Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies

Journal of Molecular Biology

Volumn 289, Issue 2, 1999, Pages 385-396

  Cicero, Daniel O ^a   Barbato, Gaetano ^a   Koch, Uwe ^a   Ingallinella, Paolo ^a   Bianchi, Elisabetta ^a   Nardi, M Chiara ^a   Steinkühler, Christian ^a   Cortese, Riccardo ^a   Matassa, Victor ^a   De Francesco, Raffaele ^a   Pessi, Antonello ^a   Bazzo, Renzo ^a  

^a IRBM   (Italy)

Author keywords

Binding; HCV; Inhibitors; NMR; NS3 proteinase

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; PEPTIDE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SOLVENT;

AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; ENZYME SUBSTRATE; HEPATITIS C VIRUS; LIGAND BINDING; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE IMAGING; PRIORITY JOURNAL;

HEPATITIS C VIRUS; RNA VIRUSES;

EID: 0033522926     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2746     Document Type: Article

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