Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation.
about
Flaviviral NS4b, chameleon and jack-in-the-box roles in viral replication and pathogenesis, and a molecular target for antiviral interventionThe DNA damage response induced by infection with human cytomegalovirus and other virusesA comparison of herpes simplex virus type 1 and varicella-zoster virus latency and reactivationAdenovirus Early Proteins and Host SumoylationKaposi's sarcoma-associated herpesvirus K-Rta exhibits SUMO-targeting ubiquitin ligase (STUbL) like activity and is essential for viral reactivationSpatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click ChemistryMurine gammaherpesvirus 68 ORF75c contains ubiquitin E3 ligase activity and requires PML SUMOylation but not other known cellular PML regulators, CK2 and E6AP, to mediate PML degradationThe chicken adenovirus Gam1 protein, an inhibitor of the sumoylation pathway, partially complements ICP0-null mutant herpes simplex virus 1Inhibition of HSV-1 Replication by Gene Editing StrategyA Phospho-SIM in the Antiviral Protein PML is Required for Its Recruitment to HSV-1 Genomes.Identification of TRIM27 as a novel degradation target of herpes simplex virus 1 ICP0.Assembly of Epstein-Barr Virus Capsid in Promyelocytic Leukemia Nuclear Bodies.Analysis of the SUMO2 Proteome during HSV-1 Infection.Identification of RNF168 as a PML nuclear body regulatorA quantitative assay to monitor HSV-1 ICP0 ubiquitin ligase activity in vitroThe replication defect of ICP0-null mutant herpes simplex virus 1 can be largely complemented by the combined activities of human cytomegalovirus proteins IE1 and pp71DNA sensing-independent inhibition of herpes simplex virus 1 replication by DAI/ZBP1Interaction of herpes simplex virus ICP0 with ND10 bodies: a sequential process of adhesion, fusion, and retentionTwo overlapping regions within the N-terminal half of the herpes simplex virus 1 E3 ubiquitin ligase ICP0 facilitate the degradation and dissociation of PML and dissociation of Sp100 from ND10.Sequences related to SUMO interaction motifs in herpes simplex virus 1 protein ICP0 act cooperatively to stimulate virus infectionRegulation of the tumor suppressor PML by sequential post-translational modifications.Differential Roles of PML Isoforms.Viral evasion mechanisms of early antiviral responses involving regulation of ubiquitin pathways.Viral Ubiquitin Ligase Stimulates Selective Host MicroRNA Expression by Targeting ZEB Transcriptional Repressors.A Tale of Two PMLs: Elements Regulating a Differential Substrate Recognition by the ICP0 E3 Ubiquitin Ligase of Herpes Simplex Virus 1.Novel Role for Protein Inhibitor of Activated STAT 4 (PIAS4) in the Restriction of Herpes Simplex Virus 1 by the Cellular Intrinsic Antiviral Immune Response.Analysis of the functional interchange between the IE1 and pp71 proteins of human cytomegalovirus and ICP0 of herpes simplex virus 1.Manipulation of ubiquitin/SUMO pathways in human herpesviruses infection.Diverse mechanisms evolved by DNA viruses to inhibit early host defenses.Herpes simplex virus type 1 virion-derived US11 inhibits type 1 interferon-induced protein kinase R phosphorylation.Components of promyelocytic leukemia nuclear bodies (ND10) act cooperatively to repress herpesvirus infection.Regulating STING in health and diseaseThe SP100 component of ND10 enhances accumulation of PML and suppresses replication and the assembly of HSV replication compartments.Viral Interplay with the Host Sumoylation System.Human Antiviral Protein IFIX Suppresses Viral Gene Expression during Herpes Simplex Virus 1 (HSV-1) Infection and Is Counteracted by Virus-induced Proteasomal Degradation.MORC3, a Component of PML Nuclear Bodies, Has a Role in Restricting Herpes Simplex Virus 1 and Human Cytomegalovirus.Regulation and function of phosphorylation on VP8, the major tegument protein of bovine herpesvirus 1.Identification of three redundant segments responsible for herpes simplex virus 1 ICP0 to fuse with ND10 nuclear bodiesThe viral ubiquitin ligase ICP0 is neither sufficient nor necessary for degradation of the cellular DNA sensor IFI16 during herpes simplex virus 1 infection.Gammaherpesviral Tegument Proteins, PML-Nuclear Bodies and the Ubiquitin-Proteasome System.
P2860
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P2860
Herpes simplex virus 1 ubiquitin ligase ICP0 interacts with PML isoform I and induces its SUMO-independent degradation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Herpes simplex virus 1 ubiquit ...... SUMO-independent degradation.
@en
Herpes simplex virus 1 ubiquit ...... SUMO-independent degradation.
@nl
type
label
Herpes simplex virus 1 ubiquit ...... SUMO-independent degradation.
@en
Herpes simplex virus 1 ubiquit ...... SUMO-independent degradation.
@nl
prefLabel
Herpes simplex virus 1 ubiquit ...... SUMO-independent degradation.
@en
Herpes simplex virus 1 ubiquit ...... SUMO-independent degradation.
@nl
P2093
P2860
P356
P1433
P1476
Herpes simplex virus 1 ubiquit ...... s SUMO-independent degradation
@en
P2093
Delphine Cuchet-Lourenço
Roger D Everett
P2860
P304
11209-11222
P356
10.1128/JVI.01145-12
P407
P577
2012-08-08T00:00:00Z