Latest advances in the discovery of fatty acid amide hydrolase inhibitors

Bibliography

• Bisogno T. Endogenous cannabinoids: structure and metabolism. J Neuroendocrinol 2008;20(Suppl 1):1-9
   PubMed Web of Science ®Google Scholar
• Muccioli GG. Endocannabinoid biosynthesis and inactivation, from simple to complex. Drug Discov Today 2010;15:474-83
   PubMed Web of Science ®Google Scholar
• Maccarrone M, Dainese E, Oddi S. Intracellular trafficking of anandamide: new concepts for signaling. Trends Biochem Sci 2010;35:601-8
   PubMed Web of Science ®Google Scholar
• Min R, Di Marzo V, Mansvelder HD. DAG lipase involvement in depolarization-induced suppression of inhibition: does endocannabinoid biosynthesis always meet the demand? Neuroscientist 2010;16:608-13
   PubMed Web of Science ®Google Scholar
• Gasperi V, Dainese E, Oddi S, GPR55 and its interaction with membrane lipids: comparison with other endocannabinoid-binding receptors. Curr Med Chem 2012;
   Web of Science ®Google Scholar
• Bouaboula M, Hilairet S, Marchand J, Anandamide induced PPARgamma transcriptional activation and 3T3-L1 preadipocyte differentiation. Eur J Pharmacol 2005;517:174-81
   PubMed Web of Science ®Google Scholar
• Di Marzo V, De Petrocellis L. Endocannabinoids as regulators of transient receptor potential (TRP) channels: a further opportunity to develop new endocannabinoid-based therapeutic drugs. Curr Med Chem 2010;17:1430-49
   PubMed Web of Science ®Google Scholar
• Sigel E, Baur R, Rácz I, The major central endocannabinoid directly acts at GABA(A) receptors. Proc Natl Acad Sci USA 2011;108:18150-5
   PubMed Web of Science ®Google Scholar
• Okamoto Y, Tsuboi K, Ueda N. Enzymatic formation of anandamide. Vitam Horm 2009;81:1-24
   PubMed Web of Science ®Google Scholar
• Leung D, Saghatelian A, Simon GM, Cravatt BF. Inactivation of N-acyl phosphatidylethanolamine phospholipase D reveals multiple mechanisms for the biosynthesis of endocannabinoids. Biochemistry 2006;45:4720-6
   PubMed Web of Science ®Google Scholar
• Bisogno T, Howell F, Williams G, Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain. J Cell Biol 2003;163:463-8
   PubMed Web of Science ®Google Scholar
• Gao Y, Vasilyev DV, Goncalves MB, Loss of retrograde endocannabinoid signaling and reduced adult neurogenesis in diacylglycerol lipase knock-out mice. J Neurosci 2010;30:2017-24
   PubMed Web of Science ®Google Scholar
• Chicca A, Marazzi J, Nicolussi S, Gertsch J. Evidence for bidirectional endocannabinoide transport across cell membranes. J Biol Chem 2012;287:34660-82
   PubMed Web of Science ®Google Scholar
• Cravatt BF, Giang DK, Mayfield SP, Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides. Nature 1996;384:83-7
   PubMed Web of Science ®Google Scholar
• Dinh TP, Carpenter D, Leslie FM, Brain monoglyceride lipase participating in endocannabinoid inactivation. Proc Natl Acad Sci USA 2002;99:10819-24
   PubMed Web of Science ®Google Scholar
• Di Marzo V. Targeting the endocannabinoid system: to enhance or reduce? Nat Rev Drug Discov 2008;7:438-55
   PubMed Web of Science ®Google Scholar
• Guindon J, Hohmann AG. The endocannabinoid system and pain. CNS Neurol Disord Drug Targets 2009;8:403-21
   PubMed Web of Science ®Google Scholar
• Bisogno T, Di Marzo V. Short- and long-term plasticity of the endocannabinoid system in neuropsychiatric and neurological disorders. Pharmacol Res 2007;56:428-42
   PubMed Web of Science ®Google Scholar
• Engeli S. Central and peripheral cannabinoid receptors as therapeutic targets in the control of food intake and body weight. Handb Exp Pharmacol 2012;209:357-81
   PubMedGoogle Scholar
• O'Sullivan SE, Kendall PJ, Kendall DA. Endocannabinoids and the cardiovascular response to stress. J Psychopharmacol 2012;26:71-82
   PubMed Web of Science ®Google Scholar
• Grimaldi C, Capasso A. The endocannabinoid system in the cancer therapy: an overview. Curr Med Chem 2011;18:1575-83
   PubMed Web of Science ®Google Scholar
• Schicho R, Storr M. Alternative targets within the endocannabinoid system for future treatment of gastrointestinal diseases. Can J Gastroenterol 2011;25:377-83
   PubMed Web of Science ®Google Scholar
• Ueda N, Tsuboi K, Uyama T. N-acylethanolamine metabolism with special reference to N-acylethanolamine-hydrolyzing acid amidase (NAAA). Prog Lipid Res 2010;49:299-315
   PubMed Web of Science ®Google Scholar
• Fu J, Gaetani S, Oveisi F, Oleylethanolamide regulates feeding and body weight through activation of the nuclear receptor PPAR-alpha. Nature 2003;425:90-3
   PubMed Web of Science ®Google Scholar
• Overton HA, Babbs AJ, Doel SM, Deorphanization of a G protein-coupled receptor for oleoylethanolamide and its use in the discovery of small-molecule hypophagic agents. Cell Metab 2006;3:167-75
   PubMed Web of Science ®Google Scholar
• Movahed P, Jönsson BA, Birnir B, Endogenous unsaturated C18 N-acylethanolamines are vanilloid receptor (TRPV1) agonists. J Biol Chem 2005;280:38496-504
   PubMed Web of Science ®Google Scholar
• Wei BQ, Mikkelsen TS, McKinney MK, A second fatty acid amide hydrolase with variable distribution among placental mammals. J Biol Chem 2006;281:36569-78
   PubMed Web of Science ®Google Scholar
• Cravatt B F, Prospero-Garcia O, Siuzdak G, Chemical characterization of a family of brain lipids that induce sleep. Science 1995;268:1506-9
   PubMed Web of Science ®Google Scholar
• Leggett JD, Aspley S, Beckett SR, Oleamide is a selective endogenous agonist of rat and human CB1 cannabinoid receptors. Br J Pharmacol 2004;141:253-62
   PubMed Web of Science ®Google Scholar
• McHugh D, Wager-Miller J, Page J, Bradshaw HB. siRNA knockdown of GPR18 receptors in BV-2 microglia attenuates N-arachidonoyl glycine-induced cell migration. J Mol Signal 2012;7:10-16
   PubMedGoogle Scholar
• Huang SM, Bisogno T, Petros TJ, Identification of a new class of molecules, the arachidonyl amino acids, and characterization of one member that inhibits pain. J Biol Chem 2001;276:42639-44
   PubMed Web of Science ®Google Scholar
• Milman G, Maor Y, Abu-Lafi S, N-Arachidonoyl L-serine, an endocannabinoidlike brain constituent with vasodilatory properties. Proc Natl Acad Sci USA 2006;103:2428-33
   PubMed Web of Science ®Google Scholar
• Saghatelian A, McKinney MK, Bandell M, A FAAH-regulated class of N-acyl taurines that activates TRP ion channels. Biochemistry 2006;45:9007-15
   PubMed Web of Science ®Google Scholar
• Blankman JL, Simon GM, Cravatt BF. A comprehensive profile of brain enzymes that hydrolyze the endocannabinoide 2-arachidonoylglycerol. Chem Biol 2007;14:1347-56
   PubMed Web of Science ®Google Scholar
• Xie S, Borazjani A, Hatfield MJ, Inactivation of lipid glyceryl ester metabolism in human THP1 monocytes/macrophages by activated organophosphorus insecticides: role of carboxylesterases 1 and 2. Chem Res Toxicol 2010;23:1890-904
   PubMed Web of Science ®Google Scholar
• Kozak KR, Marnett LJ. Oxidative metabolism of endocannabinoids. Prostaglandins, Leukotrienes Essent. Fatty Acids 2002;66:211-20
   PubMed Web of Science ®Google Scholar
• Snider NT, Walker VJ, Hollenberg PF. Oxidation of the endogenous cannabinoid arachidonoyl ethanolamide by the cytochrome P450 monooxygenases: physiological and pharmacological implications. Pharmacol Rev 2010;62:136-54
   PubMed Web of Science ®Google Scholar
• Rouzer CA, Marnett LJ. Endocannabinoid oxygenation by cyclooxygenases, lipoxygenases, and cytochromes P450: cross-talk between the eicosanoid and endocannabinoid signaling pathways. Chem Rev 2011;111:5899-921
   PubMed Web of Science ®Google Scholar
• van der Stelt M, van Kuik JA, Bari M, Oxygenated metabolites of anandamide and 2-arachidonoylglycerol: conformational analysis and interaction with cannabinoid receptors, membrane transporter, and fatty acid amide hydrolase. J Med Chem 2002;45:3709-20
   PubMed Web of Science ®Google Scholar
• Matias I, Chen J, De Petrocellis L, Prostaglandin ethanolamides (prostamides): in vitro pharmacology and metabolism. J Pharmacol Exp Ther 2004;309:745-57
   PubMed Web of Science ®Google Scholar
• Gatta L, Piscitelli F, Giordano C, Discovery of prostamide F2α and its role in inflammatory pain and dorsal horn nociceptive neuron hyperexcitability. PLoS One 2012;7:e31111
   PubMedGoogle Scholar
• Cravatt BF, Demarest K, Patricelli MP, Supersensitivity to anandamide and enhanced endogenous cannabinoid signaling in mice lacking fatty acid amide hydrolase. Proc Natl Acad Sci USA 2001;98:9371-6
   PubMed Web of Science ®Google Scholar
• Lichtman AH, Shelton CC, Advani T, Cravatt BF. Mice lacking fatty acid amide hydrolase exhibit a cannabinoid receptor-mediated phenotypic hypoalgesia. Pain 2004;109:319-27
   PubMed Web of Science ®Google Scholar
• Massa F, Marsicano G, Hermann H, The endogenous cannabinoid system protects against colonic inflammation. J Clin Inv 2004;113:1202-9
   PubMed Web of Science ®Google Scholar
• Naidu PS, Varvel SA, Ahn K, Evaluation of fatty acid amide hydrolase inhibition in murine models of emotionality. Psychopharmacology (Berl) 2007;192:61-70
   PubMed Web of Science ®Google Scholar
• Moreira FA, Kaiser N, Monory K, Lutz B. Reduced anxiety-like behaviour induced by genetic and pharmacological inhibition of the endocannabinoid-degrading enzyme fatty acid amide hydrolase (FAAH) is mediated by CB1 receptors. Neuropharmacology 2008;54:141-50
   PubMed Web of Science ®Google Scholar
• McKinney MK, Cravatt BF. Structure and function of fatty acid amide hydrolase. Annu Rev Biochem 2005;74:411-32
   PubMed Web of Science ®Google Scholar
• Fezza F, De Simone C, Amadio D, Maccarrone M. Fatty acid amide hydrolase: a gate-keeper of the endocannabinoid system. Subcell Biochem 2008;49:101-32
   PubMedGoogle Scholar
• Lodola A, Mor M, Hermann JC, QM/MM modelling of oleamide hydrolysis in fatty acid amide hydrolase (FAAH) reveals a new mechanism of nucleophile activation. Chem Commun 2005;11:4399-401
   Google Scholar
• Tubert-Brohman I, Acevedo O, Jorgensen WL. Elucidation of hydrolysis mechanisms for fatty acid amide hydrolase and its Lys142Ala variant via QM/MM simulations. J Am Chem Soc 2006;128:16904-13
   PubMed Web of Science ®Google Scholar
• Bracey MH, Hanson MA, Masuda KR, Structural adaptations in a membrane enzyme that terminates endocannabinoid signaling. Science 2002;298:1793-6
   PubMed Web of Science ®Google Scholar
• Ahn K, Johnson DS, Fitzgerald LR, Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity. Biochemistry 2007;46:13019-30
   PubMed Web of Science ®Google Scholar
• Leung D, Du W, Hardouin C, Discovery of an exceptionally potent and selective class of fatty acid amide hydrolase inhibitors enlisting proteome-wide selectivity screening: concurrent optimization of enzyme inhibitor potency and selectivity. Bioorg Med Chem Lett 2005;15:1423-8
   PubMed Web of Science ®Google Scholar
• Zhang D, Saraf A, Kolasa T, Fatty acid amide hydrolase inhibitors display broad selectivity and inhibit multiple carboxylesterases as off-targets. Neuropharmacology 2007;52:1095-105
   PubMed Web of Science ®Google Scholar
• Wang X, Sarris K, Kage K, Synthesis and evaluation of benzothiazole-based analogues as novel, potent, and selective fatty acid amide hydrolase inhibitors. J Med Chem 2009;52:170-80
   PubMed Web of Science ®Google Scholar
• Liu Y, Patricelli MP, Cravatt BF. Activity-based protein profiling: the serine hydrolases. Proc Natl Acad Sci USA 1999;96:14694-9
   PubMed Web of Science ®Google Scholar
• Patricelli MP, Giang DK, Stamp LM, Burbaum JJ. Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active site-directed probes. Proteomics 2001;1:1067-71
   PubMed Web of Science ®Google Scholar
• McDonald AG, Tipton K. Enzymes: Irreversible Inhibition. In: eLS. John Wiley & Sons, Ltd, Chichester; 2012. DOI: 10.1002/9780470015902.a0000601.pub2
   Google Scholar
• Boger DL, Sato H, Lerner AE, Trifluoromethyl ketone inhibitors of fatty acid amide hydrolase: a probe of structural and conformational features contributing to inhibition. Bioorg Med Chem Lett 1999;9:265-70
   PubMed Web of Science ®Google Scholar
• Boger DL, Sato H, Lerner AE, Exceptionally potent inhibitors of fatty acid amide hydrolase: the enzyme responsible for degradation of endogenous oleamide and anandamide. Proc Natl Acad Sci USA 2000;97:5044-9
   PubMed Web of Science ®Google Scholar
• Boger DL, Miyauchi H, Hedrick MP. alpha-Keto heterocycle inhibitors of fatty acid amide hydrolase: carbonyl group modification and alpha-substitution. Bioorg Med Chem Lett 2001;11:1517-20
   PubMed Web of Science ®Google Scholar
• Boger DL, Miyauchi H, Du W, Discovery of a potent, selective, and efficacious class of reversible alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase effective as analgesics. J Med Chem 2005;48:1849-56
   PubMed Web of Science ®Google Scholar
• Lichtman AH, Leung D, Shelton CC, Reversible inhibitors of fatty acid amide hydrolase that promote analgesia: evidence for an unprecedented combination of potency and selectivity. J Pharmacol Exp Ther 2004;311:441-8
   PubMed Web of Science ®Google Scholar
• Chang L, Luo L, Palmer JA, Inhibition of fatty acid amide hydrolase produces analgesia by multiple mechanisms. Br J Pharmacol 2006;148:102-13
   PubMed Web of Science ®Google Scholar
• Kinsey SG, Long JZ, O'Neal ST, Blockade of endocannabinoid-degrading enzymes attenuates neuropathic pain. J Pharmacol Exp Ther 2009;330:902-10
   PubMed Web of Science ®Google Scholar
• Mileni M, Garfunkle J, DeMartino JK, Binding and inactivation mechanism of a humanized fatty acid amide hydrolase by alpha-ketoheterocycle inhibitors revealed from cocrystal structures. J Am Chem Soc 2009;131:10497-506
   PubMed Web of Science ®Google Scholar
• Mileni M, Garfunkle J, Ezzili C, X-ray crystallographic analysis of alpha-ketoheterocycle inhibitors bound to a humanized variant of fatty acid amide hydrolase. J Med Chem 2010;53:230-40
   PubMed Web of Science ®Google Scholar
• Otrubova K, Boger DL. α-Ketoheterocycle-based Inhibitors of Fatty Acid Amide Hydrolase (FAAH). ACS Chem Neurosci 2012;3:340-8
   PubMed Web of Science ®Google Scholar
• Sit SY, Conway CM, Xie K, Oxime carbamate–discovery of a series of novel FAAH inhibitors. Bioorg Med Chem Lett 2010;20:1272-7
   PubMed Web of Science ®Google Scholar
• Gattinoni S, Simone CD, Dallavalle S, A new group of oxime carbamates as reversible inhibitors of fatty acid amide hydrolase. Bioorg Med Chem Lett 2010;20:4406-11
   PubMed Web of Science ®Google Scholar
• Gattinoni S, De Simone C, Dallavalle S, Enol carbamates as inhibitors of fatty acid amide hydrolase (FAAH) endowed with high selectivity for FAAH over the other targets of the endocannabinoid system. ChemMedChem 2010;5:357-60
   PubMed Web of Science ®Google Scholar
• Caprioli A, Coccurello R, Rapino C, The novel reversible fatty acid amide hydrolase inhibitor ST4070 increases endocannabinoid brain levels and counteracts neuropathic pain in different animal models. J Pharmacol Exp Ther 2012;342:188-95
   PubMed Web of Science ®Google Scholar
• Gustin DJ, Ma Z, Min X, Identification of potent, noncovalent fatty acid amide hydrolase (FAAH) inhibitors. Bioorg Med Chem Lett 2011;21:2492-6
   PubMed Web of Science ®Google Scholar
• Minkilla A, Saario SM, Kasnanen H, Discovery of boronic acids as novel and potent inhibitors of fatty acid amide hydrolase. Med Chem 2008;51:7057-60
   Web of Science ®Google Scholar
• Adams J, Behnke ML, Castro AC, Preparation of arylboronates as inhibitors of fatty acid amide hydrolase. WO2008063300; 2008
   Google Scholar
• Dembitsky VM, Quntar AA, Srebnik M. Recent advances in the medicinal chemistry of alphaaminoboronic acids, amine-carboxyboranes and their derivatives. Mini Rev Med Chem 2004;4:1001-18
   PubMed Web of Science ®Google Scholar
• Tian G, Paschetto KA, Gharahdaghi F, Mechanism of inhibition of fatty acid amide hydrolase by sulfonamide-containing benzothiazoles: long residence time derived from increased kinetic barrier and not exclusively from thermodynamic potency. Biochemistry 2011;50:6867-78
   PubMed Web of Science ®Google Scholar
• Butini S, Brindisi M, Gemma S, Discovery of potent inhibitors of human and mouse fatty acid amide hydrolases. J Med Chem 2012;55:6898-915
   PubMed Web of Science ®Google Scholar
• Marshall GR, Beusen DD. Molecular modeling in drug design. In: Abram DJ, editor. Burger's medical chemistry and drug discovery. John Wiley & Sons, Hoboken; 2003
   Google Scholar
• Lodola A, Rivara S, Mor M. Application of computational methods to the design of fatty acid amide hydrolase (FAAH) inhibitors based on a carbamic template structure. Adv Protein Chem Struct Biol 2011;85:1-26
   PubMed Web of Science ®Google Scholar
• Lodola A, Mor M, Rivara S, Identification of productive inhibitor binding orientation in fatty acid amide hydrolase (FAAH) by QM/MM mechanistic modelling. Chem Commun 2008;2:214-16
   PubMedGoogle Scholar
• Lodola A, Capoferri L, Rivara S, Understanding the role of carbamate reactivity in fatty acid amide hydrolase inhibition by QM/MM mechanistic modelling. Chem Commun 2011;47:2517-19
   PubMed Web of Science ®Google Scholar
• Palermo G, Branduardi D, Masetti M, Covalent inhibitors of fatty acid amide hydrolase: a rationale for the activity of piperidine and piperazine aryl ureas. J Med Chem 2011;54:6612-23
   PubMed Web of Science ®Google Scholar
• Tarzia G, Duranti A, Tontini A, Design, synthesis, and structure-activity relationships of alkylcarbamic acid aryl esters, a new class of fatty acid amide hydrolase inhibitors. J Med Chem 2003;46:2352-60
   PubMed Web of Science ®Google Scholar
• Mor M, Rivara S, Lodola A, Cyclohexylcarbamic acid 3'- or 4'-substituted biphenyl-3-yl esters as fatty acid amide hydrolase inhibitors: synthesis, quantitative structure-activity relationships, and molecular modeling studies. J Med Chem 2004;47:4998-5008
   PubMed Web of Science ®Google Scholar
• Alexander JP, Cravatt BF. Mechanism of carbamate inactivation of FAAH: implications for the design of covalent inhibitors and in vivo functional probes for enzymes. Chem Biol 2005;12:1179-87
   PubMed Web of Science ®Google Scholar
• Piomelli D, Tarzia G, Duranti A, Pharmacological profile of the selective FAAH inhibitor KDS-4103 (URB597). CNS Drug Rev 2006;12:21-38
   PubMedGoogle Scholar
• Holt S, Comelli F, Costa B, Fowler CJ. Inhibitors of fatty acid amide hydrolase reduce carrageenan-induced hind paw inflammation in pentobarbital-treated mice: comparison with indomethacin and possible involvement of cannabinoid receptors. Br J Pharmacol 2005;146:467-76
   PubMed Web of Science ®Google Scholar
• Jayamanne A, Greenwood R, Mitchell VA, Actions of the FAAH inhibitor URB597 in neuropathic and inflammatory chronic pain models. Br J Pharmacol 2006;147:281-8
   PubMed Web of Science ®Google Scholar
• Jhaveri MD, Richardson D, Kendall DA, Analgesic effects of fatty acid amide hydrolase inhibition in a rat model of neuropathic pain. J Neurosci 2006;26:13318-27
   PubMed Web of Science ®Google Scholar
• Storr MA, Keenan CM, Emmerdinger D, Targeting endocannabinoid degradation protects against experimental colitis in mice: involvement of CB1 and CB2 receptors. J Mol Med (Berl) 2008;86:925-36
   PubMed Web of Science ®Google Scholar
• Scherma M, Medalie J, Fratta W, The endogenous cannabinoid anandamide has effects on motivation and anxiety that are revealed by fatty acid amide hydrolase (FAAH) inhibition. Neuropharmacology 2008;54:129-40
   PubMed Web of Science ®Google Scholar
• Bortolato M, Mangieri RA, Fu J, Antidepressant-like activity of the fatty acid amide hydrolase inhibitor URB597 in a rat model of chronic mild stress. Biol Psychiatry 2007;62:1103-10
   PubMed Web of Science ®Google Scholar
• Abouabdellah A, Burnier P, Hoornaert C, Derivates of piperidinyl-and piperazinyl-alkyl carbamates, preparation methods thereof and application of some in therapeutics. US20060089344; 2006
   Google Scholar
• Ahn K, Johnson DS, Mileni M, Discovery and characterization of a highly selective FAAH inhibitor that reduces inflammatory pain. Chem Biol 2009;16:411-20
   PubMed Web of Science ®Google Scholar
• Mileni M, Johnson DS, Wang Z, Structure-guided inhibitor design for human FAAH by interspecies active site conversion. Proc Natl Acad Sci USA 2008;105:12820-4
   PubMed Web of Science ®Google Scholar
• Johnson DS, Stiff C, Lazerwith SE, Discovery of PF-04457845: A highly potent, orally bioavailable, and selective urea FAAH inhibitor. ACS Med Chem Lett 2011;2:91-6
   PubMed Web of Science ®Google Scholar
• Huggins JP, Smart TS, Langman S, An efficient randomised, placebo-controlled clinical trial with the irreversible fatty acid amide hydrolase-1 inhibitor PF-04457845, which modulates endocannabinoids but fails to induce effective analgesia in patients with pain due to osteoarthritis of the knee. Pain 2012;153:1837-46
   PubMed Web of Science ®Google Scholar
• Karbarz MJ, Luo L, Chang L, Biochemical and biological properties of 4-(3-phenyl-[1,2,4] thiadiazol-5-yl)-piperazine-1-carboxylic acid phenylamide, a mechanism-based inhibitor of fatty acid amide hydrolase. Anesth Analg 2009;108:316-29
   PubMed Web of Science ®Google Scholar
• Hart T, Macias AT, Benwell K, Fatty acid amide hydrolase inhibitors. Surprising selectivity of chiral azetidine ureas. Bioorg Med Chem Lett 2009;19:4241-4
   PubMed Web of Science ®Google Scholar
• Tichenor MS, Keith JM, Jones WM, Heteroaryl urea inhibitors of fatty acid amide hydrolase: structure-mutagenicity relationships for arylamine metabolites. Bioorg Med Chem Lett 2012;22:7357-62
   PubMed Web of Science ®Google Scholar
• Alapafuja SO, Nikas SP, Bharathan IT, Sulfonyl fluoride inhibitors of Fatty Acid amide hydrolase. J Med Chem 2012;55:10074-89
   PubMed Web of Science ®Google Scholar
• Godlewski G, Alapafuja SO, Batkai S, Inhibitor of fatty acid amide hydrolase normalizes cardiovascular function in hypertension without adverse metabolic effects. Chem Biol (Cambridge, MA, U. S.) 2010;17:1256-66
   PubMed Web of Science ®Google Scholar
• Bashashati M, Storr MA, Nikas SP, Inhibiting fatty acid amide hydrolase normalizes endotoxin-induced enhanced gastrointestinal motility in mice. Br J Pharmacol 2012;165:1556-71
   PubMed Web of Science ®Google Scholar
• Di Venere A, Dainese E, Fezza F, Rat and human fatty acid amide hydrolases: overt similarities and hidden differences. Biochim Biophys Acta 2012;1821:1425-33
   PubMed Web of Science ®Google Scholar
• Li GL, Winter H, Arends R, Assessment of the pharmacology and tolerability of PF-04457845, an irreversible inhibitor of fatty acid amide hydrolase-1, in healthy subjects. Br J Clin Pharmacol 2012;73:706-16
   PubMed Web of Science ®Google Scholar
• Ahn K, Smith SE, Liimatta MB, Mechanistic and pharmacological characterization of PF-04457845: a highly potent and selective FAAH inhibitor that reduces inflammatory and noninflammatory pain. J Pharmacol Exp Ther 2011;338:114-24
   PubMed Web of Science ®Google Scholar