The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
about
Virion assembly factories in the nucleus of polyomavirus-infected cellsEBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcriptionPML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0Evidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infectionsDifferential role of Sp100 isoforms in interferon-mediated repression of herpes simplex virus type 1 immediate-early protein expressionUS11 of herpes simplex virus type 1 interacts with HIPK2 and antagonizes HIPK2-induced cell growth arrestHuman cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expressionViral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruptionProteasome-independent disruption of PML oncogenic domains (PODs), but not covalent modification by SUMO-1, is required for human cytomegalovirus immediate-early protein IE1 to inhibit PML-mediated transcriptional repression.Epstein-barr virus immediate-early protein BZLF1 is SUMO-1 modified and disrupts promyelocytic leukemia bodiesInactivating a cellular intrinsic immune defense mediated by Daxx is the mechanism through which the human cytomegalovirus pp71 protein stimulates viral immediate-early gene expressionThe Epstein-Barr virus replication protein BBLF2/3 provides an origin-tethering function through interaction with the zinc finger DNA binding protein ZBRK1 and the KAP-1 corepressorEpstein-Barr virus (EBV) SM protein induces and recruits cellular Sp110b to stabilize mRNAs and enhance EBV lytic gene expressionAbility of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cellsFormation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexesThe 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 ICP0SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damageFunctional inaccessibility of quiescent herpes simplex virus genomesRole of ND10 nuclear bodies in the chromatin repression of HSV-1Infected cell protein 0 functional domains and their coordination in herpes simplex virus replicationThe potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1An Adenovirus DNA Replication Factor, but Not Incoming Genome Complexes, Targets PML Nuclear Bodies.Dynamic Response of IFI16 and Promyelocytic Leukemia Nuclear Body Components to Herpes Simplex Virus 1 InfectionA viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responsesHSV-1 ICP0: paving the way for viral replicationRole of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradationA viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defenceCrystal Structure of USP7 Ubiquitin-like Domains with an ICP0 Peptide Reveals a Novel Mechanism Used by Viral and Cellular Proteins to Target USP7Spatial and Temporal Resolution of Global Protein Synthesis during HSV Infection Using Bioorthogonal Precursors and Click ChemistryNuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infectionVisualization by live-cell microscopy of disruption of ND10 during herpes simplex virus type 1 infection.Genome-wide screen of three herpesviruses for protein subcellular localization and alteration of PML nuclear bodiesImplication of the lymphocyte-specific nuclear body protein Sp140 in an innate response to human immunodeficiency virus type 1.A role for cytoplasmic PML in cellular resistance to viral infectionRole of chromatin during herpesvirus infections.Epstein-Barr nuclear antigen 1 contributes to nasopharyngeal carcinoma through disruption of PML nuclear bodies.Cellular localization of the herpes simplex virus ICP0 protein dictates its ability to block IRF3-mediated innate immune responsesMurine 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 degradation
P2860
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P2860
The disruption of ND10 during herpes simplex virus infection correlates with the Vmw110- and proteasome-dependent loss of several PML isoforms
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The disruption of ND10 during ...... t loss of several PML isoforms
@ast
The disruption of ND10 during ...... t loss of several PML isoforms
@en
type
label
The disruption of ND10 during ...... t loss of several PML isoforms
@ast
The disruption of ND10 during ...... t loss of several PML isoforms
@en
prefLabel
The disruption of ND10 during ...... t loss of several PML isoforms
@ast
The disruption of ND10 during ...... t loss of several PML isoforms
@en
P2093
P2860
P1433
P1476
The disruption of ND10 during ...... t loss of several PML isoforms
@en
P2093
J Parkinson
M Kathoria
P Freemont
R D Everett
P2860
P304
P577
1998-08-01T00:00:00Z