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• W2218944944 startingPage "95" @default.
• W2218944944 abstract "HCV NS5A has three domains, which have multiple roles in the viral life cycle. We previously found that NS5A is able to down-regulate HCV RNA translation through a mechanism requiring the polyU/UC region within the viral 3'UTR to which NS5A binds. In this study, we further investigated the role of domain I in modulating viral translation. Using a series of deletion and substitution mutants, we identified a number of positively charged residues that played a role in this modulatory effect, most prominently R112. The R112A mutation negated the ability of domain I and full-length NS5A to modulate viral translation. Additionally, the R112A mutation impeded domain I binding to the polyU/UC RNA, suggesting a mechanism for this down-regulatory effect. Finally, the R112A mutation rendered HCV replication deficient. These results collectively point to a crucial role for the R112 residue of NS5A in the modulation of HCV life cycle by NS5A." @default.
• W2218944944 created "2016-06-24" @default.
• W2218944944 creator A5037768610 @default.
• W2218944944 creator A5053351195 @default.
• W2218944944 creator A5079015988 @default.
• W2218944944 date "2015-09-01" @default.
• W2218944944 modified "2023-10-01" @default.
• W2218944944 title "Arginine 112 is involved in HCV translation modulation by NS5A domain I" @default.
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• W2218944944 doi "https://doi.org/10.1016/j.bbrc.2015.07.136" @default.
• W2218944944 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26235875" @default.
• W2218944944 hasPublicationYear "2015" @default.
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