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Biochemical and structural characterization of hepatitis A virus 2C reveals an unusual ribonuclease activity on single-stranded RNA.
Title: Biochemical and structural characterization of hepatitis A virus 2C reveals an unusual ribonuclease activity on single-stranded RNA.
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Study shows the critical role of the HAV capsid codon composition in regulating translation and determining its robustness [capsid protein]
Title: The Critical Role of Codon Composition on the Translation Efficiency Robustness of the Hepatitis A Virus Capsid.
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crystals of protein 2AB belonged to space group P4(1) or P4(3), with unit-cell parameters a = b = 90.42, c = 73.43 A, and contained two molecules in the asymmetric unit[protein 2A, protein 2B ]
Title: Cloning, purification and preliminary crystallographic studies of the 2AB protein from hepatitis A virus.
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The combined results suggest that 3C-mediated cleavage of PTB might be involved in down-regulation of viral translation to give way to subsequent viral genome replication.[3C]
Title: Hepatitis A virus (HAV) proteinase 3C inhibits HAV IRES-dependent translation and cleaves the polypyrimidine tract-binding protein.
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The expression of HAV cellular receptor, cr-1 on CD4 T cells correlated significantly with the antibody responses and cytokine levels.[cr-1]
Title: Correlation between humoral and cellular immune responses and the expression of the hepatitis A receptor HAVcr-1 on T cells after hepatitis A re-vaccination in high and low-responder vaccinees.
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there seemed to be more mutations in the strains obtained from fulminant hepatitis and acute hepatitis (AH) patients than in those obtained from AH patients in the central part of HAV 2B [HA virus protein 2b]
Title: Analysis of hepatitis A virus protein 2B in sera of hepatitis A of various severities.
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Hepatitis A virus (HAV), a hepatotropic picornavirus, ablates type 1 interferon responses by targeting the 3ABC precursor of its 3C(pro) cysteine protease to mitochondria where it colocalizes with and cleaves MAVS.[3ABC]
Title: Disruption of innate immunity due to mitochondrial targeting of a picornaviral protease precursor.
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Study reports the crystal and molecular structures of the 3C proteinase and provides insight into the mechanisms underlying the proteolysis of natural substrates by this viral cysteine peptidase.
Title: An episulfide cation (thiiranium ring) trapped in the active site of HAV 3C proteinase inactivated by peptide-based ketone inhibitors.