PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15820219-1	2005	Erythrocyte acetylcholinesterase (AChE) is bound to the membrane by a complex glycosylphosphatidylinositol anchor, so the effect of alcohol on AChE activity may reflect direct and/or membrane-mediated effects.	Alcohols	132-139	acetylcholinesterase (Cartwright blood group)	Homo sapiens	12-32	
15820219-1	2005	Erythrocyte acetylcholinesterase (AChE) is bound to the membrane by a complex glycosylphosphatidylinositol anchor, so the effect of alcohol on AChE activity may reflect direct and/or membrane-mediated effects.	Alcohols	132-139	acetylcholinesterase (Cartwright blood group)	Homo sapiens	34-38	
15820219-1	2005	Erythrocyte acetylcholinesterase (AChE) is bound to the membrane by a complex glycosylphosphatidylinositol anchor, so the effect of alcohol on AChE activity may reflect direct and/or membrane-mediated effects.	Alcohols	132-139	acetylcholinesterase (Cartwright blood group)	Homo sapiens	143-147	
15820219-2	2005	The indication of a direct interaction between n-butanol and AChE molecules is the activation/inhibition of AChE by occupation of the enzyme"s active and/or regulatory sites by alcohol.	Alcohols	177-184	acetylcholinesterase (Cartwright blood group)	Homo sapiens	61-65	
15820219-2	2005	The indication of a direct interaction between n-butanol and AChE molecules is the activation/inhibition of AChE by occupation of the enzyme"s active and/or regulatory sites by alcohol.	Alcohols	177-184	acetylcholinesterase (Cartwright blood group)	Homo sapiens	108-112	
15820219-3	2005	The activation of AChE can occur only at low concentrations of alcohols, while at high concentrations AChE is inhibited.	Alcohols	63-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-22	
15820219-6	2005	From the values of the inhibition constants it was concluded that at high n-butanol concentrations two alcohol molecules usually interact with AChE.	Alcohols	103-110	acetylcholinesterase (Cartwright blood group)	Homo sapiens	143-147	
3764913-1	1986	Human erythrocytes were exposed to different concentrations of aromatic hydrocarbons, chlorinated aliphatic hydrocarbons, and alcohols in vitro to study the effects of these agents on the activity of acetylcholinesterase (AchE), a membrane integral protein.	Alcohols	126-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	200-220	
3468911-3	1986	Of the alcohols studied, only ethanol had a slight AchE inhibiting effect at +37 degrees C. The decrease in the incubation temperature increased the AchE inhibiting potency of aromatic hydrocarbons more than that of chlorinated aliphatic hydrocarbons and alcohols.	Alcohols	7-15	acetylcholinesterase (Cartwright blood group)	Homo sapiens	149-153	
3468911-3	1986	Of the alcohols studied, only ethanol had a slight AchE inhibiting effect at +37 degrees C. The decrease in the incubation temperature increased the AchE inhibiting potency of aromatic hydrocarbons more than that of chlorinated aliphatic hydrocarbons and alcohols.	Alcohols	255-263	acetylcholinesterase (Cartwright blood group)	Homo sapiens	149-153	
647082-6	1978	The different dependence of the ester substrate and appropriate alcohol binding effectiveness upon the reagent structure indicates the dissimilar location of the molecules in the active center of acetylcholinesterase.	Alcohols	64-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	196-216	
4114055-0	1971	[Isolation of acetylcholinesterase from the stroma of erythrocytes using alcohols as detergents].	Alcohols	73-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	14-34	
32992925-1	2020	Organophosphates (OPs) are esters of substituted phosphates, phosphonates or phosphoramidates that react with acetylcholinesterase (AChE) by initially transferring the organophosphityl group to a serine residue in the enzyme active site, concomitant with loss of an alcohol or halide leaving group.	Alcohols	266-273	acetylcholinesterase (Cartwright blood group)	Homo sapiens	110-130	
30366255-1	2019	Herein we envisaged the possibility of exploiting alkyl nitrates as precursors of alcohol-bearing dual inhibitors targeting acetylcholinesterase (AChE) and monoamine oxidase B (MAO B), key enzymes in neurodegenerative syndromes such as Alzheimer"s disease (AD), through biotransformation unmasking an alcoholic function upon nitric oxide (NO) release.	Alcohols	82-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	146-150	
29975450-0	2018	Intermolecular amination of allylic and benzylic alcohols leads to effective inhibitions of acetylcholinesterase enzyme and carbonic anhydrase I and II isoenzymes.	Alcohols	49-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-112