ArticleBioorganic & medicinal chemistry letters2014
UK-1 and structural analogs are potent inhibitors of hepatitis C virus replication.
Article in Bioorganic & medicinal chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Benzimidazole and Benzoxazole Zinc Chelators as Inhibitors of Metallo-β-Lactamase NDM-1.ChemMedChem · 2021Article
- Iodine-Catalyzed Functionalization of Primary Aliphatic Amines to Oxazoles, 1,4-Oxazines, and Oxazinones.ACS omega · 2019Article
- Exploring the biocombinatorial potential of benzoxazoles: generation of novel caboxamycin derivatives.Microbial cell factories · 2017Article
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Authors and funding
7 authors.
Funding
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.
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Registered trials
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