title: Oxime carbamate--discovery of a series of novel FAAH inhibitors.
abstract: A series of novel oxime carbamates have been identified as potent inhibitors of the key regulatory enzyme of the endocannabinoid signaling system, fatty acid amide hydrolase (FAAH). In this Letter, the rationale behind the discovery and the biological evaluations of this novel class of FAAH inhibitors are presented. Both in vitro and in vivo results of selected targets are discussed, along with inhibition kinetics and molecular modeling studies.(1).
authors.affiliation: Department of Chemistry, Bristol-Myers Squibb Research & Development, 5 Research Parkway, Wallingford, CT 06492-7660, USA. sits@bms.com
authors.forename: S Y
authors.initials: SY
authors.lastname: Sit
authors.forename: Charles M
authors.initials: CM
authors.lastname: Conway
authors.forename: Kai
authors.initials: K
authors.lastname: Xie
authors.forename: Robert
authors.initials: R
authors.lastname: Bertekap
authors.forename: Clotilde
authors.initials: C
authors.lastname: Bourin
authors.forename: Kevin D
authors.initials: KD
authors.lastname: Burris
mesh_terms: D000581:Amidohydrolases / Q000037:antagonists & inhibitors* / Q000502:physiology; D000818:Animals; D063385:Cannabinoid Receptor Modulators / Q000502:physiology; D002219:Carbamates / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D002460:Cell Line; D018360:Crystallography, X-Ray; D055808:Drug Discovery / Q000379:methods*; D006801:Humans; D010091:Oximes / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary; D051381:Rats; D015398:Signal Transduction / Q000187:drug effects / Q000502:physiology; D000099252:Fatty Acid Amide Hydrolases
chemical_list: D000581:Amidohydrolases; D063385:Cannabinoid Receptor Modulators; D002219:Carbamates; D010091:Oximes; D000099252:Fatty Acid Amide Hydrolases