Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28
about
Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Identification of a region in the herpes simplex virus scaffolding protein required for interaction with the portalA putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formationThe putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infectionDisulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.Direct visualization of the putative portal in the Kaposi's sarcoma-associated herpesvirus capsid by cryoelectron tomography.Characterization of the subcellular localization of herpes simplex virus type 1 proteins in living cells.Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1The 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.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.DNA methyltransferase DNMT3A associates with viral proteins and impacts HSV-1 infection.Reconstitution of the Kaposi's sarcoma-associated herpesvirus nuclear egress complex and formation of nuclear membrane vesicles by coexpression of ORF67 and ORF69 gene products.Putative terminase subunits of herpes simplex virus 1 form a complex in the cytoplasm and interact with portal protein in the nucleus.Intermolecular Complementation between Two Varicella-Zoster Virus pORF30 Terminase Domains Essential for DNA Encapsidation.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.Viral nanomotors for packaging of dsDNA and dsRNARole of a mutation in human cytomegalovirus gene UL104 in resistance to benzimidazole ribonucleosides.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.Development of Potent Antiviral Drugs Inspired by Viral Hexameric DNA-Packaging Motors with Revolving Mechanism.Human cytomegalovirus TRS1 protein is required for efficient assembly of DNA-containing capsids.Nuclear delivery mechanism of herpes simplex virus type 1 genome.A mutation in UL15 of herpes simplex virus 1 that reduces packaging of cleaved genomes.A physical link between the pseudorabies virus capsid and the nuclear egress complex.Herpesvirus Capsid Assembly and DNA Packaging.Varicella zoster virus ORF25 gene product: an essential hub protein linking encapsidation proteins and the nuclear egress complex.Interaction of the putative human cytomegalovirus portal protein pUL104 with the large terminase subunit pUL56 and its inhibition by benzimidazole-D-ribonucleosides.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.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.Genetic analysis of the vaccinia virus I6 telomere-binding protein uncovers a key role in genome encapsidation.Herpes simplex virus type 1 DNA-packaging protein UL17 is required for efficient binding of UL25 to capsids.Human Cytomegalovirus Nuclear Capsids Associate with the Core Nuclear Egress Complex and the Viral Protein Kinase pUL97.Structure of the herpes simplex virus portal-vertex
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P2860
Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28
description
2003 nî lūn-bûn
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2003 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@ast
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@en
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@nl
type
label
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@ast
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@en
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@nl
prefLabel
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@ast
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@en
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@nl
P2093
P2860
P1433
P1476
Herpes simplex virus type 1 po ...... rminase subunits UL15 and UL28
@en
P2093
Arvind H Patel
Colleen A White
Michelle Hughes
Nigel D Stow
Valerie G Preston
P2860
P304
P356
10.1128/JVI.77.11.6351-6358.2003
P407
P577
2003-06-01T00:00:00Z