PMID 1537828. & Wigley, D. B. HCV encodes a viral RNA helicase, and recent findings have shown that HIV-1 adapts a cellular RNA helicase for its viral lifecycle. Marintcheva, B. Crystal structure of the RNA-dependent RNA polymerase from hepatitis C virus reveals a fully encircled active site. SARS-coronavirus-2 (SARS-CoV-2), the causative pathogen of COVID-19, is a positive-sense single-stranded RNA virus belonging to the family Coronaviridae. Gorbalenya, A. E. & Koonin, E. V. Helicases: amino acid sequence comparisons and structure–function relationships. Salonen, A., Ahola, T. & Kaariainen, L. Viral RNA replication in association with cellular membranes. "A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction". Yao, N. & Weber, P. C. Helicase, a target for novel inhibitors of hepatitis C virus. A., Fischer, R., Kleymann, G., Hendrix, M. & Rubsamen-Waigmann, H. Potent Liuzzi, M. et al. Kim, D. W., Kim, J., Gwack, Y., Han, J. H. & Choe, J. Mutational analysis of the hepatitis C Virus RNA Helicase. Expression and purification of a hepatitis C virus NS3/4A complex, and characterization of its helicase activity with the scintillation proximity assay system. Electrostatic analysis of the HCV helicase shows both active-site and non-active-site locationsOf all these potential assays, most laboratories have relied on a simple unwinding assay for primary HTS, such as a scintillation proximity assay (SPA)However, in most screenings the initial 'hits' or candidate inhibitors are usually not very potent (μM ICOf the three major HCV enzymatic targets for drug discovery, NS3 protease inhibitors have been the most successful to date. An in-depth description can be found in detailed physical and kinetic analyses of periodic cycles of RNA unwinding and pausing by HCV NS3 helicase, which have been investigated by several laboratoriesA separate category of potential inhibitors not depicted in The solution of the crystal structure of HCV helicase complexed with oligonucleotide, as well as mutagenesis studies, have identified key residues that are essential for enzyme activity or translocation of the RNA substrateIt is important to inhibit functions that are essential for helicase activity. Globally, HIV-1 infects more than 40 million individuals; HCV is estimated to have more than 170 million carriers. Jones, P. S. Strategies for antiviral drug discovery. Schmitt, C. et al. The RNA helicase, nucleotide 5′-triphosphatase, and RNA 5′-triphosphatase activities of dengue virus protein NS3 are Mg2+-dependent and require a functional Walker B motif in the helicase catalytic core. Crystal structure of a DExx box DNA helicase. Lin, C. & Kim, J. L. Structure-based mutagenesis study of hepatitis C virus NS3 helicase. Lam, A. M., Keeney, D. & Frick, D. N. Two novel conserved motifs in the hepatitis C virus NS3 protein critical for helicase action. Reesink, H. et al. Isolation of specific and high-affinity RNA aptamers against NS3 helicase domain of hepatitis C virus. Enzymatic characterization of hepatitis C virus NS3/4A complexes expressed in mammalian cells by using the herpes simplex virus amplicon system. Lesburg, C. A. et al. Construction, expression, and characterization of a novel fully activated recombinant single-chain hepatitis C virus protease. NM283 (Idenix) has provided proof of concept for active-site polymerase inhibitors with Because there are multiple mechanisms of action that could inhibit HCV helicase, many have been surprised at the meagre array of hits from helicase screens or focused chemical librariesIt is not hard to imagine that the development of HCV helicase inhibitors for clinical use has been slow because the enzyme is a moving target and undergoes significant transient conformational changes that require the coupling of NTP hydrolysis to unwindingSuperimposition of independent hepatitis C virus helicase structures.

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