Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus.
about
A neurotropic herpesvirus infecting the gastropod, abalone, shares ancestry with oyster herpesvirus and a herpesvirus associated with the amphioxus genomeHerpesvirus capsid assembly: insights from structural analysis.The Structure of the Herpes Simplex Virus DNA-Packaging Terminase pUL15 Nuclease Domain Suggests an Evolutionary Lineage among Eukaryotic and Prokaryotic VirusesDisulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.Role of the UL25 protein in herpes simplex virus DNA encapsidationIsolation and characterization of the herpes simplex virus 1 terminase complex.Intermolecular Complementation between Two Varicella-Zoster Virus pORF30 Terminase Domains Essential for DNA Encapsidation.Vertex-Specific Proteins pUL17 and pUL25 Mechanically Reinforce Herpes Simplex Virus Capsids.Temperature-sensitive mutations in the putative herpes simplex virus type 1 terminase subunits pUL15 and pUL33 preclude viral DNA cleavage/packaging and interaction with pUL28 at the nonpermissive temperature.The human cytomegalovirus UL51 protein is essential for viral genome cleavage-packaging and interacts with the terminase subunits pUL56 and pUL89.Delivery of herpes simplex virus to retinal ganglion cell axon is dependent on viral protein Us9Domain within herpes simplex virus 1 scaffold proteins required for interaction with portal protein in infected cells and incorporation of the portal vertex into capsids.Divergent Evolution of Nuclear Localization Signal Sequences in Herpesvirus Terminase Subunits.The putative leucine zipper of the UL6-encoded portal protein of herpes simplex virus 1 is necessary for interaction with pUL15 and pUL28 and their association with capsids.The Varicella-zoster virus DNA encapsidation genes: Identification and characterization of the putative terminase subunits.Proline and tyrosine residues in scaffold proteins of herpes simplex virus 1 critical to the interaction with portal protein and its incorporation into capsids.Characterization of the Varicella-zoster virus ORF25 gene product: pORF25 interacts with multiple DNA encapsidation proteins.Tryptophan residues in the portal protein of herpes simplex virus 1 critical to the interaction with scaffold proteins and incorporation of the portal into capsids.Epstein-Barr virus BALF3 has nuclease activity and mediates mature virion production during the lytic cycle.Nuclear delivery mechanism of herpes simplex virus type 1 genome.DNA virus replication compartments.A mutation in UL15 of herpes simplex virus 1 that reduces packaging of cleaved genomes.A mutation in the DNA polymerase accessory factor of herpes simplex virus 1 restores viral DNA replication in the presence of raltegravir.An Epstein-Barr virus mutant produces immunogenic defective particles devoid of viral DNA.Herpesvirus Capsid Assembly and DNA Packaging.Release of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex.Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex.Effects of major capsid proteins, capsid assembly, and DNA cleavage/packaging on the pUL17/pUL25 complex of herpes simplex virus 1.Mutational analysis of the herpes simplex virus type 1 DNA packaging protein UL33.Characterization of pseudorabies virus (PrV) cleavage-encapsidation proteins and functional complementation of PrV pUL32 by the homologous protein of herpes simplex virus type 1.Comprehensive characterization of extracellular herpes simplex virus type 1 virions.The UL15 protein of herpes simplex virus type 1 is necessary for the localization of the UL28 and UL33 proteins to viral DNA replication centres.The essential human cytomegalovirus gene UL52 is required for cleavage-packaging of the viral genome.A Domain of Herpes Simplex Virus pUL33 Required To Release Monomeric Viral Genomes from Cleaved Concatemeric DNA.Targeting of viral capsids to nuclear pores in a cell-free reconstitution system.
P2860
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P2860
Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Putative terminase subunits of ...... portal protein in the nucleus.
@ast
Putative terminase subunits of ...... portal protein in the nucleus.
@en
type
label
Putative terminase subunits of ...... portal protein in the nucleus.
@ast
Putative terminase subunits of ...... portal protein in the nucleus.
@en
prefLabel
Putative terminase subunits of ...... portal protein in the nucleus.
@ast
Putative terminase subunits of ...... portal protein in the nucleus.
@en
P2093
P2860
P356
P1433
P1476
Putative terminase subunits of ...... portal protein in the nucleus.
@en
P2093
Joel D Baines
P2860
P304
P356
10.1128/JVI.00047-07
P407
P577
2007-03-28T00:00:00Z