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• W2107739206 abstract "The flavivirus NS2B/NS3 protease has received considerable attention as a target for the development of antiviral compounds. While substrate based inhibitors have been the primary focus to date, an approach focussing on NS2B cofactor displacement could prove to be an effective alternative. To understand better the role of the NS2B cofactor in protease activation, we conducted an alanine mutagenesis screen throughout the 42-residue central cofactor domain (NS2B 51–92 ) of West Nile virus (WNV). Two sites critical for proteolytic activity were identified (NS2B 59–62 and NS2B 75–87 ), where the majority of substitutions were found to significantly decrease proteolytic activity of a recombinant WNV NS2B/NS3 protease. These findings provide mechanistic insights into the structural and functional role that the cofactor may play in the substrate-bound and free protease complexes as well as providing novel sites for targeting new antiviral inhibitors." @default.
• W2107739206 created "2016-06-24" @default.
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• W2107739206 date "2008-04-01" @default.
• W2107739206 modified "2023-09-26" @default.
• W2107739206 title "Mutagenesis of the West Nile virus NS2B cofactor domain reveals two regions essential for protease activity" @default.
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• W2107739206 doi "https://doi.org/10.1099/vir.0.83447-0" @default.
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