ArticleScience advances2022
Biochemical and structural insights into SARS-CoV-2 polyprotein processing by Mpro.
Article in Science advances, 2022. 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, 33 citations in OpenAlex.
- A P3' methionine-to-phenylalanine substitution in the NSP6-7 substrate peptide alters SARS-CoV-2 MThe Journal of biological chemistry · 2026Article
- Differential Impact of Substrate Peptides on Interdomain Interactions in Severe Acute Respiratory Syndrome Coronavirus 2 Main Protease.Computational and structural biotechnology journal · 2026Article
- The kinetics of nsp7-11 polyprotein processing and impact on complexation with nsp16 among human coronaviruses.Nature communications · 2025Article
- Peptidomimetic Phenoxymethyl Ketone Warheads as Potent Dual-Mode Inhibitors against SARS-CoV-2 MJournal of medicinal chemistry · 2025Article
- Molecular characterization and drug resistance pattern in pol gene of HIV-1 sub-subtypes circulating in Lahore, Pakistan.Virus genes · 2025Article
- Biochemical Screening of Phytochemicals and Identification of Scopoletin as a Potential Inhibitor of SARS-CoV-2 MViruses · 2025Article
- Distal protein-protein interactions contribute to nirmatrelvir resistance.Nature communications · 2025Article
- The zymogenic form of SARS-CoV-2 main protease: A discrete target for drug discovery.The Journal of biological chemistry · 2025Article
- High-Resolution Substrate Specificity Profiling of SARS-CoV-2 MACS chemical biology · 2024Article
- Article
- Crystal structures of main protease (MMolecular biomedicine · 2023Article
- Fitness effects of mutations to SARS-CoV-2 proteins.bioRxiv : the preprint server for biology · 2023Article
- Identification of SARS-CoV-2 Main Protease (Mpro) Cleavage Sites Using Two-Dimensional Electrophoresis and In Silico Cleavage Site Prediction.International journal of molecular sciences · 2023Article
- Fitness effects of mutations to SARS-CoV-2 proteins.Virus evolution · 2023Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
SARS-CoV-2, a human coronavirus, is the causative agent of the COVID-19 pandemic. Its genome is translated into two large polyproteins subsequently cleaved by viral papain-like protease and main protease (Mpro). Polyprotein processing is essential yet incompletely understood. We studied Mpro-mediated processing of the nsp7-11 polyprotein, whose mature products include cofactors of the viral replicase, and identified the order of cleavages. Integrative modeling based on mass spectrometry (including hydrogen-deuterium exchange and cross-linking) and x-ray scattering yielded a nsp7-11 structural ensemble, demonstrating shared secondary structural elements with individual nsps. The pattern of cross-links and HDX footprint of the C145A Mpro and nsp7-11 complex demonstrate preferential binding of the enzyme active site to the polyprotein junction sites and additional transient contacts to help orient the enzyme on its substrate for cleavage. Last, proteolysis assays were used to characterize the effect of inhibitors/binders on Mpro processing/inhibition using the nsp7-11 polyprotein as substrate.
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Registered trials
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