ArticleProtein science : a publication of the Protein Society2024
Profiling of coronaviral M
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- Structure-based macrocyclization of α-ketoamides leads to potent inhibitors of coronaviral and enteroviral proteases.Communications chemistry · 2026Article
- Coupling high-throughput protease enzymology with viral replication reveals biochemical constraints of viral fitness.bioRxiv : the preprint server for biology · 2026Article
- Profiling of coronaviral MProtein science : a publication of the Protein Society · 2024Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The main protease from coronaviruses and the 3C protease from enteroviruses play a crucial role in processing viral polyproteins, making them attractive targets for the development of antiviral agents. In this study, we employed a combinatorial chemistry approach-HyCoSuL-to compare the substrate specificity profiles of the main and 3C proteases from alphacoronaviruses, betacoronaviruses, and enteroviruses. The obtained data demonstrate that coronavirus 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.