Structural and Biological Identification of Residues on the Surface of NS3 Helicase Required for Optimal Replication of the Hepatitis C Virus
Open Access
- 1 February 2006
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 281 (6) , 3528-3535
- https://doi.org/10.1074/jbc.m512100200
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- Structural biology of hepatitis C virusHepatology, 2004
- New therapies on the horizon for hepatitis C: are we close?Clinics in Liver Disease, 2003
- Hepatitis C virus biologyCell Death & Differentiation, 2003
- Hepatitis C therapeutics: current status and emerging strategiesNature Reviews Drug Discovery, 2002
- Oligomeric Interaction of Hepatitis C Virus NS5B Is Critical for Catalytic Activity of RNA-dependent RNA PolymeraseJournal of Biological Chemistry, 2002
- Efficient Initiation of HCV RNA Replication in Cell CultureScience, 2000
- Replication of Subgenomic Hepatitis C Virus RNAs in a Hepatoma Cell LineScience, 1999
- C-Terminal Domain of the Hepatitis C Virus NS3 Protein Contains an RNA Helicase ActivityBiochemical and Biophysical Research Communications, 1995
- Comparison of full-length sequences of interferon-sensitive and resistant hepatitis C virus 1b. Sensitivity to interferon is conferred by amino acid substitutions in the NS5A region.Journal of Clinical Investigation, 1995
- Nonstructural protein 3 of the hepatitis C virus encodes a serine-type proteinase required for cleavage at the NS3/4 and NS4/5 junctionsJournal of Virology, 1993