The conformation of hepatitis C virus NS3 proteinase with and without NS4A: a structural basis for the activation of the enzyme by its cofactor
- 1 July 1998
- journal article
- Published by Elsevier in Clinical and Diagnostic Virology
- Vol. 10 (2-3) , 151-156
- https://doi.org/10.1016/s0928-0197(98)00036-1
Abstract
No abstract availableKeywords
This publication has 5 references indexed in Scilit:
- Molecular Targets in Inhibition of Hepatitis C Virus ReplicationAntiviral Chemistry and Chemotherapy, 1997
- Mechanistic Role of an NS4A Peptide Cofactor with the Truncated NS3 Protease of Hepatitis C Virus: Elucidation of the NS4A Stimulatory Effect via Kinetic Analysis and Inhibitor MappingBiochemistry, 1997
- Complex Formation between the Hepatitis C Virus Serine Protease and A Synthetic NS4A Cofactor PeptideBiochemistry, 1997
- Crystal Structure of the Hepatitis C Virus NS3 Protease Domain Complexed with a Synthetic NS4A Cofactor PeptideCell, 1996
- The Crystal Structure of Hepatitis C Virus NS3 Proteinase Reveals a Trypsin-like Fold and a Structural Zinc Binding SiteCell, 1996