@article{oai:repo.qst.go.jp:00048787,
 author = {Cheng, Ran and Mori, Wakana and Ma, Longle and Alhouayek, Mireille and Hatori, Akiko and Zhang, Yiding and Ogasawara, Daisuke and Yuan, Gengyang and Chen, Zhen and Zhang, Xiaofei and Shi, Hang and Yamasaki, Tomoteru and Xie, Lin and Kumata, Katsushi and Fujinaga, Masayuki and Nagai, Yuji and Minamimoto, Takafumi and Svensson, Mona and Lu, Wang and Du, Yunfei and Jo Ondrechen, Mary and Vasdev, Neil and F Cravatt, Benjamin and Fowler, Christopher and Ming-Rong, Zhang and H Liang, Steven and Mori, Wakana and Hatori, Akiko and Zhang, Yiding and Yamasaki, Tomoteru and Xie, Lin and Kumata, Katsushi and Fujinaga, Masayuki and Nagai, Yuji and Minamimoto, Takafumi and Lu, Wang and Ming-Rong, Zhang and Liang, Huan},
 journal = {Journal of Medicinal Chemistry},
 month = {Feb},
 note = {Monoacylglycerol lipase (MAGL) is the principle enzyme for metabolizing the endogenous cannabinoid ligand, 2-arachidonylglycerol (2-AG). Blockade of MAGL increases 2-AG levels, resulting in subsequent activation of the endocannabinoid system, and has emerged as a novel therapeutic strategy to treat drug addiction, inflammation and neurodegenerative diseases. Herein we report a new series of MAGL inhibitors, which were radiolabeled by site-specific labeling technologies, including 11C-carbonylation and spirocyclic iodonium ylide (SCIDY) radiofluorination. The lead compound [11C]10 (MAGL-0519) demonstrated high specific binding and selectivity in vitro and in vivo. We also observed unexpected washout kinetics with these irreversible radiotracers, in which in vivo evidence for turnover of the covalent residue was unveiled between MAGL and azetidine carboxylates. This work may lead to new directions for drug discovery and PET tracer development based on azetidine carboxylate inhibitor scaffold.},
 pages = {2278--2291},
 title = {In vitro and in vivo evaluation of 11C-labeled azetidine-carboxylates for imaging monoacylglycerol lipase by PET imaging studies},
 volume = {61},
 year = {2018}
}