Kinetic analysis of the effects of mutagenesis of W501 and V432 of the hepatitis C virus NS3 helicase domain on ATPase and strand-separating activity

Biochemistry

Volumn 39, Issue 17, 2000, Pages 5174-5183

  Preugschat, Frank ^a   Danger, Dana P ^a   Carter III, Luke H ^a   Davis, Roderick G ^a   Porter, David J T ^a  

^a GLAXOSMITHKLINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; HELICASE; MERCAPTOETHANOL;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME KINETICS; ENZYME MECHANISM; ENZYME MODIFICATION; ENZYME SUBSTRATE; HEPATITIS C VIRUS; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ADENOSINE TRIPHOSPHATASES; BINDING SITES; DNA; ENZYME ACTIVATION; HEPACIVIRUS; HUMANS; KINETICS; MUTAGENESIS, SITE-DIRECTED; SUBSTRATE SPECIFICITY; VIRAL NONSTRUCTURAL PROTEINS;

HEPATITIS C VIRUS; RNA VIRUSES;

EID: 0034595414     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9923860     Document Type: Article

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