Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
about
ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection.Visualization by live-cell microscopy of disruption of ND10 during herpes simplex virus type 1 infection.The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication.Recruitment of cellular recombination and repair proteins to sites of herpes simplex virus type 1 DNA replication is dependent on the composition of viral proteins within prereplicative sites and correlates with the induction of the DNA damage respoProteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8.Inhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein A and its accumulation at S-phase-specific sites of DNA damage during infection.Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection.Definition of herpes simplex virus type 1 helper activities for adeno-associated virus early replication eventsA dominant-negative herpesvirus protein inhibits intranuclear targeting of viral proteins: effects on DNA replication and late gene expression.Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection.The human cytomegalovirus IE2 and UL112-113 proteins accumulate in viral DNA replication compartments that initiate from the periphery of promyelocytic leukemia protein-associated nuclear bodies (PODs or ND10)Origin-independent assembly of Kaposi's sarcoma-associated herpesvirus DNA replication compartments in transient cotransfection assays and association with the ORF-K8 protein and cellular PML.Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments.Interwoven roles of cyclin D3 and cdk4 recruited by ICP0 and ICP4 in the expression of herpes simplex virus genesNuclear interferon-inducible protein 16 promotes silencing of herpesviral and transfected DNA.Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.Determination of minimum herpes simplex virus type 1 components necessary to localize transcriptionally active DNA to ND10.Conformational changes in the herpes simplex virus ICP8 DNA-binding protein coincident with assembly in viral replication structures.Live covisualization of competing adeno-associated virus and herpes simplex virus type 1 DNA replication: molecular mechanisms of interaction.Adeno-Associated Virus Type 2 Rep68 Can Bind to Consensus Rep-Binding Sites on the Herpes Simplex Virus 1 Genome.Mitotic transcription repression in vivo in the absence of nucleosomal chromatin condensation.Efficient nuclear export of herpes simplex virus 1 transcripts requires both RNA binding by ICP27 and ICP27 interaction with TAP/NXF1ICP0 enables and monitors the function of D cyclins in herpes simplex virus 1 infected cells.Polymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated.The 60-residue C-terminal region of the single-stranded DNA binding protein of herpes simplex virus type 1 is required for cooperative DNA binding.The absence of p53 during Human Cytomegalovirus infection leads to decreased UL53 expression, disrupting UL50 localization to the inner nuclear membrane, and thereby inhibiting capsid nuclear egress.HSV-1 remodels host telomeres to facilitate viral replication.Human cytomegalovirus virions differentially incorporate viral and host cell RNA during the assembly processThe 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.ND10 protein PML is recruited to herpes simplex virus type 1 prereplicative sites and replication compartments in the presence of viral DNA polymerase.Lytic but not latent replication of epstein-barr virus is associated with PML and induces sequential release of nuclear domain 10 proteins.Pocket protein p130/Rb2 is required for efficient herpes simplex virus type 1 gene expression and viral replication.Interaction with the Epstein-Barr virus helicase targets Zta to DNA replication compartments.The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents.Recruitment of herpes simplex virus type 1 transcriptional regulatory protein ICP4 into foci juxtaposed to ND10 in live, infected cells.Mutations of amino acids in the DNA-recognition domain of Epstein-Barr virus ZEBRA protein alter its sub-nuclear localization and affect formation of replication compartments.The SP100 component of ND10 enhances accumulation of PML and suppresses replication and the assembly of HSV replication compartments.ssDNA-dependent colocalization of adeno-associated virus Rep and herpes simplex virus ICP8 in nuclear replication domains.Identification and functional evaluation of cellular and viral factors involved in the alteration of nuclear architecture during herpes simplex virus 1 infection.
P2860
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P2860
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
1997年學術文章
@zh-hant
name
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@en
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@nl
type
label
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@en
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@nl
prefLabel
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@en
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@nl
P356
P1433
P1476
Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites.
@en
P2093
Uprichard SL
P304
P356
10.1006/VIRO.1996.8430
P407
P577
1997-03-01T00:00:00Z