Biochemical properties of a minimal functional domain with ATP-binding activity of the NTPase/helicase of hepatitis C virus

European Journal of Biochemistry

Volumn 266, Issue 3, 1999, Pages 715-723

  Borowski, Peter ^a   Kuehl, Reinhard ^a   Mueller, Oliver ^a   Hwang, Lih Hwa ^b   Zur Wiesch, Julian Schulze ^a   Schmitz, Herbert ^a  

^a BERNHARD NOCHT INSTITUTE FOR TROPICAL MEDICINE   (Germany)

^b NATIONAL TAIWAN UNIVERSITY HOSPITAL   (Taiwan)

Author keywords

ATP binding domain; Helicase; Hepatitus C virus (HCV); Inhibition

Indexed keywords

ADENOSINE TRIPHOSPHATE; HELICASE; NUCLEOSIDE TRIPHOSPHATASE; PACLITAXEL; POLYNUCLEOTIDE; TRIFLUOPERAZINE; VIRUS ENZYME;

AMINO ACID SEQUENCE; ARTICLE; BINDING COMPETITION; BINDING KINETICS; BINDING SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INHIBITION; ENZYME PURIFICATION; HEPATITIS C VIRUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN;

ACID ANHYDRIDE HYDROLASES; ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BINDING SITES; HEPACIVIRUS; KINETICS; NUCLEOSIDE-TRIPHOSPHATASE; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, TERTIARY; RNA HELICASES;

EID: 0033572798     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00854.x     Document Type: Article

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