Herpes simplex virus protein kinase US3 activates and functionally overlaps protein kinase A to block apoptosis
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Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Mapping of key functions of the herpes simplex virus 1 U(S)3 protein kinase: the U(S)3 protein can form functional heteromultimeric structures derived from overlapping truncated polypeptidesNecroptosis: The Trojan horse in cell autonomous antiviral host defenseNucleocytoplasmic shuttling of the HSV-2 serine/threonine kinase Us3Effects of phosphorylation of herpes simplex virus 1 envelope glycoprotein B by Us3 kinase in vivo and in vitroHerpes simplex virus protein kinases US3 and UL13 modulate VP11/12 phosphorylation, virion packaging, and phosphatidylinositol 3-kinase/Akt signaling activityThe suppression of apoptosis by α-herpesvirus.Herpes simplex virus 1 ICP22 regulates the accumulation of a shorter mRNA and of a truncated US3 protein kinase that exhibits altered functionsHerpes simplex virus 1 protein kinase US3 hyperphosphorylates p65/RelA and dampens NF-κB activation.Could lysine supplementation prevent Alzheimer's dementia? A novel hypothesis.Herpes simplex virus type 1 infection induces activation and recruitment of protein kinase C to the nuclear membrane and increased phosphorylation of lamin B.Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31Constitutive mTORC1 activation by a herpesvirus Akt surrogate stimulates mRNA translation and viral replicationBaculovirus as versatile vectors for protein expression in insect and mammalian cells.Protein kinase B/Akt is present in activated form throughout the entire replicative cycle of deltaU(S)3 mutant virus but only at early times after infection with wild-type herpes simplex virus 1U(S)3 and U(S)3.5 protein kinases of herpes simplex virus 1 differ with respect to their functions in blocking apoptosis and in virion maturation and egress.ICP0 and the US3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression.Herpes simplex virus 1 protein kinase Us3 and major tegument protein UL47 reciprocally regulate their subcellular localization in infected cells.US3 protein kinase of HSV-1 cycles between the cytoplasm and nucleus and interacts with programmed cell death protein 4 (PDCD4) to block apoptosisThe UL13 and US3 Protein Kinases of Herpes Simplex Virus 1 Cooperate to Promote the Assembly and Release of Mature, Infectious Virions.Herpes Simplex Virus 1 US3 Phosphorylates Cellular KIF3A To Downregulate CD1d ExpressionUS3 of herpes simplex virus type 1 encodes a promiscuous protein kinase that phosphorylates and alters localization of lamin A/C in infected cellsBcl-2 blocks accretion or depletion of stored calcium but has no effect on the redistribution of IP3 receptor I mediated by glycoprotein E of herpes simplex virus 1.Functional and Structural Mimicry of Cellular Protein Kinase A Anchoring Proteins by a Viral OncoproteinIn transduced cells, the US3 protein kinase of herpes simplex virus 1 precludes activation and induction of apoptosis by transfected procaspase 3.Designing Herpes Viruses as Oncolytics.Role of group A p21-activated kinases in the anti-apoptotic activity of the pseudorabies virus US3 protein kinase.Characterization of a Herpes Simplex Virus 1 (HSV-1) Chimera in Which the Us3 Protein Kinase Gene Is Replaced with the HSV-2 Us3 Gene.The interaction of herpes simplex virus 1 regulatory protein ICP22 with the cdc25C phosphatase is enabled in vitro by viral protein kinases US3 and UL13.Human cytomegalovirus UL97 kinase activity is required for the hyperphosphorylation of retinoblastoma protein and inhibits the formation of nuclear aggresomes.Expression of gamma interferon-dependent genes is blocked independently by virion host shutoff RNase and by US3 protein kinaseIdentification of a physiological phosphorylation site of the herpes simplex virus 1-encoded protein kinase Us3 which regulates its optimal catalytic activity in vitro and influences its function in infected cells.Roles of Us8A and Its Phosphorylation Mediated by Us3 in Herpes Simplex Virus 1 Pathogenesis.Herpesvirus gB-induced fusion between the virion envelope and outer nuclear membrane during virus egress is regulated by the viral US3 kinase.Regulation of the catalytic activity of herpes simplex virus 1 protein kinase Us3 by autophosphorylation and its role in pathogenesis.Phosphorylation of the U(L)31 protein of herpes simplex virus 1 by the U(S)3-encoded kinase regulates localization of the nuclear envelopment complex and egress of nucleocapsids.Herpes simplex virus US3 tegument protein inhibits Toll-like receptor 2 signaling at or before TRAF6 ubiquitinationHerpes simplex virus 1 serine/threonine kinase US3 hyperphosphorylates IRF3 and inhibits beta interferon production.Histone deacetylases 1 and 2 are phosphorylated at novel sites during varicella-zoster virus infection.Herpes simplex virus 1 protein kinase Us3 phosphorylates viral dUTPase and regulates its catalytic activity in infected cells.
P2860
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P2860
Herpes simplex virus protein kinase US3 activates and functionally overlaps protein kinase A to block apoptosis
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@ast
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@en
type
label
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@ast
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@en
prefLabel
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@ast
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@en
P2860
P356
P1476
Herpes simplex virus protein k ...... in kinase A to block apoptosis
@en
P2093
Luca Benetti
P2860
P304
P356
10.1073/PNAS.0403160101
P407
P577
2004-06-10T00:00:00Z