ArticleBiochemical and biophysical research communications2005
Mutational and inhibitive analysis of SARS coronavirus 3C-like protease by fluorescence resonance energy transfer-based assays.
Article in Biochemical and biophysical research communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Comprehensive Understanding of the Kinetic Behaviors of Main Protease from SARS-CoV-2 and SARS-CoV: New Data and Comparison to Published Parameters.Molecules (Basel, Switzerland) · 2023Article
- Repurposing existing drugs: identification of SARS-CoV-2 3C-like protease inhibitors.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- What coronavirus 3C-like protease tells us: From structure, substrate selectivity, to inhibitor design.Medicinal research reviews · 2021Review
- Ugonin J Acts as a SARS-CoV-2 3C-like Protease Inhibitor and Exhibits Anti-inflammatory Properties.Frontiers in pharmacology · 2021Article
- Evaluation of SARS-CoV-2 3C-like protease inhibitors using self-assembled monolayer desorption ionization mass spectrometry.Antiviral research · 2020Article
- Article
- Dynamically-driven inactivation of the catalytic machinery of the SARS 3C-like protease by the N214A mutation on the extra domain.PLoS computational biology · 2011Article
- Mechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease.Journal of virology · 2008Article
- Residues on the dimer interface of SARS coronavirus 3C-like protease: dimer stability characterization and enzyme catalytic activity analysis.Journal of biochemistry · 2008Article
- Evaluating the 3C-like protease activity of SARS-Coronavirus: recommendations for standardized assays for drug discovery.Virus research · 2008Article
- Only one protomer is active in the dimer of SARS 3C-like proteinase.The Journal of biological chemistry · 2006Article
- Enzymatic activity of the SARS coronavirus main proteinase dimer.FEBS letters · 2006Article
- The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.The FEBS journal · 2006Article
- Techniques used for the discovery of therapeutic compounds: The case of SARS.Drug discovery today. Technologies · 2006Article
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Authors and funding
4 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome coronavirus (SARS-CoV) plays key roles in viral replication and is an attractive target for anti-SARS drug discovery. In this report, a fluorescence resonance energy transfer (FRET)-based method was developed to assess the proteolytic activity of SARS-CoV 3CL(pro). Two internally quenched fluorogenic peptides, 1NC and 2NC, corresponding to the N-terminal and the C-terminal autocleavage sites of SARS-CoV 3CL(pro), respectively, were used as substrates. SARS-CoV 3CL(pro) seemed to work more efficiently on 1NC than on 2NC in trans-cleavage assay. Mutational analysis demonstrated that the His41 residue, the N-terminal 7 amino acids, and the domain III of SARS-CoV 3CL(pro) were important for the enzymatic activity. Antibodies recognizing domain III could significantly inhibit the enzymatic activity of SARS-CoV 3CL(pro). The effects of class-specific protease inhibitors on the trans-cleavage activity revealed that this enzyme worked more like a serine protease rather than the papain protease.
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