Identification of nuclear and nucleolar localization signals in the herpes simplex virus regulatory protein ICP27.
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Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysNuclear and nucleolar targeting of human ribosomal protein S6Herpes simplex virus IE63 (ICP27) protein interacts with spliceosome-associated protein 145 and inhibits splicing prior to the first catalytic stepICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.Herpes simplex virus type 1 immediate-early protein ICP27 is required for efficient incorporation of ICP0 and ICP4 into virionsLocalization in the nucleolus and coiled bodies of protein subunits of the ribonucleoprotein ribonuclease PStructural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57Nuclear import and export of influenza virus nucleoprotein.Identification and functional analysis of NOL7 nuclear and nucleolar localization signals.Genome-wide screen of three herpesviruses for protein subcellular localization and alteration of PML nuclear bodiesThe major tegument structural protein VP22 targets areas of dispersed nucleolin and marginalized chromatin during productive herpes simplex virus 1 infection.Analysis of the phosphorylation sites of herpes simplex virus type 1 regulatory protein ICP27.ICP27 phosphorylation site mutants display altered functional interactions with cellular export factors Aly/REF and TAP/NXF1 but are able to bind herpes simplex virus 1 RNAICP27 recruits Aly/REF but not TAP/NXF1 to herpes simplex virus type 1 transcription sites although TAP/NXF1 is required for ICP27 export.Control of VP16 translation by the herpes simplex virus type 1 immediate-early protein ICP27.Herpesvirus mRNAs are sorted for export via Crm1-dependent and -independent pathwaysProcessing of alpha-globin and ICP0 mRNA in cells infected with herpes simplex virus type 1 ICP27 mutants.The conserved carboxyl-terminal half of herpes simplex virus type 1 regulatory protein ICP27 is dispensable for viral growth in the presence of compensatory mutationsIdentification of an export control sequence and a requirement for the KH domains in ICP27 from herpes simplex virus type 1Accumulation of herpes simplex virus type 1 early and leaky-late proteins correlates with apoptosis prevention in infected human HEp-2 cells.Epstein-Barr virus SM protein interacts with mRNA in vivo and mediates a gene-specific increase in cytoplasmic mRNA.Herpes simplex virus ICP27 activation of stress kinases JNK and p38.Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway.Direct stimulation of translation by the multifunctional herpesvirus ICP27 protein.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.Nucleolar localization elements in U8 snoRNA differ from sequences required for rRNA processingClassic nuclear localization signals and a novel nuclear localization motif are required for nuclear transport of porcine parvovirus capsid proteins.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.Functional analysis of Epstein-Barr virus SM protein: identification of amino acids essential for structure, transactivation, splicing inhibition, and virion productionHerpes simplex virus ICP27 is required for virus-induced stabilization of the ARE-containing IEX-1 mRNA encoded by the human IER3 geneKSHV ORF57, a protein of many facesICP27 mediates HSV RNA export by shuttling through a leucine-rich nuclear export signal and binding viral intronless RNAs through an RGG motifIdentification of nuclear and nucleolar localization signals of pseudorabies virus (PRV) early protein UL54 reveals that its nuclear targeting is required for efficient production of PRV.Arginine-rich regions succeeding the nuclear localization region of the herpes simplex virus type 1 regulatory protein ICP27 are required for efficient nuclear localization and late gene expressionThe C-terminal repressor region of herpes simplex virus type 1 ICP27 is required for the redistribution of small nuclear ribonucleoprotein particles and splicing factor SC35; however, these alterations are not sufficient to inhibit host cell splicinHerpes simplex virus trans-regulatory protein ICP27 stabilizes and binds to 3' ends of labile mRNA.The herpes simplex virus type 1 regulatory protein ICP27 coimmunoprecipitates with anti-Sm antiserum, and the C terminus appears to be required for this interactionThe RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation.Repression of host RNA polymerase II transcription by herpes simplex virus type 1Nucleolar and nuclear localization properties of a herpesvirus bZIP oncoprotein, MEQ.
P2860
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P2860
Identification of nuclear and nucleolar localization signals in the herpes simplex virus regulatory protein ICP27.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Identification of nuclear and ...... irus regulatory protein ICP27.
@ast
Identification of nuclear and ...... irus regulatory protein ICP27.
@en
type
label
Identification of nuclear and ...... irus regulatory protein ICP27.
@ast
Identification of nuclear and ...... irus regulatory protein ICP27.
@en
prefLabel
Identification of nuclear and ...... irus regulatory protein ICP27.
@ast
Identification of nuclear and ...... irus regulatory protein ICP27.
@en
P2093
P2860
P1433
P1476
Identification of nuclear and ...... virus regulatory protein ICP27
@en
P2093
P2860
P304
P407
P577
1995-02-01T00:00:00Z