PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12502352-4	2003	The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.	Sulfur	58-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	141-145	
27611473-3	2017	AChE catalyzes the hydrolysis of acetylthiocholine (ATC) into thiocholine which reacts with AuNPs by S-Au conjunction and results the aggregation of AuNPs and change in fluorescence of UCNPs.	Sulfur	101-102	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4	
25913282-4	2015	The sensing mechanism of this array is based on the irreversible inhibition capability of OPs and carbamates to the activity of acetylcholinesterase (AChE), preventing production of thiocholine and H2O2 from S-acetylthiocholine and acetylcholine and thus resulting in decreased or no color reactions to thiocholine and H2O2 sensitive indicators.	Sulfur	208-209	acetylcholinesterase (Cartwright blood group)	Homo sapiens	128-148	
25913282-4	2015	The sensing mechanism of this array is based on the irreversible inhibition capability of OPs and carbamates to the activity of acetylcholinesterase (AChE), preventing production of thiocholine and H2O2 from S-acetylthiocholine and acetylcholine and thus resulting in decreased or no color reactions to thiocholine and H2O2 sensitive indicators.	Sulfur	208-209	acetylcholinesterase (Cartwright blood group)	Homo sapiens	150-154	
34476614-3	2021	Acetylcholinesterase hydrolyzed acetylthiocholine to generate thiocholine that bound with Cu2+ strongly via S-Cu-S bond.	Sulfur	113-114	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20	
12449529-3	2002	Their oxons are converted further to the S-oxides, which either inhibit AChE or decompose, depending on the alkyl substituents on the sulfur atom.	Sulfur	134-140	acetylcholinesterase (Cartwright blood group)	Homo sapiens	72-76	
12449529-4	2002	It is also inferred in the case of prothiophos oxon that its S-oxide not only inhibits AChE but also conjugates with glutathione (GSH) by the action of glutathione S-transferase (GST), and the conjugate inhibits AChE.	Sulfur	61-62	acetylcholinesterase (Cartwright blood group)	Homo sapiens	87-91	
12449529-4	2002	It is also inferred in the case of prothiophos oxon that its S-oxide not only inhibits AChE but also conjugates with glutathione (GSH) by the action of glutathione S-transferase (GST), and the conjugate inhibits AChE.	Sulfur	61-62	acetylcholinesterase (Cartwright blood group)	Homo sapiens	212-216	
2937928-3	1986	In order to prove the in vivo interaction between the 16S AChE and heparan sulfate residues, the binding of exogenously added 16S enzyme to intact cells rich in cell-surface heparan sulfate proteoglycans was examined; 16S AChE form was shown to bind to intact endothelial cells in a specific, time-dependent, saturable fashion.	Sulfur	54-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	58-62	
6493583-4	1984	These results support the hypothesis that extracellular 16S AChE at mammalian skeletal muscle motor endplates is primarily derived from complete, previously assembled 16S molecules originating in myofibers.	Sulfur	56-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	60-64	
6493583-4	1984	These results support the hypothesis that extracellular 16S AChE at mammalian skeletal muscle motor endplates is primarily derived from complete, previously assembled 16S molecules originating in myofibers.	Sulfur	167-170	acetylcholinesterase (Cartwright blood group)	Homo sapiens	60-64	
32891857-0	2020	Synthesis of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds - Determination of their carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and alpha-glycosidase inhibition properties.	Sulfur	48-54	acetylcholinesterase (Cartwright blood group)	Homo sapiens	134-154	
7441241-8	1980	Our results suggest that some nerve soluble substance, other than serum contaminants or 16S AChE itself, affects the maintenance of 16S AChE at the neuromuscular junction.	Sulfur	132-135	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-96	
7441241-8	1980	Our results suggest that some nerve soluble substance, other than serum contaminants or 16S AChE itself, affects the maintenance of 16S AChE at the neuromuscular junction.	Sulfur	132-135	acetylcholinesterase (Cartwright blood group)	Homo sapiens	136-140	
30851693-2	2019	Based on the in vitro biological profile, compound S-K1035 was found to be the most potent inhibitor of human acetylcholinesterase (hAChE) and human butyrylcholinesterase (hBChE), demonstrating balanced IC50 values of 6.3 and 9.1 nM, respectively.	Sulfur	51-52	acetylcholinesterase (Cartwright blood group)	Homo sapiens	132-137