The herpes simplex virus 1 protein kinase US3 is required for protection from apoptosis induced by the virus
about
US11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrestThe protein encoded by the US3 orthologue of Marek's disease virus is required for efficient de-envelopment of perinuclear virions and involved in actin stress fiber breakdownMolecular 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 polypeptidesThe interplay between human herpes simplex virus infection and the apoptosis and necroptosis cell death pathwaysThe molecular basis of herpes simplex virus latencyNecroptosis: The Trojan horse in cell autonomous antiviral host defenseCytoskeletal rearrangements and cell extensions induced by the US3 kinase of an alphaherpesvirus are associated with enhanced spread.Nucleocytoplasmic shuttling of the HSV-2 serine/threonine kinase Us3Polarized cell migration during cell-to-cell transmission of herpes simplex virus in human skin keratinocytes.Phosphorylation of cytokeratin 17 by herpes simplex virus type 2 US3 protein kinase.Effects of phosphorylation of herpes simplex virus 1 envelope glycoprotein B by Us3 kinase in vivo and in vitroThe herpes simplex virus type 1 regulatory protein ICP27 is required for the prevention of apoptosis in infected human cells.Herpes simplex virus 1 blocks caspase-3-independent and caspase-dependent pathways to cell death.Herpes simplex virus protein kinases US3 and UL13 modulate VP11/12 phosphorylation, virion packaging, and phosphatidylinositol 3-kinase/Akt signaling activityHerpes simplex virus type 1 renders infected cells resistant to cytotoxic T-lymphocyte-induced apoptosis.Eukaryotic elongation factor 1delta is hyperphosphorylated by the protein kinase encoded by the U(L)13 gene of herpes simplex virus 1Nuclear accumulation of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, is inhibited by phosphorylation mediated by the VZV open reading frame 66 protein kinaseGlycoprotein D or J delivered in trans blocks apoptosis in SK-N-SH cells induced by a herpes simplex virus 1 mutant lacking intact genes expressing both glycoproteins.Induction and prevention of apoptosis in human HEp-2 cells by herpes simplex virus type 1.The U(S)3 protein kinase blocks apoptosis induced by the d120 mutant of herpes simplex virus 1 at a premitochondrial stage.The domains of glycoprotein D required to block apoptosis depend on whether glycoprotein D is present in the virions carrying herpes simplex virus 1 genome lacking the gene encoding the glycoprotein.Herpes simplex virus 1 ICP22 regulates the accumulation of a shorter mRNA and of a truncated US3 protein kinase that exhibits altered functionsU(L)31 and U(L)34 proteins of herpes simplex virus type 1 form a complex that accumulates at the nuclear rim and is required for envelopment of nucleocapsidsHerpes simplex virus type 1 2-kilobase latency-associated transcript intron associates with ribosomal proteins and splicing factors.Herpes simplex virus type 1 latency-associated transcript expression protects trigeminal ganglion neurons from apoptosis.Biological approaches to therapy of pancreatic cancer.Herpes simplex virus 1 protein kinase US3 hyperphosphorylates p65/RelA and dampens NF-κB activation.The combined effects of irradiation and herpes simplex virus type 1 infection on an immortal gingival cell line.The US3 protein kinase of herpes simplex virus 1 mediates the posttranslational modification of BAD and prevents BAD-induced programmed cell death in the absence of other viral proteins.HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Herpes simplex virus 1-encoded protein kinase UL13 phosphorylates viral Us3 protein kinase and regulates nuclear localization of viral envelopment factors UL34 and UL31Roles for herpes simplex virus type 1 UL34 and US3 proteins in disrupting the nuclear lamina during herpes simplex virus type 1 egress.U(S)3 protein kinase of herpes simplex virus 1 blocks caspase 3 activation induced by the products of U(S)1.5 and U(L)13 genes and modulates expression of transduced U(S)1.5 open reading frame in a cell type-specific manner.Regions of the herpes simplex virus type 1 latency-associated transcript that protect cells from apoptosis in vitro and protect neuronal cells in vivo.Ultrastructural localization of the herpes simplex virus type 1 UL31, UL34, and US3 proteins suggests specific roles in primary envelopment and egress of nucleocapsids.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.Stable cell lines expressing high levels of the herpes simplex virus type 1 LAT are refractory to caspase 3 activation and DNA laddering following cold shock induced apoptosisICP0 and the US3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression.
P2860
Q24313084-8C3E9D4B-274D-42DA-BE05-E9911C5228B0Q24519071-04952E6A-1791-4BBB-B568-692B56C3F7C0Q24531303-95764361-8846-4459-8CE6-756CB69BD51AQ24675678-51C2E047-AB9A-45B2-8AAE-B92B55C33A01Q26751441-899B9670-339C-48F1-B05D-D7AD80226CD6Q27001272-6CD48235-A6E2-4E4F-8174-CBBFDCB98482Q28087723-27E7CB44-10D4-47F7-A050-2D9A7472A451Q30475975-593486C4-80F5-44F1-98FC-88B0A43AE46DQ30503332-E5EF2964-97FB-43D3-BC8F-1FC975D72E08Q30541128-D5132659-BA0E-40CC-B1C2-7A0E4F1D7A34Q31121143-8F5B4510-6D11-4D17-8869-6A46C0E95C16Q33558633-9129F311-1EC7-48B3-AD56-C06F17FF42C8Q33643356-54AE2CA6-8C75-4B7A-8B57-1AD38EBD2082Q33644836-A17106F3-DA19-42DE-8FBF-DF2DDC946A9AQ33743987-FD734524-AB53-4CE1-9A6D-29AF9CA20158Q33782022-59ECC87B-40D8-4F23-BAD0-5D156A977AE6Q33782229-4C2D6FD3-8038-4434-92C4-DC722ABE128DQ33798767-9A7E950B-A009-439C-8102-DCB6BAA1F659Q33812868-68D5AE5C-68DD-43B7-BDDA-5040E0698936Q33825495-6DC87591-D167-4FF1-B2A2-70449CC942A5Q33841889-20A30C9E-409E-4CE1-AEBB-AA8FD530B1BEQ33842609-EB27FDB5-9754-40A9-A0F2-B423D4E41409Q33843248-1B05CBB8-7363-4565-969B-FF1E87DB2042Q33854765-81C09502-C340-47FE-93CF-0A600AB7D555Q33869971-8368BD24-0FFB-4147-BA92-F7BDCB9A31FFQ33884066-40F13D98-204A-4B0B-A35E-10DF4BE9ED15Q33899938-1FDC9F78-1D56-4A02-9403-A062C6CCFE67Q33900418-9D9E9930-A531-4C5A-B820-36F9570DF812Q33928172-58BE6043-4CC5-4079-A026-38412FDBE159Q33943249-FBBB7AE2-EEB3-49EF-8A39-8DC12BAA3609Q33995747-FA00A20F-3E19-4A5D-82B3-CA839A95B12AQ34302174-2FE7F6A9-3917-4043-9D2A-0A4FB20BAD59Q34357194-9FA000BE-028A-4994-BBEE-9DA4A1F1468AQ34358090-76AB6EC5-682A-43A1-AF85-66B1956AB5BFQ34358232-FDF8E6A9-B837-4C6F-BEC8-98F5B4545C22Q34362473-AB35FB15-5317-4CE6-BC81-D14B0F7FCA67Q34545781-C11D97B8-2D07-46EC-B37E-743379E71BC8Q34545887-CFD6A85E-6438-44E5-B3B2-DDB531FE130CQ34668446-C68A4EBF-2AAB-48F9-A615-B07EC1D774D7Q34773141-76320781-4817-4F80-81C1-74024A2482FD
P2860
The herpes simplex virus 1 protein kinase US3 is required for protection from apoptosis induced by the virus
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh
1997年學術文章
@zh-hant
name
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@ast
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@en
type
label
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@ast
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@en
prefLabel
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@ast
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@en
P2860
P356
P1476
The herpes simplex virus 1 pro ...... apoptosis induced by the virus
@en
P2093
C Van Sant
R Leopardi
P2860
P304
P356
10.1073/PNAS.94.15.7891
P407
P577
1997-07-01T00:00:00Z