 2011Article
- Viral serine/threonine protein kinases.Journal of virology · 2011Review
- Hyperphosphorylation of histone deacetylase 2 by alphaherpesvirus US3 kinases.Journal of virology · 2010Article
- The novel HSV-1 US5-1 RNA is transcribed off a domain encoding US5, US4, US3, US2 and alpha22.Virology journal · 2010Article
- The herpes simplex virus type 1 infected cell protein 22.Virologica Sinica · 2010Review
- Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids.Journal of virology · 2009Article
- Role of cdk9 in the optimization of expression of the genes regulated by ICP22 of herpes simplex virus 1.Journal of virology · 2008Article
- Identification of a physiological phosphorylation site of the herpes simplex virus 1-encoded protein kinase Us3 which regulates its optimal catalytic activity in vitro and influences its function in infected cells.Journal of virology · 2008Article
- Expression of gamma interferon-dependent genes is blocked independently by virion host shutoff RNase and by US3 protein kinase.Journal of virology · 2008Article
- Herpes simplex virus type 1 C-terminal variants of the origin binding protein (OBP), OBPC-1 and OBPC-2, cooperatively regulate viral DNA levels in vitro, and OBPC-2 affects mortality in mice.Journal of virology · 2007Article
- In transduced cells, the US3 protein kinase of herpes simplex virus 1 precludes activation and induction of apoptosis by transfected procaspase 3.Journal of virology · 2007Article
- Cathepsin B mediates cleavage of herpes simplex virus type 1 origin binding protein (OBP) to yield OBPC-1, and cleavage is dependent upon viral DNA replication.Journal of virology · 2007Article
- US3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cells.Journal of virology · 2007Article
- Mapping of key functions of the herpes simplex virus 1 U(S)3 protein kinase: the U(S)3 protein can form functional heteromultimeric structures derived from overlapping truncated polypeptides.Journal of virology · 2007Article
- Glycoprotein M of herpes simplex virus 1 is incorporated into virions during budding at the inner nuclear membrane.Journal of virology · 2007Article
- ORF66 protein kinase function is required for T-cell tropism of varicella-zoster virus in vivo.Journal of virology · 2006Article
- ICP0 and the US3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The U(S)3 open reading frame of herpes simplex virus 1 (HSV-1) was reported to encode two mRNAs each directing the synthesis of the same protein. We report that the U(S)3 gene encodes two proteins. The predominant U(S)3 protein is made in wild-type HSV-1-infected cells. The truncated mRNA and a truncated protein designated U(S)3.5 and initiating from methionine 77 were preeminent in cells infected with a mutant lacking the gene encoding ICP22. Both the wild-type and truncated proteins also accumulated in cells transduced with a baculovirus carrying the entire U(S)3 open reading frame. The U(S)3.5 protein accumulating in cells infected with the mutant lacking the gene encoding ICP22 mediated the phosphorylation of histone deacetylase 1, a function of U(S)3 protein, but failed to block apoptosis of the infected cells. The U(S)3.5 and U(S)3 proteins differ with respect to the range of functions they exhibit.
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