ArticleACS omega2026
The Enzymatic Mechanism of OAS: How Metal Ions and Quantum Effects Help Activate Innate Immunity.
Article in ACS omega, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
2'-5'-Oligoadenylate synthetases (OAS) are crucial innate immune sensors that activate antiviral responses upon detecting viral double-stranded RNA. Understanding the molecular mechanism of OAS is vital for advancing immunomodulatory therapies. This study provides a detailed enzymatic mechanism of the OAS, integrating structural, kinetic, and quantum chemical analyses. Crystallographic data of the OAS1 postreactive complexes shed light on the geometry of OAS1 following product formation and dissociation, the sequential order of product release, and the pivotal role of divalent metal ions in catalysis. Our data reveal the unanticipated involvement of a third metal ion, which may play a transient supporting role in the catalytic cycle. Moreover, they highlight the central role of quantum mechanisms in the OAS function. Strikingly, substituting catalytic Mg
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Registered trials
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