Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates.
about
The Cys-rich region of hepatitis A virus cellular receptor 1 is required for binding of hepatitis A virus and protective monoclonal antibody 190/4Broad-spectrum antivirals against 3C or 3C-like proteases of picornaviruses, noroviruses, and coronaviruses.The refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognitionCharacterization of replication-competent hepatitis A virus constructs containing insertions at the N terminus of the polyproteinInteraction of poly(rC) binding protein 2 with the 5' noncoding region of hepatitis A virus RNA and its effects on translation.Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus.Maturation of the hepatitis A virus capsid protein VP1 is not dependent on processing by the 3Cpro proteinase.Characterization of recombinant hepatitis A virus genomes containing exogenous sequences at the 2A/2B junction.Hepatitis A virus 3C protease cleaves NEMO to impair induction of beta interferonAnalysis of deletion mutants indicates that the 2A polypeptide of hepatitis A virus participates in virion morphogenesis.Genome and infection characteristics of human parechovirus type 1: the interplay between viral infection and type I interferon antiviral systemHepatitis A viruses with deletions in the 2A gene are infectious in cultured cells and marmosets.Potent inhibition of enterovirus D68 and human rhinoviruses by dipeptidyl aldehydes and α-ketoamides.Hepatitis A virus (HAV) packaging size limitProcessing of proteinase precursors and their effect on hepatitis A virus particle formation.Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC.Genetic map of the calicivirus rabbit hemorrhagic disease virus as deduced from in vitro translation studies.Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1.Poly(A) binding protein, C-terminally truncated by the hepatitis A virus proteinase 3C, inhibits viral translation.Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization.Full-length genome of wild-type hepatitis A virus (DL3) isolated in China
P2860
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P2860
Cleavage specificity of purified recombinant hepatitis A virus 3C proteinase on natural substrates.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Cleavage specificity of purifi ...... teinase on natural substrates.
@en
Cleavage specificity of purifi ...... teinase on natural substrates.
@nl
type
label
Cleavage specificity of purifi ...... teinase on natural substrates.
@en
Cleavage specificity of purifi ...... teinase on natural substrates.
@nl
prefLabel
Cleavage specificity of purifi ...... teinase on natural substrates.
@en
Cleavage specificity of purifi ...... teinase on natural substrates.
@nl
P2093
P2860
P1433
P1476
Cleavage specificity of purifi ...... oteinase on natural substrates
@en
P2093
Gauss-Müller V
Schultheiss T
Sommergruber W
P2860
P304
P407
P577
1995-03-01T00:00:00Z