PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21198549-1 2011 BACKGROUND AND PURPOSE The endocannabinoid 2-arachidonoylglycerol (2-AG) is degraded primarily by monoacylglycerol lipase (MGL). Endocannabinoids 27-42 monoglyceride lipase Rattus norvegicus 98-121 28820005-2 2017 FAAH and MAGL hydrolyze the endocannabinoids anandamide (AEA) and 2-arachidonylglycerol (2-AG), respectively. Endocannabinoids 28-44 monoglyceride lipase Rattus norvegicus 9-13 27086176-4 2016 Hypertension caused an increase in the levels of endocannabinoids [anandamide (AEA), 2-arachidonoyl-glycerol (2-AG) and N-arachidonoyl-dopamine (NADA)] and CB1 receptor and the activities of FAAH and monoacylglycerol lipase (MAGL). Endocannabinoids 49-65 monoglyceride lipase Rattus norvegicus 200-223 27086176-4 2016 Hypertension caused an increase in the levels of endocannabinoids [anandamide (AEA), 2-arachidonoyl-glycerol (2-AG) and N-arachidonoyl-dopamine (NADA)] and CB1 receptor and the activities of FAAH and monoacylglycerol lipase (MAGL). Endocannabinoids 49-65 monoglyceride lipase Rattus norvegicus 225-229 26974857-4 2016 Systemically administered drugs which elevate the endocannabinoids, anandamide (AEA) and 2-arachidonoyl glycerol (2-AG), by interfering with their respective degrading enzymes, fatty acid amide hydrolase (FAAH) and monoacyl glycerol lipase (MAGL) interfere with AN in the rat model. Endocannabinoids 50-66 monoglyceride lipase Rattus norvegicus 215-239 26974857-4 2016 Systemically administered drugs which elevate the endocannabinoids, anandamide (AEA) and 2-arachidonoyl glycerol (2-AG), by interfering with their respective degrading enzymes, fatty acid amide hydrolase (FAAH) and monoacyl glycerol lipase (MAGL) interfere with AN in the rat model. Endocannabinoids 50-66 monoglyceride lipase Rattus norvegicus 241-245 23933531-3 2013 We proposed that differential inhibition of eCB-degrading enzymes (fatty acid amide hydrolase, FAAH, and monoacylglycerol lipase, MAGL) by PS and CPF leads to differences in extracellular eCB levels and toxicity. Endocannabinoids 44-47 monoglyceride lipase Rattus norvegicus 105-128 23933531-3 2013 We proposed that differential inhibition of eCB-degrading enzymes (fatty acid amide hydrolase, FAAH, and monoacylglycerol lipase, MAGL) by PS and CPF leads to differences in extracellular eCB levels and toxicity. Endocannabinoids 44-47 monoglyceride lipase Rattus norvegicus 130-134 23933531-3 2013 We proposed that differential inhibition of eCB-degrading enzymes (fatty acid amide hydrolase, FAAH, and monoacylglycerol lipase, MAGL) by PS and CPF leads to differences in extracellular eCB levels and toxicity. Endocannabinoids 188-191 monoglyceride lipase Rattus norvegicus 105-128 23933531-3 2013 We proposed that differential inhibition of eCB-degrading enzymes (fatty acid amide hydrolase, FAAH, and monoacylglycerol lipase, MAGL) by PS and CPF leads to differences in extracellular eCB levels and toxicity. Endocannabinoids 188-191 monoglyceride lipase Rattus norvegicus 130-134 21600985-0 2011 Enhancement of endocannabinoid signaling with JZL184, an inhibitor of the 2-arachidonoylglycerol hydrolyzing enzyme monoacylglycerol lipase, produces anxiolytic effects under conditions of high environmental aversiveness in rats. Endocannabinoids 15-30 monoglyceride lipase Rattus norvegicus 116-139 32527545-1 2020 Monoacylglycerol lipase (MAGL) is the enzyme that is primarily responsible for hydrolyzing the endocannabinoid 2-arachidononylglycerol (2-AG) to arachidonic acid (AA). Endocannabinoids 95-110 monoglyceride lipase Rattus norvegicus 0-23 32527545-1 2020 Monoacylglycerol lipase (MAGL) is the enzyme that is primarily responsible for hydrolyzing the endocannabinoid 2-arachidononylglycerol (2-AG) to arachidonic acid (AA). Endocannabinoids 95-110 monoglyceride lipase Rattus norvegicus 25-29 32375160-2 2020 Inhibitors of monoacylglycerol lipase (MGL), the enzyme that deactivates the endocannabinoid 2-arachidonoyl-sn-glycerol (2-AG), exert anxiolytic-like effects in rodent models via 2-AG-dependent activation of CB1 cannabinoid receptors. Endocannabinoids 77-92 monoglyceride lipase Rattus norvegicus 14-37 32375160-2 2020 Inhibitors of monoacylglycerol lipase (MGL), the enzyme that deactivates the endocannabinoid 2-arachidonoyl-sn-glycerol (2-AG), exert anxiolytic-like effects in rodent models via 2-AG-dependent activation of CB1 cannabinoid receptors. Endocannabinoids 77-92 monoglyceride lipase Rattus norvegicus 39-42 32334914-1 2020 Monoacylglycerol lipase (MAGL) has emerged as an attractive drug target because of its important role in regulating the endocannabinoid 2-arachidonoylglycerol (2-AG) and its hydrolysis product arachidonic acid (AA) in the brain. Endocannabinoids 120-135 monoglyceride lipase Rattus norvegicus 0-23 32334914-1 2020 Monoacylglycerol lipase (MAGL) has emerged as an attractive drug target because of its important role in regulating the endocannabinoid 2-arachidonoylglycerol (2-AG) and its hydrolysis product arachidonic acid (AA) in the brain. Endocannabinoids 120-135 monoglyceride lipase Rattus norvegicus 25-29 32173532-1 2020 The endocannabinoid 2-arachidonoylglycerol (2-AG) is an anti-nociceptive lipid, which is inactivated through cellular uptake and subsequent catabolism by monoacylglycerol lipase (MAGL). Endocannabinoids 4-19 monoglyceride lipase Rattus norvegicus 154-177 32173532-1 2020 The endocannabinoid 2-arachidonoylglycerol (2-AG) is an anti-nociceptive lipid, which is inactivated through cellular uptake and subsequent catabolism by monoacylglycerol lipase (MAGL). Endocannabinoids 4-19 monoglyceride lipase Rattus norvegicus 179-183 29292159-2 2018 The present study sought to determine whether this phenotype would be normalized by increasing levels of the endocannabinoid 2-arachidonoylglycerol (2-AG) using pharmacological inhibition of monoacylglycerol lipase (MAGL). Endocannabinoids 109-124 monoglyceride lipase Rattus norvegicus 191-214 29440474-1 2018 BACKGROUND AND PURPOSE: MAGL (monoacylglycerol lipase) is an enzyme that hydrolyzes the endocannabinoid 2-arachidonoylglycerol and regulates the production of arachidonic acid and prostaglandins-substances that mediate tissue inflammatory response. Endocannabinoids 88-103 monoglyceride lipase Rattus norvegicus 24-28 29440474-1 2018 BACKGROUND AND PURPOSE: MAGL (monoacylglycerol lipase) is an enzyme that hydrolyzes the endocannabinoid 2-arachidonoylglycerol and regulates the production of arachidonic acid and prostaglandins-substances that mediate tissue inflammatory response. Endocannabinoids 88-103 monoglyceride lipase Rattus norvegicus 30-53 25869205-1 2015 BACKGROUND: Recent studies showed that the pharmacological inhibition of endocannabinoid degrading enzymes such as fatty acid amide hydrolase (FAAH) and monoacyl glycerol lipase (MAGL) elicit promising analgesic effects in a variety of nociceptive models without serious side effects. Endocannabinoids 73-88 monoglyceride lipase Rattus norvegicus 153-177 25869205-1 2015 BACKGROUND: Recent studies showed that the pharmacological inhibition of endocannabinoid degrading enzymes such as fatty acid amide hydrolase (FAAH) and monoacyl glycerol lipase (MAGL) elicit promising analgesic effects in a variety of nociceptive models without serious side effects. Endocannabinoids 73-88 monoglyceride lipase Rattus norvegicus 179-183 23386378-1 2013 2-Arachidonoylglycerol (2-AG) is recognized as a potent endocannabinoid, which reduces synaptic transmission through cannabinoid CB(1) receptors, and is hydrolyzed by monoacylglycerol lipase (MGL) to arachidonic acid (AA), a cyclooxygenase substrate. Endocannabinoids 56-71 monoglyceride lipase Rattus norvegicus 167-190 23386378-1 2013 2-Arachidonoylglycerol (2-AG) is recognized as a potent endocannabinoid, which reduces synaptic transmission through cannabinoid CB(1) receptors, and is hydrolyzed by monoacylglycerol lipase (MGL) to arachidonic acid (AA), a cyclooxygenase substrate. Endocannabinoids 56-71 monoglyceride lipase Rattus norvegicus 192-195 21198549-1 2011 BACKGROUND AND PURPOSE The endocannabinoid 2-arachidonoylglycerol (2-AG) is degraded primarily by monoacylglycerol lipase (MGL). Endocannabinoids 27-42 monoglyceride lipase Rattus norvegicus 123-126 20416378-1 2010 Monoacylglycerol lipase (MGL) and fatty-acid amide hydrolase (FAAH) degrade the endocannabinoids 2-arachidonoylglycerol (2-AG) and anandamide (AEA), respectively. Endocannabinoids 80-96 monoglyceride lipase Rattus norvegicus 0-23 20416378-1 2010 Monoacylglycerol lipase (MGL) and fatty-acid amide hydrolase (FAAH) degrade the endocannabinoids 2-arachidonoylglycerol (2-AG) and anandamide (AEA), respectively. Endocannabinoids 80-96 monoglyceride lipase Rattus norvegicus 25-28 17245358-1 2007 BACKGROUND AND PURPOSE: The endocannabinoids, N-arachidonoylethanolamide (anandamide) and 2-arachidonoylglycerol (2-AG) are rapidly degraded by fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MGL). Endocannabinoids 28-44 monoglyceride lipase Rattus norvegicus 182-205 17245358-1 2007 BACKGROUND AND PURPOSE: The endocannabinoids, N-arachidonoylethanolamide (anandamide) and 2-arachidonoylglycerol (2-AG) are rapidly degraded by fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MGL). Endocannabinoids 28-44 monoglyceride lipase Rattus norvegicus 207-210 15975510-1 2005 We have previously reported that the endocannabinoid, 2-arachidonoyl-glycerol (2-AG), is hydrolyzed in rat cerebellar membranes by monoglyceride lipase (MGL)-like enzymatic activity. Endocannabinoids 37-52 monoglyceride lipase Rattus norvegicus 131-151 15975510-1 2005 We have previously reported that the endocannabinoid, 2-arachidonoyl-glycerol (2-AG), is hydrolyzed in rat cerebellar membranes by monoglyceride lipase (MGL)-like enzymatic activity. Endocannabinoids 37-52 monoglyceride lipase Rattus norvegicus 153-156