about
Human HERC5 restricts an early stage of HIV-1 assembly by a mechanism correlating with the ISGylation of GagMitochondrial DNA stress primes the antiviral innate immune responseHerpes simplex virus virion host shutoff protein is stimulated by translation initiation factors eIF4B and eIF4HFunctional inaccessibility of quiescent herpes simplex virus genomesHerpes simplex virus VP16, but not ICP0, is required to reduce histone occupancy and enhance histone acetylation on viral genomes in U2OS osteosarcoma cells.Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27.Herpes simplex virus protein kinases US3 and UL13 modulate VP11/12 phosphorylation, virion packaging, and phosphatidylinositol 3-kinase/Akt signaling activityHerpes simplex virus ICP0 mutants are hypersensitive to interferonHerpes simplex virus ICP27 induces cytoplasmic accumulation of unspliced polyadenylated alpha-globin pre-mRNA in infected HeLa cells.Herpes simplex virus virion host shutoff protein requires a mammalian factor for efficient in vitro endoribonuclease activity.Herpes simplex virus ICP27 is required for virus-induced stabilization of the ARE-containing IEX-1 mRNA encoded by the human IER3 geneHerpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase?Herpes simplex virus eliminates host mitochondrial DNA.Cell-type-specific tyrosine phosphorylation of the herpes simplex virus tegument protein VP11/12 encoded by gene UL46.Elimination of mitochondrial DNA is not required for herpes simplex virus 1 replication.Role of Herpes simplex virus 1 VP11/12 tyrosine-based binding motifs for Src family kinases, p85, Grb2 and Shc in activation of the phosphoinositide 3-kinase-Akt pathway.The herpes simplex virus 2 virion-associated ribonuclease vhs interferes with stress granule formationThe herpes simplex virus 1 vhs protein enhances translation of viral true late mRNAs and virus production in a cell type-dependent manner.The vhs1 mutant form of herpes simplex virus virion host shutoff protein retains significant internal ribosome entry site-directed RNA cleavage activity.Cell fusion-induced activation of interferon-stimulated genes is not required for restriction of a herpes simplex virus VP16/ICP0 mutant in heterokarya formed between permissive and restrictive cells.Herpes simplex virus 1 infection of T cells causes VP11/12-dependent phosphorylation and degradation of the cellular protein Dok-2.The Herpes Simplex Virus Virion Host Shutoff Protein Enhances Translation of Viral True Late mRNAs Independently of Suppressing Protein Kinase R and Stress Granule Formation.Evidence for translational regulation by the herpes simplex virus virion host shutoff proteinActivation of expression of multiple subfamilies of human Alu elements by adenovirus type 5 and herpes simplex virus type 1.Role of herpes simplex virus VP11/12 tyrosine-based motifs in binding and activation of the Src family kinase Lck and recruitment of p85, Grb2, and Shc.The herpes simplex virus 1 virion host shutoff protein enhances translation of viral late mRNAs by preventing mRNA overload.Mitochondrial nucleases ENDOG and EXOG participate in mitochondrial DNA depletion initiated by herpes simplex virus 1 UL12.5.Herpes simplex virus vhs protein.Construction in vitro and rescue of a thymidine kinase-deficient deletion mutation of herpes simplex virus.Expression of the Vaccinia Virus Antiapoptotic F1 Protein Is Blocked by Protein Kinase R in the Absence of the Viral E3 ProteinConstruction of a double-jointed herpes simplex viral DNA molecule: inverted repeats are required for segment inversion, and direct repeats promote deletionsExpression of herpesvirus thymidine kinase gene under control of early promoter of SV40The herpes simplex virus host shutoff (vhs) RNase limits accumulation of double stranded RNA in infected cells: Evidence for accelerated decay of duplex RNA
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description
researcher
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wetenschapper
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name
J R Smiley
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James Smiley
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type
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J R Smiley
@nl
James Smiley
@en
altLabel
J R Smiley
@en
prefLabel
J R Smiley
@nl
James Smiley
@en
P106
P21
P31
P496
0000-0001-9162-4393