Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli.
about
Crystal structure of norwalk virus polymerase reveals the carboxyl terminus in the active site cleftA Structural Study of Norovirus 3C Protease Specificity: Binding of a Designed Active Site-Directed Peptide InhibitorStructural Basis of Substrate Specificity and Protease Inhibition in Norwalk VirusStructure of a Murine Norovirus NS6 Protease-Product Complex Revealed by Adventitious CrystallisationNorovirus protein structure and function.In vitro proteolytic processing of the MD145 norovirus ORF1 nonstructural polyprotein yields stable precursors and products similar to those detected in calicivirus-infected cells.Processing map and essential cleavage sites of the nonstructural polyprotein encoded by ORF1 of the feline calicivirus genomeCharacterization of a rhesus monkey calicivirus representing a new genus of CaliciviridaeExpression of the murine norovirus (MNV) ORF1 polyprotein is sufficient to induce apoptosis in a virus-free cell model.Norovirus proteinase-polymerase and polymerase are both active forms of RNA-dependent RNA polymeraseInteraction of recombinant norwalk virus particles with the 105-kilodalton cellular binding protein, a candidate receptor molecule for virus attachmentOpen reading frame 1 of the Norwalk-like virus Camberwell: completion of sequence and expression in mammalian cellsProteinase-polymerase precursor as the active form of feline calicivirus RNA-dependent RNA polymerase.Polypeptide p41 of a Norwalk-like virus is a nucleic acid-independent nucleoside triphosphataseProteolytic processing of sapovirus ORF1 polyprotein.Organization and expression of calicivirus genes.Characterization and inhibition of norovirus proteases of genogroups I and II using a fluorescence resonance energy transfer assay.Development of a Gaussia luciferase-based human norovirus protease reporter system: cell type-specific profile of Norwalk virus protease precursors and evaluation of inhibitors.The p4-p2' amino acids surrounding human norovirus polyprotein cleavage sites define the core sequence regulating self-processing order.Plasmid-based human norovirus reverse genetics system produces reporter-tagged progeny virus containing infectious genomic RNA.Characterization of an enteropathogenic bovine calicivirus representing a potentially new calicivirus genus.Crystallization and preliminary X-ray diffraction analysis of the protease from Southampton norovirus complexed with a Michael acceptor inhibitor.Trans activity of the norovirus Camberwell proteinase and cleavage of the N-terminal protein encoded by ORF1.Cleavage map and proteolytic processing of the murine norovirus nonstructural polyprotein in infected cells.Phage-protease-peptide: a novel trifecta enabling multiplex detection of viable bacterial pathogensRecovery of infectious murine norovirus using pol II-driven expression of full-length cDNA.Highly conserved configuration of catalytic amino acid residues among calicivirus-encoded proteases.Murine noroviruses comprising a single genogroup exhibit biological diversity despite limited sequence divergence.Murine norovirus: a model system to study norovirus biology and pathogenesisSubstrate specificity of Tulane virus protease.A predominant role for Norwalk-like viruses as agents of epidemic gastroenteritis in Maryland nursing homes for the elderly.Poly(A)- and primer-independent RNA polymerase of NorovirusMurine norovirus, a recently discovered and highly prevalent viral agent of mice.Mutagenesis of tyrosine 24 in the VPg protein is lethal for feline calicivirus.Structural and functional characterization of sapovirus RNA-dependent RNA polymerase.Structure-based design and functional studies of novel noroviral 3C protease chimaeras offer insights into substrate specificity.Genome prediction of putative genome-linked viral protein (VPg) of astroviruses.Epidemiology of human Sapporo-like caliciviruses in the South West of England: molecular characterisation of a genetically distinct isolate.Cleavage activity of the sapovirus 3C-like protease in Escherichia coli.
P2860
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P2860
Identification of further proteolytic cleavage sites in the Southampton calicivirus polyprotein by expression of the viral protease in E. coli.
description
1999 nî lūn-bûn
@nan
1999 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Identification of further prot ...... the viral protease in E. coli.
@ast
Identification of further prot ...... the viral protease in E. coli.
@en
type
label
Identification of further prot ...... the viral protease in E. coli.
@ast
Identification of further prot ...... the viral protease in E. coli.
@en
prefLabel
Identification of further prot ...... the viral protease in E. coli.
@ast
Identification of further prot ...... the viral protease in E. coli.
@en
P2093
P1476
Identification of further prot ...... the viral protease in E. coli
@en
P2093
P304
P356
10.1099/0022-1317-80-2-291
P407
P478
80 ( Pt 2)
P577
1999-02-01T00:00:00Z