PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31760822-2	2020	The BF framework aims to endow the conjugate molecules with ability for inhibition of AChE (bimodal way) and of amyloid-beta peptide aggregation, besides providing metal (Fe, Cu) chelating ability and concomitant extra anti-oxidant activity, for the hybrids with hydroxyl substitution.	Hydroxyl Radical	263-271	acetylcholinesterase (Cartwright blood group)	Homo sapiens	86-90	
7256355-2	1981	Both the protonated diethylamino and phenolic hydroxyl functions of amodiaquine are necessary for interaction with AChE.	Hydroxyl Radical	46-54	acetylcholinesterase (Cartwright blood group)	Homo sapiens	115-119	
7256355-3	1981	This suggests that the inhibition of AChE by amodiaquine may involve binding of the protonated diethylamino and phenolic hydroxyl functions to the anionic and esteric sites of the enzyme respectively.	Hydroxyl Radical	121-129	acetylcholinesterase (Cartwright blood group)	Homo sapiens	37-41	
31968151-4	2020	Among this series of compounds 3m bearing one ethoxy and a hydroxyl group on the phenyl ring on 2,4,5-trisubstituted imidazoles  proved potent AChE inhibitor (102.56+-0.14).	Hydroxyl Radical	59-67	acetylcholinesterase (Cartwright blood group)	Homo sapiens	143-147	
25096900-0	2014	In vitro effect of H2O 2, some transition metals and hydroxyl radical produced via fenton and fenton-like reactions, on the catalytic activity of AChE and the hydrolysis of ACh.	Hydroxyl Radical	53-69	acetylcholinesterase (Cartwright blood group)	Homo sapiens	146-150