An N-terminal arginine-rich cluster and a proline-alanine-threonine repeat region determine the cellular localization of the herpes simplex virus type 1 ICP34.5 protein and its ligand, protein phosphatase 1.
about
Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2Sequence variability in clinical and laboratory isolates of herpes simplex virus 1 reveals new mutations.Up to four distinct polypeptides are produced from the γ34.5 open reading frame of herpes simplex virus 2Signals that dictate nuclear, nucleolar, and cytoplasmic shuttling of the gamma(1)34.5 protein of herpes simplex virus type 1Strain-dependent structural variants of herpes simplex virus type 1 ICP34.5 determine viral plaque size, efficiency of glycoprotein processing, and viral release and neuroinvasive disease potentialFunctional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response.ICP34.5 protein of herpes simplex virus facilitates the initiation of protein translation by bridging eukaryotic initiation factor 2alpha (eIF2alpha) and protein phosphatase 1Replication of herpes simplex virus 1 depends on the gamma 134.5 functions that facilitate virus response to interferon and egress in the different stages of productive infection.Selective internalization of sodium channels in rat dorsal root ganglion neurons infected with herpes simplex virus-1Dephosphorylation of eIF-2alpha mediated by the gamma(1)34.5 protein of herpes simplex virus type 1 is required for viral response to interferon but is not sufficient for efficient viral replication.Herpes simplex virus 2 expresses a novel form of ICP34.5, a major viral neurovirulence factor, through regulated alternative splicing.Control of TANK-binding kinase 1-mediated signaling by the gamma(1)34.5 protein of herpes simplex virus 1Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A/C through the γ134.5 Protein That Facilitates Nuclear EgressViral forensic genomics reveals the relatedness of classic herpes simplex virus strains KOS, KOS63, and KOS79.Herpes simplex virus remodels T-cell receptor signaling, resulting in p38-dependent selective synthesis of interleukin-10.The MyD116 African swine fever virus homologue interacts with the catalytic subunit of protein phosphatase 1 and activates its phosphatase activity.
P2860
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P2860
An N-terminal arginine-rich cluster and a proline-alanine-threonine repeat region determine the cellular localization of the herpes simplex virus type 1 ICP34.5 protein and its ligand, protein phosphatase 1.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
An N-terminal arginine-rich cl ...... ligand, protein phosphatase 1.
@en
type
label
An N-terminal arginine-rich cl ...... ligand, protein phosphatase 1.
@en
prefLabel
An N-terminal arginine-rich cl ...... ligand, protein phosphatase 1.
@en
P2860
P356
P1476
An N-terminal arginine-rich cl ...... ligand, protein phosphatase 1.
@en
P2093
Hanwen Mao
Kenneth S Rosenthal
P2860
P304
11423-11431
P356
10.1074/JBC.M111553200
P407
P577
2002-01-11T00:00:00Z