ArticleJournal of virology1997
Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase.
Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 98 citations in OpenAlex.
- From vibrations to function: Spectroscopic detection and quantification of π-π stacking in drug-responsive protein complexes.Science advances · 2026Article
- Discovery of Nirmatrelvir Resistance Mutations in SARS-CoV-2 3CLpro: A Computational-Experimental Approach.Journal of chemical information and modeling · 2023Article
- 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
- Unveiling the Potentiality of Shikonin Derivatives Inhibiting SARS-CoV-2 Main Protease by Molecular Dynamic Simulation Studies.International journal of molecular sciences · 2023Article
- A C-terminal glutamine recognition mechanism revealed by E3 ligase TRIM7 structures.Nature chemical biology · 2022Article
- Flavonols and dihydroflavonols inhibit the main protease activity of SARS-CoV-2 and the replication of human coronavirus 229E.Virology · 2022Article
- Novel piperazine based compounds as potential inhibitors for SARS-CoV-2 Protease Enzyme: Synthesis and molecular docking study.Journal of molecular structure · 2021Article
- AnJournal of biomolecular structure & dynamics · 2021Article
- Targeting SARS-CoV-2 viral proteases as a therapeutic strategy to treat COVID-19.Journal of medical virology · 2021Review
- Pseudo-Dipeptide Bearing α,α-Difluoromethyl Ketone Moiety as Electrophilic Warhead with Activity against Coronaviruses.International journal of molecular sciences · 2021Article
- Characterization of Self-Processing Activities and Substrate Specificities of Porcine Torovirus 3C-Like Protease.Journal of virology · 2020Article
- The SARS-CoV-2 main protease as drug target.Bioorganic & medicinal chemistry letters · 2020Review
- An Overview of Severe Acute Respiratory Syndrome-Coronavirus (SARS-CoV) 3CL Protease Inhibitors: Peptidomimetics and Small Molecule Chemotherapy.Journal of medicinal chemistry · 2016Review
- Characterization of an alphamesonivirus 3C-like protease defines a special group of nidovirus main proteases.Journal of virology · 2014Article
- Inhibitors of SARS-3CLpro: virtual screening, biological evaluation, and molecular dynamics simulation studies.Journal of chemical information and modeling · 2011Article
- Characterization of Bafinivirus main protease autoprocessing activities.Journal of virology · 2011Article
- Structure and cleavage specificity of the chymotrypsin-like serine protease (3CLSP/nsp4) of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV).Journal of molecular biology · 2009Article
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- Development of broad-spectrum halomethyl ketone inhibitors against coronavirus main protease 3CL(pro).Chemical biology & drug design · 2008Article
- Structure-based virtual screening against SARS-3CL(pro) to identify novel non-peptidic hits.Bioorganic & medicinal chemistry · 2008Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coronavirus gene expression involves proteolytic processing of the gene 1-encoded polyprotein(s), and a key enzyme in this process is the viral 3C-like proteinase. In this report, we describe the biosynthesis of the human coronavirus 229E 3C-like proteinase in Escherichia coli and the enzymatic properties, inhibitor profile, and substrate specificity of the purified protein. Furthermore, we have introduced single amino acid substitutions and carboxyl-terminal deletions into the recombinant protein and determined the ability of these mutant 3C-like proteinases to catalyze the cleavage of a peptide substrate. Using this approach, we have identified the residues Cys-3109 and His-3006 as being indispensable for catalytic activity. Our results also support the involvement of His-3127 in substrate recognition, and they confirm the requirement of the carboxyl-terminal extension found in coronavirus 3C-like proteinases for enzymatic activity. These data provide experimental evidence for the relationship of coronavirus 3C-like proteinases to other viral chymotrypsin-like enzymes, but they also show that the coronavirus proteinase has additional, unique properties.
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