Implications of the picornavirus capsid structure for polyprotein processing.
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Poliovirus cell entry: common structural themes in viral cell entry pathwaysA viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processingCell-Free Protein Synthesis: Pros and Cons of Prokaryotic and Eukaryotic SystemsThe structure and evolution of the major capsid protein of a large, lipid-containing DNA virus.Structures of the Procapsid and Mature Virion of Enterovirus 71 Strain 1095Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolutionChimeric rhinoviruses obtained via genetic engineering or artificially induced recombination are viable only if the polyprotein coding sequence derives from the same species.NMR structure of a viral peptide inserted in artificial membranes: a view on the early steps of the birnavirus entry processA second proteinase encoded by a plant potyvirus genome.Expression, purification and characterization of enterovirus-71 virus-like particles.Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and VP4.Reovirus polypeptide sigma 3 and N-terminal myristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cellsSUMOylation promotes PML degradation during encephalomyocarditis virus infection.Picornavirus morphogenesis.Capsid protein VP4 of poliovirus is N-myristoylated.Foot-and-mouth disease.Purification and partial characterization of poliovirus protease 2A by means of a functional assayPoliovirus polypeptide precursors: expression in vitro and processing by exogenous 3C and 2A proteinasesPotential secondary and tertiary structure in the genomic RNA of foot and mouth disease virus.Molecular epidemiology of coxsackievirus A16: intratype and prevalent intertype recombination identified.Seneca Valley Virus 3Cpro Substrate Optimization Yields Efficient Substrates for Use in Peptide-Prodrug TherapyIdentification of active-site residues in protease 3C of hepatitis A virus by site-directed mutagenesis.Biochemical and mutational analysis of a plant virus polyprotein cleavage site.Viral cell recognition and entry.Cleavage site analysis in picornaviral polyproteins: discovering cellular targets by neural networks.Complementation of a poliovirus defective genome by a recombinant vaccinia virus which provides poliovirus P1 capsid precursor in transPoliovirus capsid proteins derived from P1 precursors with glutamine-valine cleavage sites have defects in assembly and RNA encapsidation.Coinfection with recombinant vaccinia viruses expressing poliovirus P1 and P3 proteins results in polyprotein processing and formation of empty capsid structuresRole of maturation cleavage in infectivity of picornaviruses: activation of an infectosomeCatalysis of poliovirus VP0 maturation cleavage is not mediated by serine 10 of VP2Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells.Myristylation of poliovirus capsid precursor P1 is required for assembly of subviral particles.Proteolytic cleavage of encephalomyocarditis virus capsid region substrates by precursors to the 3C enzyme.Temperature-sensitive poliovirus mutant fails to cleave VP0 and accumulates provirions.Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles.Three poliovirus 2B mutants exhibit noncomplementable defects in viral RNA amplification and display dosage-dependent dominance over wild-type poliovirus.Mutations in VP1 of poliovirus specifically affect both encapsidation and release of viral RNA.A mutant poliovirus containing a novel proteolytic cleavage site in VP3 is altered in viral maturationInducible expression of encephalomyocarditis virus 3C protease activity in stably transformed mouse cell linesPoliovirus proteinase 3C: large-scale expression, purification, and specific cleavage activity on natural and synthetic substrates in vitro.
P2860
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P2860
Implications of the picornavirus capsid structure for polyprotein processing.
description
1987 nî lūn-bûn
@nan
1987 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Implications of the picornavirus capsid structure for polyprotein processing.
@ast
Implications of the picornavirus capsid structure for polyprotein processing.
@en
Implications of the picornavirus capsid structure for polyprotein processing.
@nl
type
label
Implications of the picornavirus capsid structure for polyprotein processing.
@ast
Implications of the picornavirus capsid structure for polyprotein processing.
@en
Implications of the picornavirus capsid structure for polyprotein processing.
@nl
prefLabel
Implications of the picornavirus capsid structure for polyprotein processing.
@ast
Implications of the picornavirus capsid structure for polyprotein processing.
@en
Implications of the picornavirus capsid structure for polyprotein processing.
@nl
P2093
P2860
P356
P1476
Implications of the picornavirus capsid structure for polyprotein processing.
@en
P2093
Nicklin MJ
Palmenberg AC
P2860
P356
10.1073/PNAS.84.1.21
P407
P577
1987-01-01T00:00:00Z