Ontology highlight
ABSTRACT:
SUBMITTER: Ward DN
PROVIDER: S-EPMC6136245 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Ward Dawn N DN Talley Daniel C DC Tavag Mrinalini M Menji Samrawit S Schaughency Paul P Baier Andrea A Smith Paul J PJ
Bioorganic & medicinal chemistry letters 20131209 2
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 NS ...[more]