PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
20464001-0	2010	Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism.	Hydrogen	76-84	monoglyceride lipase	Homo sapiens	107-130	
20464001-0	2010	Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism.	Hydrogen	76-84	monoglyceride lipase	Homo sapiens	132-136	
20464001-0	2010	Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism.	Hydrogen	76-84	monoglyceride lipase	Homo sapiens	156-160	
20464001-6	2010	hMGL inhibition by AM6701 alters this hydrogen-bonding pattern through subtle active-site structural rearrangements without influencing hydrogen-bond occupancies.	Hydrogen	38-46	monoglyceride lipase	Homo sapiens	0-4	
20464001-8	2010	In contrast, hMGL titration with NAM, which leads to cysteine alkylation, stoichiometrically decreases the population of the active-site hydrogen bonds.	Hydrogen	137-145	monoglyceride lipase	Homo sapiens	13-17	
20464001-10	2010	These data provide detailed molecular insight into the distinctive mechanisms of two covalent hMGL inhibitors and implicate a hydrogen-bond network as a structural feature of hMGL catalytic function.	Hydrogen	126-134	monoglyceride lipase	Homo sapiens	94-98	
20464001-10	2010	These data provide detailed molecular insight into the distinctive mechanisms of two covalent hMGL inhibitors and implicate a hydrogen-bond network as a structural feature of hMGL catalytic function.	Hydrogen	126-134	monoglyceride lipase	Homo sapiens	175-179