PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28258856-3	2017	However, with the presence of reductive thiocholine (TCh), the enzymatic product, hydrolyzed from acetylthiocholine (ATCh) by AChE, the redox reaction between MnO2 and TCh occurred, leading to the destruction of the MnO2 nanosheets, and thereby IFE was diminished gradually.	Acetylthiocholine	98-115	acetylcholinesterase	Rattus norvegicus	126-130	
28258856-3	2017	However, with the presence of reductive thiocholine (TCh), the enzymatic product, hydrolyzed from acetylthiocholine (ATCh) by AChE, the redox reaction between MnO2 and TCh occurred, leading to the destruction of the MnO2 nanosheets, and thereby IFE was diminished gradually.	Acetylthiocholine	117-121	acetylcholinesterase	Rattus norvegicus	126-130	
2363176-3	1990	Chicken and rat brain AChE failed to distinguish between acetyl- and propionylthiocholine as inferred from the comparable Michaelis-Menten constants (Km), whereas trout brain AChE exhibited a much higher affinity for acetylthiocholine than for either of the two larger analogs.	Acetylthiocholine	217-234	acetylcholinesterase	Rattus norvegicus	175-179	
12633900-3	2003	AChE was determined spectrophotometrically with acetylthiocholine as substrate and 5,5-bis-2-nitrobenzoic acid as chromogen.	Acetylthiocholine	48-65	acetylcholinesterase	Rattus norvegicus	0-4	
8509385-6	1993	It is also prevented by propidium iodide, BW284C51, and d-tubocurarine, which bind to peripheral anionic sites of AChE, by Ca2+ and Mg2+, known to enhance AChE activity through an allosteric phenomenon and by acetylthiocholine concentrations which lead to excess substrate inhibition of the enzyme.	Acetylthiocholine	209-226	acetylcholinesterase	Rattus norvegicus	114-118	
8509385-6	1993	It is also prevented by propidium iodide, BW284C51, and d-tubocurarine, which bind to peripheral anionic sites of AChE, by Ca2+ and Mg2+, known to enhance AChE activity through an allosteric phenomenon and by acetylthiocholine concentrations which lead to excess substrate inhibition of the enzyme.	Acetylthiocholine	209-226	acetylcholinesterase	Rattus norvegicus	155-159	
965979-0	1976	The effect of spermine and spermidine on the hydrolysis of acetylthiocholine in the presence of rat caudate nucleus homogenate or acetylcholinesterase from Electrophorus electricus.	Acetylthiocholine	59-76	acetylcholinesterase	Rattus norvegicus	130-150	
3408583-1	1988	Acetylcholinesterase (AChE) activity has been determined using homogenized rat diaphragm and soluble AChE from the eel Electrophorus electricus, using as a substrate different amounts of acetylthiocholine in the presence or absence of 115 mM NaCl or LiCl.	Acetylthiocholine	187-204	acetylcholinesterase	Rattus norvegicus	0-20	
3408583-1	1988	Acetylcholinesterase (AChE) activity has been determined using homogenized rat diaphragm and soluble AChE from the eel Electrophorus electricus, using as a substrate different amounts of acetylthiocholine in the presence or absence of 115 mM NaCl or LiCl.	Acetylthiocholine	187-204	acetylcholinesterase	Rattus norvegicus	22-26	
2939475-3	1986	The activity of AChE (mumol acetylthiocholine hydrolysed X g-1 per hour) underwent more dramatic changes, increasing more than 4-fold during the first month of life, from 13 on the 1st to 58 on the 30th day of life and then decreasing to 42 in adult rats.	Acetylthiocholine	28-45	acetylcholinesterase	Rattus norvegicus	16-20	
4027630-1	1985	Using the acetylthiocholine staining method, it was possible to visualize acetylcholinesterase (AChE)-stained neuronal cell bodies and nerve endings as well as AChE-positive vesicles in the rat duodenum.	Acetylthiocholine	10-27	acetylcholinesterase	Rattus norvegicus	74-94	
4027630-1	1985	Using the acetylthiocholine staining method, it was possible to visualize acetylcholinesterase (AChE)-stained neuronal cell bodies and nerve endings as well as AChE-positive vesicles in the rat duodenum.	Acetylthiocholine	10-27	acetylcholinesterase	Rattus norvegicus	96-100	
4027630-1	1985	Using the acetylthiocholine staining method, it was possible to visualize acetylcholinesterase (AChE)-stained neuronal cell bodies and nerve endings as well as AChE-positive vesicles in the rat duodenum.	Acetylthiocholine	10-27	acetylcholinesterase	Rattus norvegicus	160-164	
3630858-1	1987	Ranitidine in lower doses, (100 ng and 1 microgram) accelerated the rate of reaction of the enzyme acetylcholinesterase with the substrate acetylthiocholine.	Acetylthiocholine	139-156	acetylcholinesterase	Rattus norvegicus	99-119	
7290286-2	1981	Three main molecular forms of AChE were separated by polyacrylamide gel electrophoresis followed by enzymatic reaction with acetylthiocholine, staining and scanning densitometry for their quantitative evaluation.	Acetylthiocholine	124-141	acetylcholinesterase	Rattus norvegicus	30-34	
33410430-5	2021	However, in the presence of thiocholine (TCh), a thiol-containing compound hydrolyzed from acetylthiocholine (ATCh) by AChE, a stronger coordination interaction between Cu2+ and TCh occurred, resulting in the restoration of the fluorescence of GQD@Tb/GMP ICPs.	Acetylthiocholine	91-108	acetylcholinesterase	Rattus norvegicus	119-123	
33410430-5	2021	However, in the presence of thiocholine (TCh), a thiol-containing compound hydrolyzed from acetylthiocholine (ATCh) by AChE, a stronger coordination interaction between Cu2+ and TCh occurred, resulting in the restoration of the fluorescence of GQD@Tb/GMP ICPs.	Acetylthiocholine	110-114	acetylcholinesterase	Rattus norvegicus	119-123