Mutational and inhibitive analysis of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer-based assays
- 17 June 2005
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 331 (4) , 1554-1559
- https://doi.org/10.1016/j.bbrc.2005.04.072
Abstract
No abstract availableKeywords
This publication has 18 references indexed in Scilit:
- The substrate specificity of SARS coronavirus 3C-like proteinaseBiochemical and Biophysical Research Communications, 2005
- Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase N Terminus Is Indispensable for Proteolytic Activity but Not for Enzyme DimerizationJournal of Biological Chemistry, 2005
- High-Throughput Screening Identifies Inhibitors of the SARS Coronavirus Main ProteinaseChemistry & Biology, 2004
- Dissection Study on the Severe Acute Respiratory Syndrome 3C-like Protease Reveals the Critical Role of the Extra Domain in Dimerization of the EnzymeJournal of Biological Chemistry, 2004
- Hepatitis C virus NS3 RNA helicase activity is modulated by the two domains of NS3 and NS4ABiochemical and Biophysical Research Communications, 2004
- Identification of Novel Inhibitors of the SARS Coronavirus Main Protease 3CLproBiochemistry, 2004
- 3C-like Proteinase from SARS Coronavirus Catalyzes Substrate Hydrolysis by a General Base MechanismBiochemistry, 2004
- Mechanisms and enzymes involved in SARS coronavirus genome expressionJournal of General Virology, 2003
- Coronavirus Main Proteinase (3CL pro ) Structure: Basis for Design of Anti-SARS DrugsScience, 2003
- Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyproteinCell, 1994