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- W1005113303 abstract "Monoglyceride lipase (MGL), the main enzyme responsible for the hydrolytic deactivation of the endocannabinoid 2-arachidonoyl-sn-glycerol (2-AG), is an intracellular serine hydrolase that plays critical roles in many physiological and pathological processes, such as pain, inflammation, neuroprotection and cancer. The crystal structures of MGL that are currently available provide valuable information about how this enzyme might function and interact with site-directed small-molecule inhibitors. On the other hand, its conformational equilibria and the contribution of regulatory cysteine residues present within the substrate-binding pocket or on protein surface remain open issues. Several classes of MGL inhibitors have been developed, from early reversible ones, such as URB602 and pristimerin, to carbamoylating agents that react with the catalytic serine, such as JZL184 and more recent O-hexafluoroisopropyl carbamates. Other inhibitors that modulate MGL activity by interacting with conserved regulatory cysteines act through mechanisms that deserve to be more thoroughly investigated." @default.
- W1005113303 created "2016-06-24" @default.
- W1005113303 creator A5031213755 @default.
- W1005113303 creator A5043710547 @default.
- W1005113303 creator A5085013575 @default.
- W1005113303 date "2016-05-01" @default.
- W1005113303 modified "2023-10-09" @default.
- W1005113303 title "Monoglyceride lipase: Structure and inhibitors" @default.
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