Use of Ar+ plasma etching to localize structural proteins in the capsid of herpes simplex virus type 1.
about
Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids.The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growthAssembly 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.Liquid-crystalline, phage-like packing of encapsidated DNA in herpes simplex virusStructure of the herpes simplex virus capsid: effects of extraction with guanidine hydrochloride and partial reconstitution of extracted capsidsThree-dimensional structures of the A, B, and C capsids of rhesus monkey rhadinovirus: insights into gammaherpesvirus capsid assembly, maturation, and DNA packaging.Phenotype of the herpes simplex virus type 1 protease substrate ICP35 mutant virus.Induced extrusion of DNA from the capsid of herpes simplex virus type 1.Three-dimensional structures of maturable and abortive capsids of equine herpesvirus 1 from cryoelectron microscopy.Study of herpes simplex virus maturation during a synchronous wave of assemblyAssembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminusSeparate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsids.Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein.Release of the catalytic domain N(o) from the herpes simplex virus type 1 protease is required for viral growthThe C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsidsAssembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genesEvidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsidsFinding a needle in a haystack: detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of herpes simplex virus).Distinct monoclonal antibodies separately label the hexons or the pentons of herpes simplex virus capsid.ATP depletion blocks herpes simplex virus DNA packaging and capsid maturationATP-Dependent localization of the herpes simplex virus capsid protein VP26 to sites of procapsid maturation.Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: location of UL25 product in the capsid and demonstration that it binds DNA.Identification of a novel linear B-cell epitope in the UL26 and UL26.5 proteins of Duck Enteritis VirusInvestigation of the specificity of the herpes simplex virus type 1 protease by point mutagenesis of the autoproteolysis sites.Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins.The size and symmetry of B capsids of herpes simplex virus type 1 are determined by the gene products of the UL26 open reading frameMutations in herpes simplex virus type 1 genes encoding VP5 and VP23 abrogate capsid formation and cleavage of replicated DNA.Identification and characterization of the herpes simplex virus type 1 virion protein encoded by the UL35 open reading frame.Posttranslational modification and subcellular localization of the p12 capsid protein of herpes simplex virus type 1Proline and tyrosine residues in scaffold proteins of herpes simplex virus 1 critical to the interaction with portal protein and its incorporation into capsids.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.The bovine herpesvirus 1 maturational proteinase and scaffold proteins can substitute for the homologous herpes simplex virus type 1 proteins in the formation of hybrid type B capsids.Virus-specific interaction between the human cytomegalovirus major capsid protein and the C terminus of the assembly protein precursorAutoproteolysis of herpes simplex virus type 1 protease releases an active catalytic domain found in intermediate capsid particles.The complete sequence of the capsid p40 gene from infectious laryngotracheitis virus.
P2860
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P2860
Use of Ar+ plasma etching to localize structural proteins in the capsid of herpes simplex virus type 1.
description
1989 nî lūn-bûn
@nan
1989 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Use of Ar+ plasma etching to l ...... f herpes simplex virus type 1.
@ast
Use of Ar+ plasma etching to l ...... f herpes simplex virus type 1.
@en
type
label
Use of Ar+ plasma etching to l ...... f herpes simplex virus type 1.
@ast
Use of Ar+ plasma etching to l ...... f herpes simplex virus type 1.
@en
prefLabel
Use of Ar+ plasma etching to l ...... f herpes simplex virus type 1.
@ast
Use of Ar+ plasma etching to l ...... f herpes simplex virus type 1.
@en
P2860
P1433
P1476
Use of Ar+ plasma etching to l ...... of herpes simplex virus type 1
@en
P2093
W W Newcomb
P2860
P304
P577
1989-11-01T00:00:00Z