PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
about
ICP0 dismantles microtubule networks in herpes simplex virus-infected cellsICP0 antagonizes ICP4-dependent silencing of the herpes simplex virus ICP0 genePML nuclear bodiesEBV tegument protein BNRF1 disrupts DAXX-ATRX to activate viral early gene transcriptionEvidence for a role of the cellular ND10 protein PML in mediating intrinsic immunity against human cytomegalovirus infectionsPML promotes MHC class II gene expression by stabilizing the class II transactivatorHuman cytomegalovirus infection causes degradation of Sp100 proteins that suppress viral gene expressionTRIM family proteins and their emerging roles in innate immunityRole of ND10 nuclear bodies in the chromatin repression of HSV-1Infected cell protein 0 functional domains and their coordination in herpes simplex virus replicationA comparison of herpes simplex virus type 1 and varicella-zoster virus latency and reactivationThe molecular basis of herpes simplex virus latencyThe 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 InfectionPhosphoproteomic analyses reveal signaling pathways that facilitate lytic gammaherpesvirus replication3D reconstruction of VZV infected cell nuclei and PML nuclear cages by serial section array scanning electron microscopy and electron tomographyIndependent and Cooperative Antiviral Actions of Beta Interferon and Gamma Interferon against Herpes Simplex Virus Replication in Primary Human FibroblastsThe Role of Nuclear Antiviral Factors against Invading DNA Viruses: The Immediate Fate of Incoming Viral GenomesA viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responsesHSV-1 ICP0: paving the way for viral replicationA viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defenceCellular promyelocytic leukemia protein is an important dengue virus restriction factorVaricella-zoster virus immediate-early protein ORF61 abrogates the IRF3-mediated innate immune response through degradation of activated IRF3Origin and diversification of TRIM ubiquitin ligases.Live cell dynamics of promyelocytic leukemia nuclear bodies upon entry into and exit from mitosis.BclAF1 restriction factor is neutralized by proteasomal degradation and microRNA repression during human cytomegalovirus infectionHerpesvirus tegument protein pUL37 interacts with dystonin/BPAG1 to promote capsid transport on microtubules during egress.Dystonin/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry.A proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection.Herpes Simplex Virus and Interferon Signaling Induce Novel Autophagic Clusters in Sensory NeuronsImmune Escape via a Transient Gene Expression Program Enables Productive Replication of a Latent Pathogen.Genome-wide screen of three herpesviruses for protein subcellular localization and alteration of PML nuclear bodiesFunctional connection between Rad51 and PML in homology-directed repair.Ataxin-1 fusion partners alter polyQ lethality and aggregation.A role for cytoplasmic PML in cellular resistance to viral infectionRole of chromatin during herpesvirus infections.Multiple functions for ORF75c in murid herpesvirus-4 infection.Murine 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 degradationStress induced nuclear granules form in response to accumulation of misfolded proteins in Caenorhabditis elegans.
P2860
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P2860
PML contributes to a cellular mechanism of repression of herpes simplex virus type 1 infection that is inactivated by ICP0
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
PML contributes to a cellular ...... on that is inactivated by ICP0
@ast
PML contributes to a cellular ...... on that is inactivated by ICP0
@en
PML contributes to a cellular ...... on that is inactivated by ICP0
@en-gb
PML contributes to a cellular ...... on that is inactivated by ICP0
@nl
type
label
PML contributes to a cellular ...... on that is inactivated by ICP0
@ast
PML contributes to a cellular ...... on that is inactivated by ICP0
@en
PML contributes to a cellular ...... on that is inactivated by ICP0
@en-gb
PML contributes to a cellular ...... on that is inactivated by ICP0
@nl
prefLabel
PML contributes to a cellular ...... on that is inactivated by ICP0
@ast
PML contributes to a cellular ...... on that is inactivated by ICP0
@en
PML contributes to a cellular ...... on that is inactivated by ICP0
@en-gb
PML contributes to a cellular ...... on that is inactivated by ICP0
@nl
P2093
P2860
P3181
P356
P1433
P1476
PML contributes to a cellular ...... on that is inactivated by ICP0
@en
P2093
Nina Tavalai
Peer Papior
Roger D Everett
Sabine Rechter
P2860
P304
P3181
P356
10.1128/JVI.00734-06
P407
P577
2006-08-01T00:00:00Z