Varicella-zoster virus immediate-early 63 protein interacts with human antisilencing function 1 protein and alters its ability to bind histones h3.1 and h3.3.
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Herpes simplex virus and varicella zoster virus, the house guests who never leaveA comparison of herpes simplex virus type 1 and varicella-zoster virus latency and reactivationVaricella zoster virus infection of human fetal lung cells alters mitochondrial morphologyVaricella-zosterIdentification of phosphorylated residues on varicella-zoster virus immediate-early protein ORF63.Varicella-zoster virus transcriptome in latently infected human ganglia.Simian varicella virus open reading frame 63/70 expression is required for efficient virus replication in cultureDynamic association of gammaherpesvirus DNA with core histone during de novo lytic infection of primary cells.An in vitro model of latency and reactivation of varicella zoster virus in human stem cell-derived neuronsIdentification of small molecules that inhibit the histone chaperone Asf1 and its chromatin functionVaricella zoster virus (VZV) infects and establishes latency in enteric neuronsRecombinant monoclonal antibody recognizes a unique epitope on varicella-zoster virus immediate-early 63 protein.The varicella-zoster virus genomeActivation of H2AX and ATM in varicella-zoster virus (VZV)-infected cells is associated with expression of specific VZV genesRegulation of the ORF61 promoter and ORF61 functions in varicella-zoster virus replication and pathogenesisPhosphorylation of the nuclear form of varicella-zoster virus immediate-early protein 63 by casein kinase II at serine 186.Varicella zoster virus-induced pain and post-herpetic neuralgia in the human host and in rodent animal models.Pathogens hijack the epigenome: a new twist on host-pathogen interactions.Varicella zoster virus infection.Chromatin assembly on herpes simplex virus 1 DNA early during a lytic infection is Asf1a dependent.
P2860
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P2860
Varicella-zoster virus immediate-early 63 protein interacts with human antisilencing function 1 protein and alters its ability to bind histones h3.1 and h3.3.
description
article científic
@ca
article scientifique
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articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 29 October 2008
@en
vedecký článok
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vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@en
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@nl
type
label
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@en
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@nl
prefLabel
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@en
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@nl
P2093
P2860
P356
P1433
P1476
Varicella-zoster virus immedia ...... o bind histones h3.1 and h3.3.
@en
P2093
Aruna P Ambagala
Jason J Chen
Jeffrey I Cohen
Maxim Poustovoitov
Michael D Gershon
Peter D Adams
Trent Bosma
P2860
P304
P356
10.1128/JVI.00645-08
P407
P577
2008-10-29T00:00:00Z