Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3.
about
The nuclear envelope LEM-domain protein emerinHerpesviruses and intermediate filaments: close encounters with the third typeCyclin-dependent kinase-like function is shared by the beta- and gamma- subset of the conserved herpesvirus protein kinasesO-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched "niche".Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17+)Viral mimicry of Cdc2/cyclin-dependent kinase 1 mediates disruption of nuclear lamina during human cytomegalovirus nuclear egress.Effects of phosphorylation of herpes simplex virus 1 envelope glycoprotein B by Us3 kinase in vivo and in vitroConstitutive mTORC1 activation by a herpesvirus Akt surrogate stimulates mRNA translation and viral replicationNew role for EMD (emerin), a key inner nuclear membrane protein, as an enhancer of autophagosome formation in the C16-ceramide autophagy pathwayp32 is a novel target for viral protein ICP34.5 of herpes simplex virus type 1 and facilitates viral nuclear egress.Us3 kinase encoded by herpes simplex virus 1 mediates downregulation of cell surface major histocompatibility complex class I and evasion of CD8+ T cellsHerpes simplex virus 1 protein kinase Us3 and major tegument protein UL47 reciprocally regulate their subcellular localization in infected cells.Emerin in health and disease.The UL13 and US3 Protein Kinases of Herpes Simplex Virus 1 Cooperate to Promote the Assembly and Release of Mature, Infectious Virions.An Intracellular Arrangement of Histoplasma capsulatum Yeast-Aggregates Generates Nuclear Damage to the Cultured Murine Alveolar Macrophages.Identification 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.Effects of lamin A/C, lamin B1, and viral US3 kinase activity on viral infectivity, virion egress, and the targeting of herpes simplex virus U(L)34-encoded protein to the inner nuclear membraneNuclear pore composition and gating in herpes simplex virus-infected cellsTwo viral kinases are required for sustained long distance axon transport of a neuroinvasive herpesvirus.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.Nuclear Exodus: Herpesviruses Lead the Way.Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A/C through the γ134.5 Protein That Facilitates Nuclear EgressDifferences in the regulatory and functional effects of the Us3 protein kinase activities of herpes simplex virus 1 and 2.Herpes simplex virus 1 protein kinase Us3 phosphorylates viral dUTPase and regulates its catalytic activity in infected cells.Varicella-zoster virus open reading frame 66 protein kinase and its relationship to alphaherpesvirus US3 kinases.Phosphorylation of a herpes simplex virus 1 dUTPase by a viral protein kinase, Us3, dictates viral pathogenicity in the central nervous system but not at the periphery.Viral serine/threonine protein kinasesRole of tegument proteins in herpesvirus assembly and egress.Herpesviruses remodel host membranes for virus egress.Breach of the nuclear lamina during assembly of herpes simplex viruses.Nuclear actin and lamins in viral infections.Nucleolin is required for efficient nuclear egress of herpes simplex virus type 1 nucleocapsids.A functional role for TorsinA in herpes simplex virus 1 nuclear egress.Intragenic and extragenic suppression of a mutation in herpes simplex virus 1 UL34 that affects both nuclear envelope targeting and membrane budding.Nuclear envelope breakdown induced by herpes simplex virus type 1 involves the activity of viral fusion proteins.Diseases of the Nucleoskeleton.Characterization of conserved region 2-deficient mutants of the cytomegalovirus egress protein pM53.Herpes simplex virus 1 pUL34 plays a critical role in cell-to-cell spread of virus in addition to its role in virus replication
P2860
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P2860
Emerin is hyperphosphorylated and redistributed in herpes simplex virus type 1-infected cells in a manner dependent on both UL34 and US3.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@ast
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@en
type
label
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@ast
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@en
prefLabel
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@ast
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@en
P2093
P2860
P356
P1433
P1476
Emerin is hyperphosphorylated ...... ependent on both UL34 and US3.
@en
P2093
Desire K Christensen
Jacques M Bouchard
Joel Baines
Natalie Leach
Richard J Roller
Richard Park
Susan L Bjerke
Tokuko Haraguchi
P2860
P304
10792-10803
P356
10.1128/JVI.00196-07
P407
P577
2007-07-25T00:00:00Z