PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
32739347-3	2020	Acetylcholinesterase (AChE) is well known to catalyze the hydrolysis of acetylcholine (ATCh) to produce thiocholine, whose affinity is strong enough to capture Cu2+ by thiol (-SH) group from the complex PASP-Cu, resulting in the fluorescence signal of PASP recovers up to 90%.	Thiocholine	104-115	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
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.	Thiocholine	150-161	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.	Thiocholine	150-161	acetylcholinesterase (Cartwright blood group)	Homo sapiens	267-271
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.	Thiocholine	163-166	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.	Thiocholine	163-166	acetylcholinesterase (Cartwright blood group)	Homo sapiens	267-271
33076046-4	2021	The presence of ethyl parathion can be monitored optically due to its inhibitory action towards AChE enzyme leading to suppression of thiocholine (TCh) formation and subsequently decreases TCh-Cu2+ interaction that ultimately retrieved quenched off state of bimetallic NC.	Thiocholine	134-145	acetylcholinesterase (Cartwright blood group)	Homo sapiens	96-100
33076046-4	2021	The presence of ethyl parathion can be monitored optically due to its inhibitory action towards AChE enzyme leading to suppression of thiocholine (TCh) formation and subsequently decreases TCh-Cu2+ interaction that ultimately retrieved quenched off state of bimetallic NC.	Thiocholine	147-150	acetylcholinesterase (Cartwright blood group)	Homo sapiens	96-100
33076046-4	2021	The presence of ethyl parathion can be monitored optically due to its inhibitory action towards AChE enzyme leading to suppression of thiocholine (TCh) formation and subsequently decreases TCh-Cu2+ interaction that ultimately retrieved quenched off state of bimetallic NC.	Thiocholine	189-192	acetylcholinesterase (Cartwright blood group)	Homo sapiens	96-100
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.	Thiocholine	32-43	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
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.	Thiocholine	42-53	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
33225325-5	2020	AChE can catalyze the hydrolysis of acetylthiocholine (ATCh) to form thiocholine (TCh), which can induce the fluorescence quenching of AuNCs while having no obvious influence on the fluorescence intensity of FL.	Thiocholine	56-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
32739347-3	2020	Acetylcholinesterase (AChE) is well known to catalyze the hydrolysis of acetylcholine (ATCh) to produce thiocholine, whose affinity is strong enough to capture Cu2+ by thiol (-SH) group from the complex PASP-Cu, resulting in the fluorescence signal of PASP recovers up to 90%.	Thiocholine	104-115	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
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.	Thiocholine	21-32	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
32691085-6	2020	In the absence of target molecule, a large number of thiocholines (TCh) were yielded from hydrolysis of acetylthiocholine (ATCh) by BChE.	Thiocholine	53-65	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.	Thiocholine	67-70	butyrylcholinesterase	Homo sapiens	132-136
32691085-8	2020	Furthermore, the inhibition of OPs on BChE resulted in the reduced generation of TCh, thus inducing the recovery of electrochemical signal.	Thiocholine	81-84	butyrylcholinesterase	Homo sapiens	38-42
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.	Thiocholine	34-37	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.	Thiocholine	97-100	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.	Thiocholine	58-69	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.	Thiocholine	58-69	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.	Thiocholine	72-75	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.	Thiocholine	72-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-49
32892929-5	2020	OPs, as a specific inhibitor for AChE activity, can prevent the generation of TCh and the dissociation of MnO2 nanosheets, building a relationship between OPs concentration and photocurrent.	Thiocholine	78-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	33-37
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.	Thiocholine	24-35	butyrylcholinesterase	Homo sapiens	0-4
32833082-7	2020	When AChE was present, the substrate acetylthiocholine (ATCh) was hydrolyzed to thiocholine (TCh) that is capable of decomposing MnO2 nanosheets.	Thiocholine	43-54	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.	Thiocholine	57-60	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.	Thiocholine	28-39	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.	Thiocholine	49-52	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
32597916-10	2020	Based on the thiocholine (TCh) inhibition of the excellent peroxidase-like activity of Co3O4/MoO3 and the TCh generation via acetylcholinesterase (AChE) catalyzed hydrolysis of acetylthiocholine chloride (ATCh), the colorimetric platform was extended to screen AChE activity and its inhibitor.	Thiocholine	13-24	acetylcholinesterase (Cartwright blood group)	Homo sapiens	147-151
32597916-10	2020	Based on the thiocholine (TCh) inhibition of the excellent peroxidase-like activity of Co3O4/MoO3 and the TCh generation via acetylcholinesterase (AChE) catalyzed hydrolysis of acetylthiocholine chloride (ATCh), the colorimetric platform was extended to screen AChE activity and its inhibitor.	Thiocholine	13-24	acetylcholinesterase (Cartwright blood group)	Homo sapiens	261-265
32597916-10	2020	Based on the thiocholine (TCh) inhibition of the excellent peroxidase-like activity of Co3O4/MoO3 and the TCh generation via acetylcholinesterase (AChE) catalyzed hydrolysis of acetylthiocholine chloride (ATCh), the colorimetric platform was extended to screen AChE activity and its inhibitor.	Thiocholine	26-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	147-151
32597916-10	2020	Based on the thiocholine (TCh) inhibition of the excellent peroxidase-like activity of Co3O4/MoO3 and the TCh generation via acetylcholinesterase (AChE) catalyzed hydrolysis of acetylthiocholine chloride (ATCh), the colorimetric platform was extended to screen AChE activity and its inhibitor.	Thiocholine	26-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	261-265
32597916-10	2020	Based on the thiocholine (TCh) inhibition of the excellent peroxidase-like activity of Co3O4/MoO3 and the TCh generation via acetylcholinesterase (AChE) catalyzed hydrolysis of acetylthiocholine chloride (ATCh), the colorimetric platform was extended to screen AChE activity and its inhibitor.	Thiocholine	106-109	acetylcholinesterase (Cartwright blood group)	Homo sapiens	147-151
32478771-4	2020	The QDs successfully enabled the detection of low concentrations of AChE by turning on the fluorescence of the CdTe/CP via the interaction between CP and thiocholine produced by ATCh hydrolysis and aggregation induced emission enhancement (AIEE).	Thiocholine	154-165	acetylcholinesterase (Cartwright blood group)	Homo sapiens	68-72
32676787-8	2020	Thereafter, TCh generated from hydrolysis of ATCh by BChE can reduce MnO2 NF (core) to Mn2+ and release the CdS nanoparticles (shell) from the platform electrode, significantly enhancing the PEC signal.	Thiocholine	12-15	butyrylcholinesterase	Homo sapiens	53-57
31816742-2	2020	A "turn on" fluorometric assay is described herein for AChE activity detection, according to the specific enzyme catalyzed reaction of acetylcholine (ATCh) by AChE, which generates thiocholine (TCh) as the product.	Thiocholine	181-192	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
32397331-9	2020	We monitored the enzymatic activity of AChE through the SERS spectrum of thiocholine (TC), the end product from acetylthiocholine (ATC).	Thiocholine	73-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	39-43
32397331-9	2020	We monitored the enzymatic activity of AChE through the SERS spectrum of thiocholine (TC), the end product from acetylthiocholine (ATC).	Thiocholine	86-88	acetylcholinesterase (Cartwright blood group)	Homo sapiens	39-43
32397331-10	2020	Inhibitory effects of paraoxon and carbaryl on AChE were evaluated from the TC peak intensity.	Thiocholine	76-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	47-51
31816742-2	2020	A "turn on" fluorometric assay is described herein for AChE activity detection, according to the specific enzyme catalyzed reaction of acetylcholine (ATCh) by AChE, which generates thiocholine (TCh) as the product.	Thiocholine	181-192	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-163
31816742-2	2020	A "turn on" fluorometric assay is described herein for AChE activity detection, according to the specific enzyme catalyzed reaction of acetylcholine (ATCh) by AChE, which generates thiocholine (TCh) as the product.	Thiocholine	151-154	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
31816742-2	2020	A "turn on" fluorometric assay is described herein for AChE activity detection, according to the specific enzyme catalyzed reaction of acetylcholine (ATCh) by AChE, which generates thiocholine (TCh) as the product.	Thiocholine	151-154	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-163
31816742-4	2020	The fluorescence-silent HBTP-Cu2+ complex could be broken by TCh generated from reaction of ATCh with AChE, giving rise to HBTP release which originates from competitive coordination of TCh with Cu2+.	Thiocholine	61-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
31816742-4	2020	The fluorescence-silent HBTP-Cu2+ complex could be broken by TCh generated from reaction of ATCh with AChE, giving rise to HBTP release which originates from competitive coordination of TCh with Cu2+.	Thiocholine	93-96	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
31357051-6	2020	Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine chloride (ATCh) into thiocholine (TCh), which could reduce oxTMB to decrease the absorbance in solution.	Thiocholine	67-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
31677527-6	2020	Yeast surface-displayed AChE can catalyze the hydrolysis of acetylthiocholine to produce thiocholine.	Thiocholine	66-77	Acetylcholine esterase	Drosophila melanogaster	24-28
31677527-8	2020	When AChE was incubated with paraoxon, a typical model of OPs, the activity of AChE was inhibited and the thiocholine-induced aggregation of AuNCs was reduced.	Thiocholine	106-117	Acetylcholine esterase	Drosophila melanogaster	5-9
31357051-6	2020	Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine chloride (ATCh) into thiocholine (TCh), which could reduce oxTMB to decrease the absorbance in solution.	Thiocholine	67-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
31357051-6	2020	Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine chloride (ATCh) into thiocholine (TCh), which could reduce oxTMB to decrease the absorbance in solution.	Thiocholine	90-93	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
31357051-6	2020	Acetylcholinesterase (AChE) could catalyze the hydrolysis of acetylthiocholine chloride (ATCh) into thiocholine (TCh), which could reduce oxTMB to decrease the absorbance in solution.	Thiocholine	90-93	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
31357051-7	2020	In the presence of AChE inhibitor tacrine, the generation of TCh was inhibited and the absorbance was preserved.	Thiocholine	61-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
31437810-4	2019	Exclusively, Ce/UiO-66/MWCNTs with a Ce (7%) and MWCNT (30%) matrix was found to not only load more acetylcholinesterase (AChE) onto vacant sites but also increase electron transfer and decrease the number of diffusion pathways between the thiocholine and electrode surface.	Thiocholine	240-251	acetylcholinesterase (Cartwright blood group)	Homo sapiens	100-120
31437810-4	2019	Exclusively, Ce/UiO-66/MWCNTs with a Ce (7%) and MWCNT (30%) matrix was found to not only load more acetylcholinesterase (AChE) onto vacant sites but also increase electron transfer and decrease the number of diffusion pathways between the thiocholine and electrode surface.	Thiocholine	240-251	acetylcholinesterase (Cartwright blood group)	Homo sapiens	122-126
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.	Thiocholine	54-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
31801184-5	2019	Furthermore, the enzymatic activity of BuChE rebound to the MIP was measured via the anodic oxidation of thiocholine, the reaction product of butyrylthiocholine.	Thiocholine	105-116	butyrylcholinesterase	Homo sapiens	39-44
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.	Thiocholine	4-15	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.	Thiocholine	4-15	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.	Thiocholine	4-15	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.	Thiocholine	97-108	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.	Thiocholine	97-108	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.	Thiocholine	97-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	310-314
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.	Thiocholine	54-65	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.	Thiocholine	68-71	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.	Thiocholine	68-71	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.	Thiocholine	53-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
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.	Thiocholine	53-64	acetylcholinesterase (Cartwright blood group)	Homo sapiens	210-214
30876606-9	2019	Thiocholine (TCh), which produced from acetylthiocholine(ATCh) by the hydrolysis of acetylcholinesterase (AChE), can "turn on" the fluorescence sensor.	Thiocholine	0-11	acetylcholinesterase (Cartwright blood group)	Homo sapiens	84-104
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).	Thiocholine	6-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
30959394-5	2019	The principle of BChE activity detection relies on the reaction between the enzymatic product thiocholine and Prussian Blue, giving the Prussian White with subsequently Prussian Blue"s fading, detected by a common office scanner supported by ImageJ software.	Thiocholine	94-105	butyrylcholinesterase	Homo sapiens	17-21
31020297-4	2019	AChE can hydrolyze acetylthiocholine (ATCh) to form thiocholine (TCh) which contains a thiol group.	Thiocholine	25-36	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.	Thiocholine	39-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
30876606-9	2019	Thiocholine (TCh), which produced from acetylthiocholine(ATCh) by the hydrolysis of acetylcholinesterase (AChE), can "turn on" the fluorescence sensor.	Thiocholine	0-11	acetylcholinesterase (Cartwright blood group)	Homo sapiens	106-110
30876606-9	2019	Thiocholine (TCh), which produced from acetylthiocholine(ATCh) by the hydrolysis of acetylcholinesterase (AChE), can "turn on" the fluorescence sensor.	Thiocholine	13-16	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.	Thiocholine	13-16	acetylcholinesterase (Cartwright blood group)	Homo sapiens	106-110
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.	Thiocholine	56-67	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
30888170-4	2019	OPs could irreversibly impede the activity of AChE, which caused the formation of thiocholine to decrease, thus, reduced the recovery of FL.	Thiocholine	82-93	acetylcholinesterase (Cartwright blood group)	Homo sapiens	46-50
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.	Thiocholine	56-67	butyrylcholinesterase	Homo sapiens	12-16
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.	Thiocholine	135-146	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-163
30702092-2	2019	In the presence of AChE, acetylthiocholine chloride was hydrolyzed to thiocholine.	Thiocholine	31-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
32254700-3	2018	Initially, the enzyme acetylcholinesterase (AChE) immobilized on the CdS/PEDOT photoanode could hydrolyze acetylthiocholine iodide (ATCh) into thiocholine as the electron donor to enhance the charge separation efficiency; thus, PEFC produced relatively high open circuit voltage (EOCV) upon illumination.	Thiocholine	112-123	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
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.	Thiocholine	61-72	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.	Thiocholine	61-72	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
30232815-8	2018	The current output from the oxidation of thiocholine (produced by AChE reacting with ATC) was proportional to the concentrations of ATC added to the thread.	Thiocholine	41-52	acetylcholinesterase (Cartwright blood group)	Homo sapiens	66-70
32254700-3	2018	Initially, the enzyme acetylcholinesterase (AChE) immobilized on the CdS/PEDOT photoanode could hydrolyze acetylthiocholine iodide (ATCh) into thiocholine as the electron donor to enhance the charge separation efficiency; thus, PEFC produced relatively high open circuit voltage (EOCV) upon illumination.	Thiocholine	112-123	CDP-diacylglycerol synthase 1	Homo sapiens	69-72
30307023-2	2018	However, very few works have ever found that the signal loss of thiocholine (TCh) during electrochemical processing is a key factor leading to the low sensitivity of acetylcholinesterase (AChE)-based OP electrochemical sensing platforms.	Thiocholine	64-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	166-186
30307023-2	2018	However, very few works have ever found that the signal loss of thiocholine (TCh) during electrochemical processing is a key factor leading to the low sensitivity of acetylcholinesterase (AChE)-based OP electrochemical sensing platforms.	Thiocholine	64-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	188-192
30307023-2	2018	However, very few works have ever found that the signal loss of thiocholine (TCh) during electrochemical processing is a key factor leading to the low sensitivity of acetylcholinesterase (AChE)-based OP electrochemical sensing platforms.	Thiocholine	77-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	166-186
30307023-2	2018	However, very few works have ever found that the signal loss of thiocholine (TCh) during electrochemical processing is a key factor leading to the low sensitivity of acetylcholinesterase (AChE)-based OP electrochemical sensing platforms.	Thiocholine	77-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	188-192
30307023-4	2018	For the first time, Michael addition is introduced into an AChE-based OP electrochemical sensing platform to enrich the electrochemical intermediate TCh.	Thiocholine	149-152	acetylcholinesterase (Cartwright blood group)	Homo sapiens	59-63
30187211-0	2018	A colorimetric assay for acetylcholinesterase activity and inhibitor screening based on the thiocholine-induced inhibition of the oxidative power of MnO2 nanosheets on 3,3",5,5"-tetramethylbenzidine.	Thiocholine	92-103	acetylcholinesterase (Cartwright blood group)	Homo sapiens	25-45
30187211-4	2018	If AChE hydrolyzes its substrate acetylthiocholine chloride, thiocholine is formed which blocks the oxidative power of the MnO2 nanosheets.	Thiocholine	39-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	3-7
29237266-6	2018	OPs as inhibitors for BChE activity can prevent the generation of thiocholine and decomposition of MnO2 nanosheets, accompanying the fluorescence "turn-off" of the system.	Thiocholine	66-77	butyrylcholinesterase	Homo sapiens	22-26
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.	Thiocholine	140-151	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.	Thiocholine	140-151	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.	Thiocholine	140-151	acetylcholinesterase (Cartwright blood group)	Homo sapiens	213-217
29136790-3	2018	The amperometric detection of AChE is based on the determination of thiocholine (TCh) produced from hydrolysis of acetylthiocholine chloride (ATCh) by AChE.	Thiocholine	68-79	acetylcholinesterase (Cartwright blood group)	Homo sapiens	30-34
29136790-3	2018	The amperometric detection of AChE is based on the determination of thiocholine (TCh) produced from hydrolysis of acetylthiocholine chloride (ATCh) by AChE.	Thiocholine	68-79	acetylcholinesterase (Cartwright blood group)	Homo sapiens	151-155
29136790-3	2018	The amperometric detection of AChE is based on the determination of thiocholine (TCh) produced from hydrolysis of acetylthiocholine chloride (ATCh) by AChE.	Thiocholine	81-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	30-34
29136790-3	2018	The amperometric detection of AChE is based on the determination of thiocholine (TCh) produced from hydrolysis of acetylthiocholine chloride (ATCh) by AChE.	Thiocholine	81-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	151-155
29594716-3	2018	The enzyme acetylcholinesterase (AChE) is known catalyze the hydrolysis of acetylthiocholine to produce thiocholine.	Thiocholine	81-92	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.	Thiocholine	81-92	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.	Thiocholine	74-85	acetylcholinesterase (Cartwright blood group)	Homo sapiens	17-37
28494368-2	2017	By utilizing the acetylcholinesterase (AChE) mediated hydrolysis of acetylthiocholine to thiocholine where the activity of AChE is inhibited by the presence of organophosphate pesticides (OPPs), the subsequent thiocholine-induced aggregation of 10OsCO-Au NPs can be monitored by the change in color of the NPs solution and the variation in intensity of the SERS CO signal.	Thiocholine	74-85	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.	Thiocholine	74-85	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.	Thiocholine	74-85	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	357-361
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.	Thiocholine	89-100	acetylcholinesterase (Cartwright blood group)	Homo sapiens	17-37
28494368-2	2017	By utilizing the acetylcholinesterase (AChE) mediated hydrolysis of acetylthiocholine to thiocholine where the activity of AChE is inhibited by the presence of organophosphate pesticides (OPPs), the subsequent thiocholine-induced aggregation of 10OsCO-Au NPs can be monitored by the change in color of the NPs solution and the variation in intensity of the SERS CO signal.	Thiocholine	89-100	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.	Thiocholine	89-100	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.	Thiocholine	89-100	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	357-361
28258856-3	2017	However, with the presence of reductive thiocholine (TCh), the enzymatic product, hydrolyzed from acetylthiocholine (ATCh) by AChE, the redox reaction between MnO2 and TCh occurred, leading to the destruction of the MnO2 nanosheets, and thereby IFE was diminished gradually.	Thiocholine	40-51	acetylcholinesterase	Rattus norvegicus	126-130
28315592-4	2017	Thiocholine, which was produced from acetylthiocholine (ATC) by the hydrolysis of butyrylcholinesterase (BChE), could cause the aggregation of Au NPs and the corresponding recovery of FRET-quenched fluorescence emission.	Thiocholine	0-11	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.	Thiocholine	0-11	butyrylcholinesterase	Homo sapiens	105-109
28467056-3	2017	On this basis, a rather simple amperometric biosensor construct was formed, which uses butyrylthiocholine as BChE substrate with subsequent MnO2-mediated thiocholine oxidation at a graphite-based SPE.	Thiocholine	94-105	butyrylcholinesterase	Homo sapiens	109-113
28299407-3	2017	Hence in this work, the amount of thiocholine produced during AChE inhibition has been estimated to detect the residual activity of AChE enzyme in-turn to enhance the efficiency of the biosensor.	Thiocholine	34-45	acetylcholinesterase (Cartwright blood group)	Homo sapiens	62-66
28299407-3	2017	Hence in this work, the amount of thiocholine produced during AChE inhibition has been estimated to detect the residual activity of AChE enzyme in-turn to enhance the efficiency of the biosensor.	Thiocholine	34-45	acetylcholinesterase (Cartwright blood group)	Homo sapiens	132-136
28299407-4	2017	In this context, Pt/ZnO-CeO2/AChE/Chitosan based biosensor has been developed for sensitive voltammetric quantification of thiocholine in AChE.	Thiocholine	123-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	29-33
28299407-4	2017	In this context, Pt/ZnO-CeO2/AChE/Chitosan based biosensor has been developed for sensitive voltammetric quantification of thiocholine in AChE.	Thiocholine	123-134	acetylcholinesterase (Cartwright blood group)	Homo sapiens	138-142
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.	Thiocholine	53-56	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.	Thiocholine	118-121	acetylcholinesterase	Rattus norvegicus	126-130
27251198-3	2016	The possibility to detect thiocholine at a low applied potential with high sensitivity was exploited and an acetylcholinesterase (AChE) biosensor was developed.	Thiocholine	26-37	acetylcholinesterase (Cartwright blood group)	Homo sapiens	108-128
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.	Thiocholine	39-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
27208478-4	2016	And the enzyme of AChE was used to catalyze the substrate of acetylthiocholine (ATCh) to produce thiocholine (TCh).	Thiocholine	67-78	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-22
27208478-4	2016	And the enzyme of AChE was used to catalyze the substrate of acetylthiocholine (ATCh) to produce thiocholine (TCh).	Thiocholine	81-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-22
27208478-6	2016	Upon incubated with OPs, the enzymatic activity of AChE was inhibited to produce less TCh, resulting in more TMB catalytically oxidized by PAA-CeO2 to show an increasing blue color.	Thiocholine	86-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	51-55
27251198-3	2016	The possibility to detect thiocholine at a low applied potential with high sensitivity was exploited and an acetylcholinesterase (AChE) biosensor was developed.	Thiocholine	26-37	acetylcholinesterase (Cartwright blood group)	Homo sapiens	130-134
27251198-5	2016	The enzymatic activity of the immobilized AChE was determined measuring the enzymatic product thiocholine at +300 mV.	Thiocholine	94-105	acetylcholinesterase (Cartwright blood group)	Homo sapiens	42-46
26686921-3	2016	In the presence of AChE and choline oxidase (ChOx), acetylcholine (ATCl) is hydrolyzed by AChE to generate thiocholine, then thiocholine is catalyzed by ChOx to produce H2O2 in situ, which serves as the coreactant to effectively enhance the ECL intensity in luminol-ECL system.	Thiocholine	107-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
27260432-2	2016	Compared with Au@Ag heterogeneous NRs, AuNRs exhibited excellent electrocatalytic properties, which can electrocatalytically oxidize thiocholine, the hydrolysate of acetylthiocholine chloride (ATCl) by AChE at +0.55V (vs. SCE).	Thiocholine	133-144	acetylcholinesterase (Cartwright blood group)	Homo sapiens	202-206
26979315-4	2016	The biosensor showed an oxidation peak at +0.83 V related to the oxidation of thiocholine, hydrolysis product of acetylthiocholine iodide (ATCI), catalyzed by AChE.	Thiocholine	78-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	159-163
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.	Thiocholine	94-105	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
26686921-3	2016	In the presence of AChE and choline oxidase (ChOx), acetylcholine (ATCl) is hydrolyzed by AChE to generate thiocholine, then thiocholine is catalyzed by ChOx to produce H2O2 in situ, which serves as the coreactant to effectively enhance the ECL intensity in luminol-ECL system.	Thiocholine	107-118	acetylcholinesterase (Cartwright blood group)	Homo sapiens	90-94
26686921-3	2016	In the presence of AChE and choline oxidase (ChOx), acetylcholine (ATCl) is hydrolyzed by AChE to generate thiocholine, then thiocholine is catalyzed by ChOx to produce H2O2 in situ, which serves as the coreactant to effectively enhance the ECL intensity in luminol-ECL system.	Thiocholine	125-136	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
26686921-3	2016	In the presence of AChE and choline oxidase (ChOx), acetylcholine (ATCl) is hydrolyzed by AChE to generate thiocholine, then thiocholine is catalyzed by ChOx to produce H2O2 in situ, which serves as the coreactant to effectively enhance the ECL intensity in luminol-ECL system.	Thiocholine	125-136	acetylcholinesterase (Cartwright blood group)	Homo sapiens	90-94
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.	Thiocholine	57-68	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.	Thiocholine	57-68	acetylcholinesterase (Cartwright blood group)	Homo sapiens	81-85
26841098-2	2016	ALP and AChE were integrated into the PEC system through the sandwich immunobinding and could specifically catalyze the hydrolysis of ascorbic acid 2-phosphate (AAP) or the acetylthiocholine (ATC) to in situ generate ascorbic acid (AA) or thiocholine (TC) for sacrificial electron donating.	Thiocholine	179-190	alkaline phosphatase, placental	Homo sapiens	0-3
26339933-2	2016	Upon the hydrolysis of acetylthiocholine catalyzed by AChE, the product thiocholine stabilizes the in situ formation of CdS QDs in homogenous solution.	Thiocholine	29-40	acetylcholinesterase (Cartwright blood group)	Homo sapiens	54-58
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.	Thiocholine	193-195	alkaline phosphatase, placental	Homo sapiens	0-3
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.	Thiocholine	69-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	7-27
27682399-4	2016	In the presence of paraoxon, the activity of AChE is inhibited, and thus preventing the generation of thiocholine, causing fewer NC-dots to be replaced.	Thiocholine	102-113	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-49
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.	Thiocholine	69-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	29-33
26141104-3	2015	Herein, the sensing ensemble solution exhibits a marvelous fluorescent enhancement in the presence of AChE and ATCh, where AChE hydrolyzes its active substrate ATCh into thiocholine (TCh), and then TCh captures Cu(2+) from the ensemble, accompanied by the conversion from fluorescence off-state to on-state of the AuNCs.	Thiocholine	170-181	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
26141104-3	2015	Herein, the sensing ensemble solution exhibits a marvelous fluorescent enhancement in the presence of AChE and ATCh, where AChE hydrolyzes its active substrate ATCh into thiocholine (TCh), and then TCh captures Cu(2+) from the ensemble, accompanied by the conversion from fluorescence off-state to on-state of the AuNCs.	Thiocholine	112-115	acetylcholinesterase (Cartwright blood group)	Homo sapiens	123-127
26141104-3	2015	Herein, the sensing ensemble solution exhibits a marvelous fluorescent enhancement in the presence of AChE and ATCh, where AChE hydrolyzes its active substrate ATCh into thiocholine (TCh), and then TCh captures Cu(2+) from the ensemble, accompanied by the conversion from fluorescence off-state to on-state of the AuNCs.	Thiocholine	170-181	acetylcholinesterase (Cartwright blood group)	Homo sapiens	123-127
26141104-3	2015	Herein, the sensing ensemble solution exhibits a marvelous fluorescent enhancement in the presence of AChE and ATCh, where AChE hydrolyzes its active substrate ATCh into thiocholine (TCh), and then TCh captures Cu(2+) from the ensemble, accompanied by the conversion from fluorescence off-state to on-state of the AuNCs.	Thiocholine	161-164	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
26141104-3	2015	Herein, the sensing ensemble solution exhibits a marvelous fluorescent enhancement in the presence of AChE and ATCh, where AChE hydrolyzes its active substrate ATCh into thiocholine (TCh), and then TCh captures Cu(2+) from the ensemble, accompanied by the conversion from fluorescence off-state to on-state of the AuNCs.	Thiocholine	161-164	acetylcholinesterase (Cartwright blood group)	Homo sapiens	123-127
26087169-2	2015	The detection principle is based on the irreversible inhibition of the enzymatic activity of acetylcholinesterase (AchE) by methyl parathion; AchE catalytically hydrolyzes acetylthiocholine iodine to thiocholine that in turn dissociates dithiobis-nitrobenzoate to produce a yellow product (deprotonated thio-nitrobenzoate).	Thiocholine	178-189	acetylcholinesterase (Cartwright blood group)	Homo sapiens	93-113
26087169-2	2015	The detection principle is based on the irreversible inhibition of the enzymatic activity of acetylcholinesterase (AchE) by methyl parathion; AchE catalytically hydrolyzes acetylthiocholine iodine to thiocholine that in turn dissociates dithiobis-nitrobenzoate to produce a yellow product (deprotonated thio-nitrobenzoate).	Thiocholine	178-189	acetylcholinesterase (Cartwright blood group)	Homo sapiens	115-119
26087169-2	2015	The detection principle is based on the irreversible inhibition of the enzymatic activity of acetylcholinesterase (AchE) by methyl parathion; AchE catalytically hydrolyzes acetylthiocholine iodine to thiocholine that in turn dissociates dithiobis-nitrobenzoate to produce a yellow product (deprotonated thio-nitrobenzoate).	Thiocholine	178-189	acetylcholinesterase (Cartwright blood group)	Homo sapiens	142-146
26217956-2	2015	ChE catalyzes its substrate (acetylthiocholine) and produces thiocholine and acetate acid.	Thiocholine	35-46	butyrylcholinesterase	Homo sapiens	0-3
25569873-2	2015	The detection mechanism is based on the facts that AuNPs quench the fluorescence of UCNPs and organophosphorus pesticides (OPs) inhibit the activity of acetylcholinesterase (AChE) which catalyzes the hydrolysis of acetylthiocholine (ATC) into thiocholine.	Thiocholine	220-231	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.	Thiocholine	220-231	acetylcholinesterase (Cartwright blood group)	Homo sapiens	174-178
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.	Thiocholine	182-193	acetylcholinesterase (Cartwright blood group)	Homo sapiens	128-148
25660508-3	2015	Both AChE and BChE can catalyze the hydrolysis of the acetylthiocholine (ATCh) substrate and produce positively-charged thiocholine (TCh).	Thiocholine	60-71	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).	Thiocholine	60-71	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).	Thiocholine	74-77	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).	Thiocholine	74-77	butyrylcholinesterase	Homo sapiens	14-18
25560517-6	2015	The assay was based on the reaction between Cu(2+) and thiocholine, the hydrolysis product of ATCh by AChE.	Thiocholine	55-66	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
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.	Thiocholine	182-193	acetylcholinesterase (Cartwright blood group)	Homo sapiens	150-154
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.	Thiocholine	216-227	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.	Thiocholine	216-227	acetylcholinesterase (Cartwright blood group)	Homo sapiens	150-154
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.	Thiocholine	0-11	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.	Thiocholine	13-16	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60
24929086-7	2014	First, thioesters are hydrolyzed by cholinesterase to produce thiocholine in the absence of DTNB.	Thiocholine	62-73	butyrylcholinesterase	Homo sapiens	36-50
24929086-8	2014	Then, the reaction is stopped by a cholinesterase inhibitor and the produced thiocholine is revealed by DTNB and quantified at 412 nm.	Thiocholine	77-88	butyrylcholinesterase	Homo sapiens	35-49
25050413-3	2014	The AChE-catalyzed hydrolysis of ATC releases thiocholine to cause the aggregation of the AuNCs towards a dramatic decrease in fluorescence intensities, which could be curbed by the phosphorylation-induced inhibition of AChE activity when exposed to organophosphorus compounds (OPs).	Thiocholine	46-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
25050413-3	2014	The AChE-catalyzed hydrolysis of ATC releases thiocholine to cause the aggregation of the AuNCs towards a dramatic decrease in fluorescence intensities, which could be curbed by the phosphorylation-induced inhibition of AChE activity when exposed to organophosphorus compounds (OPs).	Thiocholine	46-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	220-224
24251311-3	2014	The fluorescence of the AuNCs was quenched by thiocholine that was produced from the AChE hydrolysis of S-acetylthiocholine iodide (ACTI) to detect the AChE activity.	Thiocholine	46-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	85-89
24416761-2	2014	Due to the inherent biocompatibility of the Cd0.5Zn0.5S-rGO nanocomposite, acetylcholinesterase (AChE) immobilized on the Cd0.5Zn0.5S-rGO modified electrode can hydrolyze acetylthiocholine chloride into thiocholine, which could increase the photocurrent of the enzyme electrode, and the further inhibition of OPs on the enzyme electrode could decrease the photocurrent response.	Thiocholine	177-188	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-95
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.	Thiocholine	117-128	acetylcholinesterase (Cartwright blood group)	Homo sapiens	148-152
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.	Thiocholine	240-251	acetylcholinesterase (Cartwright blood group)	Homo sapiens	148-152
24225492-0	2014	Thiocholine mediated stabilization of in situ produced CdS quantum dots: application for the detection of acetylcholinesterase activity and inhibitors.	Thiocholine	0-11	acetylcholinesterase (Cartwright blood group)	Homo sapiens	106-126
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).	Thiocholine	67-78	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).	Thiocholine	81-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-93
24251311-3	2014	The fluorescence of the AuNCs was quenched by thiocholine that was produced from the AChE hydrolysis of S-acetylthiocholine iodide (ACTI) to detect the AChE activity.	Thiocholine	46-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	152-156
24001830-2	2014	AChE catalyses the cleavage of acetylthiocholine chloride (ASChCl or substrate) to thiocholine, which was oxidised to give a disulphide compound by dimerisation at 0.60V versus saturated calomel electrode.	Thiocholine	37-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
23919577-2	2013	The detection mechanism is based on the concept, that is, AChE hydrolyzes the acetylthiocholine (ATCh) chloride to produce thiocholine (TCh).	Thiocholine	84-95	acetylcholinesterase (Cartwright blood group)	Homo sapiens	58-62
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.	Thiocholine	39-50	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.	Thiocholine	39-50	acetylcholinesterase (Cartwright blood group)	Homo sapiens	140-144
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.	Thiocholine	79-90	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.	Thiocholine	79-90	acetylcholinesterase (Cartwright blood group)	Homo sapiens	140-144
24020883-6	2013	Greatly enhanced sensitivity was achieved by using Fe3O4/Au nanocomposites to enrich thiocholine, the hydrolysis product of active AChE, followed by electrochemical oxidative desorption of the adsorbed thiocholine.	Thiocholine	85-96	acetylcholinesterase (Cartwright blood group)	Homo sapiens	131-135
23603132-2	2013	In this assay, AChE catalyzes the hydrolysis of acetylthiocholine (ATCh) to form thiocholine which induces fluorescence quenching of DNA-Cu/AgNCs.	Thiocholine	54-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	15-19
23919577-2	2013	The detection mechanism is based on the concept, that is, AChE hydrolyzes the acetylthiocholine (ATCh) chloride to produce thiocholine (TCh).	Thiocholine	98-101	acetylcholinesterase (Cartwright blood group)	Homo sapiens	58-62
23919577-5	2013	Due to the sensitive and rapid fluorescence turn-on response of dC12-Ag NCs to TCh, AChE with activity as low as 0.5 x 10(-4) U/mL (signal/noise = 3) can be analyzed with a dynamic range of 0.1 to 1.25 x 10(-3) U/mL.	Thiocholine	79-82	acetylcholinesterase (Cartwright blood group)	Homo sapiens	84-88
23345579-10	2013	BChE was inhibited with Sp- and Rp-tabun thiocholine nerve agent model compounds to make adducts identical to those of tabun with known stereochemistry.	Thiocholine	41-52	butyrylcholinesterase	Homo sapiens	0-4
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.	Thiocholine	69-80	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.	Thiocholine	69-80	acetylcholinesterase (Cartwright blood group)	Homo sapiens	351-355
23618147-0	2013	Development of an acetylcholinesterase immobilized flow through amperometric detector based on thiocholine detection at a silver electrode.	Thiocholine	95-106	acetylcholinesterase (Cartwright blood group)	Homo sapiens	18-38
23379662-3	2013	In the presence of AChE, ATCh was hydrolyzed to thiocholine and acetate.	Thiocholine	48-59	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
22868055-3	2013	By integrating the flow injection analysis (FIA) with amperometric detection, the resulting AChE-LDHs modified electrode greatly catalyzed the oxidation of the enzymatically generated thiocholine product, and facilitated the detection automation, thus increasing the detection sensitivity.	Thiocholine	184-195	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-96
23354570-4	2013	The AChE biosensor showed favorable affinity for acetylthiocholine chloride and catalyzed the hydrolysis of acetylthiocholine chloride with an apparent Michaelis-Menten constant of 134 muM to form thiocholine, which was then oxidized to produce a detectable and fast response.	Thiocholine	55-66	acetylcholinesterase (Cartwright blood group)	Homo sapiens	4-8
23354570-5	2013	Based on the inhibition by pesticides of the enzymatic activity of AChE, detection of the amperometric response from thiocholine on the biosensor is a simple and effective way to biomonitor exposure to pesticides.	Thiocholine	117-128	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-71
22946763-5	2012	The immobilized AChE on the 3DOM composite displayed favorable affinity to substrate acetylthiocholine chloride (ATCh), and the 3DOM composite showed excellent electrocatalytic effect on thiocholine, the hydrolysis product of ATCh.	Thiocholine	91-102	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
22421347-0	2012	The stabilization of Au NP-AChE nanocomposites by biosilica encapsulation for the development of a thiocholine biosensor.	Thiocholine	99-110	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-31
23013022-1	2012	The comparative study of the cholinesterase activity in some crab species was carried out for the first time with use of a set of thiocholine substrates.	Thiocholine	130-141	butyrylcholinesterase	Homo sapiens	29-43
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.	Thiocholine	54-65	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
22503679-2	2012	The enzyme AChE catalyzes the hydrolysis of acetylthiocholine to thiocholine, which can be electrochemically oxidized.	Thiocholine	50-61	acetylcholinesterase (Cartwright blood group)	Homo sapiens	11-15
22503679-3	2012	The presence of permethrin inhibits the AChE activity, resulting in a lower thiocholine production and thus, a decrease in the amperometric oxidation current.	Thiocholine	76-87	acetylcholinesterase (Cartwright blood group)	Homo sapiens	40-44
22475016-2	2012	The detection mechanism is based on the fact that these pesticides can inhibit the activity of acetylcholinesterase (AChE), thus preventing the generation of thiocholine (which turns the RB-AuNP solutions blue and unquenches the fluorescence of RB simultaneously).	Thiocholine	158-169	acetylcholinesterase (Cartwright blood group)	Homo sapiens	95-115
22475016-2	2012	The detection mechanism is based on the fact that these pesticides can inhibit the activity of acetylcholinesterase (AChE), thus preventing the generation of thiocholine (which turns the RB-AuNP solutions blue and unquenches the fluorescence of RB simultaneously).	Thiocholine	158-169	acetylcholinesterase (Cartwright blood group)	Homo sapiens	117-121
21377346-1	2011	A novel, low potential and highly sensitive acetylcholinesterase (AChE) biosensor was developed based on 1-butyl-3-methylimidazolium tetrafluoroborate/multiwalled carbon nanotube composite gel thiocholine sensor.	Thiocholine	193-204	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-64
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.	Thiocholine	62-73	acetylcholinesterase (Cartwright blood group)	Homo sapiens	94-114
21994917-0	2011	An electrochemical platform for acetylcholinesterase activity assay and inhibitors screening based on Michael addition reaction between thiocholine and catechol-terminated SAMs.	Thiocholine	136-147	acetylcholinesterase (Cartwright blood group)	Homo sapiens	32-52
21994917-0	2011	An electrochemical platform for acetylcholinesterase activity assay and inhibitors screening based on Michael addition reaction between thiocholine and catechol-terminated SAMs.	Thiocholine	136-147	methionine adenosyltransferase 1A	Homo sapiens	172-176
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.	Thiocholine	159-170	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.	Thiocholine	159-170	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.	Thiocholine	159-170	acetylcholinesterase (Cartwright blood group)	Homo sapiens	242-246
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.	Thiocholine	159-170	methionine adenosyltransferase 1A	Homo sapiens	307-311
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.	Thiocholine	61-72	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.	Thiocholine	61-72	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
21767560-5	2011	The present report summarizes our observations on plasma acetylcholinesterase activity in mice treated with chlorpyrifos, chlorpyrifos oxon, diazinon, tri-ortho-cresyl phosphate, tri-cresyl phosphate, tabun thiocholine, parathion, dichlorvos, and diisopropylfluorophosphate.	Thiocholine	207-218	acetylcholinesterase	Mus musculus	57-77
21514816-0	2011	Oxidative desorption of thiocholine assembled on core-shell Fe3O4/AuNPs magnetic nanocomposites for highly sensitive determination of acetylcholinesterase activity: an exposure biomarker of organophosphates.	Thiocholine	24-35	acetylcholinesterase (Cartwright blood group)	Homo sapiens	134-154
21514816-2	2011	In this work, we described a novel electrochemical oxidative desorption-process of thiocholine, the product of enzymatic reaction, for rapid and highly sensitive determination of AChE activity in human serum.	Thiocholine	83-94	acetylcholinesterase (Cartwright blood group)	Homo sapiens	179-183
21377346-1	2011	A novel, low potential and highly sensitive acetylcholinesterase (AChE) biosensor was developed based on 1-butyl-3-methylimidazolium tetrafluoroborate/multiwalled carbon nanotube composite gel thiocholine sensor.	Thiocholine	193-204	acetylcholinesterase (Cartwright blood group)	Homo sapiens	66-70
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.	Thiocholine	65-76	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.	Thiocholine	65-76	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.	Thiocholine	79-82	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.	Thiocholine	79-82	acetylcholinesterase (Cartwright blood group)	Homo sapiens	52-56
21376964-3	2011	Subsequently, AChE catalytic activity was inhibited with the addition of paraoxon, which caused TCh decreased, leading to a significant decrease of the blue fluorescent compound.	Thiocholine	96-99	acetylcholinesterase (Cartwright blood group)	Homo sapiens	14-18
19715346-5	2009	Inhibition kinetic studies of the thiomethyl- and thiocholine-substituted series of nerve agent model compounds revealed that the S(p) enantiomers of both series of compounds showed greater inhibition potency toward AChE and BChE.	Thiocholine	50-61	acetylcholinesterase (Cartwright blood group)	Homo sapiens	216-220
21156143-1	2010	A molecular dynamics study of traffic of thiocholine within the active-site gorge of acetylcholinesterase.	Thiocholine	41-52	acetylcholinesterase (Cartwright blood group)	Homo sapiens	85-105
21156143-6	2010	Here, multiple conventional molecular dynamics simulations have been performed to investigate the clearance of the product, thiocholine, from the active-site gorge of acetylcholinesterase.	Thiocholine	124-135	acetylcholinesterase (Cartwright blood group)	Homo sapiens	167-187
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.	Thiocholine	135-146	acetylcholinesterase (Cartwright blood group)	Homo sapiens	164-168
21133088-4	2010	The immobilized AChE catalyzed the hydrolysis of acetylthiocholine chloride to produce thiocholine, which engendered an irreversible oxidation peak.	Thiocholine	55-66	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
20678652-4	2010	The PEDOT:PSS polymer was shown to be suitable for thiocholine oxidation, allowing the measurement of AChE activity at 100 mV vs Ag/AgCl.	Thiocholine	51-62	acetylcholinesterase (Cartwright blood group)	Homo sapiens	102-106
20593080-3	2010	Biocatalyzed hydrolysis of ATCh via AChE leads to formation of thiocholine, which in turn reduces the Au(III) onto the entrapped nanoparticles, producing particle growth and a concomitant increase in color intensity that can be correlated to the amount of substrate or inhibitor present in test solutions.	Thiocholine	63-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	36-40
20143889-4	2010	Acetylcholinesterase was used as the labeling enzyme to convert acetylthiocholine to thiocholine.	Thiocholine	70-81	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
20143889-9	2010	As a result, high sensitivity and a low detection limit of 0.2 pM (3.4 pg/mL) TNF-alpha were achieved with excellent reproducibility by optimizing the conditions for the immuno-reaction, thiocholine accumulation, and ECL generation.	Thiocholine	187-198	tumor necrosis factor	Homo sapiens	78-87
19715346-5	2009	Inhibition kinetic studies of the thiomethyl- and thiocholine-substituted series of nerve agent model compounds revealed that the S(p) enantiomers of both series of compounds showed greater inhibition potency toward AChE and BChE.	Thiocholine	50-61	butyrylcholinesterase	Homo sapiens	225-229
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.	Thiocholine	23-34	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.	Thiocholine	23-34	butyrylcholinesterase	Homo sapiens	72-75
19446058-3	2009	This strategy was found to catalyze the oxidative reaction of thiocholine effectively, make the AChE/PbO2/TiO2/Ti biosensor detect the substrate at 0.30 V (vs. SCE), hundreds milli-volts lower than others reported.	Thiocholine	62-73	acetylcholinesterase (Cartwright blood group)	Homo sapiens	96-100
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).	Thiocholine	95-106	acetylcholinesterase (Cartwright blood group)	Homo sapiens	168-188
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).	Thiocholine	66-77	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
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).	Thiocholine	224-227	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
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).	Thiocholine	95-106	acetylcholinesterase (Cartwright blood group)	Homo sapiens	190-194
19238297-5	2009	The rapid and sensitive detection of thiocholine allowed monitoring the inhibition of acetylcholinesterase in the presence of the pesticide, carbofuran.	Thiocholine	37-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	86-106
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.	Thiocholine	215-226	butyrylcholinesterase	Homo sapiens	0-14
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.	Thiocholine	350-361	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.	Thiocholine	350-361	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-79
18804659-6	2008	Reactivation was realized in the 96-wells photometric microplates and activity of human recombinant AChE was followed by reaction of Ellman"s reagent with one of enzyme digestion product: thiocholine.	Thiocholine	188-199	acetylcholinesterase (Cartwright blood group)	Homo sapiens	100-104
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.	Thiocholine	128-139	acetylcholinesterase (Cartwright blood group)	Homo sapiens	55-59
17716616-3	2007	Oximes, reactivators of inhibited cholinesterase, are nucleophiles that also react with ATCh (oximolysis), producing thiocholine and (indirectly) TNB ion.	Thiocholine	117-128	butyrylcholinesterase	Homo sapiens	34-48
17702992-9	2007	In the latter case, substrate bound to the peripheral anionic site of acetylcholinesterase has been shown to reduce enzyme activity by blocking the release of the product thiocholine from the active site gorge.	Thiocholine	171-182	acetylcholinesterase (Cartwright blood group)	Homo sapiens	70-90
17046138-2	2007	Through enlargement of the active site gorge of mouse AChE by mutations Y337A, F295L and F297I, we studied continuous enzymatic degradation of S(P)-cycloheptyl methylphosphonyl thiocholine (S(P)-CHMPTCh) in the presence of HI-6.	Thiocholine	177-188	acetylcholinesterase	Mus musculus	54-58
17499494-3	2007	The immobilized AChE could catalyze the hydrolysis of acetylthiocholine chloride (ATCl) with a Kmapp value of 450 microM to form thiocholine, which was then oxidized to produce detectable single with a linear range of 10-1000 microM.	Thiocholine	60-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
17046138-4	2007	The rates of hydrolysis expressed as moles of formed thiocholine per mole of enzyme per minute were 3.3, 0.69, 0.34 and 0.15min(-1) for F295L/Y337A, Y337A, F297I/Y337A and AChE wild-type, respectively.	Thiocholine	53-64	acetylcholinesterase	Mus musculus	172-176
17113251-0	2006	The liberation of thiocholine from acetylthiocholine (ASCh) by pralidoxime iodide (2=PAM) and other oximes (obidoxime and diacetylmonoxime).	Thiocholine	18-29	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	85-88
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.	Thiocholine	222-233	acetylcholinesterase (Cartwright blood group)	Homo sapiens	75-79
16864509-2	2006	A microtitre-based adaptation of methodology described for the thiourea-dependent oxidation of thiocholine was used to determine the turnover of thiourea-containing compounds by human FMO1 and FMO3.	Thiocholine	95-106	flavin containing dimethylaniline monoxygenase 1	Homo sapiens	184-188
16971069-3	2006	This result indicates that 2-PAM produced a thiocholine from the ASCh by hydrolysis.	Thiocholine	44-55	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	29-32
16864509-2	2006	A microtitre-based adaptation of methodology described for the thiourea-dependent oxidation of thiocholine was used to determine the turnover of thiourea-containing compounds by human FMO1 and FMO3.	Thiocholine	95-106	flavin containing dimethylaniline monoxygenase 3	Homo sapiens	193-197
16243302-9	2005	Within days the livers showed intense thiocholine staining for BChE activity.	Thiocholine	38-49	butyrylcholinesterase	Homo sapiens	63-67
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.	Thiocholine	60-71	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-20
12420757-4	2002	Cyclic voltammetry, performed at Pt and AChE/Pt disk electrodes, confirmed the irreversible, monoelectronic thiocholine oxidation process and showed that a working potential of +0.410 V vs. Ag/AgCl, KCl(sat) was suitable for a selective and sensitive amperometric detection of thiocholine.	Thiocholine	108-119	acetylcholinesterase (Cartwright blood group)	Homo sapiens	40-44
15987132-7	2005	To determine the trace level of the recovered antibody-enzyme conjugate, the AChE activity was determined with high sensitivity on the basis of the chemisorption/electrochemical desorption process of thiocholine, which was produced through the enzymatic reaction, on a silver surface.	Thiocholine	200-211	acetylcholinesterase (Cartwright blood group)	Homo sapiens	77-81
15987132-8	2005	The thiocholine chemisorption (i.e., accumulation) on the silver electrode surface resulted in a sensitivity for the electrochemical determination of the AChE activity that was 2 orders of magnitude greater than that obtained when using direct measurement without accumulation.	Thiocholine	4-15	acetylcholinesterase (Cartwright blood group)	Homo sapiens	154-158
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)(-).	Thiocholine	63-74	acetylcholinesterase (Cartwright blood group)	Homo sapiens	28-32
15223749-7	2004	We report a detailed thiocholine protocol that is a modification of the Koelle-Friedenwald method to amplify the AChE signal in brain sections previously processed for autoradiography.	Thiocholine	21-32	acetylcholinesterase (Cartwright blood group)	Homo sapiens	113-117
15568740-2	2004	Butyrylcholinesterase-(BuChE)-positive nerve components of the organ were visualized by the direct thiocholine method.	Thiocholine	99-110	butyrylcholinesterase	Rattus norvegicus	0-21
14686935-8	2004	BuChE-catalyzed hydrolysis of the thiocholine analogue of BzCh showed neither lags nor oscillations, under the same conditions.	Thiocholine	34-45	butyrylcholinesterase	Homo sapiens	0-5
11673363-9	2001	The substrates were stable in aqueous solution and in the solid state as the iodides for at least 5 years at 5 degrees C. CONCLUSIONS: The isobutyrate and cyclohexane-carboxylate of thiocholine are suitable for the specific assay of human serum cholinesterase.	Thiocholine	182-193	butyrylcholinesterase	Homo sapiens	245-259
11151034-7	2001	Total, membrane-bound and soluble Achase activities (nmol of thiocholine formed min(-1) mg protein(-1)) were assayed photometrically.	Thiocholine	61-72	acetylcholinesterase	Rattus norvegicus	34-40
11163034-2	2001	METHODS: Acetylthiocholine, used as substrate, is hydrolysed by acetylcholinesterase to yield acetate and thiocholine.	Thiocholine	15-26	acetylcholinesterase (Cartwright blood group)	Homo sapiens	64-84
10679638-4	2000	Variations in enzyme activity due to inhibition are measured from the changes of concentrations of thiocholine produced when the substrate (acetylthiocholine chloride) is pumped before and after the passage of the solution containing the pesticide through the immobilized AChE reactor.	Thiocholine	99-110	acetylcholinesterase (Cartwright blood group)	Homo sapiens	272-276
33588332-5	2021	The sensing mechanism is that OPs-treated acetylcholinesterase (AChE) prevents the formation of thiocholine, thereby minimizing the reduction of MnO2 into Mn2+ and changing the output signal.	Thiocholine	96-107	acetylcholinesterase (Cartwright blood group)	Homo sapiens	64-68
9496440-10	1997	A statistically significant decrease in membrane-bound Achase activity (nmol thiocholine formed min-1 mg protein-1) (control 182.6 +/- 14.8, ECS 162.2 +/- 14.2, P < 0.05) and an increase in soluble Achase activity in the medulla oblongata (control 133.6 +/- 4.2, ECS 145.8 +/- 12.3, P < 0.05) were observed.	Thiocholine	77-88	acetylcholinesterase	Rattus norvegicus	55-61
9361724-8	1997	Membrane-bound Achase activity (nmol thiocholine formed min-1 mg protein-1) after chronic imipramine treatment was significantly decreased in the hippocampus (control = 188.8 +/- 19.4, imipramine = 154.4 +/- 7.5, P < 0.005) and striatum (control = 850.9 +/- 59.6, imipramine = 742.5 +/- 34.7, P < 0.005).	Thiocholine	37-48	acetylcholinesterase	Rattus norvegicus	15-21
9283633-10	1997	REM sleep deprivation induced a significant decrease of 16% in the membrane-bound Achase activity (nmol thiocholine formed min-1 mg protein-1) in the 100,000 g pellet enzyme preparation (home-cage group 152.1 +/- 5.7, large platform group 152.7 +/- 24.9 and REM sleep-deprived group 127.9 +/- 13.8).	Thiocholine	104-115	acetylcholinesterase	Rattus norvegicus	82-88
7750137-3	1995	A thiocholine method revealed that AChE activity was localized in the subventral glands, which have a secretory and excretory function via a duct connected to the excretory pore.	Thiocholine	2-13	acetylcholinesterase (Cartwright blood group)	Homo sapiens	35-39
7750137-7	1995	When AChE activity in the nematode excretory-secretory product was examined by SDS polyacrylamide gel electrophoresis combined with the thiocholine method, intense activity was demonstrated as a single band at 74 kDa.	Thiocholine	136-147	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-9
8364473-2	1993	The procedure involves ultrafiltration to remove endogenous plasma cholinesterase, followed by colorimetric measurement of the inhibitory activity to acetylcholinesterase by the thiocholine method.	Thiocholine	178-189	acetylcholinesterase	Rattus norvegicus	150-170
1706733-2	1991	A modification of the Koelle copper thiocholine method was employed for the histochemical demonstration of AChE.	Thiocholine	36-47	acetylcholinesterase	Mus musculus	107-111
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.	Thiocholine	52-63	acetylcholinesterase (Cartwright blood group)	Homo sapiens	5-25
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.	Thiocholine	49-60	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.	Thiocholine	49-60	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.	Thiocholine	49-60	acetylcholinesterase (Cartwright blood group)	Homo sapiens	252-256
33032200-4	2020	When acetylcholinesterase (AChE) was present, acetylthiocholine (ATCh) was catalytically hydrolyzed into thiocholine, which reduced MnO2 of PTDNP-MnNFs into Mn2+, subsequently blocking the FRET and enhancing the fluorescence.	Thiocholine	52-63	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-31
34801807-5	2022	Nanocomposite promoted the electron transfer reaction to catalyze the electro-oxidation of thiocholine and a large current response was obtained by cyclic voltammetry at 0.77 V, indicating successful immobilization of AChE.	Thiocholine	91-102	acetylcholinesterase	Apis mellifera	218-222
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.	Thiocholine	120-131	acetylcholinesterase (Cartwright blood group)	Homo sapiens	86-90
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.	Thiocholine	133-136	acetylcholinesterase (Cartwright blood group)	Homo sapiens	86-90
34865979-4	2022	However, in the absence of PM, AChE hydrolyzed ATCh to TCh, which then reacted with the AuNPs, preventing the oxidation of TMB to oxTMB and rendering the solution colorless.	Thiocholine	55-58	acetylcholinesterase (Cartwright blood group)	Homo sapiens	31-35
34952437-5	2022	The hydrolysate of substrates, thiocholine, under the catalysis of BChE can reduce dopamine, which results in the inhibition of self-polymerization and the fluorescence recovery of S-dots.	Thiocholine	31-42	butyrylcholinesterase	Homo sapiens	67-71
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.	Thiocholine	163-174	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.	Thiocholine	163-174	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.	Thiocholine	163-174	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.	Thiocholine	176-179	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.	Thiocholine	176-179	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.	Thiocholine	176-179	acetylcholinesterase (Cartwright blood group)	Homo sapiens	184-188
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).	Thiocholine	97-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34875277-0	2022	Interactions of human acetylcholinesterase with phenyl valerate and acetylthiocholine: Thiocholine as an enhancer of phenyl valerate esterase activity.	Thiocholine	87-98	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).	Thiocholine	97-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
34625266-4	2021	Acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylcholine (ATCh) to produce thiocholine (TCh).	Thiocholine	88-99	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34625266-4	2021	Acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylcholine (ATCh) to produce thiocholine (TCh).	Thiocholine	88-99	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
34625266-4	2021	Acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylcholine (ATCh) to produce thiocholine (TCh).	Thiocholine	101-104	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34625266-4	2021	Acetylcholinesterase (AChE) catalyzes the hydrolysis of acetylcholine (ATCh) to produce thiocholine (TCh).	Thiocholine	101-104	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-26
34625266-6	2021	Organophosphorus pesticides (OPs) can inhibit the activity of AChE enzymes, thereby preventing the production of TCh and the decomposition of MnO2 nanosheets, resulting in the fluorescence "turn-off".	Thiocholine	113-116	acetylcholinesterase (Cartwright blood group)	Homo sapiens	62-66
34476614-3	2021	Acetylcholinesterase hydrolyzed acetylthiocholine to generate thiocholine that bound with Cu2+ strongly via S-Cu-S bond.	Thiocholine	62-73	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-20
34697648-4	2021	BChE can catalyze the decomposition of butyrylcholine, producing thiocholine, which further reduce and coordinate with CuO on surface of Cu2O nanoparticle.	Thiocholine	65-76	butyrylcholinesterase	Homo sapiens	0-4
34623807-3	2021	In the detection system, thiocholine (Tch), the hydrolysis product of thioacetylcholine (ATch) by acetylcholinesterase (AchE), could trigger the aggregation of CTAB-Au NPs, resulting in a significant color change from red to purple.	Thiocholine	25-36	acetylcholinesterase (Cartwright blood group)	Homo sapiens	98-118
34623807-3	2021	In the detection system, thiocholine (Tch), the hydrolysis product of thioacetylcholine (ATch) by acetylcholinesterase (AchE), could trigger the aggregation of CTAB-Au NPs, resulting in a significant color change from red to purple.	Thiocholine	25-36	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-124
34623807-3	2021	In the detection system, thiocholine (Tch), the hydrolysis product of thioacetylcholine (ATch) by acetylcholinesterase (AchE), could trigger the aggregation of CTAB-Au NPs, resulting in a significant color change from red to purple.	Thiocholine	38-41	acetylcholinesterase (Cartwright blood group)	Homo sapiens	98-118
34623807-3	2021	In the detection system, thiocholine (Tch), the hydrolysis product of thioacetylcholine (ATch) by acetylcholinesterase (AchE), could trigger the aggregation of CTAB-Au NPs, resulting in a significant color change from red to purple.	Thiocholine	38-41	acetylcholinesterase (Cartwright blood group)	Homo sapiens	120-124
34476614-4	2021	Dichlorvos as competitive inhibitor for acetylcholinesterase prevented the generation of thiocholine, which blocked the formation of Cu-thiocholine complex and changed the ratiometric fluorescence signal.	Thiocholine	89-100	acetylcholinesterase (Cartwright blood group)	Homo sapiens	40-60
35421656-2	2022	Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh).	Thiocholine	76-87	acetylcholinesterase (Cartwright blood group)	Homo sapiens	14-34
35421656-2	2022	Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh).	Thiocholine	76-87	acetylcholinesterase (Cartwright blood group)	Homo sapiens	36-40
35421656-2	2022	Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh).	Thiocholine	89-92	acetylcholinesterase (Cartwright blood group)	Homo sapiens	14-34
35421656-2	2022	Specifically, acetylcholinesterase (AChE) hydrolyzes acetylthiocholine into thiocholine (TCh).	Thiocholine	89-92	acetylcholinesterase (Cartwright blood group)	Homo sapiens	36-40
35533565-4	2022	Meanwhile thiocholine is catalytically produced by acetylcholinesterase (AChE) to directly reduce blue ox-TMB into colorless TMB.	Thiocholine	10-21	acetylcholinesterase (Cartwright blood group)	Homo sapiens	51-71
35533565-4	2022	Meanwhile thiocholine is catalytically produced by acetylcholinesterase (AChE) to directly reduce blue ox-TMB into colorless TMB.	Thiocholine	10-21	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-77
35533565-5	2022	But the activity of AChE will be suppressed by carbaryl, thus generating less thiocholine and resulting in more ox-TMB for colorimetric analysis.	Thiocholine	78-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	20-24
35623791-8	2022	AChE could hydrolyze the acetylcholine chloride (ATCl) to produce an electron donor of thiocholine which led to the elevated photocurrent output.	Thiocholine	87-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
35623791-9	2022	When the bioactivity of AChE was inhibited by the organophosphate pesticides (chlorpyrifos as substrate), the reduced production of thiocholine resulted in a decline in photocurrent.	Thiocholine	132-143	acetylcholinesterase (Cartwright blood group)	Homo sapiens	24-28
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.	Thiocholine	106-117	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48
35473871-5	2022	Herein, thiocholine could be produced in hydrolysis reaction of acetylthiocholine catalyzed by the acetylcholinesterase (AChE), of which the catalytic activity could be irreversibly inhibitted by the introduction of organophosphates.	Thiocholine	8-19	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.	Thiocholine	8-19	acetylcholinesterase (Cartwright blood group)	Homo sapiens	121-125
35414394-5	2022	Butyrylcholinesterase (BChE) can catalyze the hydrolysis of S-butyrylthiocholine iodide (BTCh) to produce thiocholine, which could prevent the oxidation of ABTS, resulting in the fluorescence of oxidized UiO-66-NH2@Ce recovered.	Thiocholine	106-117	butyrylcholinesterase	Homo sapiens	0-21
35414394-5	2022	Butyrylcholinesterase (BChE) can catalyze the hydrolysis of S-butyrylthiocholine iodide (BTCh) to produce thiocholine, which could prevent the oxidation of ABTS, resulting in the fluorescence of oxidized UiO-66-NH2@Ce recovered.	Thiocholine	106-117	butyrylcholinesterase	Homo sapiens	23-27
35572106-4	2022	Chlorpyrifos as an acetylcholinesterase inhibitor controls the enzymatic hydrolysis reaction and further regulates the production of thiocholine that could decompose CoOOH nanoflakes into Co2+, resulting in the fluorescence response of AuNC-based hydrogel.	Thiocholine	133-144	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-39
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.	Thiocholine	251-262	acetylcholinesterase (Cartwright blood group)	Homo sapiens	276-296
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.	Thiocholine	251-262	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.	Thiocholine	251-262	acetylcholinesterase (Cartwright blood group)	Homo sapiens	326-330
35414329-2	2022	Since MnO2 NS can quench the fluorescence of g-C3N4 via the inner-filter effect (IFE), enzymatic hydrolysate (thiocholine, TCh) can efficiently trigger the decomposition of MnO2 nanosheets in the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCh), resulting in the fluorescence recovery of g-C3N4.	Thiocholine	110-121	acetylcholinesterase (Cartwright blood group)	Homo sapiens	208-228
34978797-5	2022	Taking advantage of the sensitive photocurrent response of thiocholine (TCl) on AgNWs/C60-CR, an acetylcholinesterase (AChE)-based PEC biosensing system with tunable detection throughput for the on-site screening of ultratrace organophosphorus pesticides (OPs) was established.	Thiocholine	59-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	97-117
34978797-5	2022	Taking advantage of the sensitive photocurrent response of thiocholine (TCl) on AgNWs/C60-CR, an acetylcholinesterase (AChE)-based PEC biosensing system with tunable detection throughput for the on-site screening of ultratrace organophosphorus pesticides (OPs) was established.	Thiocholine	59-70	acetylcholinesterase (Cartwright blood group)	Homo sapiens	119-123
34978797-5	2022	Taking advantage of the sensitive photocurrent response of thiocholine (TCl) on AgNWs/C60-CR, an acetylcholinesterase (AChE)-based PEC biosensing system with tunable detection throughput for the on-site screening of ultratrace organophosphorus pesticides (OPs) was established.	Thiocholine	72-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	97-117
34978797-5	2022	Taking advantage of the sensitive photocurrent response of thiocholine (TCl) on AgNWs/C60-CR, an acetylcholinesterase (AChE)-based PEC biosensing system with tunable detection throughput for the on-site screening of ultratrace organophosphorus pesticides (OPs) was established.	Thiocholine	72-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	119-123
35414329-2	2022	Since MnO2 NS can quench the fluorescence of g-C3N4 via the inner-filter effect (IFE), enzymatic hydrolysate (thiocholine, TCh) can efficiently trigger the decomposition of MnO2 nanosheets in the presence of acetylcholinesterase (AChE) and acetylthiocholine (ATCh), resulting in the fluorescence recovery of g-C3N4.	Thiocholine	110-121	acetylcholinesterase (Cartwright blood group)	Homo sapiens	230-234
3052242-4	1988	Contemporary methods employ acylthiocholine as substrate for serum cholinesterase and a second coupled reaction of thiocholine and chromogenic disulfide agents.	Thiocholine	32-43	butyrylcholinesterase	Homo sapiens	67-81
2444629-3	1987	A modification of the Koelle copper thiocholine method was used for the histochemical demonstration of AChE.	Thiocholine	36-47	ACE-1	Oryctolagus cuniculus	103-107
3308498-1	1987	We traced the origin and path of autonomic nerves to the rat eye using, as an aid to dissection, a modified thiocholine method for the histochemical demonstration of cholinesterase.	Thiocholine	108-119	butyrylcholinesterase	Rattus norvegicus	166-180
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.	Thiocholine	64-76	cholinesterase	Oryctolagus cuniculus	32-35
6189639-3	1983	We evaluated four direct and indirect procedures for measuring AChE in which thiocholine is generated.	Thiocholine	77-88	acetylcholinesterase (Cartwright blood group)	Homo sapiens	63-67
3721921-1	1986	The "direct coloring" thiocholine method of Karnovsky and Roots (1964) for the demonstration of acetylcholinesterase (AChE) activity was modified and adapted to the technique of semipermeable membranes.	Thiocholine	22-33	acetylcholinesterase (Cartwright blood group)	Homo sapiens	96-116
3721921-1	1986	The "direct coloring" thiocholine method of Karnovsky and Roots (1964) for the demonstration of acetylcholinesterase (AChE) activity was modified and adapted to the technique of semipermeable membranes.	Thiocholine	22-33	acetylcholinesterase (Cartwright blood group)	Homo sapiens	118-122
4041620-3	1985	This study presents the ultrastructural localization of AChE activity in human thymus cells, using the indirect thiocholine method.	Thiocholine	112-123	acetylcholinesterase (Cartwright blood group)	Homo sapiens	56-60
3965482-4	1985	AchE synthesized in culture cleaved acetylthiocholine to thiocholine, which stochiometrically reduced the colorless indicator DTNB to a highly colored product.	Thiocholine	42-53	acetylcholinesterase	Mus musculus	0-4
6467040-4	1984	We report a detailed thiocholine protocol and observations on several experimental factors which affect the sensitivity, consistency and the discreteness of localization of AChE in histological material.	Thiocholine	21-32	acetylcholinesterase (Cartwright blood group)	Homo sapiens	173-177
6193086-0	1983	A modification of thiocholine-ferricyanide method of Karnovsky and Roots for localization of acetylcholinesterase activity without interference by Koelle"s copper thiocholine iodide precipitate.	Thiocholine	18-29	acetylcholinesterase (Cartwright blood group)	Homo sapiens	93-113
6193086-1	1983	In the original Karnovsky and Roots" method for the localization of acetylcholinesterase (AChE), thiocholine reduces the ferricyanide and cupric ions of this medium competitively, giving simultaneously cupric (Koelle"s precipitate) as histochemical products.	Thiocholine	97-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	68-88
6193086-1	1983	In the original Karnovsky and Roots" method for the localization of acetylcholinesterase (AChE), thiocholine reduces the ferricyanide and cupric ions of this medium competitively, giving simultaneously cupric (Koelle"s precipitate) as histochemical products.	Thiocholine	97-108	acetylcholinesterase (Cartwright blood group)	Homo sapiens	90-94
7066709-2	1982	First, catecholamine cells were visualized by their formaldehyde/glutaraldehyde induced specific histofluorescence and then poststained in the same tissue with a thiocholine technique for acetylcholinesterase (AChE).	Thiocholine	162-173	acetylcholinesterase	Rattus norvegicus	188-208
98962-1	1978	The cutaneous nodules obtained from seven patients with von Recklinghausen"s neurofibromatosis were investigated by electron microscopy, and ultrastructural localization of acetylcholinesterase activity was demonstrated in the nerve fibers of this tumor for the first time using Karnovsky"s thiocholine method.	Thiocholine	291-302	acetylcholinesterase (Cartwright blood group)	Homo sapiens	173-193
7273852-0	1981	Thiocholine methods for the demonstration of acetylcholinesterase in neuromuscular junctions.	Thiocholine	0-11	acetylcholinesterase	Rattus norvegicus	45-65
6157438-1	1980	The direct-coloring thiocholine technique used for determining cholinesterase in intra- and extrafusal muscle fibers disclosed the presence of two kinds of nerve endings (twitch and grape types) in these fibers.	Thiocholine	20-31	butyrylcholinesterase	Homo sapiens	63-77
4137210-0	1974	Studies of the direct coloring thiocholine method for localizing cholinesterase activity.	Thiocholine	31-42	butyrylcholinesterase	Homo sapiens	65-79
955984-3	1976	The cellular and subcellular localization of acetylcholinesterase activity in cultured neurons was studied by the thiocholine techniques of Karnovsky and Roots and Lewis and Shute.	Thiocholine	114-125	acetylcholinesterase (Cartwright blood group)	Gallus gallus	45-65
1180234-6	1975	The thiocholine technique of Karnovsky and Roots was used to demonstrate acetylcholinesterase (AChE) activity at the light microscope level.	Thiocholine	4-15	acetylcholinesterase	Mus musculus	73-93
1180234-6	1975	The thiocholine technique of Karnovsky and Roots was used to demonstrate acetylcholinesterase (AChE) activity at the light microscope level.	Thiocholine	4-15	acetylcholinesterase	Mus musculus	95-99
4611985-0	1974	On the chemical basis of thiocholine methods for demonstration of acetylcholinesterase activities.	Thiocholine	25-36	acetylcholinesterase (Cartwright blood group)	Homo sapiens	66-86
4506787-1	1972	Esters of thiocholine were shown to inhibit the crosslinking of fibrin clots by the transamidating enzyme, fibrinoligase (thrombin-activated fibrin-stabilizing factor or activated Factor XIII).	Thiocholine	10-21	coagulation factor XIII A chain	Homo sapiens	107-120
5672830-0	1968	Ageing and reactivation of acetylcholinesterase inhibited with Soman and its thiocholine-like analogue.	Thiocholine	77-88	acetylcholinesterase (Cartwright blood group)	Homo sapiens	27-47
4172645-0	1967	A thiocholine-lead ferrocyanide method for acetylcholinesterase.	Thiocholine	2-13	acetylcholinesterase (Cartwright blood group)	Homo sapiens	43-63
5336055-0	1966	Electron microscopic localization of cholinesterase by a copper-lead-thiocholine technique.	Thiocholine	69-80	butyrylcholinesterase	Homo sapiens	37-51
13874167-0	1961	Quantitative evaluation of the thiocholine method for cholinesterase as applied to single end-plates from mouse gastrocnemius muscle.	Thiocholine	31-42	butyrylcholinesterase	Mus musculus	54-68
13478499-0	1957	A modification of the thiocholine method for the determination of cholinesterase.	Thiocholine	22-33	butyrylcholinesterase	Homo sapiens	66-80
33601648-2	2021	OPs effectively reduce the production of thiocholine in the acetylcholinesterase/acetylthiocholine reaction by inhibiting the activity of acetylcholinesterase.	Thiocholine	41-52	acetylcholinesterase (Cartwright blood group)	Homo sapiens	60-80
33601648-2	2021	OPs effectively reduce the production of thiocholine in the acetylcholinesterase/acetylthiocholine reaction by inhibiting the activity of acetylcholinesterase.	Thiocholine	41-52	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.	Thiocholine	145-156	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.	Thiocholine	145-156	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
33839958-3	2021	In the presence of AChE, acetylthiocholine (ATCh), a typical AChE substrate, is hydrolyzed to thiocholine (TCh).	Thiocholine	31-42	acetylcholinesterase (Cartwright blood group)	Homo sapiens	19-23
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.	Thiocholine	217-228	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.	Thiocholine	217-228	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.	Thiocholine	217-228	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).	Thiocholine	31-42	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).	Thiocholine	45-48	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).	Thiocholine	45-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	61-65
33379049-3	2021	When the target BChE is introduced to form thiocholine in the presence of S-butyrylthiocholine iodide (BTCh), MnO2 nanosheets are reduced by thiocholine to Mn2+, resulting in the loss of their oxidase-like activity and the reduction of TC fluorescence.	Thiocholine	43-54	butyrylcholinesterase	Homo sapiens	16-20
34012694-4	2021	Acetylthiocholine (ATCh) could be catalytically hydrolyzed by acetylcholinesterase (AChE) to form thiocholine, which induces aggregation of the AgNPs.	Thiocholine	6-17	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.	Thiocholine	6-17	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.	Thiocholine	32-43	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.	Thiocholine	32-43	acetylcholinesterase (Cartwright blood group)	Homo sapiens	123-127
33379049-3	2021	When the target BChE is introduced to form thiocholine in the presence of S-butyrylthiocholine iodide (BTCh), MnO2 nanosheets are reduced by thiocholine to Mn2+, resulting in the loss of their oxidase-like activity and the reduction of TC fluorescence.	Thiocholine	83-94	butyrylcholinesterase	Homo sapiens	16-20
33280706-4	2021	The positively charged thiocholine (TCh) produced by enzyme hydrolysis triggers the AgNPs aggregation on GO sheets, which ultimately decreases the intensity of the corresponding SPR absorption peak.	Thiocholine	23-34	sepiapterin reductase	Homo sapiens	178-181
33280706-4	2021	The positively charged thiocholine (TCh) produced by enzyme hydrolysis triggers the AgNPs aggregation on GO sheets, which ultimately decreases the intensity of the corresponding SPR absorption peak.	Thiocholine	36-39	sepiapterin reductase	Homo sapiens	178-181
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.	Thiocholine	21-32	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.	Thiocholine	34-37	acetylcholinesterase (Cartwright blood group)	Homo sapiens	92-96
33057486-6	2021	AChE can specifically catalyze the decomposition of its substrate acetylthiocholine chloride to thiocholine.	Thiocholine	72-83	acetylcholinesterase (Cartwright blood group)	Homo sapiens	0-4
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.	Thiocholine	28-39	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.	Thiocholine	41-44	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.	Thiocholine	111-114	acetylcholinesterase	Rattus norvegicus	119-123