PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 105-108 butyrylcholinesterase Homo sapiens 31-45 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 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 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 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 5315359-8 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 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 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 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 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 14340030-0 1965 A POLAROGRAPHIC METHOD FOR FOLLOWING THE RATES OF CHOLINESTERASE-CATALYZED HYDROLYSES OF ACETYLTHIOCHOLINE. Acetylthiocholine 89-106 butyrylcholinesterase Homo sapiens 50-64 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 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 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 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 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 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 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 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 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 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 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 122-139 acetylcholinesterase (Cartwright blood group) Homo sapiens 182-186 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 28258856-3 2017 However, with the presence of reductive thiocholine (TCh), the enzymatic product, hydrolyzed from acetylthiocholine (ATCh) by AChE, the redox reaction between MnO2 and TCh occurred, leading to the destruction of the MnO2 nanosheets, and thereby IFE was diminished gradually. Acetylthiocholine 98-115 acetylcholinesterase Rattus norvegicus 126-130 28258856-3 2017 However, with the presence of reductive thiocholine (TCh), the enzymatic product, hydrolyzed from acetylthiocholine (ATCh) by AChE, the redox reaction between MnO2 and TCh occurred, leading to the destruction of the MnO2 nanosheets, and thereby IFE was diminished gradually. Acetylthiocholine 117-121 acetylcholinesterase Rattus norvegicus 126-130 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 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 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 125-145 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 192-195 alkaline phosphatase, placental Homo sapiens 0-3 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 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 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 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 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 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 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 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 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 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 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 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 26217956-2 2015 ChE catalyzes its substrate (acetylthiocholine) and produces thiocholine and acetate acid. Acetylthiocholine 29-46 butyrylcholinesterase Homo sapiens 0-3 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 16971069-0 2006 Hydrolysis of an acetylthiocholine by pralidoxime iodide (2-PAM). Acetylthiocholine 17-34 peptidylglycine alpha-amidating monooxygenase Homo sapiens 60-63 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 302-311 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 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 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 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 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 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 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 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 35421656-2 2022 Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh). Acetylthiocholine 53-70 acetylcholinesterase (Cartwright blood group) Homo sapiens 14-34 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 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 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 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