PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21994917-1	2011	An electrochemical platform for acetylcholinesterase (AChE) activity assay and its inhibitors screening is developed based on the Michael addition reaction of thiocholine, the hydrolysis product of acetylthiocholine (AsCh) in the presence of AChE, with the electrogenerated o-quinone of catechol-terminated SAMs on a gold electrode.	asch	217-221	acetylcholinesterase (Cartwright blood group)	Homo sapiens	32-52	
21994917-1	2011	An electrochemical platform for acetylcholinesterase (AChE) activity assay and its inhibitors screening is developed based on the Michael addition reaction of thiocholine, the hydrolysis product of acetylthiocholine (AsCh) in the presence of AChE, with the electrogenerated o-quinone of catechol-terminated SAMs on a gold electrode.	asch	217-221	acetylcholinesterase (Cartwright blood group)	Homo sapiens	54-58	
21994917-1	2011	An electrochemical platform for acetylcholinesterase (AChE) activity assay and its inhibitors screening is developed based on the Michael addition reaction of thiocholine, the hydrolysis product of acetylthiocholine (AsCh) in the presence of AChE, with the electrogenerated o-quinone of catechol-terminated SAMs on a gold electrode.	asch	217-221	acetylcholinesterase (Cartwright blood group)	Homo sapiens	242-246	
3729986-5	1986	These three inhibitors compete with TC in the inhibition of enzymatic hydrolysis of acetylthiocholine (ASCh); all three of them affect the noncompetitive component of the inhibition of the hydrolysis of ASCh by TC, which arises from the binding of TC to the peripheral anionic site of AChE, but TEA and C-10 affect also the competitive component of this inhibition, which arises from the binding of TC at the catalytic anionic site.	asch	103-107	acetylcholinesterase (Cartwright blood group)	Homo sapiens	285-289	
3729986-5	1986	These three inhibitors compete with TC in the inhibition of enzymatic hydrolysis of acetylthiocholine (ASCh); all three of them affect the noncompetitive component of the inhibition of the hydrolysis of ASCh by TC, which arises from the binding of TC to the peripheral anionic site of AChE, but TEA and C-10 affect also the competitive component of this inhibition, which arises from the binding of TC at the catalytic anionic site.	asch	203-207	acetylcholinesterase (Cartwright blood group)	Homo sapiens	285-289	
16971069-1	2006	Pralidoxime iodide (2-PAM), an antidote approved for the reactivation of inhibited acetylcholinesterase (AChE) in organophosphate poisoning, dose-dependently hydrolyzed an acetylthiocholine iodide (ASCh).	asch	198-202	acetylcholinesterase (Cartwright blood group)	Homo sapiens	83-103	
16971069-1	2006	Pralidoxime iodide (2-PAM), an antidote approved for the reactivation of inhibited acetylcholinesterase (AChE) in organophosphate poisoning, dose-dependently hydrolyzed an acetylthiocholine iodide (ASCh).	asch	198-202	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109	
16971069-10	2006	We therefore strongly caution that the method of determining AChE activity with ASCh is not suitable for examining the effects of oximes.	asch	80-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	61-65	
9494556-2	1997	The Ks for the hydrolysis of acetylthiocholine iodide (ASCh) by AChE was 0.077 mM in the control system, the value decreased by 14-38% in the DDP treated systems.	asch	55-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	64-68	
8813709-4	1996	The Michaelis-Menten constant (Ks) for the hydrolysis of acetylthiocholine iodide (ASCh) by AChE was 0.13 mM in the control system, a value decreased by 30-61% in the MTX treated systems.	asch	83-87	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-96