Evaluating the 3C-like protease activity of SARS-Coronavirus: Recommendations for standardized assays for drug discovery
- 30 March 2007
- journal article
- research article
- Published by Elsevier in Virus Research
- Vol. 133 (1) , 63-73
- https://doi.org/10.1016/j.virusres.2007.02.015
Abstract
No abstract availableKeywords
This publication has 50 references indexed in Scilit:
- Only One Protomer Is Active in the Dimer of SARS 3C-like ProteinaseJournal of Biological Chemistry, 2006
- pH-dependent Conformational Flexibility of the SARS-CoV Main Proteinase (Mpro) Dimer: Molecular Dynamics Simulations and Multiple X-ray Structure AnalysesJournal of Molecular Biology, 2005
- Screening of drugs by FRET analysis identifies inhibitors of SARS-CoV 3CL proteaseBiochemical and Biophysical Research Communications, 2005
- Characterization of SARS main protease and inhibitor assay using a fluorogenic substrateBiochemical 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
- Ultrastructural Characterization of SARS CoronavirusEmerging Infectious Diseases, 2004
- Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like ProteinaseJournal of Biological Chemistry, 2004
- Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domainThe EMBO Journal, 2002
- RNA Replication of Mouse Hepatitis Virus Takes Place at Double-Membrane VesiclesJournal of Virology, 2002