RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection.
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Herpes simplex virus 1 regulatory protein ICP22 interacts with a new cell cycle-regulated factor and accumulates in a cell cycle-dependent fashion in infected cells.A novel cellular protein, p60, interacting with both herpes simplex virus 1 regulatory proteins ICP22 and ICP0 is modified in a cell-type-specific manner and Is recruited to the nucleus after infectionFunctional anatomy of herpes simplex virus 1 overlapping genes encoding infected-cell protein 22 and US1.5 proteinAssociation of herpes simplex virus type 1 ICP8 and ICP27 proteins with cellular RNA polymerase II holoenzymeLentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactorP-TEFb goes viralShutoff of Host Gene Expression in Influenza A Virus and Herpesviruses: Similar Mechanisms and Common ThemesRecruitment of cellular recombination and repair proteins to sites of herpes simplex virus type 1 DNA replication is dependent on the composition of viral proteins within prereplicative sites and correlates with the induction of the DNA damage respoProteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8.Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27.A dominant-negative herpesvirus protein inhibits intranuclear targeting of viral proteins: effects on DNA replication and late gene expression.ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.Transcription of herpes simplex virus immediate-early and early genes is inhibited by roscovitine, an inhibitor specific for cellular cyclin-dependent kinasesRole of herpes simplex virus 1 immediate early protein ICP22 in viral nuclear egress.Requirement for cellular cyclin-dependent kinases in herpes simplex virus replication and transcription.The PK domain of the large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is required for immediate-early gene expression and virus growthAnalysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells.The conserved carboxyl-terminal half of herpes simplex virus type 1 regulatory protein ICP27 is dispensable for viral growth in the presence of compensatory mutationsICP22 and the UL13 protein kinase are both required for herpes simplex virus-induced modification of the large subunit of RNA polymerase II.Herpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Posttranslational processing of infected cell protein 22 mediated by viral protein kinases is sensitive to amino acid substitutions at distant sites and can be cell-type specificRNA polymerase II holoenzyme modifications accompany transcription reprogramming in herpes simplex virus type 1-infected cells.Herpes simplex virus type 1 infection leads to loss of serine-2 phosphorylation on the carboxyl-terminal domain of RNA polymerase II.Dissection of a novel nuclear localization signal in open reading frame 29 of varicella-zoster virus.Nuclear translocation and carboxyl-terminal domain phosphorylation of RNA polymerase II delineate the two phases of zygotic gene activation in mammalian embryos.Mapping of functional regions in the amino-terminal portion of the herpes simplex virus ICP27 regulatory protein: importance of the leucine-rich nuclear export signal and RGG Box RNA-binding domain.ICP27 interacts with the C-terminal domain of RNA polymerase II and facilitates its recruitment to herpes simplex virus 1 transcription sites, where it undergoes proteasomal degradation during infection.The ICP22 protein selectively modifies the transcription of different kinetic classes of pseudorabies virus genes.Heat-shock inactivation of the TFIIH-associated kinase and change in the phosphorylation sites on the C-terminal domain of RNA polymerase II.Schizophrenia susceptibility genes directly implicated in the life cycles of pathogens: cytomegalovirus, influenza, herpes simplex, rubella, and Toxoplasma gondii.Herpesviral replication compartments move and coalesce at nuclear speckles to enhance export of viral late mRNA.HSV-1 Cgal+ infection promotes quaking RNA binding protein production and induces nuclear-cytoplasmic shuttling of quaking I-5 isoform in human hepatoma cells.Inhibition of cdk9 during herpes simplex virus 1 infection impedes viral transcriptionHerpes simplex virus virion host shutoff protein: immune evasion mediated by a viral RNase?Intracellular localization of the herpes simplex virus type 1 major transcriptional regulatory protein, ICP4, is affected by ICP27Herpes simplex virus immediate-early protein ICP22 is required for viral modification of host RNA polymerase II and establishment of the normal viral transcription program.Functional interactions between herpes simplex virus immediate-early proteins during infection: gene expression as a consequence of ICP27 and different domains of ICP4.Herpes simplex virus immediate-early protein ICP22 triggers loss of serine 2-phosphorylated RNA polymerase IIIdentification and characterization of a filament-associated protein encoded by Amsacta moorei entomopoxvirus.Repression of the alpha0 gene by ICP4 during a productive herpes simplex virus infection.
P2860
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P2860
RNA polymerase II is aberrantly phosphorylated and localized to viral replication compartments following herpes simplex virus infection.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@ast
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@en
type
label
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@ast
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@en
prefLabel
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@ast
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@en
P2093
P2860
P1433
P1476
RNA polymerase II is aberrantl ...... erpes simplex virus infection.
@en
P2093
P2860
P304
P407
P577
1994-02-01T00:00:00Z