1: Chem Biodivers. 2007 Aug;4(8):1882-902. Fatty acid amide hydrolase: from characterization to therapeutics. Labar G, Michaux C. Unité de Chimie pharmaceutique et de Radiopharmacie, Ecole de Pharmacie, Faculté de Médecine, Université catholique de Louvain, Avenue E. Mounier 73.40, B-1200 Bruxelles. Fatty acid amide hydrolase (FAAH) is an integral membrane enzyme within the amidase-signature family that terminates the action of several endogenous lipid messengers, including oleamide and the endocannabinoid anandamide. The hydrolysis of such messengers leads to molecules devoid of biological activity, and, therefore, modulates a number of neurobehavioral processes in mammals, including pain, sleep, feeding, and locomotor activity. Investigations into the structure and function of FAAH, its biological and therapeutic implications, as well as a description of different families of FAAH inhibitors are the topic of this review. PMID: 17712824 [PubMed - indexed for MEDLINE] Related Links A second fatty acid amide hydrolase with variable distribution among placental mammals. [J Biol Chem. 2006] PMID:17015445 Structure and function of fatty acid amide hydrolase. [Annu Rev Biochem. 2005] PMID:15952893 The enzymatic inactivation of the fatty acid amide class of signaling lipids. [Chem Phys Lipids. 2002] PMID:12505696 Pharmacological activity of fatty acid amides is regulated, but not mediated, by fatty acid amide hydrolase in vivo. [J Pharmacol Exp Ther. 2002] PMID:12065702 Partial QSAR analysis of some selected natural inhibitors of FAAH suggests a working hypothesis for the development of endocannabinoid-based drugs. [Curr Drug Targets CNS Neurol Disord. 2005] PMID:16375688