Herpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to its maturation.
about
Involvement of the portal at an early step in herpes simplex virus capsid assembly.Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formationBinding of pRNA to the N-terminal 14 amino acids of connector protein of bacteriophage phi29Proposed ancestors of phage nucleic acid packaging motors (and cells)The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid.Inhibition of herpes simplex virus replication by WAY-150138: assembly of capsids depleted of the portal and terminase proteins involved in DNA encapsidationThe putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infectionCondensed genome structure.Internal catalase protects herpes simplex virus from inactivation by hydrogen peroxide.Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton.Structure and capsid association of the herpesvirus large tegument protein UL36.Time-dependent transformation of the herpesvirus tegument.Murine cytomegalovirus capsid assembly is dependent on US22 family gene M140 in infected macrophagesRole of the UL25 protein in herpes simplex virus DNA encapsidationHerpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the verticesDynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus.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 infectionElectron tomography of nascent herpes simplex virus virionsVisualizing Herpesvirus Procapsids in Living CellsIsolation and preliminary characterization of herpes simplex virus 1 primary enveloped virions from the perinuclear spaceThe herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartmentsPackaging of genomic and amplicon DNA by the herpes simplex virus type 1 UL25-null mutant KUL25NSThree-dimensional structure of the bacteriophage P22 tail machine.Major capsid reinforcement by a minor protein in herpesviruses and phage.Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons.Structural characterization of the UL25 DNA-packaging protein from herpes simplex virus type 1Identification of small molecule compounds that selectively inhibit varicella-zoster virus replicationHuman cytomegalovirus terminase as a target for antiviral chemotherapy.Isolation and characterization of the herpes simplex virus 1 terminase complex.Dynamics of the T4 bacteriophage DNA packasome motor: endonuclease VII resolvase release of arrested Y-DNA substrates.Residues of the UL25 protein of herpes simplex virus that are required for its stable interaction with capsidsSelection of HSV capsids for envelopment involves interaction between capsid surface components pUL31, pUL17, and pUL25Linker 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.A hypothesis for bacteriophage DNA packaging motors.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.
P2860
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P2860
Herpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to its maturation.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Herpes simplex virus DNA cleav ...... apsid prior to its maturation.
@ast
Herpes simplex virus DNA cleav ...... apsid prior to its maturation.
@en
type
label
Herpes simplex virus DNA cleav ...... apsid prior to its maturation.
@ast
Herpes simplex virus DNA cleav ...... apsid prior to its maturation.
@en
prefLabel
Herpes simplex virus DNA cleav ...... apsid prior to its maturation.
@ast
Herpes simplex virus DNA cleav ...... apsid prior to its maturation.
@en
P2093
P2860
P1433
P1476
Herpes simplex virus DNA cleav ...... capsid prior to its maturation
@en
P2093
P2860
P304
P356
10.1128/JVI.75.2.687-698.2001
P577
2001-01-01T00:00:00Z