ArticleCommunications biology2026
Allosteric ensembles elucidate mechanisms of inhibition in the human soluble epoxide hydrolase.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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1 citing paper in PubMed.
- Allosteric ensembles elucidate mechanisms of inhibition in the human soluble epoxide hydrolase.Communications biology · 2026Article
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5 authors.
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Abstract
Human soluble epoxide hydrolase (sEH) is an important modulator of cardiovascular, brain and renal health, and a promising therapeutical target for several pathologies. Its C-terminal domain (CTD) possesses hydrolytic activity which is responsible for decreasing the level of beneficial bioactive epoxy fatty acids. In this work we uncover the mechanisms of allosteric inhibition exerted on sEH CTD through the cysteine residues C522 and C423. In silico investigations coupled with biophysical and biochemical characterizations revealed that allosteric inhibition by the endogenous lipid mediator 15-deoxy-Δ
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