Protease required for processing picornaviral coat protein resides in the viral replicase gene.
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Molecular cloning of poliovirus cDNA and determination of the complete nucleotide sequence of the viral genomeThe Language of LifeNucleotide sequence of the 26S mRNA of Sindbis virus and deduced sequence of the encoded virus structural proteinsRapamycin and wortmannin enhance replication of a defective encephalomyocarditis virusPicornaviral VPg sequences are contained in the replicase precursor.Stimulation of encephalomyocarditis virus RNA translation in wheat embryo extracts by rabbit reticulocyte ribosomal washEncephalomyocarditis virus 3C protease: efficient cell-free expression from clones which link viral 5' noncoding sequences to the P3 region.Sequence and structural elements that contribute to efficient encephalomyocarditis virus RNA translationThe nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region.Purification and partial characterization of poliovirus protease 2A by means of a functional assayImplications of the picornavirus capsid structure for polyprotein processing.Two-dimensional electrophoretic analysis of encephalomyocarditis viral proteins.Poliovirus replication proteins: RNA sequence encoding P3-1b and the sites of proteolytic processing.Tandem mengovirus 5' pseudoknots are linked to viral RNA synthesis, not poly(C)-mediated virulenceBiologically active protease of foot and mouth disease virus is expressed from cloned viral cDNA in Escherichia coliProteolytic processing of poliovirus polypeptides: antibodies to polypeptide P3-7c inhibit cleavage at glutamine-glycine pairs.The structural polypeptides of aphthovirus are phosphoproteinsExpression, purification, and properties of recombinant encephalomyocarditis virus RNA-dependent RNA polymerase.Proteolytic cleavage of encephalomyocarditis virus capsid region substrates by precursors to the 3C enzyme.Limited expression of poliovirus by vaccinia virus recombinants due to inhibition of the vector by proteinase 2A.Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificityInducible expression of encephalomyocarditis virus 3C protease activity in stably transformed mouse cell linesCleavage of a viral polyprotein by a cellular proteolytic activity.Analysis of the complete nucleotide sequence of the picornavirus Theiler's murine encephalomyelitis virus indicates that it is closely related to cardiovirusesTrypsin sensitivity of the Sabin strain of type 1 poliovirus: cleavage sites in virions and related particlesAntibody to a synthetic nonapeptide corresponding to the NH2 terminus of poliovirus genome-linked protein VPg reacts with native VPg and inhibits in vitro replication of poliovirus RNAProteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts.Site-specific mutations at a picornavirus VP3/VP1 cleavage site disrupt in vitro processing and assembly of capsid precursorsAntibodies against a synthetic peptide of the poliovirus replicase protein: reaction with native, virus-encoded proteins and inhibition of virus-specific polymerase activities in vitroIn vitro synthesis and assembly of picornaviral capsid intermediate structures.Evidence for intramolecular self-cleavage of picornaviral replicase precursors.Identification of the polyprotein termination site on encephalomyocarditis viral RNA.Functional characterization of cleavage-defective mutants of encephalomyocarditis virus.Rapid method for the preparation of encephalomyocarditis virus protease from rabbit reticulocyte lysates.Enhancement of respiratory syncytial virus-induced cytopathology by trypsin, thrombin, and plasmin.Sequence analysis of three Sindbis virus mutants temperature-sensitive in the capsid protein autoprotease.Cell-free synthesis of encephalomyocarditis virus.Encephalomyocarditis viral RNA can be translated under conditions of poliovirus-induced translation shutoff in vivo.Internal translation initiation on poliovirus RNA: further characterization of La function in poliovirus translation in vitro.Intermolecular cleavage of hepatitis A virus (HAV) precursor protein P1-P2 by recombinant HAV proteinase 3C.
P2860
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P2860
Protease required for processing picornaviral coat protein resides in the viral replicase gene.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 1979
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Protease required for processi ...... s in the viral replicase gene.
@en
Protease required for processi ...... s in the viral replicase gene.
@nl
type
label
Protease required for processi ...... s in the viral replicase gene.
@en
Protease required for processi ...... s in the viral replicase gene.
@nl
prefLabel
Protease required for processi ...... s in the viral replicase gene.
@en
Protease required for processi ...... s in the viral replicase gene.
@nl
P2093
P2860
P1433
P1476
Protease required for processi ...... s in the viral replicase gene.
@en
P2093
Pallansch MA
Palmenberg AC
Rueckert RR
P2860
P304
P407
P577
1979-12-01T00:00:00Z