Structure and function of hepatitis C virus NS3 helicase

Current Topics in Microbiology and Immunology

Volumn 242, Issue , 2000, Pages 171-196

  Kwong, A D ^a   Kim, J L ^a  

^a VERTEX PHARMACEUTICALS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; VIRUS ENZYME;

AMINO ACID SEQUENCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; ENZYME STRUCTURE; HEPATITIS C VIRUS; NONHUMAN; PRIORITY JOURNAL; REVIEW; SITE DIRECTED MUTAGENESIS; VIRUS GENOME;

HEPATITIS C VIRUS;

EID: 0033992576     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-642-59605-6_9     Document Type: Review

References (4)

1. Bartenschlager R (1997) Candidate targets for hepatitis C virus-specific antiviral therapy. Intervirology 40:378-393
2. Bartenschlager R, Lohmann V, Wilkinson T, Koch JO (1995) Complex formation between the NS3 Serine-type proteinase of the hepatitis C virus and NS4A and its importance for polyprotein maturation. J Virol 69:7519-7528
3. Bayliss CD, Smith GL (1996) Vaccinia virion protein 18R has both DNA and RNA helicase activities implications for vaccinia virus transcription. J Virol 70:794-800
4. Bilderback T, Fulmer T, Mantulin WW, Glaser M (1996) Substrate binding causes movement in the ATP binding domain of Escherichia coli adenylate kinase. Biochemistry 35:6100-6106