{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["1(9)"],"submitter":["Cheng CC"],"pubmed_abstract":["Pyridine carboxamide-based inhibitors of the hepatitis C virus (HCV) NS5B polymerase were diversified and optimized to a variety of topologically related scaffolds. In particular, the 2-methyl nicotinic acid scaffold was developed into inhibitors with improved biochemical (IC50-GT1b = 0.014 μM) and cell-based HCV replicon potency (EC50-GT1b = 0.7 μM). Biophysical and biochemical characterization identified this novel series of compounds as palm site binders to HCV polymerase."],"journal":["ACS medicinal chemistry letters"],"pagination":["466-71"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4007899"],"repository":["biostudies-literature"],"pubmed_title":["Pyridine Carboxamides: Potent Palm Site Inhibitors of HCV NS5B Polymerase."],"pmcid":["PMC4007899"],"pubmed_authors":["Agrawal S","Wyss DF","Soucy KA","Jiang CK","He Z","Wang YS","Ferrari E","Huang X","Shipps GW","Cheng CC","Huang HC"],"additional_accession":[]},"is_claimable":false,"name":"Pyridine Carboxamides: Potent Palm Site Inhibitors of HCV NS5B Polymerase.","description":"Pyridine carboxamide-based inhibitors of the hepatitis C virus (HCV) NS5B polymerase were diversified and optimized to a variety of topologically related scaffolds. In particular, the 2-methyl nicotinic acid scaffold was developed into inhibitors with improved biochemical (IC50-GT1b = 0.014 μM) and cell-based HCV replicon potency (EC50-GT1b = 0.7 μM). Biophysical and biochemical characterization identified this novel series of compounds as palm site binders to HCV polymerase.","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Dec","modification":"2025-04-05T10:37:29.912Z","creation":"2019-03-27T01:27:30Z"},"accession":"S-EPMC4007899","cross_references":{"pubmed":["24900232"],"doi":["10.1021/ml100128h"]}}