Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.
about
MDA-5 recognition of a murine norovirusStructures of the compact helical core domains of feline calicivirus and murine norovirus VPg proteinsA 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 CrystallisationPathogenesis of noroviruses, emerging RNA virusesIn 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 genomeExpression 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 polymeraseCleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase.Interaction of recombinant norwalk virus particles with the 105-kilodalton cellular binding protein, a candidate receptor molecule for virus attachmentMapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.Open 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.Replication and packaging of Norwalk virus RNA in cultured mammalian cells.A norovirus protease structure provides insights into active and substrate binding site integrityDevelopment 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.The genome-linked protein VPg of the Norwalk virus binds eIF3, suggesting its role in translation initiation complex recruitmentSeneca Valley Virus 3Cpro Substrate Optimization Yields Efficient Substrates for Use in Peptide-Prodrug TherapyCalicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein.Coexistence of multiple genotypes, including newly identified genotypes, in outbreaks of gastroenteritis due to Norovirus in JapanRecovery 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 pathogenesisA single-amino-acid change in murine norovirus NS1/2 is sufficient for colonic tropism and persistence.A one-tube method of reverse transcription-PCR to efficiently amplify a 3-kilobase region from the RNA polymerase gene to the poly(A) tail of small round-structured viruses (Norwalk-like viruses)Norwalk virus N-terminal nonstructural protein is associated with disassembly of the Golgi complex in transfected cells.Molecular characterization of a bovine enteric calicivirus: relationship to the Norwalk-like viruses.Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies.Norwalk virus nonstructural protein p48 forms a complex with the SNARE regulator VAP-A and prevents cell surface expression of vesicular stomatitis virus G protein.
P2860
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P2860
Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.
description
1996 nî lūn-bûn
@nan
1996 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի ապրիլին 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
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@ast
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@en
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@nl
type
label
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@ast
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@en
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@nl
prefLabel
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@ast
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@en
Polyprotein processing in Sout ...... sites by in vitro mutagenesis.
@nl
P2860
P1433
P1476
Polyprotein processing in Sout ...... sites by in vitro mutagenesis
@en
P2093
P2860
P304
P407
P577
1996-04-01T00:00:00Z