| Literature DB >> 24360997 |
Dawn N Ward1, Daniel C Talley1, Mrinalini Tavag1, Samrawit Menji1, Paul Schaughency1, Andrea Baier2, Paul J Smith3.
Abstract
The bacterial natural product UK-1 and several structural analogs inhibit replication of the hepatitis C virus in the replicon assay, with IC50 values as low as 0.50 μM. The NS3 helicase has been identified as a possible target of inhibition for several of these compounds, while the remaining inhibitors act via an undetermined mechanism. Gel shift assays suggest that helicase inhibition is a direct result of inhibitor-enzyme binding as opposed to direct RNA binding, and the ATPase activity of NS3 is not affected. The syntheses and biological results are presented herein.Entities:
Keywords: Helicase; Hepatitis C; Inhibitor; NS3
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Year: 2013 PMID: 24360997 PMCID: PMC6136245 DOI: 10.1016/j.bmcl.2013.12.012
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN: 0960-894X Impact factor: 2.823