PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9871776-1	1998	Based upon modeling results obtained using the crystal structure of huperzine A in complex with acetylcholinesterase (AChE), two novel analogues of this potent AChE inhibitor were designed with phenol or catechol rings replacing the pyridone ring.	Phenol	194-200	acetylcholinesterase (Cartwright blood group)	Homo sapiens	118-122	
9871776-1	1998	Based upon modeling results obtained using the crystal structure of huperzine A in complex with acetylcholinesterase (AChE), two novel analogues of this potent AChE inhibitor were designed with phenol or catechol rings replacing the pyridone ring.	Phenol	194-200	acetylcholinesterase (Cartwright blood group)	Homo sapiens	160-164	
12207238-4	2002	When phenyl acetate was used as substrate for AChE activity the phenol generated by enzymatic hydrolysis was determined with a second enzyme, tyrosinase.	Phenol	64-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	46-50	
33557647-4	2021	Molecular docking study showed that 23 binds to the active site of AChE and interacts via extensive pi-pi stacking with the indole and phenol side chains of Trp86 and Tyr337, besides the hydrogen bonding with the hydration site and pi-pi interaction with the phenol side chain of Y72.	Phenol	135-141	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-71	
33557647-4	2021	Molecular docking study showed that 23 binds to the active site of AChE and interacts via extensive pi-pi stacking with the indole and phenol side chains of Trp86 and Tyr337, besides the hydrogen bonding with the hydration site and pi-pi interaction with the phenol side chain of Y72.	Phenol	259-265	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-71	
2837347-1	1988	The acetylcholinesterase (EC 3.1.1.7) in 50 microL of a 61-fold dilution of erythrocytes in water hydrolyzes acetylcholine during a timed 20-min reaction at 37 degrees C. The resulting choline is measured by use of choline oxidase coupled to peroxidase, with phenol and aminoantipyrene to give a pink product that absorbs maximally at 500 nm.	Phenol	259-265	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-24	
1447418-2	1992	In terms of estimated kinetic characteristics of AChE-reaction (KM, Vmax, KI), the pattern of enzyme inhibition by the hindered phenol compounds was found to be of non-competitive or mixed type depending on the inhibitor structure or on the substrate acetylcholine or acetylthiocholine used.	Phenol	128-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	49-53	
33488212-2	2020	Biological activities of the compounds bearing phenol and heteroaryl groups make them popular groups in drug design targeting important enzymes such as acetylcholinesterase (AChE, E.C.3.1.1.7) and carbonic anhydrases (CAs, EC 4.2.1.1).	Phenol	47-53	acetylcholinesterase (Cartwright blood group)	Homo sapiens	152-172	
33488212-2	2020	Biological activities of the compounds bearing phenol and heteroaryl groups make them popular groups in drug design targeting important enzymes such as acetylcholinesterase (AChE, E.C.3.1.1.7) and carbonic anhydrases (CAs, EC 4.2.1.1).	Phenol	47-53	acetylcholinesterase (Cartwright blood group)	Homo sapiens	174-178	
20056426-3	2010	Compound 8c, berberine linked with phenol by a 4-carbon spacer, showed the most potent inhibition of AChE.	Phenol	35-41	acetylcholinesterase (Cartwright blood group)	Homo sapiens	101-105