fatty acid amide hydrolase 3.5.1.99
Author:
Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/978-3-642-36260-6_10
Reference29 articles.
1. Patricelli, M.P.; Lashuel, H.A.; Giang, D.K.; Kelly, J.W.; Cravatt, B.F.: Comparative characterization of wild type and transmembrane domain-deleted fatty acid amide hydrolase identification of the transmembrane domain as a site for oligomerization. Biochemistry, 37, 15177-15187 (1998)
2. Vandevoorde, S.; Fowler, C.J.: Inhibition of fatty acid amide hydrolase and monoacylglycerol lipase by the anandamide uptake inhibitor VDM11: evidence that VDM11 acts as an FAAH substrate. Br. J. Pharmacol., 145, 885-893 (2005)
3. Quistad, G.B.; Klintenberg, R.; Caboni, P.; Liang, S.N.; Casida, J.E.: Monoacylglycerol lipase inhibition by organophosphorus compounds leads to elevation of brain 2-arachidonoylglycerol and the associated hypomotility in mice. Toxicol. Appl. Pharmacol., 211, 78-83 (2006)
4. Cisneros, J.A.; Vandevoorde, S.; Ortega-Gutierrez, S.; Paris, C.; Fowler, C.J.; Lopez-Rodriguez, M.L.: Structure-activity relationship of a series of inhibitors of monoacylglycerol hydrolysis - comparison with effects upon fatty acid amide hydrolase. J. Med. Chem., 50, 5012-5023 (2007)
5. Muccioli, G.G.; Xu, C.; Odah, E.; Cudaback, E.; Cisneros, J.A.; Lambert, D.M.; Lopez Rodriguez, M.L.; Bajjalieh, S.; Stella, N.: Identification of a novel endocannabinoid-hydrolyzing enzyme expressed by microglial cells. J. Neurosci., 27, 2883-2889 (2007)
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