Structure-based design of inhibitors of NS3 serine protease of hepatitis C virus
Authors:
- Martin KabeláčMKMartin Kabeláč
- Piergiuseppe De NardiPNPiergiuseppe De Nardi
- Sabrina PriclSPSabrina Pricl
- Stanislav MiertušSMStanislav Miertuš
- 1 January 2004
- journal article
- Published by Elsevier in Journal of Molecular Graphics and Modelling
- Vol. 22 (3) , 209-220
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Therapy for Acute Hepatitis CNew England Journal of Medicine, 2001
- Probing the Active Site of the Hepatitis C Virus Serine Protease by Fluorescence Resonance Energy TransferJournal of Biological Chemistry, 2000
- Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domainThe EMBO Journal, 2000
- Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studiesJournal of Molecular Biology, 1999
- Potent Peptide Inhibitors of Human Hepatitis C Virus NS3 Protease Are Obtained by Optimizing the Cleavage ProductsBiochemistry, 1998
- Hepatitis CCurrent Opinion in Infectious Diseases, 1998
- The Treatment of Chronic Viral HepatitisNew England Journal of Medicine, 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
- Conservation and Variability in the Structures of Serine Proteinases of the Chymotrypsin FamilyJournal of Molecular Biology, 1996