{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,15]],"date-time":"2026-10-15T20:24:42Z","timestamp":1792095882179,"version":"4.4.0"},"reference-count":113,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2020,4,1]],"date-time":"2020-04-01T00:00:00Z","timestamp":1585699200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,4,1]],"date-time":"2020-04-01T00:00:00Z","timestamp":1585699200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2019,10,15]],"date-time":"2019-10-15T00:00:00Z","timestamp":1571097600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21807076"],"award-info":[{"award-number":["21807076"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Acta Pharmaceutica Sinica B"],"published-print":{"date-parts":[[2020,4]]},"DOI":"10.1016\/j.apsb.2019.10.006","type":"journal-article","created":{"date-parts":[[2019,10,18]],"date-time":"2019-10-18T19:32:06Z","timestamp":1571427126000},"page":"582-602","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":165,"title":["Monoacylglycerol lipase inhibitors: modulators for lipid metabolism in cancer malignancy, neurological and metabolic disorders"],"prefix":"10.1016","volume":"10","author":[{"given":"Hui","family":"Deng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weimin","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.apsb.2019.10.006_bib1","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1172\/JCI104705","article-title":"Demonstration of an intestinal monoglyceride lipase: an enzyme with a possible role in the intracellular completion of fat digestion","volume":"42","author":"Senior","year":"1963","journal-title":"J Clin Invest"},{"key":"10.1016\/j.apsb.2019.10.006_bib2","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S0021-9258(18)51692-6","article-title":"Hormone-sensitive lipase and monoglyceride lipase activities in adipose tissue","volume":"239","author":"Vaughan","year":"1964","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib3","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1016\/S0022-2275(20)39286-5","article-title":"Partial purification of monoglyceride lipase from adipose tissue","volume":"7","author":"Kupiecki","year":"1966","journal-title":"J Lipid Res"},{"key":"10.1016\/j.apsb.2019.10.006_bib4","doi-asserted-by":"crossref","first-page":"27218","DOI":"10.1074\/jbc.272.43.27218","article-title":"cDNA cloning, tissue distribution, and identification of the catalytic triad of monoglyceride lipase. Evolutionary relationship to esterases, lysophospholipases, and haloperoxidases","volume":"272","author":"Karlsson","year":"1997","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib5","doi-asserted-by":"crossref","first-page":"10819","DOI":"10.1073\/pnas.152334899","article-title":"Brain monoglyceride lipase participating in endocannabinoid inactivation","volume":"99","author":"Dinh","year":"2002","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.apsb.2019.10.006_bib6","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1016\/j.tips.2015.02.008","article-title":"Endocannabinoid signaling at the periphery: 50 years after THC","volume":"36","author":"Maccarrone","year":"2015","journal-title":"Trends Pharmacol Sci"},{"key":"10.1016\/j.apsb.2019.10.006_bib7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.plipres.2018.05.002","article-title":"2-Arachidonoylglycerol: a signaling lipid with manifold actions in the brain","volume":"71","author":"Baggelaar","year":"2018","journal-title":"Prog Lipid Res"},{"key":"10.1016\/j.apsb.2019.10.006_bib8","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1126\/science.1209200","article-title":"Endocannabinoid hydrolysis generates brain prostaglandins that promote neuroinflammation","volume":"334","author":"Nomura","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.apsb.2019.10.006_bib9","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1038\/nchembio.129","article-title":"Selective blockade of 2-arachidonoylglycerol hydrolysis produces cannabinoid behavioral effects","volume":"5","author":"Long","year":"2009","journal-title":"Nat Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib10","doi-asserted-by":"crossref","first-page":"996","DOI":"10.1124\/mol.110.068304","article-title":"Monoacylglycerol lipase activity is a critical modulator of the tone and integrity of the endocannabinoid system","volume":"78","author":"Chanda","year":"2010","journal-title":"Mol Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib11","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1038\/nn.2616","article-title":"Chronic monoacylglycerol lipase blockade causes functional antagonism of the endocannabinoid system","volume":"13","author":"Schlosburg","year":"2010","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.apsb.2019.10.006_bib12","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1111\/j.1476-5381.2010.00735.x","article-title":"The endocannabinoid system as a target for the treatment of neurodegenerative disease","volume":"160","author":"Glass","year":"2010","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib13","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1038\/sj.bjp.0704110","article-title":"The synthetic cannabinoid WIN55, 212-2 attenuates hyperalgesia and allodynia in a rat model of neuropathic pain","volume":"133","author":"Bridges","year":"2001","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib14","doi-asserted-by":"crossref","first-page":"10529","DOI":"10.1073\/pnas.1834309100","article-title":"Activation of CB2 cannabinoid receptors by AM1241 inhibits experimental neuropathic pain: pain inhibition by receptors not present in the CNS","volume":"100","author":"Ibrahim","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.apsb.2019.10.006_bib15","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1124\/jpet.110.175778","article-title":"Inhibition of monoacylglycerol lipase attenuates nonsteroidal anti-inflammatory drug-induced gastric hemorrhages in mice","volume":"338","author":"Kinsey","year":"2011","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/j.apsb.2019.10.006_bib16","doi-asserted-by":"crossref","first-page":"1609","DOI":"10.1111\/j.1476-5381.2012.02179.x","article-title":"Spinal administration of the monoacylglycerol lipase inhibitor JZL184 produces robust inhibitory effects on nociceptive processing and the development of central sensitization in the rat","volume":"167","author":"Woodhams","year":"2012","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib17","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1194\/jlr.M058586","article-title":"Global deletion of MGL in mice delays lipid absorption and alters energy homeostasis and diet-induced obesity","volume":"56","author":"Douglass","year":"2015","journal-title":"J Lipid Res"},{"key":"10.1016\/j.apsb.2019.10.006_bib18","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.cell.2009.11.027","article-title":"Monoacylglycerol lipase regulates a fatty acid network that promotes cancer pathogenesis","volume":"140","author":"Nomura","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.apsb.2019.10.006_bib19","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.bbrc.2005.09.015","article-title":"Influence of the degree of unsaturation of the acyl side chain upon the interaction of analogues of 1-arachidonoylglycerol with monoacylglycerol lipase and fatty acid amide hydrolase","volume":"337","author":"Vandevoorde","year":"2005","journal-title":"Biochem Biophys Res Commun"},{"key":"10.1016\/j.apsb.2019.10.006_bib20","doi-asserted-by":"crossref","first-page":"1382","DOI":"10.1189\/jlb.0307180","article-title":"Cannabinoid-2 receptor agonist HU-308 protects against hepatic ischemia\/reperfusion injury by attenuating oxidative stress, inflammatory response, and apoptosis","volume":"82","author":"Rajesh","year":"2007","journal-title":"J Leukoc Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib21","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/28393","article-title":"Control of pain initiation by endogenous cannabinoids","volume":"394","author":"Calignano","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.apsb.2019.10.006_bib22","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.clim.2011.02.010","article-title":"Neuroprotective agents: cannabinoids","volume":"142","author":"S\u00e1nchez","year":"2012","journal-title":"Clin Immunol"},{"key":"10.1016\/j.apsb.2019.10.006_bib23","doi-asserted-by":"crossref","first-page":"822","DOI":"10.1038\/35071088","article-title":"Leptin-regulated endocannabinoids are involved in maintaining food intake","volume":"410","author":"Di Marzo","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.apsb.2019.10.006_bib24","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.tins.2006.01.008","article-title":"Involvement of the endocannabinoid system in drug addiction","volume":"29","author":"Maldonado","year":"2006","journal-title":"Trends Neurosci"},{"key":"10.1016\/j.apsb.2019.10.006_bib25","doi-asserted-by":"crossref","first-page":"5899","DOI":"10.1021\/cr2002799","article-title":"Endocannabinoid oxygenation by cyclooxygenases, lipoxygenases, and cytochromes P450: cross-talk between the eicosanoid and endocannabinoid signaling pathways","volume":"111","author":"Rouzer","year":"2011","journal-title":"Chem Rev"},{"key":"10.1016\/j.apsb.2019.10.006_bib26","doi-asserted-by":"crossref","first-page":"17558","DOI":"10.1073\/pnas.1314017110","article-title":"Implication of the anti-inflammatory bioactive lipid prostaglandin D2-glycerol ester in the control of macrophage activation and inflammation by ABHD6","volume":"110","author":"Alhouayek","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.apsb.2019.10.006_bib27","doi-asserted-by":"crossref","first-page":"744","DOI":"10.1016\/j.chembiol.2009.05.009","article-title":"Characterization of monoacylglycerol lipase inhibition reveals differences in central and peripheral endocannabinoid metabolism","volume":"16","author":"Long","year":"2009","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib28","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1038\/nrc1143","article-title":"The emerging role of lysophosphatidic acid in cancer","volume":"3","author":"Mills","year":"2003","journal-title":"Nat Rev Cancer"},{"key":"10.1016\/j.apsb.2019.10.006_bib29","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1002\/cbic.200900621","article-title":"Crystal structure of the human monoacylglycerol lipase, a key actor in endocannabinoid signaling","volume":"11","author":"Labar","year":"2010","journal-title":"ChemBioChem"},{"key":"10.1016\/j.apsb.2019.10.006_bib30","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1002\/pro.596","article-title":"Crystal structure of a soluble form of human monoglyceride lipase in complex with an inhibitor at 1.35 \u00c5 resolution","volume":"20","author":"Schalk-Hihi","year":"2011","journal-title":"Protein Sci"},{"key":"10.1016\/j.apsb.2019.10.006_bib31","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1080\/13543776.2018.1389899","article-title":"A patent review of monoacylglycerol lipase (MAGL) inhibitors (2013\u20132017)","volume":"27","author":"Granchi","year":"2017","journal-title":"Expert Opin Ther Pat"},{"key":"10.1016\/j.apsb.2019.10.006_bib32","doi-asserted-by":"crossref","first-page":"231","DOI":"10.2174\/156802608783498032","article-title":"The medicinal chemistry of agents targeting monoacylglycerol lipase","volume":"8","author":"Viso","year":"2008","journal-title":"Curr Top Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib33","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1016\/S0021-9258(17)33857-7","article-title":"Purification and some properties of a monoacylglycerol-hydrolyzing enzyme of rat adipose tissue","volume":"251","author":"Tornqvist","year":"1976","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib34","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1111\/j.1476-5381.2009.00276.x","article-title":"A critical cysteine residue in monoacylglycerol lipase is targeted by a new class of isothiazolinone-based enzyme inhibitors","volume":"157","author":"King","year":"2009","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib35","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1038\/sj.bjp.0705948","article-title":"Inhibition of monoacylglycerol lipase and fatty acid amide hydrolase by analogues of 2-arachidonoylglycerol","volume":"143","author":"Ghafouri","year":"2004","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib36","doi-asserted-by":"crossref","first-page":"2113","DOI":"10.1046\/j.1471-4159.1999.0722113.x","article-title":"Phosphatidic acid as the biosynthetic precursor of the endocannabinoid 2-arachidonoylglycerol in intact mouse neuroblastoma cells stimulated with ionomycin","volume":"72","author":"Bisogno","year":"1999","journal-title":"J Neurochem"},{"key":"10.1016\/j.apsb.2019.10.006_bib37","doi-asserted-by":"crossref","first-page":"1347","DOI":"10.1016\/j.chembiol.2007.11.006","article-title":"A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol","volume":"14","author":"Blankman","year":"2007","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib38","doi-asserted-by":"crossref","first-page":"1260","DOI":"10.1124\/mol.104.002071","article-title":"RNA interference suggests a primary role for monoacylglycerol lipase in the degradation of the endocannabinoid 2-arachidonoylglycerol","volume":"66","author":"Dinh","year":"2004","journal-title":"Mol Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib39","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/S0014-5793(97)01603-7","article-title":"Anandamide amidohydrolase reacting with 2-arachidonoylglycerol, another cannabinoid receptor ligand","volume":"422","author":"Goparaju","year":"1998","journal-title":"FEBS Lett"},{"key":"10.1016\/j.apsb.2019.10.006_bib40","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1124\/mol.114.094284","article-title":"Robust hydrolysis of prostaglandin glycerol esters by human monoacylglycerol lipase (MAGL)","volume":"86","author":"Savinainen","year":"2014","journal-title":"Mol Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib41","doi-asserted-by":"crossref","first-page":"11865","DOI":"10.1074\/jbc.M115.705541","article-title":"Monoacylglycerol lipases act as evolutionarily conserved regulators of non-oxidative ethanol metabolism","volume":"291","author":"Heier","year":"2016","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib42","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1111\/j.1460-9568.2004.03428.x","article-title":"Segregation of two endocannabinoid-hydrolyzing enzymes into pre- and postsynaptic compartments in the rat hippocampus, cerebellum and amygdala","volume":"20","author":"Gulyas","year":"2004","journal-title":"Eur J Neurosci"},{"key":"10.1016\/j.apsb.2019.10.006_bib43","doi-asserted-by":"crossref","first-page":"2588","DOI":"10.2174\/092986710791859414","article-title":"A review on the monoacylglycerol lipase: at the interface between fat and endocannabinoid signalling","volume":"17","author":"Labar","year":"2010","journal-title":"Curr Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib44","doi-asserted-by":"crossref","first-page":"4847","DOI":"10.1113\/jphysiol.2011.215509","article-title":"Genetic deletion of monoacylglycerol lipase alters endocannabinoid-mediated retrograde synaptic depression in the cerebellum","volume":"589","author":"Zhong","year":"2011","journal-title":"J Physiol"},{"key":"10.1016\/j.apsb.2019.10.006_bib45","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1074\/jbc.M115.683615","article-title":"Deletion of monoglyceride lipase in astrocytes attenuates lipopolysaccharide-induced neuroinflammation","volume":"291","author":"Grabner","year":"2016","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib46","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1038\/nn.2601","article-title":"The serine hydrolase ABHD6 controls the accumulation and efficacy of 2-AG at cannabinoid receptors","volume":"13","author":"Marrs","year":"2010","journal-title":"Nat Neurosci"},{"key":"10.1016\/j.apsb.2019.10.006_bib47","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1038\/37635","article-title":"Reduced fertility and postischaemic brain injury in mice deficient in cytosolic phospholipase A2","volume":"390","author":"Bonventre","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.apsb.2019.10.006_bib48","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1146\/annurev-psych-113011-143739","article-title":"The endocannabinoid system and the brain","volume":"64","author":"Mechoulam","year":"2013","journal-title":"Annu Rev Psychol"},{"key":"10.1016\/j.apsb.2019.10.006_bib49","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1189\/jlb.3RU0115-021R","article-title":"Regulation of inflammation by cannabinoids, the endocannabinoids 2-arachidonoyl-glycerol and arachidonoyl-ethanolamide, and their metabolites","volume":"97","author":"Turcotte","year":"2015","journal-title":"J Leukoc Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib50","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1016\/j.cell.2010.02.016","article-title":"Mechanisms underlying inflammation in neurodegeneration","volume":"140","author":"Glass","year":"2010","journal-title":"Cell"},{"key":"10.1016\/j.apsb.2019.10.006_bib51","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1038\/nri1602","article-title":"Cannabinoid-based drugs as anti-inflammatory therapeutics","volume":"5","author":"Klein","year":"2005","journal-title":"Nat Rev Immunol"},{"key":"10.1016\/j.apsb.2019.10.006_bib52","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1097\/MOG.0b013e32833e91eb","article-title":"NSAID-induced gastrointestinal and cardiovascular injury","volume":"26","author":"Ng","year":"2010","journal-title":"Curr Opin Gastroenterol"},{"key":"10.1016\/j.apsb.2019.10.006_bib53","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1126\/science.1224398","article-title":"Physiology: COX-2 inhibitors and cardiovascular risk","volume":"336","author":"Cannon","year":"2012","journal-title":"Science"},{"key":"10.1016\/j.apsb.2019.10.006_bib54","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/j.celrep.2012.05.001","article-title":"A dysregulated endocannabinoid\u2013eicosanoid network supports pathogenesis in a mouse model of Alzheimer's disease","volume":"1","author":"Piro","year":"2012","journal-title":"Cell Rep"},{"key":"10.1016\/j.apsb.2019.10.006_bib55","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1016\/j.molmed.2011.05.002","article-title":"Energy balance regulation by endocannabinoids at central and peripheral levels","volume":"17","author":"Quarta","year":"2011","journal-title":"Trends Mol Med"},{"key":"10.1016\/j.apsb.2019.10.006_bib56","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1172\/JCI17725","article-title":"The endogenous cannabinoid system affects energy balance via central orexigenic drive and peripheral lipogenesis","volume":"112","author":"Cota","year":"2003","journal-title":"J Clin Invest"},{"key":"10.1016\/j.apsb.2019.10.006_bib57","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.cmet.2010.02.015","article-title":"CB1 signaling in forebrain and sympathetic neurons is a key determinant of endocannabinoid actions on energy balance","volume":"11","author":"Quarta","year":"2010","journal-title":"Cell Metab"},{"key":"10.1016\/j.apsb.2019.10.006_bib58","doi-asserted-by":"crossref","first-page":"1706","DOI":"10.1016\/S0140-6736(07)61721-8","article-title":"Efficacy and safety of the weight-loss drug rimonabant: a meta-analysis of randomised trials","volume":"370","author":"Christensen","year":"2007","journal-title":"Lancet"},{"key":"10.1016\/j.apsb.2019.10.006_bib59","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0149008","article-title":"Inhibition of monoacylglycerol lipase activity decreases glucose-stimulated insulin secretion in INS-1 (832\/13) cells and rat islets","volume":"11","author":"Berdan","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.apsb.2019.10.006_bib60","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1016\/j.chembiol.2011.05.009","article-title":"Monoacylglycerol lipase exerts dual control over endocannabinoid and fatty acid pathways to support prostate cancer","volume":"18","author":"Nomura","year":"2011","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib61","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.canlet.2011.03.007","article-title":"Monoacylglycerol lipase (MAGL) knockdown inhibits tumor cells growth in colorectal cancer","volume":"307","author":"Ye","year":"2011","journal-title":"Cancer Lett"},{"key":"10.1016\/j.apsb.2019.10.006_bib62","doi-asserted-by":"crossref","first-page":"35784","DOI":"10.1038\/srep35784","article-title":"Monoacylglycerol lipase: a novel potential therapeutic target and prognostic indicator for hepatocellular carcinoma","volume":"6","author":"Zhang","year":"2016","journal-title":"Sci Rep"},{"key":"10.1016\/j.apsb.2019.10.006_bib63","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1186\/s13045-016-0361-3","article-title":"Monoacylglycerol lipase promotes progression of hepatocellular carcinoma via NF-\u03baB-mediated epithelial-mesenchymal transition","volume":"9","author":"Zhu","year":"2016","journal-title":"J Hematol Oncol"},{"key":"10.1016\/j.apsb.2019.10.006_bib64","doi-asserted-by":"crossref","first-page":"2425","DOI":"10.1111\/j.1476-5381.2011.01407.x","article-title":"Inhibition of monoacylglycerol lipase attenuates vomiting in Suncus murinus and 2-arachidonoyl glycerol attenuates nausea in rats","volume":"165","author":"Sticht","year":"2012","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib65","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3109\/14756366.2015.1010530","article-title":"4-Aryliden-2-methyloxazol-5(4H)-one as a new scaffold for selective reversible MAGL inhibitors","volume":"31","author":"Granchi","year":"2016","journal-title":"J Enzyme Inhib Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib66","doi-asserted-by":"crossref","first-page":"9860","DOI":"10.1021\/acs.jmedchem.7b01531","article-title":"Azetidine and piperidine carbamates as efficient, covalent inhibitors of monoacylglycerol lipase","volume":"60","author":"Butler","year":"2017","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib67","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1002\/cbic.200700139","article-title":"Disulfiram is an inhibitor of human purified monoacylglycerol lipase, the enzyme regulating 2-arachidonoylglycerol signaling","volume":"8","author":"Labar","year":"2007","journal-title":"ChemBioChem"},{"key":"10.1016\/j.apsb.2019.10.006_bib68","doi-asserted-by":"crossref","first-page":"7642","DOI":"10.1038\/srep07642","article-title":"Selective blockade of the hydrolysis of the endocannabinoid 2-arachidonoylglycerol impairs learning and memory performance while producing antinociceptive activity in rodents","volume":"5","author":"Griebel","year":"2015","journal-title":"Sci Rep"},{"key":"10.1016\/j.apsb.2019.10.006_bib69","doi-asserted-by":"crossref","first-page":"1357","DOI":"10.1016\/j.chembiol.2007.10.017","article-title":"URB602 inhibits monoacylglycerol lipase and selectively blocks 2-arachidonoylglycerol degradation in intact brain slices","volume":"14","author":"King","year":"2007","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib70","doi-asserted-by":"crossref","first-page":"9205","DOI":"10.1021\/acs.jmedchem.8b00824","article-title":"Design, synthesis, and evaluation of piperazinyl pyrrolidin-2-ones as a novel series of reversible monoacylglycerol lipase inhibitors","volume":"61","author":"Aida","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib71","doi-asserted-by":"crossref","first-page":"2413","DOI":"10.1194\/jlr.M030411","article-title":"Biochemical and pharmacological characterization of human \u03b1\/\u03b2-hydrolase domain containing 6 (ABHD6) and 12 (ABHD12)","volume":"53","author":"Navia-Paldanius","year":"2012","journal-title":"J Lipid Res"},{"key":"10.1016\/j.apsb.2019.10.006_bib72","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1146\/annurev.biochem.75.101304.124125","article-title":"Activity-based protein profiling: from enzyme chemistry to proteomic chemistry","volume":"77","author":"Cravatt","year":"2008","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.apsb.2019.10.006_bib73","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1146\/annurev-biochem-060713-035708","article-title":"Enzyme inhibitor discovery by activity-based protein profiling","volume":"83","author":"Niphakis","year":"2014","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.apsb.2019.10.006_bib74","doi-asserted-by":"crossref","first-page":"14694","DOI":"10.1073\/pnas.96.26.14694","article-title":"Activity-based protein profiling: the serine hydrolases","volume":"96","author":"Liu","year":"1999","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.apsb.2019.10.006_bib75","doi-asserted-by":"crossref","first-page":"1590","DOI":"10.1021\/cb400261h","article-title":"Proteome-wide reactivity profiling identifies diverse carbamate chemotypes tuned for serine hydrolase inhibition","volume":"8","author":"Chang","year":"2013","journal-title":"ACS Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib76","doi-asserted-by":"crossref","first-page":"9062","DOI":"10.1021\/acs.jmedchem.8b00951","article-title":"Identification of ABX-1431, a selective inhibitor of monoacylglycerol lipase and clinical candidate for treatment of neurological disorders","volume":"61","author":"Cisar","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib77","series-title":"Enzyme inhibition and bioapplications","author":"Sharma","year":"2012"},{"key":"10.1016\/j.apsb.2019.10.006_bib78","doi-asserted-by":"crossref","first-page":"13019","DOI":"10.1021\/bi701378g","article-title":"Novel mechanistic class of fatty acid amide hydrolase inhibitors with remarkable selectivity","volume":"46","author":"Ahn","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.apsb.2019.10.006_bib79","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1016\/j.chembiol.2005.04.013","article-title":"Characterization of the sulfhydryl-sensitive site in the enzyme responsible for hydrolysis of 2-arachidonoyl-glycerol in rat cerebellar membranes","volume":"12","author":"Saario","year":"2005","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib80","doi-asserted-by":"crossref","first-page":"7410","DOI":"10.1021\/jm900461w","article-title":"Synthesis and in\u00a0vitro evaluation of N-substituted maleimide derivatives as selective monoglyceride lipase inhibitors","volume":"52","author":"Matuszak","year":"2009","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib81","doi-asserted-by":"crossref","first-page":"7310","DOI":"10.1021\/jm901323s","article-title":"Bis(dialkylaminethiocarbonyl)disulfides as potent and selective monoglyceride lipase inhibitors","volume":"52","author":"Kapanda","year":"2009","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib82","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.1038\/nature03658","article-title":"An endocannabinoid mechanism for stress-induced analgesia","volume":"435","author":"Hohmann","year":"2005","journal-title":"Nature"},{"key":"10.1016\/j.apsb.2019.10.006_bib83","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1016\/j.chembiol.2013.01.012","article-title":"Piperazine and piperidine triazole ureas as ultrapotent and highly selective inhibitors of monoacylglycerol lipase","volume":"20","author":"Aaltonen","year":"2013","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib84","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.chembiol.2012.03.009","article-title":"Highly selective inhibitors of monoacylglycerol lipase bearing a reactive group that is bioisosteric with endocannabinoid substrates","volume":"19","author":"Chang","year":"2012","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib85","doi-asserted-by":"crossref","first-page":"1322","DOI":"10.1021\/cn400116z","article-title":"Evaluation of NHS carbamates as a potent and selective class of endocannabinoid hydrolase inhibitors","volume":"4","author":"Niphakis","year":"2013","journal-title":"ACS Chem Neurosci"},{"key":"10.1016\/j.apsb.2019.10.006_bib86","doi-asserted-by":"crossref","first-page":"3008","DOI":"10.1021\/acs.jmedchem.8b00070","article-title":"Discovery of trifluoromethyl glycol carbamates as potent and selective covalent monoacylglycerol lipase (MAGL) inhibitors for treatment of neuroinflammation","volume":"61","author":"McAllister","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib87","doi-asserted-by":"crossref","first-page":"6260","DOI":"10.1016\/j.bmc.2012.09.011","article-title":"Development and characterization of endocannabinoid hydrolases FAAH and MAGL inhibitors bearing a benzotriazol-1-yl carboxamide scaffold","volume":"20","author":"Morera","year":"2012","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib88","doi-asserted-by":"crossref","first-page":"5774","DOI":"10.1021\/jm3006004","article-title":"Synthesis and pharmacological evaluation of 2,4-dinitroaryldithiocarbamate derivatives as novel monoacylglycerol lipase inhibitors","volume":"55","author":"Kapanda","year":"2012","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib89","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.bbalip.2008.10.007","article-title":"Development of a potent inhibitor of 2-arachidonoylglycerol hydrolysis with antinociceptive activity in\u00a0vivo","volume":"1791","author":"Bisogno","year":"2009","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.apsb.2019.10.006_bib90","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1016\/j.chembiol.2009.09.012","article-title":"Discovery of potent and reversible monoacylglycerol lipase inhibitors","volume":"16","author":"King","year":"2009","journal-title":"Chem Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib91","doi-asserted-by":"crossref","first-page":"13765","DOI":"10.1002\/anie.201407807","article-title":"A reversible and selective inhibitor of monoacylglycerol lipase ameliorates multiple sclerosis","volume":"53","author":"Hern\u00e1ndez-Torres","year":"2014","journal-title":"Angew Chem Int Ed Engl"},{"key":"10.1016\/j.apsb.2019.10.006_bib92","doi-asserted-by":"crossref","first-page":"10299","DOI":"10.1021\/acs.jmedchem.6b01459","article-title":"Structural optimization of 4-chlorobenzoylpiperidine derivatives for the development of potent, reversible, and selective monoacylglycerol lipase (MAGL) inhibitors","volume":"59","author":"Granchi","year":"2016","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib93","doi-asserted-by":"crossref","first-page":"1932","DOI":"10.1021\/acs.jmedchem.8b01483","article-title":"Optimization of a benzoylpiperidine class identifies a highly potent and selective reversible monoacylglycerol lipase (MAGL) inhibitor","volume":"62","author":"Granchi","year":"2019","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib94","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1038\/sj.bjp.0706971","article-title":"Lack of selectivity of URB602 for 2-oleoylglycerol compared to anandamide hydrolysis in\u00a0vitro","volume":"150","author":"Vandevoorde","year":"2007","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib95","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1124\/jpet.112.201426","article-title":"Repeated low-dose administration of the monoacylglycerol lipase inhibitor JZL184 retains cannabinoid receptor type 1-mediated antinociceptive and gastroprotective effects","volume":"345","author":"Kinsey","year":"2013","journal-title":"J Pharmacol Exp Ther"},{"key":"10.1016\/j.apsb.2019.10.006_bib96","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1002\/hipo.22344","article-title":"Blockade of 2-arachidonoylglycerol hydrolysis produces antidepressant-like effects and enhances adult hippocampal neurogenesis and synaptic plasticity","volume":"25","author":"Zhang","year":"2015","journal-title":"Hippocampus"},{"key":"10.1016\/j.apsb.2019.10.006_bib97","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.neuropharm.2014.12.001","article-title":"Comparative biochemical characterization of the monoacylglycerol lipase inhibitor KML29 in brain, spinal cord, liver, spleen, fat and muscle tissue","volume":"91","author":"Pasquarelli","year":"2015","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.apsb.2019.10.006_bib98","doi-asserted-by":"crossref","first-page":"1392","DOI":"10.1111\/bph.12298","article-title":"In\u00a0vivo characterization of the highly selective monoacylglycerol lipase inhibitor KML29: antinociceptive activity without cannabimimetic side effects","volume":"171","author":"Ignatowska-Jankowska","year":"2014","journal-title":"Br J Pharmacol"},{"key":"10.1016\/j.apsb.2019.10.006_bib99","doi-asserted-by":"crossref","first-page":"9059","DOI":"10.1021\/acs.jmedchem.8b01405","article-title":"Activity-based protein profiling delivers selective drug candidate ABX-1431, a monoacylglycerol lipase inhibitor, to control lipid metabolism in neurological disorders","volume":"61","author":"Jiang","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib100","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/j.jmb.2009.11.060","article-title":"Structural basis for human monoglyceride lipase inhibition","volume":"396","author":"Bertrand","year":"2010","journal-title":"J Mol Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib101","doi-asserted-by":"crossref","first-page":"1436","DOI":"10.1016\/j.bmcl.2015.02.037","article-title":"Loratadine analogues as MAGL inhibitors","volume":"25","author":"Patel","year":"2015","journal-title":"Bioorg Med Chem Lett"},{"key":"10.1016\/j.apsb.2019.10.006_bib102","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1083\/jcb.200305129","article-title":"Cloning of the first sn1-DAG lipases points to the spatial and temporal regulation of endocannabinoid signaling in the brain","volume":"163","author":"Bisogno","year":"2003","journal-title":"J Cell Biol"},{"key":"10.1016\/j.apsb.2019.10.006_bib103","doi-asserted-by":"crossref","first-page":"6970","DOI":"10.1021\/jm800978m","article-title":"Tetrahydrolipstatin analogues as modulators of endocannabinoid 2-arachidonoylglycerol metabolism","volume":"51","author":"Ortar","year":"2008","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib104","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/0005-2760(88)90260-3","article-title":"Mode of action of tetrahydrolipstatin: a derivative of the naturally occurring lipase inhibitor lipstatin","volume":"962","author":"Borgstrom","year":"1988","journal-title":"Biochim Biophys Acta"},{"key":"10.1016\/j.apsb.2019.10.006_bib105","doi-asserted-by":"crossref","first-page":"2021","DOI":"10.1016\/S0021-9258(18)52203-1","article-title":"The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase","volume":"266","author":"Hadv\u00e1ry","year":"1991","journal-title":"J Biol Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib106","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/S0009-2797(97)00079-3","article-title":"Influence of quinone methide reactivity on the alkylation of thiol and amino groups in proteins: studies utilizing amino acid and peptide models","volume":"107","author":"Bolton","year":"1997","journal-title":"Chem Biol Interact"},{"key":"10.1016\/j.apsb.2019.10.006_bib107","series-title":"Heteroaromatic and aromatic piperazinyl azetidinyl amides as monoacyglycerol lipase inhibitors","author":"Janssen Pharmaceutica","year":"2010"},{"key":"10.1016\/j.apsb.2019.10.006_bib108","series-title":"Heteroaromatic and aromatic piperazinyl azetidinyl amides as monoacyglycerol lipase inhibitors","author":"Janssen Pharmaceutica","year":"2010"},{"key":"10.1016\/j.apsb.2019.10.006_bib109","series-title":"Monoacylglycerol lipase inhibitors for the treatment of metabolic diseases and related disorders","author":"Janssen Pharmaceutica","year":"2013"},{"key":"10.1016\/j.apsb.2019.10.006_bib110","series-title":"Piperidin-4-yl-azetidine diamides as monoacylglycerol lipase inhibitors","author":"Connolly","year":"2012"},{"key":"10.1016\/j.apsb.2019.10.006_bib111","doi-asserted-by":"crossref","first-page":"3285","DOI":"10.1016\/j.bmc.2014.04.057","article-title":"Identification and characterization of a new reversible MAGL inhibitor","volume":"22","author":"Tuccinardi","year":"2014","journal-title":"Bioorg Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib112","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1021\/acs.jmedchem.7b01845","article-title":"Discovery of 1,5-diphenylpyrazole-3-carboxamide derivatives as potent, reversible, and selective monoacylglycerol lipase (MAGL) inhibitors","volume":"61","author":"Aghazadeh Tabrizi","year":"2018","journal-title":"J Med Chem"},{"key":"10.1016\/j.apsb.2019.10.006_bib113","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1126\/science.aaf7497","article-title":"Activity-based protein profiling reveals off-target proteins of the FAAH inhibitor BIA 10-2474","volume":"356","author":"van Esbroeck","year":"2017","journal-title":"Science"}],"container-title":["Acta Pharmaceutica Sinica B"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211383519305003?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2211383519305003?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,31]],"date-time":"2025-10-31T16:42:25Z","timestamp":1761928945000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2211383519305003"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,4]]},"references-count":113,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2020,4]]}},"alternative-id":["S2211383519305003"],"URL":"https:\/\/doi.org\/10.1016\/j.apsb.2019.10.006","relation":{},"ISSN":["2211-3835"],"issn-type":[{"value":"2211-3835","type":"print"}],"subject":[],"published":{"date-parts":[[2020,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Monoacylglycerol lipase inhibitors: modulators for lipid metabolism in cancer malignancy, neurological and metabolic disorders","name":"articletitle","label":"Article Title"},{"value":"Acta Pharmaceutica Sinica B","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.apsb.2019.10.006","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Chinese Pharmaceutical Association and Institute of Materia Medica, Chinese Academy of Medical Sciences. Production and hosting by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}