ArticleIUCrJ2021
Michaelis-like complex of SARS-CoV-2 main protease visualized by room-temperature X-ray crystallography.
Article in IUCrJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
22 citing papers in PubMed.
- Cleavage at the nsp5-nsp6 site of SARS-CoV-2 main protease intermediate precursor is faster from a monomer than a dimer form.The Journal of biological chemistry · 2026Article
- Computational design of 3C-like protease substrate peptide for modular detection of protease activity of coronavirus.Engineering in life sciences · 2026Article
- Characterization of an unusual SARS-CoV-2 main protease natural variant exhibiting resistance to nirmatrelvir and ensitrelvir.Communications biology · 2025Article
- Article
- Catalytic Mechanism of SARS-CoV-2 3-Chymotrypsin-Like Protease as Determined by Steady-State and Pre-Steady-State Kinetics.ACS catalysis · 2024Article
- Allostery in homodimeric SARS-CoV-2 main protease.Communications biology · 2024Article
- The S2 Pocket Governs the Genus-Specific Substrate Selectivity of Coronavirus 3C-Like Protease.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Visualizing the Active Site Oxyanion Loop Transition Upon Ensitrelvir Binding and Transient Dimerization of SARS-CoV-2 Main Protease.Journal of molecular biology · 2024Article
- Insights into the mechanism of SARS-CoV-2 main protease autocatalytic maturation from model precursors.Communications biology · 2023Article
- Article
- Autoprocessing and oxyanion loop reorganization upon GC373 and nirmatrelvir binding of monomeric SARS-CoV-2 main protease catalytic domain.Communications biology · 2022Article
- Structural and functional characterization of NEMO cleavage by SARS-CoV-2 3CLpro.Nature communications · 2022Article
- X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation.Nature communications · 2022Article
- The SARS-CoV-2 main protease (MMedComm · 2022Review
- Review
- Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease.Nature communications · 2022Article
- Potential Resistance of SARS-CoV-2 Main Protease (Mpro) against Protease Inhibitors: Lessons Learned from HIV-1 Protease.International journal of molecular sciences · 2022Review
- Modulation of the monomer-dimer equilibrium and catalytic activity of SARS-CoV-2 main protease by a transition-state analog inhibitor.Communications biology · 2022Article
- A new inactive conformation of SARS-CoV-2 main protease.Acta crystallographica. Section D, Structural biology · 2022Article
- Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease: room-temperature X-ray and neutron crystallography, binding thermodynamics, and antiviral activity.Research square · 2022Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SARS-CoV-2 emerged at the end of 2019 to cause an unprecedented pandemic of the deadly respiratory disease COVID-19 that continues to date. The viral main protease (M
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.