PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
17113251-0	2006	The liberation of thiocholine from acetylthiocholine (ASCh) by pralidoxime iodide (2=PAM) and other oximes (obidoxime and diacetylmonoxime).	Acetylthiocholine	35-52	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	85-88
17454383-2	2007	The voltammetric results have shown that the formal potential shifts anodically as the Au/MBT/PANI/AChE/PVAc thick-film biosensor responded to acetylthiocholine substrate addition under anaerobic conditions in selected organic solvent media containing 2% v/v 0.05 M phosphate buffer, 0.1 M KCl (pH 7.2) solution.	Acetylthiocholine	143-160	acetylcholinesterase (Cartwright blood group)	Homo sapiens	99-103
17186224-0	2007	An amperometric acetylthiocholine sensor based on immobilization of acetylcholinesterase on a multiwall carbon nanotube-cross-linked chitosan composite.	Acetylthiocholine	16-33	acetylcholinesterase (Cartwright blood group)	Homo sapiens	68-88
17186224-1	2007	A simple method has been devised for immobilization of acetylcholinesterase (AChE)--covalent bonding to a multiwall carbon nanotube (MWNT)--cross-linked chitosan composite (CMC)-and a sensitive amperometric sensor for rapid detection of acetylthiocholine (ATCl) has been based on this.	Acetylthiocholine	237-254	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-75
17186224-1	2007	A simple method has been devised for immobilization of acetylcholinesterase (AChE)--covalent bonding to a multiwall carbon nanotube (MWNT)--cross-linked chitosan composite (CMC)-and a sensitive amperometric sensor for rapid detection of acetylthiocholine (ATCl) has been based on this.	Acetylthiocholine	237-254	acetylcholinesterase (Cartwright blood group)	Homo sapiens	77-81
17186224-1	2007	A simple method has been devised for immobilization of acetylcholinesterase (AChE)--covalent bonding to a multiwall carbon nanotube (MWNT)--cross-linked chitosan composite (CMC)-and a sensitive amperometric sensor for rapid detection of acetylthiocholine (ATCl) has been based on this.	Acetylthiocholine	256-260	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-75
17186224-1	2007	A simple method has been devised for immobilization of acetylcholinesterase (AChE)--covalent bonding to a multiwall carbon nanotube (MWNT)--cross-linked chitosan composite (CMC)-and a sensitive amperometric sensor for rapid detection of acetylthiocholine (ATCl) has been based on this.	Acetylthiocholine	256-260	acetylcholinesterase (Cartwright blood group)	Homo sapiens	77-81
17186224-4	2007	Because of the inherent conductive properties of the MWNT, the immobilized AChE had greater affinity for ATCl and excellent catalytic effect in the hydrolysis of ATCl, with a K(app)(m) value of 132 micromol L(-1), forming thiocholine, which was then oxidized to produce a detectable and rapid response.	Acetylthiocholine	105-109	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-79
17186224-4	2007	Because of the inherent conductive properties of the MWNT, the immobilized AChE had greater affinity for ATCl and excellent catalytic effect in the hydrolysis of ATCl, with a K(app)(m) value of 132 micromol L(-1), forming thiocholine, which was then oxidized to produce a detectable and rapid response.	Acetylthiocholine	162-166	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-79
16971069-0	2006	Hydrolysis of an acetylthiocholine by pralidoxime iodide (2-PAM).	Acetylthiocholine	17-34	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	60-63
16498728-1	2005	Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied.	Acetylthiocholine	26-43	butyrylcholinesterase	Homo sapiens	101-105
16837465-6	2006	Moreover, the structures of the AChE mutant in complexes with acetylthiocholine and succinyldicholine reveal additional substrate binding sites on the enzyme surface, distal to the gorge entry.	Acetylthiocholine	62-79	acetylcholinesterase	Mus musculus	32-36
16240314-4	2006	The immobilized AChE could catalyze the hydrolysis of acetylthiocholine with a K(M)app value of 177 microM to form thiocholine, which was then oxidized to produce detectable signal in a linear range of 1.0-500 microM and fast response.	Acetylthiocholine	54-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
16498728-1	2005	Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied.	Acetylthiocholine	26-43	acetylcholinesterase (Cartwright blood group)	Homo sapiens	111-131
16498728-1	2005	Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied.	Acetylthiocholine	26-43	acetylcholinesterase (Cartwright blood group)	Homo sapiens	133-137
16498728-1	2005	Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied.	Acetylthiocholine	45-49	butyrylcholinesterase	Homo sapiens	101-105
16498728-1	2005	Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied.	Acetylthiocholine	45-49	acetylcholinesterase (Cartwright blood group)	Homo sapiens	111-131
16498728-1	2005	Kinetics of hydrolysis of acetylthiocholine (ATCH) and acetylcholine (ACH) by butyrylcholinesterase (BCHE) and acetylcholinesterase (ACHE) are studied.	Acetylthiocholine	45-49	acetylcholinesterase (Cartwright blood group)	Homo sapiens	133-137
15994894-4	2005	It was found that the encounter process between AChE and acetylthiocholine was promoted in solutions with less structured water.	Acetylthiocholine	57-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	48-52
16135075-3	2005	AChE activity in normal thymus (mean +/- SD 1.42 +/- 0.28 micromol acetylthiocholine/h/mg protein, U/mg) was decreased by approximately 50% in dystrophic thymus (0.77 +/- 0.23 U/mg) (p = 0.007), whereas butyrylcholinesterase activity was little affected.	Acetylthiocholine	67-84	acetylcholinesterase	Mus musculus	0-4
15052610-6	2004	Cholinesterase activities (with acetylthiocholine [ChE-A] and butyrylthiocholine [ChE-B] as substrates) in human plasma were measured photometrically in the presence of different MPFX concentrations and the IC(50) was calculated.	Acetylthiocholine	32-49	butyrylcholinesterase	Homo sapiens	0-14
15733936-3	2005	Total ChE activities measured in presence of acetylthiocholine (ACTI, 1 mM) in intact vascular preparations were 45+/-04 and 114+/-07 mU/g tissue in human pulmonary arteries (n=14) and veins (n=14), respectively.	Acetylthiocholine	45-62	butyrylcholinesterase	Homo sapiens	6-9
15082230-2	2004	AChE activity was higher in mouse spleen (0.46 +/- 0.13 micromol of acetylthiocholine split per hour and per mg protein) than in muscle or heart, but lower than in brain.	Acetylthiocholine	68-85	acetylcholinesterase	Mus musculus	0-4
15980188-4	2005	The AChE hydrolyzed acetylthiocholine and propyonylthiocholine, but not S-butyrylthiocholine, and the AChE-specific inhibitor neostigmine bromide competitively inhibited its activity, implying that maize AChE functions in a similar manner as the animal enzyme.	Acetylthiocholine	20-37	GDSL esterase/lipase ACHE	Zea mays	4-8
15826103-1	2005	The acetylcholine esterase, AChE, mediated hydrolysis of acetylthiocholine (1) yields a reducing agent thiocholine (2) that stimulates the catalytic enlargement of Au NP seeds in the presence of AuCl(4)(-).	Acetylthiocholine	57-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	28-32
12110369-9	2002	Wild-type rat BChE had an 8- to 9-fold higher K(m) for the positively charged substrates butyrylthiocholine, acetylthiocholine, propionylthiocholine, benzoylcholine, and cocaine compared with wild-type human BChE.	Acetylthiocholine	109-126	butyrylcholinesterase	Rattus norvegicus	14-18
15241943-1	2004	The power of chosen carbamates and hydrazinium derivatives (carbazates) to inhibit the hydrolysis of acetylthiocholine by butyrylcholinesterase or acetylcholinesterase was tested.	Acetylthiocholine	101-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	147-167
12731886-9	2003	Values of a >1 give rise to a hydrolysis profile called substrate activation, and the AChE site-specific mutant W86F, and to a lesser extent wild-type human AChE itself, showed substrate activation with acetylthiocholine as the substrate.	Acetylthiocholine	206-223	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-93
12731886-9	2003	Values of a >1 give rise to a hydrolysis profile called substrate activation, and the AChE site-specific mutant W86F, and to a lesser extent wild-type human AChE itself, showed substrate activation with acetylthiocholine as the substrate.	Acetylthiocholine	206-223	acetylcholinesterase (Cartwright blood group)	Homo sapiens	160-164
12706630-2	2003	The AChE of TKD had lower affinity to acetylthiocholine and propionylthiocholine than that of NCN, and the inhibition of AChE by DDVP, ambenonium, eserine and n-methyl-eserine showed that NCN was more insensitive than TKD.	Acetylthiocholine	38-55	acetylcholinesterase-like	Tetranychus urticae	4-8
12562097-0	2002	Kinetics and mechanism of hydrolysis of acetylthiocholine by butyrylcholine esterase.	Acetylthiocholine	40-57	butyrylcholinesterase	Homo sapiens	61-84
12562097-1	2002	Kinetics and mechanism of hydrolysis of acetylthiocholine by the enzyme butyrylcholine esterase was studied.	Acetylthiocholine	40-57	butyrylcholinesterase	Homo sapiens	72-95
12094012-2	2002	It was established that this enzyme activity is acetylcholinesterase by substrate specificity (acetylthiocholine, acetyl-beta-methylthiocholine>propionylthiocholine>butyrylthiocholine), substrate inhibition, and specificity of inhibitors (BW284c51>iso-OMPA).	Acetylthiocholine	95-112	acetylcholinesterase (Cartwright blood group)	Homo sapiens	48-68
14577154-3	2003	The hydrolysis velocity of 1-thionaphthylacetate was comparable with hydrolysis velocity of acetylthiocholine (the well known cholinesterase substrate), but 2-thionaphthylacetate was hydrolysed more slowly.	Acetylthiocholine	92-109	butyrylcholinesterase	Homo sapiens	126-140
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
12583698-1	2003	Pralidoxime (2-PAM) hydrolyzes both acetylthiocholine and butytylthiocholine in an apparent first-order manner, with higher rates observed at pH 8.0 compared to those at pH 7.4.	Acetylthiocholine	36-53	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	15-18
12132693-3	2002	The activity of the pure AChE was also determined using as a substrate different amounts of acetylthiocholine.	Acetylthiocholine	92-109	acetylcholinesterase (Cartwright blood group)	Homo sapiens	25-29
12132691-5	2002	The validity of the method is demonstrated by four inhibitors of hydrolysis of acetylthiocholine by butyrylcholine esterase.	Acetylthiocholine	79-96	butyrylcholinesterase	Homo sapiens	100-123
11378416-12	2001	The K(m) of wild type AChE for acetylthiocholine (ASCh) is 23.13 microM and the point mutations change the affinity to the substrate.	Acetylthiocholine	31-48	Acetylcholine esterase	Drosophila melanogaster	22-26
12420757-5	2002	The acetylthiocholine detection under enzyme kinetic control was found in the range of 0.01-0.3 U cm(-2) of immobilised AChE.	Acetylthiocholine	4-21	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-124
11904227-2	2002	To understand the mechanism of substrate inhibition, the pH dependence of acetylthiocholine hydrolysis by AChE was studied between pH 5 and 8.	Acetylthiocholine	74-91	acetylcholinesterase (Cartwright blood group)	Homo sapiens	106-110
11848688-6	2002	At all of these locations, the BChE enzyme could hydrolyze the acetylcholine surrogate acetylthiocholine.	Acetylthiocholine	87-104	butyrylcholinesterase	Homo sapiens	31-35
11676619-3	2001	In whole blood of ruminants and pigs, acetylthiocholine yielded the highest cholinesterase activity and other substrates were poorly hydrolysed; in dogs and cats, although acetylthiocholine showed the highest cholinesterase activity, butyryl- and propionylthiocholine also produced high cholinesterase values; in horses, propionylthiocholine was the substrate that yielded the highest cholinesterase activity, closely followed by butyrylthiocholine.	Acetylthiocholine	38-55	cholinesterase	Sus scrofa	76-90
10421442-4	1999	We also report here that acetylthiocholine can bind to the AChE peripheral site with an equilibrium dissociation constant K(S) of about 1 mM.	Acetylthiocholine	25-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	59-63
11676619-3	2001	In whole blood of ruminants and pigs, acetylthiocholine yielded the highest cholinesterase activity and other substrates were poorly hydrolysed; in dogs and cats, although acetylthiocholine showed the highest cholinesterase activity, butyryl- and propionylthiocholine also produced high cholinesterase values; in horses, propionylthiocholine was the substrate that yielded the highest cholinesterase activity, closely followed by butyrylthiocholine.	Acetylthiocholine	172-189	butyrylcholinesterase	Felis catus	209-223
11676619-3	2001	In whole blood of ruminants and pigs, acetylthiocholine yielded the highest cholinesterase activity and other substrates were poorly hydrolysed; in dogs and cats, although acetylthiocholine showed the highest cholinesterase activity, butyryl- and propionylthiocholine also produced high cholinesterase values; in horses, propionylthiocholine was the substrate that yielded the highest cholinesterase activity, closely followed by butyrylthiocholine.	Acetylthiocholine	172-189	butyrylcholinesterase	Felis catus	209-223
11676619-3	2001	In whole blood of ruminants and pigs, acetylthiocholine yielded the highest cholinesterase activity and other substrates were poorly hydrolysed; in dogs and cats, although acetylthiocholine showed the highest cholinesterase activity, butyryl- and propionylthiocholine also produced high cholinesterase values; in horses, propionylthiocholine was the substrate that yielded the highest cholinesterase activity, closely followed by butyrylthiocholine.	Acetylthiocholine	172-189	butyrylcholinesterase	Equus caballus	209-223
11676619-5	2001	Butyryl- and propionylthiocholine were the substrates that yielded higher inhibitions after coumaphos exposure, whereas the use of acetylthiocholine showed the highest cholinesterase inhibition after imidocarb exposure.	Acetylthiocholine	131-148	butyrylcholinesterase	Equus caballus	168-182
11676619-7	2001	However, acetylthiocholine could be used as a unique substrate for whole blood cholinesterase determination in porcine and ruminant samples since butyrylcholinesterase activity is very low in these species.	Acetylthiocholine	9-26	butyrylcholinesterase	Equus caballus	79-93
11163034-2	2001	METHODS: Acetylthiocholine, used as substrate, is hydrolysed by acetylcholinesterase to yield acetate and thiocholine.	Acetylthiocholine	9-26	acetylcholinesterase (Cartwright blood group)	Homo sapiens	64-84
11061961-2	2000	Cholinesterase activity was characterized using two substrates: acetylthiocholine and butyrylthiocholine.	Acetylthiocholine	64-81	butyrylcholinesterase	Canis lupus familiaris	0-14
11061961-3	2000	Acetylcholinesterase was the only form of cholinesterase present on erythrocytes and hydrolysed only acetylthiocholine.	Acetylthiocholine	101-118	acetylcholinesterase	Canis lupus familiaris	0-20
11061961-3	2000	Acetylcholinesterase was the only form of cholinesterase present on erythrocytes and hydrolysed only acetylthiocholine.	Acetylthiocholine	101-118	butyrylcholinesterase	Canis lupus familiaris	6-20
11275256-1	2000	We have previously described a catalytic monoclonal antibody, raised against acetylcholinesterase (AChE) and capable of hydrolysing acetylthiocholine.	Acetylthiocholine	132-149	acetylcholinesterase (Cartwright blood group)	Homo sapiens	77-97
11275256-1	2000	We have previously described a catalytic monoclonal antibody, raised against acetylcholinesterase (AChE) and capable of hydrolysing acetylthiocholine.	Acetylthiocholine	132-149	acetylcholinesterase (Cartwright blood group)	Homo sapiens	99-103
10869180-0	2000	Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway.	Acetylthiocholine	0-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	65-85
10869180-6	2000	In this report, we demonstrate that a key residue in the human AChE peripheral site with which the substrate acetylthiocholine interacts is D74.	Acetylthiocholine	109-126	acetylcholinesterase (Cartwright blood group)	Homo sapiens	63-67
10869180-8	2000	For human AChE, a K(S) of 1.9+/-0.7 mM obtained by fitting this substrate inhibition curve agreed with a K(S) of 1.3+/-1.0 mM measured directly from acetylthiocholine inhibition of the binding of the neurotoxin fasciculin to the peripheral site.	Acetylthiocholine	149-166	acetylcholinesterase (Cartwright blood group)	Homo sapiens	10-14
14564607-2	2000	METHODS: The activities of plasma ChE and erythrocyte AChE were determined by the calorimetric method of Ellman et al., using acetylthiocholine as the substrate.	Acetylthiocholine	126-143	butyrylcholinesterase	Homo sapiens	34-37
14564607-2	2000	METHODS: The activities of plasma ChE and erythrocyte AChE were determined by the calorimetric method of Ellman et al., using acetylthiocholine as the substrate.	Acetylthiocholine	126-143	acetylcholinesterase (Cartwright blood group)	Homo sapiens	54-58
14564607-4	2000	RESULTS: The dissociation constants (K(m)) of plasma ChE and erythrocyte AChE were 5.00 x 10(-5) M and 5.28 x 10(-5) M, respectively, indicating that both enzymes have similar affinity to acetylthiocholine.	Acetylthiocholine	188-205	butyrylcholinesterase	Homo sapiens	53-56
14564607-4	2000	RESULTS: The dissociation constants (K(m)) of plasma ChE and erythrocyte AChE were 5.00 x 10(-5) M and 5.28 x 10(-5) M, respectively, indicating that both enzymes have similar affinity to acetylthiocholine.	Acetylthiocholine	188-205	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-77
10340441-2	1999	It is based on our finding that the individual activity ratios of BChE on both its substrates acetylthiocholine (ACh) and butyrylthiocholine (BCh) in the CSF and in the parallel serum are identical under conditions of at least 5 mmol/l substrate concentration (Q(BChE)SE = Q(BChe)CSF).	Acetylthiocholine	94-111	butyrylcholinesterase	Homo sapiens	66-70
10340441-2	1999	It is based on our finding that the individual activity ratios of BChE on both its substrates acetylthiocholine (ACh) and butyrylthiocholine (BCh) in the CSF and in the parallel serum are identical under conditions of at least 5 mmol/l substrate concentration (Q(BChE)SE = Q(BChe)CSF).	Acetylthiocholine	113-116	butyrylcholinesterase	Homo sapiens	66-70
10340441-3	1999	Considering that AChE only reacts with ACh as substrate and occurs with negligible activities in the serum, the measured individual activity ratio of BChE in the serum (Q(BChE)SE) and the total hydrolysis rate of ACh and BCh in the CSF do allow a precise calculation of the AChE activity in the cerebrospinal fluid.	Acetylthiocholine	17-20	butyrylcholinesterase	Homo sapiens	150-154
10340441-3	1999	Considering that AChE only reacts with ACh as substrate and occurs with negligible activities in the serum, the measured individual activity ratio of BChE in the serum (Q(BChE)SE) and the total hydrolysis rate of ACh and BCh in the CSF do allow a precise calculation of the AChE activity in the cerebrospinal fluid.	Acetylthiocholine	17-20	acetylcholinesterase (Cartwright blood group)	Homo sapiens	274-278
10340441-3	1999	Considering that AChE only reacts with ACh as substrate and occurs with negligible activities in the serum, the measured individual activity ratio of BChE in the serum (Q(BChE)SE) and the total hydrolysis rate of ACh and BCh in the CSF do allow a precise calculation of the AChE activity in the cerebrospinal fluid.	Acetylthiocholine	39-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	17-21
9427520-4	1997	Enhancement of acetylthiocholine hydrolysis also occurred with Torpedo AChE, which has no consensus motif for PKA phosphorylation.	Acetylthiocholine	15-32	acetylcholinesterase (Cartwright blood group)	Homo sapiens	71-75
9890890-6	1999	Previous reaction schemes for substrate hydrolysis by AChE were extended to include product dissociation steps, and acetylthiocholine hydrolysis rates in the presence of propidium under nonequilibrium conditions were simulated with assigned rate constants in the program SCoP.	Acetylthiocholine	116-133	acetylcholinesterase (Cartwright blood group)	Homo sapiens	54-58
9568379-4	1998	The fluorescence intensity of physostigmine-inhibited AChE decreased with increasing the substrate (acetylthiocholine) concentration, thus indicating that physostigmine binding to the active site is essential for the development of fluorescence.	Acetylthiocholine	100-117	acetylcholinesterase (Cartwright blood group)	Homo sapiens	54-58
8766007-12	1996	A fourth parameter influencing the choline+ transporter is the presence of an OH group on the C atom next to that bearing the N atom (as in choline+) or an ester-OCOR group (acetylcholine+, butyrylcholine+) or a thioester-SCOR-group (acetylthiocholine+, butyrylthiocholine+); or an -OP(OH)2(OR) group (glycerylphosphoryl-choline+), resulting in app.Ki,l,choline+ values of 0.3-1.0 mmol x l-1.	Acetylthiocholine	234-251	solute carrier family 6 member 8	Rattus norvegicus	35-55
9192101-1	1997	The activity characteristics of membrane acetylcholinesterase from red blood cells of diabetic patients are very different from those of healthy donors: the limiting enzyme reaction rate is 17.2 +/- 0.8 mumol acetylthiocholine per ml packed cells per min compared with 13.1 +/- 0.8 mumol for control cells.	Acetylthiocholine	209-226	acetylcholinesterase (Cartwright blood group)	Homo sapiens	41-61
8951045-3	1996	The kinetic parameter, Km, for the substrate acetylthiocholine was found to be 0.22 mM, and the Kis and Kii for MPDP+ inhibition of AChE were found to be 0.265 and 0.578 mM, respectively.	Acetylthiocholine	45-62	acetylcholinesterase (Cartwright blood group)	Homo sapiens	132-136
8302294-3	1993	The kinetic parameter, Km for the substrate (acetylthiocholine), was found to be 0.216 mM and Ki for MPP+ for the inactivation of AChE was found to be 0.197 mM.	Acetylthiocholine	45-62	acetylcholinesterase (Cartwright blood group)	Homo sapiens	130-134
7974841-5	1994	For objective evaluation of efficiency of reversible inhibitors it is suggested to determine the generalized inhibitory constant Ki at the cholinesterase hydrolysis in acetylcholine or acetylthiocholine.	Acetylthiocholine	185-202	butyrylcholinesterase	Homo sapiens	139-153
8264551-2	1993	AE-2 partially inhibited the rate of hydrolysis of the charged substrate acetylthiocholine by FBS AChE, whereas it increased the rate of hydrolysis of the neutral substrate indophenyl acetate.	Acetylthiocholine	73-90	solute carrier family 4 member 2	Homo sapiens	0-4
8264551-2	1993	AE-2 partially inhibited the rate of hydrolysis of the charged substrate acetylthiocholine by FBS AChE, whereas it increased the rate of hydrolysis of the neutral substrate indophenyl acetate.	Acetylthiocholine	73-90	acetylcholinesterase (Cartwright blood group)	Homo sapiens	98-102
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
8367669-2	1993	The asymptomatic microfilaremic sera showed 3 to 4 times more cholinesterase activity for acetylthiocholine (ATCh) as compared to sera of symptomatic amicrofilaremic, hookworm infected and endemic normals, whereas the activities for butyrylthiocholine (BTCh) did not significantly differ.	Acetylthiocholine	90-107	butyrylcholinesterase	Homo sapiens	62-76
8367669-2	1993	The asymptomatic microfilaremic sera showed 3 to 4 times more cholinesterase activity for acetylthiocholine (ATCh) as compared to sera of symptomatic amicrofilaremic, hookworm infected and endemic normals, whereas the activities for butyrylthiocholine (BTCh) did not significantly differ.	Acetylthiocholine	109-113	butyrylcholinesterase	Homo sapiens	62-76
1446827-6	1992	The purified (specific activity of 6000 units per mg protein) homodimer and tetramer enzyme molecules displayed typical AChE biochemical properties: a Km value of 120 microM for acetylthiocholine; a kcat value of 3.9 x 10(5)/min, and selective by AChE-specific inhibitors.	Acetylthiocholine	178-195	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-124
1293431-2	1992	Because AChE shows substrate specificity and hydrolyzes acetylthiocholine but not butrylthiocholine, this parasitic enzyme is likely a true acetylcholinesterase.	Acetylthiocholine	56-73	acetylcholinesterase (Cartwright blood group)	Homo sapiens	8-12
1293431-2	1992	Because AChE shows substrate specificity and hydrolyzes acetylthiocholine but not butrylthiocholine, this parasitic enzyme is likely a true acetylcholinesterase.	Acetylthiocholine	56-73	acetylcholinesterase	Bos taurus	140-160
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.	Acetylthiocholine	268-285	acetylcholinesterase (Cartwright blood group)	Homo sapiens	49-53
1459669-1	1992	In vitro inhibitory effect of dimethylsulfoxide (DMSO) on acetylcholinesterase of erythrocyte membranes and synaptosomes of mice was observed using acetylthiocholine as substrate.	Acetylthiocholine	148-165	acetylcholinesterase	Mus musculus	58-78
1504265-3	1992	2-Substituted-2-hydroxy-4,4-dimethylmorpholiniums (hemicholiniums) inhibit acetylcholinesterase (EC 3.1.1.7)-catalyzed hydrolysis of acetylthiocholine (ATCh).	Acetylthiocholine	133-150	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-95
1504265-3	1992	2-Substituted-2-hydroxy-4,4-dimethylmorpholiniums (hemicholiniums) inhibit acetylcholinesterase (EC 3.1.1.7)-catalyzed hydrolysis of acetylthiocholine (ATCh).	Acetylthiocholine	152-156	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-95
1907148-4	1991	Control values for red cell acetylcholinesterase (AChE) activity (mumol/min/mL blood) using acetylthiocholine (1 mM) were higher in the human (4.98) and the rhesus monkey (4.14) than in the marmoset (0.84) and the guinea-pig (0.83).	Acetylthiocholine	92-109	acetylcholinesterase (Cartwright blood group)	Homo sapiens	28-48
1522715-1	1992	Pralidoxime chloride (PAM) hydrolyzes acetylthiocholine, the substrate used in the assay of red cell cholinesterase.	Acetylthiocholine	38-55	butyrylcholinesterase	Homo sapiens	101-115
1538717-2	1992	THA causes linear mixed inhibition of AchE hydrolysis of acetylthiocholine, a cationic substrate (KI = 3.8 x 10(-9) M), and linear competitive inhibition of AchE hydrolysis of 7-acetoxy-4-methylcoumarin, an uncharged substrate (KI = 6.8 x 10(-9) M), and N-methyl-7-dimethylcarbamoxyquinolinium, a cationic carbamate (KI = 1.5 x 10(-8) M).	Acetylthiocholine	57-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	38-42
1907148-4	1991	Control values for red cell acetylcholinesterase (AChE) activity (mumol/min/mL blood) using acetylthiocholine (1 mM) were higher in the human (4.98) and the rhesus monkey (4.14) than in the marmoset (0.84) and the guinea-pig (0.83).	Acetylthiocholine	92-109	acetylcholinesterase (Cartwright blood group)	Homo sapiens	50-54
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
1908687-3	1991	For both sensitized and control specimens, saturation of AChase was obtained at approximately 3.12 mM substrate (acetylthiocholine); however, maximal enzyme activity in homogenates of ragweed-sensitized tissues was significantly less (0.862 +/- 0.088 absorbance units/min/mg protein [AU/min/mg]) compared to control homogenates (1.590 +/- 0.129 AU/min/mg; P less than 0.001).	Acetylthiocholine	113-130	acetylcholinesterase	Canis lupus familiaris	57-63
1849451-5	1991	The recombinant gene product exhibits biochemical traits similar to native "true" acetylcholinesterase as manifested by characteristic substrate inhibition, a Km of 117 microM toward acetylthiocholine, and a high sensitivity to the specific acetylcholinesterase inhibitor BW284C51.	Acetylthiocholine	183-200	acetylcholinesterase (Cartwright blood group)	Homo sapiens	82-102
1849451-5	1991	The recombinant gene product exhibits biochemical traits similar to native "true" acetylcholinesterase as manifested by characteristic substrate inhibition, a Km of 117 microM toward acetylthiocholine, and a high sensitivity to the specific acetylcholinesterase inhibitor BW284C51.	Acetylthiocholine	183-200	acetylcholinesterase (Cartwright blood group)	Homo sapiens	241-261
2263619-5	1990	When ligated to the cDNA and constructed into a transcription vector, this sequence encoded a synthetic mRNA translated in microinjected oocytes into catalytically active AcChoEase with marked preference for acetylthiocholine over butyrylthiocholine as a substrate, susceptibility to inhibition by the AcChoEase inhibitor BW284C51, and resistance to the BtChoEase inhibitor tetraisopropylpyrophosphoramide.	Acetylthiocholine	208-225	acetylcholinesterase (Cartwright blood group)	Homo sapiens	171-180
2263619-5	1990	When ligated to the cDNA and constructed into a transcription vector, this sequence encoded a synthetic mRNA translated in microinjected oocytes into catalytically active AcChoEase with marked preference for acetylthiocholine over butyrylthiocholine as a substrate, susceptibility to inhibition by the AcChoEase inhibitor BW284C51, and resistance to the BtChoEase inhibitor tetraisopropylpyrophosphoramide.	Acetylthiocholine	208-225	acetylcholinesterase (Cartwright blood group)	Homo sapiens	302-311
34865979-2	2022	In this assay, the analyte PM inhibited the hydrolysis of acetylthiocholine (ATCh) by AChE, preventing the formation of thiocholine (TCh) that would otherwise react with the AuNPs catalyst and deactivate the catalyst.	Acetylthiocholine	58-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	86-90
33588528-4	2021	Obviously, MnNS display an excellent response to thiocholine, deriving from the catalyzing hydrolysis of acetylthiocholine (ATCh) by acetylcholinesterase (AChE), which switches a homogeneous electrochemical OP detection process based on the depressing AChE activity with a limit of detection (LOD) of 0.025 ng mL-1.	Acetylthiocholine	105-122	acetylcholinesterase (Cartwright blood group)	Homo sapiens	133-153
33588528-4	2021	Obviously, MnNS display an excellent response to thiocholine, deriving from the catalyzing hydrolysis of acetylthiocholine (ATCh) by acetylcholinesterase (AChE), which switches a homogeneous electrochemical OP detection process based on the depressing AChE activity with a limit of detection (LOD) of 0.025 ng mL-1.	Acetylthiocholine	105-122	acetylcholinesterase (Cartwright blood group)	Homo sapiens	155-159
33588528-4	2021	Obviously, MnNS display an excellent response to thiocholine, deriving from the catalyzing hydrolysis of acetylthiocholine (ATCh) by acetylcholinesterase (AChE), which switches a homogeneous electrochemical OP detection process based on the depressing AChE activity with a limit of detection (LOD) of 0.025 ng mL-1.	Acetylthiocholine	105-122	acetylcholinesterase (Cartwright blood group)	Homo sapiens	252-256
33032200-4	2020	When acetylcholinesterase (AChE) was present, acetylthiocholine (ATCh) was catalytically hydrolyzed into thiocholine, which reduced MnO2 of PTDNP-MnNFs into Mn2+, subsequently blocking the FRET and enhancing the fluorescence.	Acetylthiocholine	46-63	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-25
33032200-4	2020	When acetylcholinesterase (AChE) was present, acetylthiocholine (ATCh) was catalytically hydrolyzed into thiocholine, which reduced MnO2 of PTDNP-MnNFs into Mn2+, subsequently blocking the FRET and enhancing the fluorescence.	Acetylthiocholine	46-63	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-31
33032200-4	2020	When acetylcholinesterase (AChE) was present, acetylthiocholine (ATCh) was catalytically hydrolyzed into thiocholine, which reduced MnO2 of PTDNP-MnNFs into Mn2+, subsequently blocking the FRET and enhancing the fluorescence.	Acetylthiocholine	65-69	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-25
33032200-4	2020	When acetylcholinesterase (AChE) was present, acetylthiocholine (ATCh) was catalytically hydrolyzed into thiocholine, which reduced MnO2 of PTDNP-MnNFs into Mn2+, subsequently blocking the FRET and enhancing the fluorescence.	Acetylthiocholine	65-69	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-31
34968836-3	2022	In this system, OPs can suppress the activity of acetylcholinesterase (AChE) efficiently, blocking the hydrolysis reaction of acetylthiocholine (ATCh) to generate thiocholine (TCh) by AChE.	Acetylthiocholine	126-143	acetylcholinesterase (Cartwright blood group)	Homo sapiens	49-69
34968836-3	2022	In this system, OPs can suppress the activity of acetylcholinesterase (AChE) efficiently, blocking the hydrolysis reaction of acetylthiocholine (ATCh) to generate thiocholine (TCh) by AChE.	Acetylthiocholine	126-143	acetylcholinesterase (Cartwright blood group)	Homo sapiens	71-75
34968836-3	2022	In this system, OPs can suppress the activity of acetylcholinesterase (AChE) efficiently, blocking the hydrolysis reaction of acetylthiocholine (ATCh) to generate thiocholine (TCh) by AChE.	Acetylthiocholine	126-143	acetylcholinesterase (Cartwright blood group)	Homo sapiens	184-188
34968836-3	2022	In this system, OPs can suppress the activity of acetylcholinesterase (AChE) efficiently, blocking the hydrolysis reaction of acetylthiocholine (ATCh) to generate thiocholine (TCh) by AChE.	Acetylthiocholine	145-149	acetylcholinesterase (Cartwright blood group)	Homo sapiens	49-69
34968836-3	2022	In this system, OPs can suppress the activity of acetylcholinesterase (AChE) efficiently, blocking the hydrolysis reaction of acetylthiocholine (ATCh) to generate thiocholine (TCh) by AChE.	Acetylthiocholine	145-149	acetylcholinesterase (Cartwright blood group)	Homo sapiens	71-75
34968836-3	2022	In this system, OPs can suppress the activity of acetylcholinesterase (AChE) efficiently, blocking the hydrolysis reaction of acetylthiocholine (ATCh) to generate thiocholine (TCh) by AChE.	Acetylthiocholine	145-149	acetylcholinesterase (Cartwright blood group)	Homo sapiens	184-188
34865979-2	2022	In this assay, the analyte PM inhibited the hydrolysis of acetylthiocholine (ATCh) by AChE, preventing the formation of thiocholine (TCh) that would otherwise react with the AuNPs catalyst and deactivate the catalyst.	Acetylthiocholine	77-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	86-90
34862575-3	2021	Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine (ATCh) to produce thiocholine which was further reacted with Ehrman"s reagent and decomposed to form a yellow product 2-nitro-5-thiobenate anion (TNB).	Acetylthiocholine	61-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34875277-0	2022	Interactions of human acetylcholinesterase with phenyl valerate and acetylthiocholine: Thiocholine as an enhancer of phenyl valerate esterase activity.	Acetylthiocholine	68-85	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-42
34862575-3	2021	Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine (ATCh) to produce thiocholine which was further reacted with Ehrman"s reagent and decomposed to form a yellow product 2-nitro-5-thiobenate anion (TNB).	Acetylthiocholine	61-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
35166114-5	2022	Interestingly, the 2D CMNSs with peroxidase-like properties exhibited a unique response to thiol compounds and were thus employed as highly efficient catalysts to develop HEC sensors for OPs based on the hydrolysis of acetylthiocholine (ATCh) to form thiocholine catalyzed by acetylcholinesterase (AChE) and the inhibition of AChE activity by OPs.	Acetylthiocholine	218-235	acetylcholinesterase (Cartwright blood group)	Homo sapiens	276-296
34476614-3	2021	Acetylcholinesterase hydrolyzed acetylthiocholine to generate thiocholine that bound with Cu2+ strongly via S-Cu-S bond.	Acetylthiocholine	32-49	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34404888-4	2021	This was a prospective study of 57 patients undergoing ambulatory or vascular surgery under GA. Cholinesterase activity was measured before the induction of anesthesia, after 15 min and at the end of surgery by calculating the capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase to hydrolyze AcetylThioCholine.	Acetylthiocholine	312-329	butyrylcholinesterase	Homo sapiens	96-110
34404888-4	2021	This was a prospective study of 57 patients undergoing ambulatory or vascular surgery under GA. Cholinesterase activity was measured before the induction of anesthesia, after 15 min and at the end of surgery by calculating the capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase to hydrolyze AcetylThioCholine.	Acetylthiocholine	312-329	acetylcholinesterase (Cartwright blood group)	Homo sapiens	245-265
35421656-2	2022	Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh).	Acetylthiocholine	53-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	14-34
35421656-2	2022	Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh).	Acetylthiocholine	53-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	36-40
35579472-4	2022	After the addition of acetylcholinesterase (AChE), the substrate acetylthiocholine could be hydrolyzed to thiocholine, which has a stronger binding power with mercury ions than T-Hg2+-T base pairs.	Acetylthiocholine	65-82	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
35473871-5	2022	Herein, thiocholine could be produced in hydrolysis reaction of acetylthiocholine catalyzed by the acetylcholinesterase (AChE), of which the catalytic activity could be irreversibly inhibitted by the introduction of organophosphates.	Acetylthiocholine	64-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	99-119
35473871-5	2022	Herein, thiocholine could be produced in hydrolysis reaction of acetylthiocholine catalyzed by the acetylcholinesterase (AChE), of which the catalytic activity could be irreversibly inhibitted by the introduction of organophosphates.	Acetylthiocholine	64-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	121-125
35166114-5	2022	Interestingly, the 2D CMNSs with peroxidase-like properties exhibited a unique response to thiol compounds and were thus employed as highly efficient catalysts to develop HEC sensors for OPs based on the hydrolysis of acetylthiocholine (ATCh) to form thiocholine catalyzed by acetylcholinesterase (AChE) and the inhibition of AChE activity by OPs.	Acetylthiocholine	218-235	acetylcholinesterase (Cartwright blood group)	Homo sapiens	298-302
35166114-5	2022	Interestingly, the 2D CMNSs with peroxidase-like properties exhibited a unique response to thiol compounds and were thus employed as highly efficient catalysts to develop HEC sensors for OPs based on the hydrolysis of acetylthiocholine (ATCh) to form thiocholine catalyzed by acetylcholinesterase (AChE) and the inhibition of AChE activity by OPs.	Acetylthiocholine	218-235	acetylcholinesterase (Cartwright blood group)	Homo sapiens	326-330
2906603-4	1988	Bambuterol was an extremely effective inhibitor of cholinesterase when butyrylthiocholine was used as substrate (I50 = 1.7 +/- 0.3 x 10(-8) M, N = 10) whereas it was 2400-fold less efficient in inhibiting cholinesterase with acetylthiocholine as substrate (I50 = 4.1 +/- 0.5 x 10(-5) M, N = 10).	Acetylthiocholine	225-242	butyrylcholinesterase	Homo sapiens	51-65
2765560-1	1989	The monoclonal antibody (mAb) AE-2 decreases the rate of hydrolysis of acetylthiocholine (ATC) by fetal bovine serum acetylcholinesterase (acetylcholine acetylhydrolase EC 3.1.1.7) (FBS-AChE) (Doctor, B.P.	Acetylthiocholine	71-88	acetylcholinesterase (Cartwright blood group)	Homo sapiens	117-137
2765560-1	1989	The monoclonal antibody (mAb) AE-2 decreases the rate of hydrolysis of acetylthiocholine (ATC) by fetal bovine serum acetylcholinesterase (acetylcholine acetylhydrolase EC 3.1.1.7) (FBS-AChE) (Doctor, B.P.	Acetylthiocholine	71-88	acetylcholinesterase (Cartwright blood group)	Homo sapiens	186-190
2765560-1	1989	The monoclonal antibody (mAb) AE-2 decreases the rate of hydrolysis of acetylthiocholine (ATC) by fetal bovine serum acetylcholinesterase (acetylcholine acetylhydrolase EC 3.1.1.7) (FBS-AChE) (Doctor, B.P.	Acetylthiocholine	90-93	acetylcholinesterase (Cartwright blood group)	Homo sapiens	117-137
2765560-1	1989	The monoclonal antibody (mAb) AE-2 decreases the rate of hydrolysis of acetylthiocholine (ATC) by fetal bovine serum acetylcholinesterase (acetylcholine acetylhydrolase EC 3.1.1.7) (FBS-AChE) (Doctor, B.P.	Acetylthiocholine	90-93	acetylcholinesterase (Cartwright blood group)	Homo sapiens	186-190
2906603-5	1988	Because butyrylthiocholine is the preferred substrate for cholinesterase (EC 3.1.1.8) and acetylthiocholine for acetylcholinesterase (EC 3.1.1.7), these results indicate that bambuterol is a remarkably selective and potent inhibitor of cholinesterase.	Acetylthiocholine	90-107	acetylcholinesterase (Cartwright blood group)	Homo sapiens	112-132
2906603-5	1988	Because butyrylthiocholine is the preferred substrate for cholinesterase (EC 3.1.1.8) and acetylthiocholine for acetylcholinesterase (EC 3.1.1.7), these results indicate that bambuterol is a remarkably selective and potent inhibitor of cholinesterase.	Acetylthiocholine	90-107	butyrylcholinesterase	Homo sapiens	118-132
3188254-1	1988	Sodium chloride, phosphate buffer and ethanol were studied for their effect on butyryl cholinesterase hydrolysis rate of acetylcholine, acetylthiocholine, butyrylthiocholine and nonion substrate of indophenylacetate.	Acetylthiocholine	136-153	butyrylcholinesterase	Homo sapiens	87-101
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
3123928-4	1987	The enzyme has true acetylcholinesterase (AChE) activity as hydrolysis of acetylthiocholine is three times faster than butyrylthiocholine and is inhibited by eserine, a specific inhibitor of AChE.	Acetylthiocholine	74-91	acetylcholinesterase	Mus musculus	42-46
3123928-4	1987	The enzyme has true acetylcholinesterase (AChE) activity as hydrolysis of acetylthiocholine is three times faster than butyrylthiocholine and is inhibited by eserine, a specific inhibitor of AChE.	Acetylthiocholine	74-91	acetylcholinesterase	Mus musculus	191-195
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
3229626-2	1988	Rabbit serum was shown to contain two cholinesterases which hydrolysed acetylthiocholine and butyrylthiocholine and one cholinesterase which hydrolysed only butyrylthiocholine.	Acetylthiocholine	71-88	acetylcholinesterase (Cartwright blood group)	Homo sapiens	38-52
3229626-6	1988	Using selective inhibitors (iso-OMPA, eserine, BNPP and BW-284C51) it was shown that the hydrolysis of acetylthiocholine and butyrylthiocholine in untreated native serum had properties of acetylcholinesterase (EC 3.1.1.7), butyrylcholinesterase (EC 3.1.1.8) and also some properties of carboxylesterase (EC 3.1.1.1).	Acetylthiocholine	103-120	acetylcholinesterase (Cartwright blood group)	Homo sapiens	188-208
3115978-9	1987	The catalytic properties of the enzyme were examined by titration with a fluorogenic reagent which revealed a turnover number for acetylthiocholine that was 6-fold lower than eel and 3-fold lower than human erythrocyte acetylcholinesterase.	Acetylthiocholine	130-147	Acetylcholine esterase	Drosophila melanogaster	219-239
3980478-6	1985	FBS acetylcholinesterase exhibited typical substrate inhibition, had a Km of 120 microM, and a turnover number of 5300 s-1 with the substrate acetylthiocholine.	Acetylthiocholine	142-159	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-24
3609156-3	1987	Electrophoretic patterns of the ChE were obtained by use of two thiocholines as substrate, and the number of fractions against acetylthiocholine were more than against butyrylthiocholine in dogs, miniature pigs, rabbits, and hamsters.	Acetylthiocholine	127-144	cholinesterase	Oryctolagus cuniculus	32-35
3954797-1	1986	The kinetic properties of cholinesterase (ChE) present in plasma were compared with those of purified human ChE using the substrates succinyldithiocholine (SDTCh), acetylthiocholine (AcTCh) and butyrylthiocholine (BuTCh).	Acetylthiocholine	183-188	butyrylcholinesterase	Homo sapiens	42-45
3580004-2	1987	For this reaction measured by irreversible inhibition of the acetylcholinesterase-catalyzed hydrolysis of acetylthiocholine the activation parameters delta H not equal to = 94 kJ/mole and delta S not equal to (25 degrees C) = -9.4 J/mol X deg were obtained.	Acetylthiocholine	106-123	acetylcholinesterase (Cartwright blood group)	Homo sapiens	61-81
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.	Acetylthiocholine	84-101	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.	Acetylthiocholine	84-101	homeobox C10	Homo sapiens	303-307
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
3968080-2	1985	Tetranitromethane inhibits acetylcholinesterase with respect to the hydrolysis of both acetylthiocholine and indophenyl acetate.	Acetylthiocholine	87-104	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-47
3970723-2	1985	Acetylcholinesterase was purified from bovine caudate nucleus by affinity chromatography to a specific activity of 1.1 mmoles acetylthiocholine X hr-1 X (mg protein)-1.	Acetylthiocholine	126-143	acetylcholinesterase	Bos taurus	0-20
3965482-4	1985	AchE synthesized in culture cleaved acetylthiocholine to thiocholine, which stochiometrically reduced the colorless indicator DTNB to a highly colored product.	Acetylthiocholine	36-53	acetylcholinesterase	Mus musculus	0-4
2861064-5	1985	As expected for an acetylcholinesterase, the enzyme has a high affinity for acetylthiocholine and is inhibited by excess concentrations of acetylthiocholine.	Acetylthiocholine	76-93	Acetylcholine esterase	Drosophila melanogaster	19-39
2861064-5	1985	As expected for an acetylcholinesterase, the enzyme has a high affinity for acetylthiocholine and is inhibited by excess concentrations of acetylthiocholine.	Acetylthiocholine	139-156	Acetylcholine esterase	Drosophila melanogaster	19-39
6870909-4	1983	The kinetics of irreversible cholinesterase inhibition were studied using two substrates, acetylthiocholine and butyrylthiocholine.	Acetylthiocholine	90-107	butyrylcholinesterase	Homo sapiens	29-43
6704184-2	1984	The reaction of acetylcholinesterase (EC 3.1.1.7; human erythrocytes) with phosphostigmine, haloxon and VX was studied, and the effect of three reversible ligands (TMA, edrophonium, coumarin) and of acetylthiocholine upon the time-dependent and time-independent (reversible) inhibition by the organophosphates was evaluated.	Acetylthiocholine	199-216	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-36
6704158-7	1984	True AChE activity (measured in the presence of a maximally effective concentration of tetraisopropylpyrophosphoramide) had a Vmax of 13.4 +/- 0.17 nmoles X min-1 X mg protein)-1 and an apparent Km value of 1 X 10(-4)M acetylthiocholine.	Acetylthiocholine	219-236	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
6704158-7	1984	True AChE activity (measured in the presence of a maximally effective concentration of tetraisopropylpyrophosphoramide) had a Vmax of 13.4 +/- 0.17 nmoles X min-1 X mg protein)-1 and an apparent Km value of 1 X 10(-4)M acetylthiocholine.	Acetylthiocholine	219-236	CD59 molecule (CD59 blood group)	Homo sapiens	157-162
6849970-7	1983	(c) Hereditary spherocytosis was singly differentiated by an elevated acetylcholinesterase activity with acetylthiocholine and by a vastly diminished sensitivity to stearic acid, while activity with phenylacetate was equal to control.	Acetylthiocholine	105-122	acetylcholinesterase (Cartwright blood group)	Homo sapiens	70-90
6807282-6	1982	Although the "resistant" AChE had a lower activity (Vm) on either a per milligram protein or a per individual basis, its apparent Km for acetylthiocholine was lower than that of "susceptible" AChE.	Acetylthiocholine	137-154	Acetylcholine esterase	Drosophila melanogaster	25-29
7108127-7	1982	7, 88-95) procedure for acetylthiocholine as substrate, are described as a rapid screening technique for reversible competitive and noncompetitive inhibitors of acetylcholinesterase activity.	Acetylthiocholine	24-41	acetylcholinesterase (Cartwright blood group)	Homo sapiens	161-181
6136252-1	1983	The measurement of low levels of cholinesterase or acetylcholinesterase by the Ellman method requires correction for a non-enzymatic increase in absorption at 412 millimicron that is due both to non-enzymatic hydrolysis of the acetylthiocholine substrate and to modification of the colour reagent.	Acetylthiocholine	227-244	butyrylcholinesterase	Homo sapiens	33-47
6136252-1	1983	The measurement of low levels of cholinesterase or acetylcholinesterase by the Ellman method requires correction for a non-enzymatic increase in absorption at 412 millimicron that is due both to non-enzymatic hydrolysis of the acetylthiocholine substrate and to modification of the colour reagent.	Acetylthiocholine	227-244	acetylcholinesterase (Cartwright blood group)	Homo sapiens	51-71
6807282-6	1982	Although the "resistant" AChE had a lower activity (Vm) on either a per milligram protein or a per individual basis, its apparent Km for acetylthiocholine was lower than that of "susceptible" AChE.	Acetylthiocholine	137-154	Acetylcholine esterase	Drosophila melanogaster	192-196
6894279-2	1981	Dipalmitoyllecithin- and egg lecithin-acetylcholinesterase complexes exhibit an affinity for acetylthiocholine different from that of the free enzyme.	Acetylthiocholine	93-110	acetylcholinesterase (Cartwright blood group)	Homo sapiens	38-58
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
6894279-3	1981	The binding to lecithin apparently abolishes the excess substrate inhibition of acetylcholinesterase; the affinity constants of acetylthiocholine, acetylcholine and acetylcarnitine for the lecithin-bound enzymes are higher than the ones found for the free enzyme.	Acetylthiocholine	128-145	acetylcholinesterase (Cartwright blood group)	Homo sapiens	80-100
222070-2	1979	The Km value of acetylcholinesterase for acetyl thiocholine was not altered in the reaction and the enzyme proved to be more resistant to heat denaturation.	Acetylthiocholine	41-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-36
7370307-1	1980	Comparative assays were made in a spectrophotometer and a microcalorimeter for the reaction between acetylcholinesterase (EC 3.1.1.7) and acetylthiocholine.	Acetylthiocholine	138-155	acetylcholinesterase (Cartwright blood group)	Homo sapiens	100-120
7248346-1	1980	The effect of pH on the kinetic constants of cholinesterase-catalyzed hydrolysis of isoamylacetate and acetylthiocholine was investigated.	Acetylthiocholine	103-120	butyrylcholinesterase	Homo sapiens	45-59
546451-1	1979	The activity of locust ganglia cholinesterase is found to depend on concentrations of acetylthiocholine (ATC), propionylthiocholine (PTC) and butyrylthiocholine (BTC); that of carboxylesterase--on concentration of p-nitrophenylacetate (25 degrees, pH 7,5).	Acetylthiocholine	86-103	butyrylcholinesterase	Homo sapiens	31-45
546451-1	1979	The activity of locust ganglia cholinesterase is found to depend on concentrations of acetylthiocholine (ATC), propionylthiocholine (PTC) and butyrylthiocholine (BTC); that of carboxylesterase--on concentration of p-nitrophenylacetate (25 degrees, pH 7,5).	Acetylthiocholine	105-108	butyrylcholinesterase	Homo sapiens	31-45
1009118-4	1976	The presence of a substrate (acetylthiocholine) decreased the rate of inactivation of bovine erythrocyte acetylcholinesterase by sodium dodecyl sulphate, but increased the rate of inactivation by propanol.	Acetylthiocholine	29-46	acetylcholinesterase	Bos taurus	105-125
748338-2	1978	The enzyme proved to be acetylcholinesterase (AChE) since acetylthiocholine was the preferred substrate, and eserine or BW284C5I inhibited the enzyme activity, while isoOMPA was without effect.	Acetylthiocholine	58-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	24-44
748338-2	1978	The enzyme proved to be acetylcholinesterase (AChE) since acetylthiocholine was the preferred substrate, and eserine or BW284C5I inhibited the enzyme activity, while isoOMPA was without effect.	Acetylthiocholine	58-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	46-50
603347-1	1977	Two kinetic evidences revealed that two cholinesterase forms are present in rat brain homogenate and involved in the hydrolysis of acetylthiocholine.	Acetylthiocholine	131-148	butyrylcholinesterase	Rattus norvegicus	40-54
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
970243-1	1976	The localization of acetylcholinesterase (AChE) activity in the nuclei of the amygdaloid body of man was studied by Gerebtzoff"s modification of Koelle"s acetylthiocholine method on 10 human brains.	Acetylthiocholine	154-171	acetylcholinesterase (Cartwright blood group)	Homo sapiens	20-40
970243-1	1976	The localization of acetylcholinesterase (AChE) activity in the nuclei of the amygdaloid body of man was studied by Gerebtzoff"s modification of Koelle"s acetylthiocholine method on 10 human brains.	Acetylthiocholine	154-171	acetylcholinesterase (Cartwright blood group)	Homo sapiens	42-46
18631530-1	1970	Housefly brain cholinesterase was histochemically demonstrated to hydrolyse phenylthioacetate at a very high rate, similar in distribution to that previously reported for acetylthiocholine.	Acetylthiocholine	171-188	butyrylcholinesterase	Homo sapiens	15-29
799612-3	1976	The activities of AChE and PChE were examined with the use of the substrates of acetylthiocholine and butrylthiocholine iodides (Koelle-Friedenwald"s method in Gomori"s modification).	Acetylthiocholine	80-97	acetylcholinesterase	Mus musculus	18-22
1238116-6	1975	With either of these inhibitors the measured rate of inactivation of eel acetylcholinesterase is the same whether activity is determined with this poor substrate or with a good substrate, acetylthiocholine.	Acetylthiocholine	188-205	acetylcholinesterase	Bos taurus	73-93
5315359-4	1971	The utility of histochemistry in conjunction with in vitro methods is discussed.The substrates acetylthiocholine and phenyl thioacetate were utilized in demonstrating cholinesterase.	Acetylthiocholine	95-112	butyrylcholinesterase	Homo sapiens	167-181
5315359-8	1971	A unique cholinesterase was found in motor end-plates of cricket muscle, which hydrolyses acetylthiocholine and which was inhibited by physostigmine.	Acetylthiocholine	90-107	butyrylcholinesterase	Homo sapiens	9-23
5378376-9	1969	Haloxon also combines with acetylcholinesterase by a non-progressive reaction, producing a complex that is reversible by dilution and by high concentrations of acetylcholine and acetylthiocholine.	Acetylthiocholine	178-195	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-47
18631530-2	1970	However, teleost neural retina cholinesterase would not hydrolyse the aromatic substrate, but the enzyme did cleave acetylthiocholine.	Acetylthiocholine	116-133	butyrylcholinesterase	Homo sapiens	31-45
14340030-0	1965	A POLAROGRAPHIC METHOD FOR FOLLOWING THE RATES OF CHOLINESTERASE-CATALYZED HYDROLYSES OF ACETYLTHIOCHOLINE.	Acetylthiocholine	89-106	butyrylcholinesterase	Homo sapiens	50-64
5358248-0	1969	Electronmicroscopic localization of cholinesterase at the neuromuscular junction by a quaternary carbon analogue of acetylthiocholine as substrate.	Acetylthiocholine	116-133	butyrylcholinesterase	Homo sapiens	36-50
33601648-2	2021	OPs effectively reduce the production of thiocholine in the acetylcholinesterase/acetylthiocholine reaction by inhibiting the activity of acetylcholinesterase.	Acetylthiocholine	81-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	60-80
33601648-2	2021	OPs effectively reduce the production of thiocholine in the acetylcholinesterase/acetylthiocholine reaction by inhibiting the activity of acetylcholinesterase.	Acetylthiocholine	81-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	138-158
34012694-4	2021	Acetylthiocholine (ATCh) could be catalytically hydrolyzed by acetylcholinesterase (AChE) to form thiocholine, which induces aggregation of the AgNPs.	Acetylthiocholine	0-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	62-82
33839958-3	2021	In the presence of AChE, acetylthiocholine (ATCh), a typical AChE substrate, is hydrolyzed to thiocholine (TCh).	Acetylthiocholine	25-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
33839958-3	2021	In the presence of AChE, acetylthiocholine (ATCh), a typical AChE substrate, is hydrolyzed to thiocholine (TCh).	Acetylthiocholine	25-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	61-65
33839958-3	2021	In the presence of AChE, acetylthiocholine (ATCh), a typical AChE substrate, is hydrolyzed to thiocholine (TCh).	Acetylthiocholine	44-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
33839958-3	2021	In the presence of AChE, acetylthiocholine (ATCh), a typical AChE substrate, is hydrolyzed to thiocholine (TCh).	Acetylthiocholine	44-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	61-65
34018740-6	2021	Further, MnNFs-Ru are employed for the homogeneous ECL determination of OPs, where acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine (ATCh) into thiocholine, which in turn decomposes MnNFs of MnNFs-Ru into Mn2+, and OPs inhibit AChE activity.	Acetylthiocholine	139-156	acetylcholinesterase (Cartwright blood group)	Homo sapiens	83-103
34018740-6	2021	Further, MnNFs-Ru are employed for the homogeneous ECL determination of OPs, where acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine (ATCh) into thiocholine, which in turn decomposes MnNFs of MnNFs-Ru into Mn2+, and OPs inhibit AChE activity.	Acetylthiocholine	139-156	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
34018740-6	2021	Further, MnNFs-Ru are employed for the homogeneous ECL determination of OPs, where acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine (ATCh) into thiocholine, which in turn decomposes MnNFs of MnNFs-Ru into Mn2+, and OPs inhibit AChE activity.	Acetylthiocholine	139-156	acetylcholinesterase (Cartwright blood group)	Homo sapiens	252-256
34018740-6	2021	Further, MnNFs-Ru are employed for the homogeneous ECL determination of OPs, where acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine (ATCh) into thiocholine, which in turn decomposes MnNFs of MnNFs-Ru into Mn2+, and OPs inhibit AChE activity.	Acetylthiocholine	158-162	acetylcholinesterase (Cartwright blood group)	Homo sapiens	83-103
34018740-6	2021	Further, MnNFs-Ru are employed for the homogeneous ECL determination of OPs, where acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine (ATCh) into thiocholine, which in turn decomposes MnNFs of MnNFs-Ru into Mn2+, and OPs inhibit AChE activity.	Acetylthiocholine	158-162	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
34018740-6	2021	Further, MnNFs-Ru are employed for the homogeneous ECL determination of OPs, where acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine (ATCh) into thiocholine, which in turn decomposes MnNFs of MnNFs-Ru into Mn2+, and OPs inhibit AChE activity.	Acetylthiocholine	158-162	acetylcholinesterase (Cartwright blood group)	Homo sapiens	252-256
33961403-4	2021	Interestingly, S-S-AuNCs displayed a unique response to thiol compounds and low pH values and were thus pioneered as a high-efficiency sensor for OPs based on acetylcholinesterase (AChE)-catalyzed hydrolysis of acetylthiocholine into thiocholine and CH3COOH and OP inhibition of AChE activity.	Acetylthiocholine	211-228	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-179
33961403-4	2021	Interestingly, S-S-AuNCs displayed a unique response to thiol compounds and low pH values and were thus pioneered as a high-efficiency sensor for OPs based on acetylcholinesterase (AChE)-catalyzed hydrolysis of acetylthiocholine into thiocholine and CH3COOH and OP inhibition of AChE activity.	Acetylthiocholine	211-228	acetylcholinesterase (Cartwright blood group)	Homo sapiens	181-185
33961403-4	2021	Interestingly, S-S-AuNCs displayed a unique response to thiol compounds and low pH values and were thus pioneered as a high-efficiency sensor for OPs based on acetylcholinesterase (AChE)-catalyzed hydrolysis of acetylthiocholine into thiocholine and CH3COOH and OP inhibition of AChE activity.	Acetylthiocholine	211-228	acetylcholinesterase (Cartwright blood group)	Homo sapiens	279-283
33872129-3	2021	Cholinesterase activity in whole blood, erythrocyte, and plasma was detected using acetylthiocholine and the dithio-bis-(nitrobenzoic acid) method.	Acetylthiocholine	83-100	butyrylcholinesterase	Homo sapiens	0-14
34012694-4	2021	Acetylthiocholine (ATCh) could be catalytically hydrolyzed by acetylcholinesterase (AChE) to form thiocholine, which induces aggregation of the AgNPs.	Acetylthiocholine	0-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	84-88
33186817-3	2021	This is because that MnO2 NS have oxidized characteristic, and they can react with choline (TCh), which is the product of acetylthiocholine (ATCh) catalyzed by acetylcholinesterase (AChE).	Acetylthiocholine	122-139	acetylcholinesterase (Cartwright blood group)	Homo sapiens	182-186
33592758-7	2021	Thiol-bearing compounds such as thiocholine generated through the hydrolysis of acetylthiocholine by acetylcholinesterase (AChE) interacted with the surface of CdS QDs thus blocking the ECL.	Acetylthiocholine	80-97	acetylcholinesterase (Cartwright blood group)	Homo sapiens	101-121
33592758-7	2021	Thiol-bearing compounds such as thiocholine generated through the hydrolysis of acetylthiocholine by acetylcholinesterase (AChE) interacted with the surface of CdS QDs thus blocking the ECL.	Acetylthiocholine	80-97	acetylcholinesterase (Cartwright blood group)	Homo sapiens	123-127
33186817-3	2021	This is because that MnO2 NS have oxidized characteristic, and they can react with choline (TCh), which is the product of acetylthiocholine (ATCh) catalyzed by acetylcholinesterase (AChE).	Acetylthiocholine	141-145	acetylcholinesterase (Cartwright blood group)	Homo sapiens	182-186
33076048-3	2021	When AChE was introduced, acetylthiocholine could be hydrolyzed to generate thiocholine, which efficiently triggered the reduction of MnO2 NSs into Mn2+, resulting in the decrease of fluorescence.	Acetylthiocholine	26-43	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
33406172-3	2021	With the presence of thiocholine (TCh), derived from acetylthiocholine (ATCh) hydrolyzed by AChE, the coordination environment of the CDs@Eu/GMP ICPs was interrupted, leading to the collapse of the CDs@Eu/GMP ICP network and the corresponding release of guest CDs into the surrounding environment.	Acetylthiocholine	53-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-96
33406172-3	2021	With the presence of thiocholine (TCh), derived from acetylthiocholine (ATCh) hydrolyzed by AChE, the coordination environment of the CDs@Eu/GMP ICPs was interrupted, leading to the collapse of the CDs@Eu/GMP ICP network and the corresponding release of guest CDs into the surrounding environment.	Acetylthiocholine	72-76	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-96
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
33076046-2	2021	The sensing assay is based on the "quenched off" state of bimetallic NC with the addition of Cu2+ ions that can be "switched on" due to generation of thiocholine (TCh), a catalytic product of enzymatic reaction of acetylthiocholine (ATCh) using acetylcholinesterase (AChE) enzyme.	Acetylthiocholine	214-231	acetylcholinesterase (Cartwright blood group)	Homo sapiens	245-265
33280706-1	2021	Herein, we propose rapid, precise acetylcholinesterase (AChE) inhibition-based sensing strategy for malathion detection in the presence of Ag-GO and acetylthiocholine (ATCh).	Acetylthiocholine	149-166	acetylcholinesterase (Cartwright blood group)	Homo sapiens	34-54
33280706-1	2021	Herein, we propose rapid, precise acetylcholinesterase (AChE) inhibition-based sensing strategy for malathion detection in the presence of Ag-GO and acetylthiocholine (ATCh).	Acetylthiocholine	149-166	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60
33280706-1	2021	Herein, we propose rapid, precise acetylcholinesterase (AChE) inhibition-based sensing strategy for malathion detection in the presence of Ag-GO and acetylthiocholine (ATCh).	Acetylthiocholine	168-172	acetylcholinesterase (Cartwright blood group)	Homo sapiens	34-54
33280706-1	2021	Herein, we propose rapid, precise acetylcholinesterase (AChE) inhibition-based sensing strategy for malathion detection in the presence of Ag-GO and acetylthiocholine (ATCh).	Acetylthiocholine	168-172	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60
33076046-2	2021	The sensing assay is based on the "quenched off" state of bimetallic NC with the addition of Cu2+ ions that can be "switched on" due to generation of thiocholine (TCh), a catalytic product of enzymatic reaction of acetylthiocholine (ATCh) using acetylcholinesterase (AChE) enzyme.	Acetylthiocholine	214-231	acetylcholinesterase (Cartwright blood group)	Homo sapiens	267-271
33049656-5	2020	We measured blood acetylcholinesterase (AChE) activity using the acetylcholine analog acetylthiocholine.	Acetylthiocholine	86-103	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-38
33225325-5	2020	AChE can catalyze the hydrolysis of acetylthiocholine (ATCh) to form thiocholine (TCh), which can induce the fluorescence quenching of AuNCs while having no obvious influence on the fluorescence intensity of FL.	Acetylthiocholine	36-53	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
33225325-5	2020	AChE can catalyze the hydrolysis of acetylthiocholine (ATCh) to form thiocholine (TCh), which can induce the fluorescence quenching of AuNCs while having no obvious influence on the fluorescence intensity of FL.	Acetylthiocholine	55-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
33049656-5	2020	We measured blood acetylcholinesterase (AChE) activity using the acetylcholine analog acetylthiocholine.	Acetylthiocholine	86-103	acetylcholinesterase (Cartwright blood group)	Homo sapiens	40-44
32691085-6	2020	In the absence of target molecule, a large number of thiocholines (TCh) were yielded from hydrolysis of acetylthiocholine (ATCh) by BChE.	Acetylthiocholine	104-121	butyrylcholinesterase	Homo sapiens	132-136
32691085-6	2020	In the absence of target molecule, a large number of thiocholines (TCh) were yielded from hydrolysis of acetylthiocholine (ATCh) by BChE.	Acetylthiocholine	123-127	butyrylcholinesterase	Homo sapiens	132-136
32676787-2	2020	TCH is produced from the butyrylcholinesterase-acetylthiocholine system, accompanied by target-triggered rolling circle amplification (RCA).	Acetylthiocholine	47-64	butyrylcholinesterase	Homo sapiens	25-46
32805836-4	2020	With the presence of thiocholine (TCh), an enzymatic product hydrolyzed from acetylthiocholine (ATCh) by AChE, the competitive coordination of Tb3+ between GMP and TCh results in the collapse of ICP network and thereby the release of GQDs into the solution, thus, the fluorescence of Tb/GMP turns off and the fluorescence of GQDs turns on.	Acetylthiocholine	77-94	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
32805836-4	2020	With the presence of thiocholine (TCh), an enzymatic product hydrolyzed from acetylthiocholine (ATCh) by AChE, the competitive coordination of Tb3+ between GMP and TCh results in the collapse of ICP network and thereby the release of GQDs into the solution, thus, the fluorescence of Tb/GMP turns off and the fluorescence of GQDs turns on.	Acetylthiocholine	96-100	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
32892929-3	2020	With the assistance of acetylcholinesterase (AChE), acetylthiocholine (ATCh) is hydrolyzed into thiocholine (TCh) which can effectively etch the ultrathin MnO2 nanosheets, resulting in the dissociation of MnO2-CdS from the photoelectrode.	Acetylthiocholine	52-69	acetylcholinesterase (Cartwright blood group)	Homo sapiens	23-43
32892929-3	2020	With the assistance of acetylcholinesterase (AChE), acetylthiocholine (ATCh) is hydrolyzed into thiocholine (TCh) which can effectively etch the ultrathin MnO2 nanosheets, resulting in the dissociation of MnO2-CdS from the photoelectrode.	Acetylthiocholine	52-69	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-49
32892929-3	2020	With the assistance of acetylcholinesterase (AChE), acetylthiocholine (ATCh) is hydrolyzed into thiocholine (TCh) which can effectively etch the ultrathin MnO2 nanosheets, resulting in the dissociation of MnO2-CdS from the photoelectrode.	Acetylthiocholine	71-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	23-43
32892929-3	2020	With the assistance of acetylcholinesterase (AChE), acetylthiocholine (ATCh) is hydrolyzed into thiocholine (TCh) which can effectively etch the ultrathin MnO2 nanosheets, resulting in the dissociation of MnO2-CdS from the photoelectrode.	Acetylthiocholine	71-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-49
32833082-7	2020	When AChE was present, the substrate acetylthiocholine (ATCh) was hydrolyzed to thiocholine (TCh) that is capable of decomposing MnO2 nanosheets.	Acetylthiocholine	37-54	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
32833082-7	2020	When AChE was present, the substrate acetylthiocholine (ATCh) was hydrolyzed to thiocholine (TCh) that is capable of decomposing MnO2 nanosheets.	Acetylthiocholine	56-60	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
32833082-15	2020	When AChE is present, acetylthiocholine iodide (ATCh) is hydrolyzed to thiocholine (TCh) with reducibility for decomposing MnO2 nanosheets.	Acetylthiocholine	48-52	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
32578586-4	2020	BChE can catalyze acetylthiocholine and produce thiocholine, which effectively decomposes the MnO2 NSs into Mn2+, resulting in the disappearance of the IFE and recovery of fluorescence of S-dots.	Acetylthiocholine	18-35	butyrylcholinesterase	Homo sapiens	0-4
31352306-9	2019	RESULTS: It is the first demonstration that RBP-8000 catalyzes the hydrolysis of acetylthiocholine (ATC).	Acetylthiocholine	81-98	SURP and G-patch domain containing 1	Homo sapiens	44-47
32397331-9	2020	We monitored the enzymatic activity of AChE through the SERS spectrum of thiocholine (TC), the end product from acetylthiocholine (ATC).	Acetylthiocholine	112-129	acetylcholinesterase (Cartwright blood group)	Homo sapiens	39-43
31756075-4	2019	In the presence of BChE and acetylthiocholine (ATCh), nano FeOOH can be effectively decomposed by the enzymatic hydrolysate (thiocholine), leading to the recovery of AuNCs fluorescence.	Acetylthiocholine	47-51	butyrylcholinesterase	Homo sapiens	19-23
31560517-5	2019	The thiocholine generated from acetylcholinesterase (AChE)-induced catalyzed hydrolysis of acetylthiocholine (ATCh) efficiently directed CdS QDs away from PPT/ITO via electrostatic repulsion, subsequently decreasing PEC current, whereas chlorpyrifos prohibited the generation of thiocholine through inhibiting AChE activity.	Acetylthiocholine	91-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	31-51
31560517-5	2019	The thiocholine generated from acetylcholinesterase (AChE)-induced catalyzed hydrolysis of acetylthiocholine (ATCh) efficiently directed CdS QDs away from PPT/ITO via electrostatic repulsion, subsequently decreasing PEC current, whereas chlorpyrifos prohibited the generation of thiocholine through inhibiting AChE activity.	Acetylthiocholine	91-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	53-57
31560517-5	2019	The thiocholine generated from acetylcholinesterase (AChE)-induced catalyzed hydrolysis of acetylthiocholine (ATCh) efficiently directed CdS QDs away from PPT/ITO via electrostatic repulsion, subsequently decreasing PEC current, whereas chlorpyrifos prohibited the generation of thiocholine through inhibiting AChE activity.	Acetylthiocholine	91-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	310-314
31560517-5	2019	The thiocholine generated from acetylcholinesterase (AChE)-induced catalyzed hydrolysis of acetylthiocholine (ATCh) efficiently directed CdS QDs away from PPT/ITO via electrostatic repulsion, subsequently decreasing PEC current, whereas chlorpyrifos prohibited the generation of thiocholine through inhibiting AChE activity.	Acetylthiocholine	110-114	acetylcholinesterase (Cartwright blood group)	Homo sapiens	31-51
31560517-5	2019	The thiocholine generated from acetylcholinesterase (AChE)-induced catalyzed hydrolysis of acetylthiocholine (ATCh) efficiently directed CdS QDs away from PPT/ITO via electrostatic repulsion, subsequently decreasing PEC current, whereas chlorpyrifos prohibited the generation of thiocholine through inhibiting AChE activity.	Acetylthiocholine	110-114	acetylcholinesterase (Cartwright blood group)	Homo sapiens	53-57
31560517-5	2019	The thiocholine generated from acetylcholinesterase (AChE)-induced catalyzed hydrolysis of acetylthiocholine (ATCh) efficiently directed CdS QDs away from PPT/ITO via electrostatic repulsion, subsequently decreasing PEC current, whereas chlorpyrifos prohibited the generation of thiocholine through inhibiting AChE activity.	Acetylthiocholine	110-114	acetylcholinesterase (Cartwright blood group)	Homo sapiens	310-314
31677527-6	2020	Yeast surface-displayed AChE can catalyze the hydrolysis of acetylthiocholine to produce thiocholine.	Acetylthiocholine	60-77	Acetylcholine esterase	Drosophila melanogaster	24-28
31247192-5	2019	For AChE, two visible substrates were used, acetylthiocholine and 3-(acetamido)-N,N,N-trimethylanilinium.	Acetylthiocholine	44-61	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
31061298-4	2019	With AChE, its substrate ACh will be hydrolyzed into thiocholine and the fluorescence signals exhibit a dramatic decrease at 465 nm, Under optimal conditions, the fluorescent probe shows sensitive responses to AChE in the range of 0.01-0.6 mU/mL.	Acetylthiocholine	5-8	acetylcholinesterase (Cartwright blood group)	Homo sapiens	210-214
31353389-5	2019	In the presence of acetylcholinesterase (AChE), acetylthiocholine (ATCh) could be hydrolyzed to thiocholine (TCh), which can reduce MnO2 to Mn2+ and trigger the decomposition of MnO2 nanosheets.	Acetylthiocholine	48-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
31353389-5	2019	In the presence of acetylcholinesterase (AChE), acetylthiocholine (ATCh) could be hydrolyzed to thiocholine (TCh), which can reduce MnO2 to Mn2+ and trigger the decomposition of MnO2 nanosheets.	Acetylthiocholine	48-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	41-45
31353389-5	2019	In the presence of acetylcholinesterase (AChE), acetylthiocholine (ATCh) could be hydrolyzed to thiocholine (TCh), which can reduce MnO2 to Mn2+ and trigger the decomposition of MnO2 nanosheets.	Acetylthiocholine	67-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
31353389-5	2019	In the presence of acetylcholinesterase (AChE), acetylthiocholine (ATCh) could be hydrolyzed to thiocholine (TCh), which can reduce MnO2 to Mn2+ and trigger the decomposition of MnO2 nanosheets.	Acetylthiocholine	67-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	41-45
31363918-4	2019	Acetylthiocholine is enzymatically split by AChE to produce thiocholine which triggers the decomposition of Ellmans"s reagent to form a yellow colored product (2-nitro-5-thiobenzoate anion).	Acetylthiocholine	0-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
30888170-3	2019	Upon addition of AChE and acetylthiocholine (ATCh), the enzymatic hydrolysate (thiocholine) could seize Cu2+ from UCNPs-Cu2+ mixture, resulting in the quenched FL triggered on.	Acetylthiocholine	45-49	acetylcholinesterase (Cartwright blood group)	Homo sapiens	17-21
30876606-9	2019	Thiocholine (TCh), which produced from acetylthiocholine(ATCh) by the hydrolysis of acetylcholinesterase (AChE), can "turn on" the fluorescence sensor.	Acetylthiocholine	39-56	acetylcholinesterase (Cartwright blood group)	Homo sapiens	84-104
30876606-9	2019	Thiocholine (TCh), which produced from acetylthiocholine(ATCh) by the hydrolysis of acetylcholinesterase (AChE), can "turn on" the fluorescence sensor.	Acetylthiocholine	39-56	acetylcholinesterase (Cartwright blood group)	Homo sapiens	106-110
30822441-2	2019	Ellman"s method using Acetylthiocholine (ATCh) is the standard approach for the detection of AChE activity.	Acetylthiocholine	22-39	acetylcholinesterase (Cartwright blood group)	Homo sapiens	93-97
30822441-2	2019	Ellman"s method using Acetylthiocholine (ATCh) is the standard approach for the detection of AChE activity.	Acetylthiocholine	41-45	acetylcholinesterase (Cartwright blood group)	Homo sapiens	93-97
30849722-3	2019	The AChE or BChE catalyzed hydrolysis reaction of acetylthiocholine or butyrylthiocholine to generate thiocholine, whose sulfhydryl group strongly captured Cu2+ to inhibit the oxidization of OPD, thus effectively preserving the natural fluorescence emission of CDs.	Acetylthiocholine	50-67	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
30849722-3	2019	The AChE or BChE catalyzed hydrolysis reaction of acetylthiocholine or butyrylthiocholine to generate thiocholine, whose sulfhydryl group strongly captured Cu2+ to inhibit the oxidization of OPD, thus effectively preserving the natural fluorescence emission of CDs.	Acetylthiocholine	50-67	butyrylcholinesterase	Homo sapiens	12-16
30672607-8	2019	Enzyme stability was also studied, which exhibited that immobilized AChE retained its catalytic activity up to 60 days and retained 80% of the hydrolytic activity even at 37 C. On the basis of the success of immobilized enzyme (covalent) being inhibited by acetylthiocholine, the sensor was administered for the inhibition by monocrotophos and dimethoate that are used widely as pesticides in agricultural.	Acetylthiocholine	257-274	acetylcholinesterase (Cartwright blood group)	Homo sapiens	68-72
31020297-4	2019	AChE can hydrolyze acetylthiocholine (ATCh) to form thiocholine (TCh) which contains a thiol group.	Acetylthiocholine	19-36	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
31020297-4	2019	AChE can hydrolyze acetylthiocholine (ATCh) to form thiocholine (TCh) which contains a thiol group.	Acetylthiocholine	38-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
30565170-3	2019	Based on this discovery, a highly sensitive detection of acetylthiocholine (ATCl) was achieved using the acetylcholinesterase (AChE) biosensor.	Acetylthiocholine	57-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-125
30938485-4	2019	Taking advantage of their favorable structure and composition, the optimized product exhibits superior electrochemical activity toward thiocholine produced by AChE-catalyzed hydrolysis of acetylthiocholine.	Acetylthiocholine	188-205	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-163
30702092-10	2019	The hydrolysis of acetylthiocholine was catalyzed by AChE on the AuNPs, and the metal coordination polymer was then formed which resulted in the aggregation of the perylene probe and the formation of the excimer emission.	Acetylthiocholine	18-35	acetylcholinesterase (Cartwright blood group)	Homo sapiens	53-57
30565170-3	2019	Based on this discovery, a highly sensitive detection of acetylthiocholine (ATCl) was achieved using the acetylcholinesterase (AChE) biosensor.	Acetylthiocholine	57-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	127-131
30565170-3	2019	Based on this discovery, a highly sensitive detection of acetylthiocholine (ATCl) was achieved using the acetylcholinesterase (AChE) biosensor.	Acetylthiocholine	76-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-125
30565170-3	2019	Based on this discovery, a highly sensitive detection of acetylthiocholine (ATCl) was achieved using the acetylcholinesterase (AChE) biosensor.	Acetylthiocholine	76-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	127-131
30565170-5	2019	ATCl was catalyzed by acetylcholinesterase (AChE) to produce thiocholine, which served as the coreactant accelerator to improve the ECL signal of Au NC-S2O82- system.	Acetylthiocholine	0-4	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-42
30565170-5	2019	ATCl was catalyzed by acetylcholinesterase (AChE) to produce thiocholine, which served as the coreactant accelerator to improve the ECL signal of Au NC-S2O82- system.	Acetylthiocholine	0-4	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
30201403-2	2018	Acetylthiocholine (ATCh) is the most popular substrate for the detection of AChE activity.	Acetylthiocholine	0-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	76-80
30201403-2	2018	Acetylthiocholine (ATCh) is the most popular substrate for the detection of AChE activity.	Acetylthiocholine	19-23	acetylcholinesterase (Cartwright blood group)	Homo sapiens	76-80
29594716-3	2018	The enzyme acetylcholinesterase (AChE) is known catalyze the hydrolysis of acetylthiocholine to produce thiocholine.	Acetylthiocholine	75-92	acetylcholinesterase (Cartwright blood group)	Homo sapiens	11-31
29567179-4	2018	The detection mechanism monitors the inhibition of the activity of acetylcholinesterase (AChE) by the pesticide, in which the production of thiocholine from the hydrolysis of acetylthiocholine (ATCh) catalyzed by AChE is reduced.	Acetylthiocholine	194-198	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-87
29567179-4	2018	The detection mechanism monitors the inhibition of the activity of acetylcholinesterase (AChE) by the pesticide, in which the production of thiocholine from the hydrolysis of acetylthiocholine (ATCh) catalyzed by AChE is reduced.	Acetylthiocholine	194-198	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-93
29567179-4	2018	The detection mechanism monitors the inhibition of the activity of acetylcholinesterase (AChE) by the pesticide, in which the production of thiocholine from the hydrolysis of acetylthiocholine (ATCh) catalyzed by AChE is reduced.	Acetylthiocholine	194-198	acetylcholinesterase (Cartwright blood group)	Homo sapiens	213-217
29892419-3	2018	The acetylthiocholine and dithio-bis-(nitrobenzoic acid) method was used to detect the cholinesterase activities in whole blood, erythrocytes and plasma.	Acetylthiocholine	4-21	butyrylcholinesterase	Homo sapiens	87-101
29929132-3	2018	Cholinesterase activities in whole blood, red blood cell and plasma were detected using acetylthiocholine and dithio-bis-(nitrobenzoic acid) method; Genetic Genotyping of POT1 rs1034794, POT1 rs10250202, TERF1 rs3863242 and TERT rs2736098 were performed with PCR-RFLP.	Acetylthiocholine	88-105	butyrylcholinesterase	Homo sapiens	0-14
29908755-5	2018	PoBChE hydrolyzed acetylthiocholine slightly faster than butyrylthiocholine, but was sensitive to BChE-specific inhibitors.	Acetylthiocholine	18-35	butyrylcholinesterase	Homo sapiens	2-6
29567179-4	2018	The detection mechanism monitors the inhibition of the activity of acetylcholinesterase (AChE) by the pesticide, in which the production of thiocholine from the hydrolysis of acetylthiocholine (ATCh) catalyzed by AChE is reduced.	Acetylthiocholine	175-192	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-87
29567179-4	2018	The detection mechanism monitors the inhibition of the activity of acetylcholinesterase (AChE) by the pesticide, in which the production of thiocholine from the hydrolysis of acetylthiocholine (ATCh) catalyzed by AChE is reduced.	Acetylthiocholine	175-192	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-93
29567179-4	2018	The detection mechanism monitors the inhibition of the activity of acetylcholinesterase (AChE) by the pesticide, in which the production of thiocholine from the hydrolysis of acetylthiocholine (ATCh) catalyzed by AChE is reduced.	Acetylthiocholine	175-192	acetylcholinesterase (Cartwright blood group)	Homo sapiens	213-217
29594716-3	2018	The enzyme acetylcholinesterase (AChE) is known catalyze the hydrolysis of acetylthiocholine to produce thiocholine.	Acetylthiocholine	75-92	acetylcholinesterase (Cartwright blood group)	Homo sapiens	33-37
28494368-2	2017	By utilizing the acetylcholinesterase (AChE) mediated hydrolysis of acetylthiocholine to thiocholine where the activity of AChE is inhibited by the presence of organophosphate pesticides (OPPs), the subsequent thiocholine-induced aggregation of 10OsCO-Au NPs can be monitored by the change in color of the NPs solution and the variation in intensity of the SERS CO signal.	Acetylthiocholine	68-85	acetylcholinesterase (Cartwright blood group)	Homo sapiens	17-37
28494368-2	2017	By utilizing the acetylcholinesterase (AChE) mediated hydrolysis of acetylthiocholine to thiocholine where the activity of AChE is inhibited by the presence of organophosphate pesticides (OPPs), the subsequent thiocholine-induced aggregation of 10OsCO-Au NPs can be monitored by the change in color of the NPs solution and the variation in intensity of the SERS CO signal.	Acetylthiocholine	68-85	acetylcholinesterase (Cartwright blood group)	Homo sapiens	39-43
28494368-2	2017	By utilizing the acetylcholinesterase (AChE) mediated hydrolysis of acetylthiocholine to thiocholine where the activity of AChE is inhibited by the presence of organophosphate pesticides (OPPs), the subsequent thiocholine-induced aggregation of 10OsCO-Au NPs can be monitored by the change in color of the NPs solution and the variation in intensity of the SERS CO signal.	Acetylthiocholine	68-85	acetylcholinesterase (Cartwright blood group)	Homo sapiens	123-127
28494368-2	2017	By utilizing the acetylcholinesterase (AChE) mediated hydrolysis of acetylthiocholine to thiocholine where the activity of AChE is inhibited by the presence of organophosphate pesticides (OPPs), the subsequent thiocholine-induced aggregation of 10OsCO-Au NPs can be monitored by the change in color of the NPs solution and the variation in intensity of the SERS CO signal.	Acetylthiocholine	68-85	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	357-361
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
28315592-4	2017	Thiocholine, which was produced from acetylthiocholine (ATC) by the hydrolysis of butyrylcholinesterase (BChE), could cause the aggregation of Au NPs and the corresponding recovery of FRET-quenched fluorescence emission.	Acetylthiocholine	37-54	butyrylcholinesterase	Homo sapiens	82-103
28315592-4	2017	Thiocholine, which was produced from acetylthiocholine (ATC) by the hydrolysis of butyrylcholinesterase (BChE), could cause the aggregation of Au NPs and the corresponding recovery of FRET-quenched fluorescence emission.	Acetylthiocholine	37-54	butyrylcholinesterase	Homo sapiens	105-109
28315592-4	2017	Thiocholine, which was produced from acetylthiocholine (ATC) by the hydrolysis of butyrylcholinesterase (BChE), could cause the aggregation of Au NPs and the corresponding recovery of FRET-quenched fluorescence emission.	Acetylthiocholine	56-59	butyrylcholinesterase	Homo sapiens	82-103
28315592-4	2017	Thiocholine, which was produced from acetylthiocholine (ATC) by the hydrolysis of butyrylcholinesterase (BChE), could cause the aggregation of Au NPs and the corresponding recovery of FRET-quenched fluorescence emission.	Acetylthiocholine	56-59	butyrylcholinesterase	Homo sapiens	105-109
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
27208478-4	2016	And the enzyme of AChE was used to catalyze the substrate of acetylthiocholine (ATCh) to produce thiocholine (TCh).	Acetylthiocholine	61-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-22
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.	Acetylthiocholine	33-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
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.	Acetylthiocholine	52-55	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
27498323-6	2016	The hydrolysis product of acetylthiocholine catalyzed by AChE induced the maleimide ring destruction and activated the fluorescence performance of TPE.	Acetylthiocholine	26-43	acetylcholinesterase (Cartwright blood group)	Homo sapiens	57-61
27208478-4	2016	And the enzyme of AChE was used to catalyze the substrate of acetylthiocholine (ATCh) to produce thiocholine (TCh).	Acetylthiocholine	80-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-22
26839920-3	2016	The competitive binding by a thiol group (-SH), produced in the hydrolysis reaction of acetylthiocholine (ACh) chloride with acetylcholinesterase (AChE), removes mercury ions from the base pairs, causing a nuclease-catalyzed digestion, and the subsequent electrochemical response increase due to the weak electrostatic repulsion between the product-mononucleotides and the ITO electrode.	Acetylthiocholine	87-106	acetylcholinesterase (Cartwright blood group)	Homo sapiens	125-145
27136042-4	2016	The fluorescence of PhO-dex-GO remarkably increased as AChE catalyzed the hydrolysis of acetylthiocholine (ATCh) to give thiocholine and acetic acid.	Acetylthiocholine	88-105	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
27136042-4	2016	The fluorescence of PhO-dex-GO remarkably increased as AChE catalyzed the hydrolysis of acetylthiocholine (ATCh) to give thiocholine and acetic acid.	Acetylthiocholine	107-111	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
26839920-3	2016	The competitive binding by a thiol group (-SH), produced in the hydrolysis reaction of acetylthiocholine (ACh) chloride with acetylcholinesterase (AChE), removes mercury ions from the base pairs, causing a nuclease-catalyzed digestion, and the subsequent electrochemical response increase due to the weak electrostatic repulsion between the product-mononucleotides and the ITO electrode.	Acetylthiocholine	87-106	acetylcholinesterase (Cartwright blood group)	Homo sapiens	147-151
26841098-2	2016	ALP and AChE were integrated into the PEC system through the sandwich immunobinding and could specifically catalyze the hydrolysis of ascorbic acid 2-phosphate (AAP) or the acetylthiocholine (ATC) to in situ generate ascorbic acid (AA) or thiocholine (TC) for sacrificial electron donating.	Acetylthiocholine	173-190	alkaline phosphatase, placental	Homo sapiens	0-3
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	51-68	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	51-68	acetylcholinesterase (Cartwright blood group)	Homo sapiens	81-85
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	70-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	70-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	41-45
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	70-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	81-85
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	114-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	114-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	41-45
26547618-4	2016	In the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCl), the AChE catalyzes the hydrolysis of ATCl into positively charged thiocholine which would replace the citrate on AuNPs through the strong AuS bond and convert the negative charged surface to be positively charged.	Acetylthiocholine	114-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	81-85
26841098-2	2016	ALP and AChE were integrated into the PEC system through the sandwich immunobinding and could specifically catalyze the hydrolysis of ascorbic acid 2-phosphate (AAP) or the acetylthiocholine (ATC) to in situ generate ascorbic acid (AA) or thiocholine (TC) for sacrificial electron donating.	Acetylthiocholine	192-195	alkaline phosphatase, placental	Homo sapiens	0-3
26339933-2	2016	Upon the hydrolysis of acetylthiocholine catalyzed by AChE, the product thiocholine stabilizes the in situ formation of CdS QDs in homogenous solution.	Acetylthiocholine	23-40	acetylcholinesterase (Cartwright blood group)	Homo sapiens	54-58
26141104-2	2015	Subsequently, an AuNCs@11-MUA-Cu(2+) ensemble-based fluorescent chemosensor, which is amenable to convenient, sensitive, selective, turn-on and real-time assay of acetylcholinesterase (AChE), could be developed by using acetylthiocholine (ATCh) as the substrate.	Acetylthiocholine	220-237	acetylcholinesterase (Cartwright blood group)	Homo sapiens	163-183
27682399-3	2016	Active acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine into -SH containing thiocholine to replace the NC-dots and trigger the aggregation of AuNPs.	Acetylthiocholine	63-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	7-27
27682399-3	2016	Active acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylthiocholine into -SH containing thiocholine to replace the NC-dots and trigger the aggregation of AuNPs.	Acetylthiocholine	63-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	29-33
26141104-2	2015	Subsequently, an AuNCs@11-MUA-Cu(2+) ensemble-based fluorescent chemosensor, which is amenable to convenient, sensitive, selective, turn-on and real-time assay of acetylcholinesterase (AChE), could be developed by using acetylthiocholine (ATCh) as the substrate.	Acetylthiocholine	220-237	acetylcholinesterase (Cartwright blood group)	Homo sapiens	185-189
26141104-2	2015	Subsequently, an AuNCs@11-MUA-Cu(2+) ensemble-based fluorescent chemosensor, which is amenable to convenient, sensitive, selective, turn-on and real-time assay of acetylcholinesterase (AChE), could be developed by using acetylthiocholine (ATCh) as the substrate.	Acetylthiocholine	239-243	acetylcholinesterase (Cartwright blood group)	Homo sapiens	163-183
26141104-2	2015	Subsequently, an AuNCs@11-MUA-Cu(2+) ensemble-based fluorescent chemosensor, which is amenable to convenient, sensitive, selective, turn-on and real-time assay of acetylcholinesterase (AChE), could be developed by using acetylthiocholine (ATCh) as the substrate.	Acetylthiocholine	239-243	acetylcholinesterase (Cartwright blood group)	Homo sapiens	185-189
25569873-2	2015	The detection mechanism is based on the facts that AuNPs quench the fluorescence of UCNPs and organophosphorus pesticides (OPs) inhibit the activity of acetylcholinesterase (AChE) which catalyzes the hydrolysis of acetylthiocholine (ATC) into thiocholine.	Acetylthiocholine	214-231	acetylcholinesterase (Cartwright blood group)	Homo sapiens	152-172
26217956-2	2015	ChE catalyzes its substrate (acetylthiocholine) and produces thiocholine and acetate acid.	Acetylthiocholine	29-46	butyrylcholinesterase	Homo sapiens	0-3
25569873-2	2015	The detection mechanism is based on the facts that AuNPs quench the fluorescence of UCNPs and organophosphorus pesticides (OPs) inhibit the activity of acetylcholinesterase (AChE) which catalyzes the hydrolysis of acetylthiocholine (ATC) into thiocholine.	Acetylthiocholine	214-231	acetylcholinesterase (Cartwright blood group)	Homo sapiens	174-178
25660508-3	2015	Both AChE and BChE can catalyze the hydrolysis of the acetylthiocholine (ATCh) substrate and produce positively-charged thiocholine (TCh).	Acetylthiocholine	54-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
25569873-2	2015	The detection mechanism is based on the facts that AuNPs quench the fluorescence of UCNPs and organophosphorus pesticides (OPs) inhibit the activity of acetylcholinesterase (AChE) which catalyzes the hydrolysis of acetylthiocholine (ATC) into thiocholine.	Acetylthiocholine	233-236	acetylcholinesterase (Cartwright blood group)	Homo sapiens	152-172
25660508-3	2015	Both AChE and BChE can catalyze the hydrolysis of the acetylthiocholine (ATCh) substrate and produce positively-charged thiocholine (TCh).	Acetylthiocholine	54-71	butyrylcholinesterase	Homo sapiens	14-18
25569873-2	2015	The detection mechanism is based on the facts that AuNPs quench the fluorescence of UCNPs and organophosphorus pesticides (OPs) inhibit the activity of acetylcholinesterase (AChE) which catalyzes the hydrolysis of acetylthiocholine (ATC) into thiocholine.	Acetylthiocholine	233-236	acetylcholinesterase (Cartwright blood group)	Homo sapiens	174-178
25660508-3	2015	Both AChE and BChE can catalyze the hydrolysis of the acetylthiocholine (ATCh) substrate and produce positively-charged thiocholine (TCh).	Acetylthiocholine	73-77	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
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.	Acetylthiocholine	210-227	acetylcholinesterase (Cartwright blood group)	Homo sapiens	128-148
25660508-3	2015	Both AChE and BChE can catalyze the hydrolysis of the acetylthiocholine (ATCh) substrate and produce positively-charged thiocholine (TCh).	Acetylthiocholine	73-77	butyrylcholinesterase	Homo sapiens	14-18
26165279-2	2015	Thiocholine (TCh) produced in the enzymatic reaction of AChE with acetylthiocholine (ATCh) as a substrate was oxidized on a microelectrode array formed in a main flow channel.	Acetylthiocholine	66-83	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60
26165279-2	2015	Thiocholine (TCh) produced in the enzymatic reaction of AChE with acetylthiocholine (ATCh) as a substrate was oxidized on a microelectrode array formed in a main flow channel.	Acetylthiocholine	85-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60
25560517-5	2015	Using acetylthiocholine (ATCh) as the substrate, this H39GFP/Cu(2+) complex-based sensor was further applied for the turn-on fluorescence detection of acetylcholinesterase (AChE) activity.	Acetylthiocholine	6-23	acetylcholinesterase (Cartwright blood group)	Homo sapiens	151-171
25560517-5	2015	Using acetylthiocholine (ATCh) as the substrate, this H39GFP/Cu(2+) complex-based sensor was further applied for the turn-on fluorescence detection of acetylcholinesterase (AChE) activity.	Acetylthiocholine	6-23	acetylcholinesterase (Cartwright blood group)	Homo sapiens	173-177
25560517-5	2015	Using acetylthiocholine (ATCh) as the substrate, this H39GFP/Cu(2+) complex-based sensor was further applied for the turn-on fluorescence detection of acetylcholinesterase (AChE) activity.	Acetylthiocholine	25-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	151-171
25560517-5	2015	Using acetylthiocholine (ATCh) as the substrate, this H39GFP/Cu(2+) complex-based sensor was further applied for the turn-on fluorescence detection of acetylcholinesterase (AChE) activity.	Acetylthiocholine	25-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	173-177
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.	Acetylthiocholine	210-227	acetylcholinesterase (Cartwright blood group)	Homo sapiens	150-154
24395570-3	2014	Cholinergic status was determined by measuring the cumulative capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) to hydrolyze the AChE substrate acetylthiocholine.	Acetylthiocholine	173-190	acetylcholinesterase (Cartwright blood group)	Homo sapiens	80-100
24576786-9	2014	The interactions observed between the substrates of AChE and PVase suggest that part of PVase activity might be a protein with acetylthiocholine-hydrolyzing activity.	Acetylthiocholine	127-144	acetylcholinesterase (Cartwright blood group)	Gallus gallus	52-56
23125138-7	2014	Erythrocyte acetylcholinesterase (AChE) activity was evaluated by acetylthiocholine inhibition as an index of overall toxicity.	Acetylthiocholine	66-83	acetylcholinesterase	Mus musculus	34-38
24395570-3	2014	Cholinergic status was determined by measuring the cumulative capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) to hydrolyze the AChE substrate acetylthiocholine.	Acetylthiocholine	173-190	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
24395570-3	2014	Cholinergic status was determined by measuring the cumulative capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) to hydrolyze the AChE substrate acetylthiocholine.	Acetylthiocholine	173-190	butyrylcholinesterase	Homo sapiens	112-133
24395570-3	2014	Cholinergic status was determined by measuring the cumulative capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) to hydrolyze the AChE substrate acetylthiocholine.	Acetylthiocholine	173-190	butyrylcholinesterase	Homo sapiens	135-139
24395570-3	2014	Cholinergic status was determined by measuring the cumulative capacity of serum acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) to hydrolyze the AChE substrate acetylthiocholine.	Acetylthiocholine	173-190	acetylcholinesterase (Cartwright blood group)	Homo sapiens	158-162
24433789-5	2014	Physiological plasma cholinesterase activity was 198.9 +- 5.8 nmol/min/ml for male and 205.2 +- 5.0 nmol/min/ml for female using acetylthiocholine as substrate.	Acetylthiocholine	129-146	cholinesterase	Oryctolagus cuniculus	21-35
24360998-3	2014	The colorimetric and fluorometric assays were based on the following processes: (1) owing to the hydrolysis of acetylthiocholine in the presence of AChE, the fluorescein-based probe can rapidly induce 1,4-addition of the hydrolysis product thiocholine to alpha,beta-unsaturated ketone in the compound 1, resulting in strong fluorescence and absorption changes; (2) in the presence of the corresponding inhibitor, the fluorescence enhancement or the absorption change would be inhibited in that the formation of thiocholine was hindered.	Acetylthiocholine	111-128	acetylcholinesterase (Cartwright blood group)	Homo sapiens	148-152
24077614-5	2013	In the present study, we carried out both computational modeling and experimental kinetic analysis on the catalytic activities of these promising new BChE mutants against other known substrates, including neurotransmitter acetylcholine (ACh), acetylthiocholine (ATC), butyrylthiocholine (BTC), and (+)-cocaine, in comparison with the corresponding catalytic activity against (-)-cocaine.	Acetylthiocholine	243-260	butyrylcholinesterase	Homo sapiens	150-154
24225492-4	2014	The principle of this approach is based on the hydrolysis of acetylthiocholine (ATCh) by AChE, which yields the thiol-bearing compound thiocholine (TCh) that at trace concentrations stabilized the in situ generated CdS quantum dots (QDs).	Acetylthiocholine	61-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-93
24225492-4	2014	The principle of this approach is based on the hydrolysis of acetylthiocholine (ATCh) by AChE, which yields the thiol-bearing compound thiocholine (TCh) that at trace concentrations stabilized the in situ generated CdS quantum dots (QDs).	Acetylthiocholine	80-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-93
24299064-9	2013	The AChE-catalyzed hydrolysis of acetylthiocholine to the thiol-functionalized thiocholine enabled the probing of the enzymatic activity of AChE through the hemin/G-quadruplex-catalyzed aerobic oxidation of thiocholine to the respective disulfide and the concomitant generation of the fluorescent resorufin product.	Acetylthiocholine	33-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
24299064-9	2013	The AChE-catalyzed hydrolysis of acetylthiocholine to the thiol-functionalized thiocholine enabled the probing of the enzymatic activity of AChE through the hemin/G-quadruplex-catalyzed aerobic oxidation of thiocholine to the respective disulfide and the concomitant generation of the fluorescent resorufin product.	Acetylthiocholine	33-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	140-144
24077614-5	2013	In the present study, we carried out both computational modeling and experimental kinetic analysis on the catalytic activities of these promising new BChE mutants against other known substrates, including neurotransmitter acetylcholine (ACh), acetylthiocholine (ATC), butyrylthiocholine (BTC), and (+)-cocaine, in comparison with the corresponding catalytic activity against (-)-cocaine.	Acetylthiocholine	262-265	butyrylcholinesterase	Homo sapiens	150-154
23603132-2	2013	In this assay, AChE catalyzes the hydrolysis of acetylthiocholine (ATCh) to form thiocholine which induces fluorescence quenching of DNA-Cu/AgNCs.	Acetylthiocholine	48-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	15-19
23777789-5	2013	We were able to demonstrate that this is caused by competition between the MWCNTs and acetylthiocholine for the active sites of AChE.	Acetylthiocholine	86-103	acetylcholinesterase (Cartwright blood group)	Homo sapiens	128-132
23603132-2	2013	In this assay, AChE catalyzes the hydrolysis of acetylthiocholine (ATCh) to form thiocholine which induces fluorescence quenching of DNA-Cu/AgNCs.	Acetylthiocholine	67-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	15-19
23597308-2	2013	In this method, the AChE molecules catalyzed the hydrolysis of acetylthiocholine (ATCl) to form thiocholine, which in turn can specifically react with fluorescent squaraine derivative, a specific chemodosimeter for thiol-containing compounds, resulting in fluorescence quenching and offering a low fluorometric background for the further detection of AChE inhibitor.	Acetylthiocholine	63-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	20-24
23597308-2	2013	In this method, the AChE molecules catalyzed the hydrolysis of acetylthiocholine (ATCl) to form thiocholine, which in turn can specifically react with fluorescent squaraine derivative, a specific chemodosimeter for thiol-containing compounds, resulting in fluorescence quenching and offering a low fluorometric background for the further detection of AChE inhibitor.	Acetylthiocholine	63-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	351-355
23597308-2	2013	In this method, the AChE molecules catalyzed the hydrolysis of acetylthiocholine (ATCl) to form thiocholine, which in turn can specifically react with fluorescent squaraine derivative, a specific chemodosimeter for thiol-containing compounds, resulting in fluorescence quenching and offering a low fluorometric background for the further detection of AChE inhibitor.	Acetylthiocholine	82-86	acetylcholinesterase (Cartwright blood group)	Homo sapiens	20-24
23597308-2	2013	In this method, the AChE molecules catalyzed the hydrolysis of acetylthiocholine (ATCl) to form thiocholine, which in turn can specifically react with fluorescent squaraine derivative, a specific chemodosimeter for thiol-containing compounds, resulting in fluorescence quenching and offering a low fluorometric background for the further detection of AChE inhibitor.	Acetylthiocholine	82-86	acetylcholinesterase (Cartwright blood group)	Homo sapiens	351-355
23379291-13	2013	Recombinant P. papatasi AChE1 was expressed in the baculovirus system and characterized as an insect acetylcholinesterase with substrate preference for acetylthiocholine and inhibition at high substrate concentration.	Acetylthiocholine	152-169	Acetylcholine esterase	Drosophila melanogaster	101-121
23047027-0	2013	Hydrolysis of low concentrations of the acetylthiocholine analogs acetyl(homo)thiocholine and acetyl(nor)thiocholine by acetylcholinesterase may be limited by selective gating at the enzyme peripheral site.	Acetylthiocholine	40-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-140
23379662-3	2013	In the presence of AChE, ATCh was hydrolyzed to thiocholine and acetate.	Acetylthiocholine	25-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
21600321-2	2011	AChE hydrolyses acetylthiocholine (ATCh) in thiocoline (TC) and acetic acid (AA).	Acetylthiocholine	16-33	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
23386352-7	2013	This chapter describes both techniques using the deacetylation of acetyl-lysine residues in model peptides by sirtuin enzymes as well as the hydrolysis of acetylthiocholine by acetylcholinesterase as examples.	Acetylthiocholine	155-172	acetylcholinesterase (Cartwright blood group)	Homo sapiens	176-196
22503679-2	2012	The enzyme AChE catalyzes the hydrolysis of acetylthiocholine to thiocholine, which can be electrochemically oxidized.	Acetylthiocholine	44-61	acetylcholinesterase (Cartwright blood group)	Homo sapiens	11-15
22145985-5	2012	Blood AChE activity determined using acetylthiocholine as substrate showed 20% activity remaining in sarin-exposed animals compare to controls.	Acetylthiocholine	37-54	acetylcholinesterase	Cavia porcellus	6-10
21872994-4	2012	The recombinant enzyme was inhibited by eserine, coroxon, and paraoxon and exhibited K(m) values of 63.9muM for acetylthiocholine and 96.7muM for butyrylthiocholine, confirming its biochemical identity as an acetylcholinesterase (EC 3.1.1.7).	Acetylthiocholine	112-129	acetylcholinesterase	Stomoxys calcitrans	208-228
22148672-2	2012	In this method, AChE mediates the hydrolysis of acetylthiocholine (ATCl) to form thiocholine, and the latter further reduces AuCl(4)(-) to Au NPs without Au nanoseeds.	Acetylthiocholine	48-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
22148672-2	2012	In this method, AChE mediates the hydrolysis of acetylthiocholine (ATCl) to form thiocholine, and the latter further reduces AuCl(4)(-) to Au NPs without Au nanoseeds.	Acetylthiocholine	67-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
22148672-4	2012	On the other hand, the hydrolysis of ATCl is inhibited in the presence of ACh or organophosphate pesticides (OPs, a AChE inhibitor), which will decrease the catalytic growth of Au NPs and, as a result, reduce the orientational response of LCs.	Acetylthiocholine	37-41	acetylcholinesterase (Cartwright blood group)	Homo sapiens	116-120
21600321-2	2011	AChE hydrolyses acetylthiocholine (ATCh) in thiocoline (TC) and acetic acid (AA).	Acetylthiocholine	35-39	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
21376964-2	2011	Under the catalytic effect of acetylcholinesterase (AChE), acetylthiocholine (ATCh) hydrolysis released thiocholine (TCh) which could react with N-(7-dimethylamino-4-methylcoumarin-3-yl) maleimide (DACM) to produce a blue fluorescence compound.	Acetylthiocholine	59-76	acetylcholinesterase (Cartwright blood group)	Homo sapiens	30-50
22099654-2	2011	The assay principle is based on catalytic hydrolysis of acetylthiocholine into thiocholine by acetylcholinesterase, which induces the aggregation of Au nanoparticles and the color change from claret-red to purple or even grey.	Acetylthiocholine	56-73	acetylcholinesterase (Cartwright blood group)	Homo sapiens	94-114
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.	Acetylthiocholine	198-215	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.	Acetylthiocholine	198-215	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.	Acetylthiocholine	198-215	acetylcholinesterase (Cartwright blood group)	Homo sapiens	242-246
21889639-2	2011	Acetylcholinesterase (AChE) mediated the hydrolysis of acetylthiocholine to produce thiocholine, which interacted with the silver nanoparticles to give a specific SERS spectrum.	Acetylthiocholine	55-72	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
21889639-2	2011	Acetylcholinesterase (AChE) mediated the hydrolysis of acetylthiocholine to produce thiocholine, which interacted with the silver nanoparticles to give a specific SERS spectrum.	Acetylthiocholine	55-72	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
21740955-1	2011	Stereoselectivity of reversible inhibition of butyrylcholinesterase (BChE; EC 3.1.1.8) by optically pure ethopropazine [10-(2-diethylaminopropyl)phenothiazine hydrochloride] enantiomers and racemate was studied with acetylthiocholine (0.002-250 mM) as substrate.	Acetylthiocholine	216-233	butyrylcholinesterase	Homo sapiens	46-67
21740955-1	2011	Stereoselectivity of reversible inhibition of butyrylcholinesterase (BChE; EC 3.1.1.8) by optically pure ethopropazine [10-(2-diethylaminopropyl)phenothiazine hydrochloride] enantiomers and racemate was studied with acetylthiocholine (0.002-250 mM) as substrate.	Acetylthiocholine	216-233	butyrylcholinesterase	Homo sapiens	69-73
21376964-2	2011	Under the catalytic effect of acetylcholinesterase (AChE), acetylthiocholine (ATCh) hydrolysis released thiocholine (TCh) which could react with N-(7-dimethylamino-4-methylcoumarin-3-yl) maleimide (DACM) to produce a blue fluorescence compound.	Acetylthiocholine	59-76	acetylcholinesterase (Cartwright blood group)	Homo sapiens	52-56
21376964-2	2011	Under the catalytic effect of acetylcholinesterase (AChE), acetylthiocholine (ATCh) hydrolysis released thiocholine (TCh) which could react with N-(7-dimethylamino-4-methylcoumarin-3-yl) maleimide (DACM) to produce a blue fluorescence compound.	Acetylthiocholine	78-82	acetylcholinesterase (Cartwright blood group)	Homo sapiens	30-50
21376964-2	2011	Under the catalytic effect of acetylcholinesterase (AChE), acetylthiocholine (ATCh) hydrolysis released thiocholine (TCh) which could react with N-(7-dimethylamino-4-methylcoumarin-3-yl) maleimide (DACM) to produce a blue fluorescence compound.	Acetylthiocholine	78-82	acetylcholinesterase (Cartwright blood group)	Homo sapiens	52-56
21364766-8	2011	The atypical BChE hydrolyzes acetylthiocholine (ATCh) and propionylthiocholine (PTCh) preferentially but butyrylthiocholine (BTCh) to a considerable extent, which is different from the substrate specificity of AChE or BChE.	Acetylthiocholine	48-52	acetylcholinesterase	Oryzias latipes	210-214
20381645-5	2010	Immediately after sacrifice, hearts were placed in a buffered solution containing acetylthiocholine, which precipitates with acetylcholinesterase, allowing identification of cholinergic nerves.	Acetylthiocholine	82-99	acetylcholinesterase (Yt blood group)	Sus scrofa	125-145
21105647-1	2010	In a previous communication, kinetic beta-deuterium secondary isotope effects were reported that support a mechanism for substrate-activated turnover of acetylthiocholine by human butyrylcholinesterase (BuChE) wherein the accumulating reactant state is a tetrahedral intermediate ( Tormos , J. R. ; et al.	Acetylthiocholine	153-170	butyrylcholinesterase	Homo sapiens	180-201
21105647-1	2010	In a previous communication, kinetic beta-deuterium secondary isotope effects were reported that support a mechanism for substrate-activated turnover of acetylthiocholine by human butyrylcholinesterase (BuChE) wherein the accumulating reactant state is a tetrahedral intermediate ( Tormos , J. R. ; et al.	Acetylthiocholine	153-170	butyrylcholinesterase	Homo sapiens	203-208
21105647-7	2010	In this contribution additional isotope effect experiments are described with acetyl-labeled acetylthiocholines (CL(3)COSCH(2)CH(2)N(+)Me(3); L = H or D) that also support accumulation of the tetrahedral intermediate in Drosophila melanogaster acetylcholinesterase (DmAChE) catalysis.	Acetylthiocholine	93-111	Acetylcholine esterase	Drosophila melanogaster	244-264
21105647-7	2010	In this contribution additional isotope effect experiments are described with acetyl-labeled acetylthiocholines (CL(3)COSCH(2)CH(2)N(+)Me(3); L = H or D) that also support accumulation of the tetrahedral intermediate in Drosophila melanogaster acetylcholinesterase (DmAChE) catalysis.	Acetylthiocholine	93-111	Acetylcholine esterase	Drosophila melanogaster	266-272
21105647-11	2010	Transition states for Drosophila melanogaster AChE-catalyzed hydrolysis of acetylthiocholine were further characterized by measuring solvent isotope effects and determining proton inventories.	Acetylthiocholine	75-92	Acetylcholine esterase	Drosophila melanogaster	46-50
20949898-2	2010	The assay is based on a disulfide-thiol interchange reaction between the intramolecularly quenched dimeric dye BODIPY FL l-cystine and thiocholine generated by the AChE-catalyzed hydrolysis of acetylthiocholine (ATCh), which results in a brightly fluorescent monomeric product owing to the cleavage of the disulfide-coupled form of the dye.	Acetylthiocholine	193-210	acetylcholinesterase (Cartwright blood group)	Homo sapiens	164-168
20949898-2	2010	The assay is based on a disulfide-thiol interchange reaction between the intramolecularly quenched dimeric dye BODIPY FL l-cystine and thiocholine generated by the AChE-catalyzed hydrolysis of acetylthiocholine (ATCh), which results in a brightly fluorescent monomeric product owing to the cleavage of the disulfide-coupled form of the dye.	Acetylthiocholine	212-216	acetylcholinesterase (Cartwright blood group)	Homo sapiens	164-168
19487014-2	2009	The substrate of acetylthiocholine is hydrolysed by the cholinesterase (ChE) from soil animal pheretima, and the produced thiocholine reacts with the 2,6-DCIP to give obvious shift of electrochemical signal.	Acetylthiocholine	17-34	butyrylcholinesterase	Homo sapiens	56-70
20143889-4	2010	Acetylcholinesterase was used as the labeling enzyme to convert acetylthiocholine to thiocholine.	Acetylthiocholine	64-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
20410609-5	2010	The hydrolysis rate of the novel compounds by human AChE was one order of magnitude lower than that of the traditional substrates, acetylthiocholine and acetyl-beta-methylthiocholine, whereas the hydrolysis rate using human butyrylcholinesterase was two orders of magnitude lower than that of the traditional substrates.	Acetylthiocholine	131-148	acetylcholinesterase (Cartwright blood group)	Homo sapiens	52-56
19757435-1	2009	The hydrolysis of acetylcholine and acetylthiocholine as catalyzed by the enzyme acetylcholinesterase was monitored by CE with contactless conductivity detection by determining the acetate produced in the reaction.	Acetylthiocholine	36-53	acetylcholinesterase (Cartwright blood group)	Homo sapiens	81-101
19487014-2	2009	The substrate of acetylthiocholine is hydrolysed by the cholinesterase (ChE) from soil animal pheretima, and the produced thiocholine reacts with the 2,6-DCIP to give obvious shift of electrochemical signal.	Acetylthiocholine	17-34	butyrylcholinesterase	Homo sapiens	72-75
19154124-1	2009	We report herein a new colorimetric assay method for acetylcholinesterase (AChE) activity and its inhibitor screening by making use of the following facts: (1) the aggregation of gold nanoparticles (Au-NPs) results in the red-shift of the plasmon absorption due to interparticle plasmon interactions and (2) AChE can catalyze the hydrolysis of acetylthiocholine into thiocholine which can induce the aggregation of Au-NPs.	Acetylthiocholine	344-361	acetylcholinesterase (Cartwright blood group)	Homo sapiens	53-73
19778238-4	2009	There are reports of non-enzymatic hydrolysis by oximes of acetylthiocholine in in vitro preparations in the widely used Ellman assay for AChE activity, which may confound the interpretation of AChE activity by producing elevated results.	Acetylthiocholine	59-76	acetylcholinesterase	Cavia porcellus	138-142
19778238-4	2009	There are reports of non-enzymatic hydrolysis by oximes of acetylthiocholine in in vitro preparations in the widely used Ellman assay for AChE activity, which may confound the interpretation of AChE activity by producing elevated results.	Acetylthiocholine	59-76	acetylcholinesterase	Cavia porcellus	194-198
19428926-2	2009	In this assay, AChE was immobilized on particle filters which were perfused with acetylthiocholine, Ellman"s reagent and phosphate buffer.	Acetylthiocholine	81-98	acetylcholinesterase	Sus scrofa	15-19
19238297-4	2009	The PQQ electrode was then utilized as a thiol-specific sensor for the real-time monitoring of thiocholine generated from the hydrolysis of acetylthiocholine (ASCh) by acetylcholinesterase (AChE).	Acetylthiocholine	140-157	acetylcholinesterase (Cartwright blood group)	Homo sapiens	168-188
19238297-4	2009	The PQQ electrode was then utilized as a thiol-specific sensor for the real-time monitoring of thiocholine generated from the hydrolysis of acetylthiocholine (ASCh) by acetylcholinesterase (AChE).	Acetylthiocholine	140-157	acetylcholinesterase (Cartwright blood group)	Homo sapiens	190-194
19472276-2	2009	The progress of the enzymatic reaction of the hydrolysis of acetylthiocholine at pH 8 in the presence of AChE and the inhibitor studied is determined by measuring at 230 nm the peak area of the reaction product thiocholine (TCh).	Acetylthiocholine	60-77	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
19154124-1	2009	We report herein a new colorimetric assay method for acetylcholinesterase (AChE) activity and its inhibitor screening by making use of the following facts: (1) the aggregation of gold nanoparticles (Au-NPs) results in the red-shift of the plasmon absorption due to interparticle plasmon interactions and (2) AChE can catalyze the hydrolysis of acetylthiocholine into thiocholine which can induce the aggregation of Au-NPs.	Acetylthiocholine	344-361	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-79
19130375-5	2009	The voltammetric results have shown that the current shifts more anodically as the Au/MBT/PANI/AChE/PVAc biosensor responded to successive acetylthiocholine (ATCh) substrate addition under anaerobic conditions in 0.1 M phosphate buffer, KCl (pH 7.2) solution and aqueous organic solvent solutions.	Acetylthiocholine	139-156	proteinase 3	Homo sapiens	86-89
19130375-5	2009	The voltammetric results have shown that the current shifts more anodically as the Au/MBT/PANI/AChE/PVAc biosensor responded to successive acetylthiocholine (ATCh) substrate addition under anaerobic conditions in 0.1 M phosphate buffer, KCl (pH 7.2) solution and aqueous organic solvent solutions.	Acetylthiocholine	139-156	acetylcholinesterase (Cartwright blood group)	Homo sapiens	95-99
19130375-5	2009	The voltammetric results have shown that the current shifts more anodically as the Au/MBT/PANI/AChE/PVAc biosensor responded to successive acetylthiocholine (ATCh) substrate addition under anaerobic conditions in 0.1 M phosphate buffer, KCl (pH 7.2) solution and aqueous organic solvent solutions.	Acetylthiocholine	158-162	proteinase 3	Homo sapiens	86-89
19130375-5	2009	The voltammetric results have shown that the current shifts more anodically as the Au/MBT/PANI/AChE/PVAc biosensor responded to successive acetylthiocholine (ATCh) substrate addition under anaerobic conditions in 0.1 M phosphate buffer, KCl (pH 7.2) solution and aqueous organic solvent solutions.	Acetylthiocholine	158-162	acetylcholinesterase (Cartwright blood group)	Homo sapiens	95-99
18096154-3	2008	Competition assays with the substrate acetylthiocholine showed a concentration-dependent reduction in rat brain cholinesterase Vmax without changes in apparent Km.	Acetylthiocholine	38-55	butyrylcholinesterase	Rattus norvegicus	112-126
27873775-2	2008	Cyclic voltammetric experiments performed with the SAM-AchE biosensor in phosphate buffer solutions (pH = 7.2) containing acetylthiocholine confirmed the formation of thiocholine and its electrochemical oxidation at Ep = 0.28 V vs Ag/AgCl.	Acetylthiocholine	122-139	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
18602908-0	2008	Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis.	Acetylthiocholine	96-113	acetylcholinesterase (Cartwright blood group)	Homo sapiens	42-62
18602908-5	2008	Here we show that the reaction of carbachol (carbamoylcholine) with AChE can be monitored both with acetylthiocholine as a reporter substrate and with thioflavin T as a fluorescent reporter group.	Acetylthiocholine	100-117	acetylcholinesterase (Cartwright blood group)	Homo sapiens	68-72
17300836-3	2007	Acetylthiocholine and butyrylthiocholine (identified in mammalian studies as diagnostic substrates for AChE and BChE respectively) were hydrolyzed mainly, but not exclusively, by these enzymes.	Acetylthiocholine	0-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	103-107
17300836-3	2007	Acetylthiocholine and butyrylthiocholine (identified in mammalian studies as diagnostic substrates for AChE and BChE respectively) were hydrolyzed mainly, but not exclusively, by these enzymes.	Acetylthiocholine	0-17	butyrylcholinesterase	Homo sapiens	112-116
17716616-2	2007	Cholinesterase activity is measured indirectly by quantifying the concentration of 5-thio-2-nitrobenzoic acid (TNB) ion formed in the reaction between the thiol reagent 5,5"-dithiobis-2-nitrobenzoic acid (DTNB) and thiocholine, a product of substrate (i.e., acetylthiocholine [ATCh]) hydrolysis by the cholinesterase.	Acetylthiocholine	258-275	butyrylcholinesterase	Homo sapiens	0-14
17716616-2	2007	Cholinesterase activity is measured indirectly by quantifying the concentration of 5-thio-2-nitrobenzoic acid (TNB) ion formed in the reaction between the thiol reagent 5,5"-dithiobis-2-nitrobenzoic acid (DTNB) and thiocholine, a product of substrate (i.e., acetylthiocholine [ATCh]) hydrolysis by the cholinesterase.	Acetylthiocholine	277-281	butyrylcholinesterase	Homo sapiens	0-14
17702992-8	2007	These results suggest that the concentration-dependent interactions of chlorpyrifos oxon with acetylcholinesterase resulted from a different mechanism than the concentration-dependent interactions of acetylthiocholine.	Acetylthiocholine	200-217	acetylcholinesterase (Cartwright blood group)	Homo sapiens	94-114
17097792-8	2007	Immobilized human erythrocytes were continuously perfused for real-time measurement of acetylcholinesterase activity by a modified Ellman method using 0.45mM acetylthiocholine.	Acetylthiocholine	158-175	acetylcholinesterase (Cartwright blood group)	Homo sapiens	87-107