The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation.
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Protein methylation is required to maintain optimal HIV-1 infectivityHeterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysProtein arginine methylation during lytic adenovirus infectionHerpes simplex virus IE63 (ICP27) protein interacts with spliceosome-associated protein 145 and inhibits splicing prior to the first catalytic stepThe arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Association of herpes simplex virus type 1 ICP8 and ICP27 proteins with cellular RNA polymerase II holoenzymeICP27 interacts with the RNA export factor Aly/REF to direct herpes simplex virus type 1 intronless mRNAs to the TAP export pathway.Molecular dissection of mRNA poly(A) tail length control in yeastThe RNA binding protein hnRNP Q modulates the utilization of exon 7 in the survival motor neuron 2 (SMN2) geneHerpes simplex virus type 1 immediate-early protein ICP27 is required for efficient incorporation of ICP0 and ICP4 into virionsRNA-binding of the human cytomegalovirus transactivator protein UL69, mediated by arginine-rich motifs, is not required for nuclear export of unspliced RNA.The new (dis)order in RNA regulationStructural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57Competitive and Cooperative Interactions Mediate RNA Transfer from Herpesvirus Saimiri ORF57 to the Mammalian Export Adaptor ALYREFArginine methylation facilitates the nuclear export of hnRNP proteinsCARM1 regulates proliferation of PC12 cells by methylating HuDMta has properties of an RNA export protein and increases cytoplasmic accumulation of Epstein-Barr virus replication gene mRNA.Varicella-zoster virus IE4 protein interacts with SR proteins and exports mRNAs through the TAP/NXF1 pathway.Analysis of the phosphorylation sites of herpes simplex virus type 1 regulatory protein ICP27.ICP27 phosphorylation site mutants are defective in herpes simplex virus 1 replication and gene expression.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 pathwaysHerpes simplex virus ICP27 induces cytoplasmic accumulation of unspliced polyadenylated alpha-globin pre-mRNA in infected HeLa cells.Processing 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 1Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap bindingHerpes simplex virus 1 regulatory protein ICP27 undergoes a head-to-tail intramolecular interaction.Accumulation 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.Three arginine residues within the RGG box are crucial for ICP27 binding to herpes simplex virus 1 GC-rich sequences and for efficient viral RNA export.Herpes simplex virus ICP27 protein provides viral mRNAs with access to the cellular mRNA export pathway.Epstein-Barr virus mRNA export factor EB2 is essential for intranuclear capsid assembly and production of gp350Head-to-tail intramolecular interaction of herpes simplex virus type 1 regulatory protein ICP27 is important for its interaction with cellular mRNA export receptor TAP/NXF1.Direct stimulation of translation by the multifunctional herpesvirus ICP27 protein.
P2860
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P2860
The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
The RGG box motif of the herpe ...... etermines in vivo methylation.
@ast
The RGG box motif of the herpe ...... etermines in vivo methylation.
@en
type
label
The RGG box motif of the herpe ...... etermines in vivo methylation.
@ast
The RGG box motif of the herpe ...... etermines in vivo methylation.
@en
prefLabel
The RGG box motif of the herpe ...... etermines in vivo methylation.
@ast
The RGG box motif of the herpe ...... etermines in vivo methylation.
@en
P2860
P1433
P1476
The RGG box motif of the herpe ...... determines in vivo methylation
@en
P2093
P2860
P304
P407
P577
1996-11-01T00:00:00Z