Picornavirus protein processing--enzymes, substrates, and genetic regulation.
about
Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypesStructure-based design, synthesis, and biological evaluation of peptidomimetic SARS-CoV 3CLpro inhibitorsSimple in vitro translation assay to analyze inhibitors of rhinovirus proteasesMouse hepatitis virus 3C-like protease cleaves a 22-kilodalton protein from the open reading frame 1a polyprotein in virus-infected cells and in vitro.Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase.Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.Requirements for RNA replication of a poliovirus replicon by coxsackievirus B3 RNA polymerase.2A protease is not a prerequisite for poliovirus replication.Polyprotein processing in cis and in trans by hepatitis A virus 3C protease cloned and expressed in Escherichia coliPoliovirus CRE-dependent VPg uridylylation is required for positive-strand RNA synthesis but not for negative-strand RNA synthesisCapsid coding sequence is required for efficient replication of human rhinovirus 14 RNAInhibition of host cell transcription by poliovirus: cleavage of transcription factor CREB by poliovirus-encoded protease 3Cpro.Cleavage site analysis in picornaviral polyproteins: discovering cellular targets by neural networks.Transduction of a human RNA sequence by poliovirustrans processing of vaccinia virus core proteins.Direct cleavage of human TATA-binding protein by poliovirus protease 3C in vivo and in vitro.Proteolytic activity of hepatitis A virus 3C proteincis-acting lesions targeted to the hydrophobic domain of a poliovirus membrane protein involved in RNA replication.cis- and trans-cleavage activities of poliovirus 2A protease expressed in Escherichia coli.Role for the P4 amino acid residue in substrate utilization by the poliovirus 3CD proteinase.Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymesA rapid method for determination of endoproteinase substrate specificity: specificity of the 3C proteinase from hepatitis A virus.Protease inhibitors as antiviral agents.Translation of polioviral mRNA is inhibited by cleavage of polypyrimidine tract-binding proteins executed by polioviral 3C(pro)The antiviral compound enviroxime targets the 3A coding region of rhinovirus and poliovirus.A new cis-acting element for RNA replication within the 5' noncoding region of poliovirus type 1 RNA.Identification of the cleavage site and determinants required for poliovirus 3CPro-catalyzed cleavage of human TATA-binding transcription factor TBP.Temperature-sensitive mouse cell factors for strand-specific initiation of poliovirus RNA synthesis.Mutational analysis of the proposed FG loop of poliovirus proteinase 3C identifies amino acids that are necessary for 3CD cleavage and might be determinants of a function distinct from proteolytic activity.Separation of native and truncated forms of poliovirus protease 3C produced in Escherichia coli.
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Picornavirus protein processing--enzymes, substrates, and genetic regulation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1990
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@en
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@nl
type
label
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@en
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@nl
prefLabel
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@en
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@nl
P1476
Picornavirus protein processing--enzymes, substrates, and genetic regulation.
@en
P2093
B L Semler
M A Lawson
P577
1990-01-01T00:00:00Z