The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication.
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Functional interaction between class II histone deacetylases and ICP0 of herpes simplex virus type 1The herpes simplex virus ICP0 RING finger domain inhibits IRF3- and IRF7-mediated activation of interferon-stimulated genesPML is critical for ND10 formation and recruits the PML-interacting protein daxx to this nuclear structure when modified by SUMO-1PML residue lysine 160 is required for the degradation of PML induced by herpes simplex virus type 1 regulatory protein ICP0The role of the CoREST/REST repressor complex in herpes simplex virus 1 productive infection and in latencyProteomic approaches to uncovering virus-host protein interactions during the progression of viral infectionA viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responsesHSV-1 ICP0: paving the way for viral replicationCrystal Structure of USP7 Ubiquitin-like Domains with an ICP0 Peptide Reveals a Novel Mechanism Used by Viral and Cellular Proteins to Target USP7ICP0 induces the accumulation of colocalizing conjugated ubiquitin.ATR and ATRIP are recruited to herpes simplex virus type 1 replication compartments even though ATR signaling is disabled.Herpes simplex virus ICP0 mutants are hypersensitive to interferonInactivation of HAUSP in vivo modulates p53 function.Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0.Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 renders expression of the immediate-early genes almost entirely dependent on ICP0HSV-1 ICP0: An E3 Ubiquitin Ligase That Counteracts Host Intrinsic and Innate ImmunityHerpes simplex virus 1-infected cell protein 0 contains two E3 ubiquitin ligase sites specific for different E2 ubiquitin-conjugating enzymesNovel roles of cytoplasmic ICP0: proteasome-independent functions of the RING finger are required to block interferon-stimulated gene production but not to promote viral replication.HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Characterization of the novel E3 ubiquitin ligase encoded in exon 3 of herpes simplex virus-1-infected cell protein 0.Herpes simplex virus 1 mutant in which the ICP0 HUL-1 E3 ubiquitin ligase site is disrupted stabilizes cdc34 but degrades D-type cyclins and exhibits diminished neurotoxicityIdentification of TRIM27 as a novel degradation target of herpes simplex virus 1 ICP0.A pre-immediate-early role for tegument ICP0 in the proteasome-dependent entry of herpes simplex virusThe checkpoints of viral gene expression in productive and latent infection: the role of the HDAC/CoREST/LSD1/REST repressor complexA survey of the interactome of Kaposi's sarcoma-associated herpesvirus ORF45 revealed its binding to viral ORF33 and cellular USP7, resulting in stabilization of ORF33 that is required for production of progeny virusesProteomic profiling of the human cytomegalovirus UL35 gene products reveals a role for UL35 in the DNA repair responseRole of ICP0 in the strategy of conquest of the host cell by herpes simplex virus 1HSV ICP0 recruits USP7 to modulate TLR-mediated innate responseA herpesvirus ubiquitin-specific protease is critical for efficient T cell lymphoma formation.Intracellular localization of proteasomal degradation of a viral antigen.Overexpression of the ubiquitin-specific protease 7 resulting from transfection or mutations in the ICP0 binding site accelerates rather than depresses herpes simplex virus 1 gene expressionA single amino acid substitution in the cyclin D binding domain of the infected cell protein no. 0 abrogates the neuroinvasiveness of herpes simplex virus without affecting its ability to replicateUbiquitin-specific protease 9X in host cells interacts with herpes simplex virus 1 ICP0.The ubiquitin E3 ligase MARCH7 is differentially regulated by the deubiquitylating enzymes USP7 and USP9XComponents of nuclear domain 10 bodies regulate varicella-zoster virus replicationHSV-I and the cellular DNA damage response.Viral Ubiquitin Ligase Stimulates Selective Host MicroRNA Expression by Targeting ZEB Transcriptional Repressors.Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1.Cellular Protein WDR11 Interacts with Specific Herpes Simplex Virus Proteins at the trans-Golgi Network To Promote Virus Replication.Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation.
P2860
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P2860
The ability of herpes simplex virus type 1 immediate-early protein Vmw110 to bind to a ubiquitin-specific protease contributes to its roles in the activation of gene expression and stimulation of virus replication.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
The ability of herpes simplex ...... mulation of virus replication.
@en
The ability of herpes simplex ...... mulation of virus replication.
@nl
type
label
The ability of herpes simplex ...... mulation of virus replication.
@en
The ability of herpes simplex ...... mulation of virus replication.
@nl
prefLabel
The ability of herpes simplex ...... mulation of virus replication.
@en
The ability of herpes simplex ...... mulation of virus replication.
@nl
P2093
P2860
P1433
P1476
The ability of herpes simplex ...... imulation of virus replication
@en
P2093
P2860
P304
P407
P577
1999-01-01T00:00:00Z