PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
35351947-3	2022	Here, we targeted MAGL in TNBCs, using a potent carbamate-based inhibitor AM9928 (hMAGL IC50 = 9 nM) with prolonged pharmacodynamic effects (46 h of target residence time).	Carbamates	48-57	monoglyceride lipase	Homo sapiens	18-22	
21982493-6	2011	The carbamate analogue 16 displayed the most significant inhibitory activity, reducing MAGL activity to 26% of controls at 100 muM compared to 73% for the parent compound URB602.	Carbamates	4-13	monoglyceride lipase	Homo sapiens	87-91	
25282655-0	2014	Piperazine and piperidine carboxamides and carbamates as inhibitors of fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL).	Carbamates	43-53	monoglyceride lipase	Homo sapiens	109-132	
25282655-0	2014	Piperazine and piperidine carboxamides and carbamates as inhibitors of fatty acid amide hydrolase (FAAH) and monoacylglycerol lipase (MAGL).	Carbamates	43-53	monoglyceride lipase	Homo sapiens	134-138	
25282655-2	2014	In this paper, we present more extensively the results of our previous work on piperazine and piperidine carboxamides and carbamates as FAAH and MAGL inhibitors.	Carbamates	122-132	monoglyceride lipase	Homo sapiens	145-149	
23553709-7	2013	Covalent modification of membrane-associated hMGL by the irreversible carbamate inhibitor, AM6580, shielded the active site region, but did not increase solvent exposure of the lid domain, suggesting that the inactive, carbamylated enzyme remains intact and membrane associated.	Carbamates	70-79	monoglyceride lipase	Homo sapiens	45-49	
20464001-7	2010	Rapid carbamoylation of hMGL Ser122 by AM6701 and elimination of the leaving group is followed by a slow hydrolysis of the carbamate group, ultimately regenerating catalytically competent hMGL.	Carbamates	123-132	monoglyceride lipase	Homo sapiens	24-28	
20464001-7	2010	Rapid carbamoylation of hMGL Ser122 by AM6701 and elimination of the leaving group is followed by a slow hydrolysis of the carbamate group, ultimately regenerating catalytically competent hMGL.	Carbamates	123-132	monoglyceride lipase	Homo sapiens	188-192	
29148769-3	2017	Herein we describe highly efficient MAGL inhibitors, identified through a parallel medicinal chemistry approach that highlighted the improved efficiency of azetidine and piperidine-derived carbamates.	Carbamates	189-199	monoglyceride lipase	Homo sapiens	36-40	
29678535-0	2018	Design, synthesis, molecular modelling and in vitro cytotoxicity analysis of novel carbamate derivatives as inhibitors of Monoacylglycerol lipase.	Carbamates	83-92	monoglyceride lipase	Homo sapiens	122-145	
34056494-3	2021	While most of the synthesized derivatives were potent inhibitors of FAAH, a considerable inhibition of MAGL and BuChE was elicited only by compounds with a high carbamate reactivity, as evidenced by a significant hydrolysis of these compounds in an aqueous solution.	Carbamates	161-170	monoglyceride lipase	Homo sapiens	103-107	
30446439-2	2019	Herein, we report the discovery of new series of carbamates as highly potent and selective MGL inhibitors.	Carbamates	49-59	monoglyceride lipase	Homo sapiens	91-94