VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells.
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High-level expression of Marek's disease virus glycoprotein C is detrimental to virus growth in vitroDetermination of interactions between tegument proteins of herpes simplex virus type 1HCF-dependent nuclear import of VP16Tegument Assembly and Secondary Envelopment of AlphaherpesvirusesA comparison of herpes simplex virus type 1 and varicella-zoster virus latency and reactivationThe C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virusA proteomic perspective of inbuilt viral protein regulation: pUL46 tegument protein is targeted for degradation by ICP0 during herpes simplex virus type 1 infection.Identification and characterization of the pseudorabies virus tegument proteins UL46 and UL47: role for UL47 in virion morphogenesis in the cytoplasm.The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2)Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells.Anterograde transport of herpes simplex virus type 1 in cultured, dissociated human and rat dorsal root ganglion neurons.Evidence that herpes simplex virus VP16 is required for viral egress downstream of the initial envelopment event.A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells.Modified VP22 localizes to the cell nucleus during synchronized herpes simplex virus type 1 infection.Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 renders expression of the immediate-early genes almost entirely dependent on ICP0Tyrosine phosphorylation of bovine herpesvirus 1 tegument protein VP22 correlates with the incorporation of VP22 into virions.Virion association of IE62, the varicella-zoster virus (VZV) major transcriptional regulatory protein, requires expression of the VZV open reading frame 66 protein kinaseBovine herpesvirus 1 tegument protein VP22 interacts with histones, and the carboxyl terminus of VP22 is required for nuclear localization.Deletion of the herpes simplex virus VP22-encoding gene (UL49) alters the expression, localization, and virion incorporation of ICP0.Characterization of VP22 in herpes simplex virus-infected cells.Composition of pseudorabies virus particles lacking tegument protein US3, UL47, or UL49 or envelope glycoprotein E.Characterization of Marek's disease virus serotype 1 (MDV-1) deletion mutants that lack UL46 to UL49 genes: MDV-1 UL49, encoding VP22, is indispensable for virus growth.Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain.In rat dorsal root ganglion neurons, herpes simplex virus type 1 tegument forms in the cytoplasm of the cell bodySequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domainsA subpopulation of tegument protein vhs localizes to detergent-insoluble lipid rafts in herpes simplex virus-infected cells.Herpesvirus assembly and egressHerpes simplex virus type 1 accumulation, envelopment, and exit in growth cones and varicosities in mid-distal regions of axonsMembrane association of VP22, a herpes simplex virus type 1 tegument protein.Physical interaction between envelope glycoproteins E and M of pseudorabies virus and the major tegument protein UL49.Characterization of a UL49-null mutant: VP22 of herpes simplex virus type 1 facilitates viral spread in cultured cells and the mouse corneaEpstein-Barr virus BNRF1 protein allows efficient transfer from the endosomal compartment to the nucleus of primary B lymphocytes.Retrograde axonal transport of herpes simplex virus: evidence for a single mechanism and a role for tegumentInteraction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.Phosphorylation of the VP16 transcriptional activator protein during herpes simplex virus infection and mutational analysis of putative phosphorylation sites.Proteomic analysis of the herpes simplex virus 1 virion protein 16 transactivator protein in infected cellsCytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gDAnalysis of the interaction between the essential herpes simplex virus 1 tegument proteins VP16 and VP1/2.Truncation of the C-terminal acidic transcriptional activation domain of herpes simplex virus VP16 produces a phenotype similar to that of the in1814 linker insertion mutation.Interaction of herpes simplex virus RNase with VP16 and VP22 is required for the accumulation of the protein but not for accumulation of mRNA
P2860
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P2860
VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@ast
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@en
type
label
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@ast
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@en
prefLabel
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@ast
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@en
P2093
P2860
P1433
P1476
VP16 interacts via its activat ...... ssembly in coexpressing cells.
@en
P2093
P2860
P304
P407
P577
1995-12-01T00:00:00Z