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Fatty acid amide hydrolase: from characterization to therapeutics.
Chem Biodivers 2007; 4(8):1882-902CB

Abstract

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.

Authors+Show Affiliations

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.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

17712824

Citation

Labar, Geoffray, and Catherine Michaux. "Fatty Acid Amide Hydrolase: From Characterization to Therapeutics." Chemistry & Biodiversity, vol. 4, no. 8, 2007, pp. 1882-902.
Labar G, Michaux C. Fatty acid amide hydrolase: from characterization to therapeutics. Chem Biodivers. 2007;4(8):1882-902.
Labar, G., & Michaux, C. (2007). Fatty acid amide hydrolase: from characterization to therapeutics. Chemistry & Biodiversity, 4(8), pp. 1882-902.
Labar G, Michaux C. Fatty Acid Amide Hydrolase: From Characterization to Therapeutics. Chem Biodivers. 2007;4(8):1882-902. PubMed PMID: 17712824.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Fatty acid amide hydrolase: from characterization to therapeutics. AU - Labar,Geoffray, AU - Michaux,Catherine, PY - 2007/8/23/pubmed PY - 2007/9/29/medline PY - 2007/8/23/entrez SP - 1882 EP - 902 JF - Chemistry & biodiversity JO - Chem. Biodivers. VL - 4 IS - 8 N2 - 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. SN - 1612-1880 UR - https://www.unboundmedicine.com/medline/citation/17712824/Fatty_acid_amide_hydrolase:_from_characterization_to_therapeutics_ L2 - https://doi.org/10.1002/cbdv.200790157 DB - PRIME DP - Unbound Medicine ER -