Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation.
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Involvement of the portal at an early step in herpes simplex virus capsid assembly.Structure and polymorphism of the UL6 portal protein of herpes simplex virus type 1Herpesvirus capsid assembly: insights from structural analysis.Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids.Herpes simplex virus type 1 portal protein UL6 interacts with the putative terminase subunits UL15 and UL28Visualization of the herpes simplex virus portal in situ by cryo-electron tomographyVirus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity.Structure of the herpesvirus major capsid proteinP22 Coat Protein Structures Reveal a Novel Mechanism for Capsid Maturation: Stability without Auxiliary Proteins or Chemical CrosslinksThe Structure of the Herpes Simplex Virus DNA-Packaging Terminase pUL15 Nuclease Domain Suggests an Evolutionary Lineage among Eukaryotic and Prokaryotic VirusesThree-dimensional visualization of gammaherpesvirus life cycle in host cells by electron tomography.Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins.Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.Lytic replication of Kaposi's sarcoma-associated herpesvirus results in the formation of multiple capsid species: isolation and molecular characterization of A, B, and C capsids from a gammaherpesvirus.Inhibition of herpes simplex virus replication by WAY-150138: assembly of capsids depleted of the portal and terminase proteins involved in DNA encapsidationDisulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Cryo-electron tomography of Kaposi's sarcoma-associated herpesvirus capsids reveals dynamic scaffolding structures essential to capsid assembly and maturationHerpes 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.Three-dimensional structures of the A, B, and C capsids of rhesus monkey rhadinovirus: insights into gammaherpesvirus capsid assembly, maturation, and DNA packaging.Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminusHandedness of the herpes simplex virus capsid and procapsidFunction of dynein and dynactin in herpes simplex virus capsid transport.The product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA.Capsid structure of Kaposi's sarcoma-associated herpesvirus, a gammaherpesvirus, compared to those of an alphaherpesvirus, herpes simplex virus type 1, and a betaherpesvirus, cytomegalovirusHerpes 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 capsidsAssembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid.The herpes simplex virus type 1 cleavage/packaging protein, UL32, is involved in efficient localization of capsids to replication compartmentsElectron tomography of nascent herpes simplex virus virionsVisualizing Herpesvirus Procapsids in Living CellsThe herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartmentsThe 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)ATP depletion blocks herpes simplex virus DNA packaging and capsid maturationCapsid structure of simian cytomegalovirus from cryoelectron microscopy: evidence for tegument attachment sites.Capsid assembly and DNA packaging in 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 herpes simplex virus triplex protein, VP23, exists as a molten globule.
P2860
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P2860
Assembly of the herpes simplex virus capsid: characterization of intermediates observed during cell-free capsid formation.
description
1996 nî lūn-bûn
@nan
1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@ast
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@en
type
label
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@ast
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@en
prefLabel
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@ast
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@en
P2093
P356
P1476
Assembly of the herpes simplex ...... ng cell-free capsid formation.
@en
P2093
Newcomb WW
Spencer JV
Thomsen DR
P304
P356
10.1006/JMBI.1996.0587
P407
P577
1996-11-01T00:00:00Z