Herpes simplex virus DNA cleavage and packaging: association of multiple forms of U(L)15-encoded proteins with B capsids requires at least the U(L)6, U(L)17, and U(L)28 genes.
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Novel class of thiourea compounds that inhibit herpes simplex virus type 1 DNA cleavage and encapsidation: resistance maps to the UL6 gene.A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formationThe Structure of the Herpes Simplex Virus DNA-Packaging Terminase pUL15 Nuclease Domain Suggests an Evolutionary Lineage among Eukaryotic and Prokaryotic VirusesIsolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid.Condensed genome structure.Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-Filled HSV-1 capsids.Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infectionHerpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to its maturation.Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsidsEngineering of the fluorescent-energy-conversion arm of phi29 DNA packaging motor for single-molecule studiesATP depletion blocks herpes simplex virus DNA packaging and capsid maturationInteraction domains of the UL16 and UL21 tegument proteins of herpes simplex virus.The herpes simplex virus type 1 U(L)17 gene encodes virion tegument proteins that are required for cleavage and packaging of viral DNA.Herpes simplex virus type 1 cleavage and packaging proteins UL15 and UL28 are associated with B but not C capsids during packaging.The effect of N- or C-terminal alterations of the connector of bacteriophage phi29 DNA packaging motor on procapsid assembly, pRNA binding, and DNA packagingHSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells.An early regulatory function required in a cell type-dependent manner is expressed by the genomic but not the cDNA copy of the herpes simplex virus 1 gene encoding infected cell protein 0.The putative terminase subunit of herpes simplex virus 1 encoded by UL28 is necessary and sufficient to mediate interaction between pUL15 and pUL33.Herpes simplex virus 1 DNA packaging proteins encoded by UL6, UL15, UL17, UL28, and UL33 are located on the external surface of the viral capsid.Robust properties of membrane-embedded connector channel of bacterial virus phi29 DNA packaging motor.Linker insertion mutations in the herpes simplex virus type 1 UL28 gene: effects on UL28 interaction with UL15 and UL33 and identification of a second-site mutation in the UL15 gene that suppresses a lethal UL28 mutation.Quantification of the DNA cleavage and packaging proteins U(L)15 and U(L)28 in A and B capsids of herpes simplex virus type 1.Role of channel lysines and the "push through a one-way valve" mechanism of the viral DNA packaging motor.Point mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging.Real-time sensing and discrimination of single chemicals using the channel of phi29 DNA packaging nanomotor.Procapsid assembly, maturation, nuclear exit: dynamic steps in the production of infectious herpesvirions.The C Terminus of the Herpes Simplex Virus UL25 Protein Is Required for Release of Viral Genomes from Capsids Bound to Nuclear Pores.Viral nanomotors for packaging of dsDNA and dsRNAThe Varicella-zoster virus DNA encapsidation genes: Identification and characterization of the putative terminase subunits.Herpesvirus Capsid Assembly and DNA Packaging.Physical and functional interactions between the herpes simplex virus UL15 and UL28 DNA cleavage and packaging proteins.Proteolytic cleavage of the amino terminus of the U(L)15 gene product of herpes simplex virus type 1 is coupled with maturation of viral DNA into unit-length genomesIdentification, subviral localization, and functional characterization of the pseudorabies virus UL17 protein.Single-molecule and FRET fluorescence correlation spectroscopy analyses of phage DNA packaging: colocalization of packaged phage T4 DNA ends within the capsid.Experimental Dissection of the Lytic Replication Cycles of Herpes Simplex Viruses
P2860
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P2860
Herpes simplex virus DNA cleavage and packaging: association of multiple forms of U(L)15-encoded proteins with B capsids requires at least the U(L)6, U(L)17, and U(L)28 genes.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@en
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@nl
type
label
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@en
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@nl
prefLabel
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@en
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@nl
P2860
P1433
P1476
Herpes simplex virus DNA cleav ...... L)6, U(L)17, and U(L)28 genes.
@en
P2093
P2860
P304
P407
P577
1998-04-01T00:00:00Z