Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
about
Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathwaysHerpes simplex virus IE63 (ICP27) protein interacts with spliceosome-associated protein 145 and inhibits splicing prior to the first catalytic stepInteractions between rubella virus capsid and host protein p32 are important for virus replication.Association of herpes simplex virus type 1 ICP8 and ICP27 proteins with cellular RNA polymerase II holoenzymeStructure of the T. brucei p22 protein, a cytochrome oxidase subunit II (COII) specific RNA editing accessory factorIdentification of herpes simplex virus RNAs that interact specifically with regulatory protein ICP27 in vivo.Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32.Identification of human cytomegalovirus UL84 virus- and cell-encoded binding partners by using proteomics analysisThe Herpesvirus Saimiri open reading frame 73 gene product interacts with the cellular protein p32.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.Interaction network of proteins associated with human cytomegalovirus IE2-p86 protein during infection: a proteomic analysis.Host factors in enterovirus 71 replicationInvestigating the biology of alpha herpesviruses with MS-based proteomicsRole of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear EgressOcular and neuronal cell apoptosis during HSV-1 infection: a review.A proteomic approach to discover and compare interacting partners of papillomavirus E2 proteins from diverse phylogenetic groupsHerpes simplex virus type 1 ICP27 regulates expression of a variant, secreted form of glycoprotein C by an intron retention mechanism.Heterogeneous nuclear ribonucleoprotein K (hnRNP-K) promotes tumor metastasis by induction of genes involved in extracellular matrix, cell movement, and angiogenesis.Cell death-independent functions of granzymes: hit viruses where it hurts.Herpes simplex virus type 1 ICP27-dependent activation of NF-kappaB.Protein kinase CK2 phosphorylation of EB2 regulates its function in the production of Epstein-Barr virus infectious viral particles.In vitro and in vivo interactions between the hepatitis B virus protein P22 and the cellular protein gC1qR.Inhibition of interferon-mediated antiviral activity by murine gammaherpesvirus 68 latency-associated M2 protein.Cellular p32 recruits cytomegalovirus kinase pUL97 to redistribute the nuclear lamina.
P2860
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P2860
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
description
2000 nî lūn-bûn
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2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
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2000年论文
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2000年论文
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name
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@en
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@nl
type
label
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@en
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@nl
prefLabel
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@en
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@nl
P2093
P2860
P1433
P1476
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
@en
P2093
D A Matthews
H E Bryant
J B Clements
W C Russell
P2860
P304
11322-11328
P356
10.1128/JVI.74.23.11322-11328.2000
P407
P50
P577
2000-12-01T00:00:00Z