Ontology highlight
ABSTRACT:
SUBMITTER: Matthew AN
PROVIDER: S-EPMC6260965 | biostudies-literature | 2018 Oct
REPOSITORIES: biostudies-literature
Matthew Ashley N AN Leidner Florian F Newton Alicia A Petropoulos Christos J CJ Huang Wei W Ali Akbar A KurtYilmaz Nese N Schiffer Celia A CA
Structure (London, England : 1993) 20180823 10
Despite significant progress in hepatitis C virus (HCV) protease inhibitor (PI) drug design, resistance remains a problem causing treatment failure. Double-substitution variants, notably Y56H/D168A, have emerged in patients who fail therapy with a PI-containing regimen. The resistance conferred by Asp168 substitutions has been well characterized and avoided in newer inhibitors. However, an additional mutation at Tyr56 confers resistance to even the most robust inhibitors. Here, we elucidate the ...[more]