ArticleAnalytical chemistry2026
Decoding Enzyme-Inhibitor Kinetic Mechanisms by Isothermal Titration Calorimetry: The Case of SARS-CoV-2 3CL
Article in Analytical chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed.
- Slowly exchanging bound states of SARS-CoV-2 3CLStructural dynamics (Melville, N.Y.) · 2026Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
Accurate kinetic and thermodynamic characterization of enzyme inhibitors remains difficult because conventional activity assays can miss nonequilibrium behavior and provide limited mechanistic resolution. Here, we present an inverse single-injection isothermal titration calorimetry (ITC) workflow that extracts qualitative and quantitative inhibition parameters directly from heat-flow traces by distinguishing rapid reversible, tight-, or slow-binding, and covalent inhibition within a single experimental format. The inhibition of SARS-CoV-2 main protease (3CL
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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.