ArticleScientific reports2016
Free-energy studies reveal a possible mechanism for oxidation-dependent inhibition of MGL.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Iso- and Benzisothiazolinone Inhibitors of Monoacylglycerol Lipase: Exploring On-Target Activity Through Scaffold Decoration and In Situ Warhead Generation.ChemMedChem · 2026Article
- Recent Progress in the Development of Selective MAGL Modulators (2020-2026).Molecules (Basel, Switzerland) · 2026Review
- Early occurrence of caffeoylshikimic acid esterase (CSE) activity in the hornwort Anthoceros agrestis.Planta · 2026Article
- Unbinding Kinetics of Muscarinic M3 Receptor Antagonists Explained by Metadynamics Simulations.Journal of chemical information and modeling · 2023Article
- Lipid-Based Molecules on Signaling Pathways in Autism Spectrum Disorder.International journal of molecular sciences · 2022Review
- Mechanistic Modeling of Monoglyceride Lipase Covalent Modification Elucidates the Role of Leaving Group Expulsion and Discriminates Inhibitors with High and Low Potency.Journal of chemical information and modeling · 2022Article
- Conformational gating, dynamics and allostery in human monoacylglycerol lipase.Scientific reports · 2020Article
- Direct cysteine sulfenylation drives activation of the Src kinase.Nature communications · 2018Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The function of monoacylglycerol lipase (MGL), a key actor in the hydrolytic deactivation of the endocannabinoid 2-arachidonoyl-sn-glycerol (2AG), is tightly controlled by the cell's redox state: oxidative signals such as hydrogen peroxide suppress MGL activity in a reversible manner through sulfenylation of the peroxidatic cysteines, C201 and C208. Here, using as a starting point the crystal structures of human MGL (hMGL), we present evidence from molecular dynamics and metadynamics simulations along with high-resolution mass spectrometry studies indicating that sulfenylation of C201 and C208 alters the conformational equilibrium of the membrane-associated lid domain of MGL to favour closed conformations of the enzyme that do not permit the entry of substrate into the active site.
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