Inhibition of the hepatitis C virus helicase-associated ATPase activity by the combination of ADP, NaF, MgCl2, and poly(rU). Two ADP binding sites on the enzyme-nucleic acid complex.

Porter, D J

Inhibition of the hepatitis C virus helicase-associated ATPase activity by the combination of ADP, NaF, MgCl2, and poly(rU). Two ADP binding sites on the enzyme-nucleic acid complex. [electronic resource] - The Journal of biological chemistry Mar 1998 - 7390-6 p. digital

Publication Type: Journal Article

0021-9258

10.1074/jbc.273.13.7390 doi


Adenosine Diphosphate--metabolism
Adenosine Triphosphatases--antagonists & inhibitors
Aluminum--metabolism
Animals
Beryllium--metabolism
Binding Sites
Binding, Competitive
Deferoxamine--metabolism
Hepacivirus--enzymology
Kinetics
Macromolecular Substances
Magnesium Chloride--metabolism
Poly U--metabolism
Pyruvate Kinase--metabolism
Rabbits
Sodium Fluoride--metabolism
Viral Nonstructural Proteins--antagonists & inhibitors