PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19101643-7 2009 We concluded that dithiothreitol-induced activation of erythrocyte thiol status decreases NO efflux and allows greater intracellular NO mobilization onto different derivative molecules, both in the absence and presence of acetylcholinesterase substrate and inhibitor. Sulfhydryl Compounds 67-72 acetylcholinesterase (Cartwright blood group) Homo sapiens 222-242 19101643-1 2009 We assessed the redox thiol status influence on nitric oxide (NO) metabolism and efflux in erythrocytes stimulated with acetylcholinesterase substrate (acetylcholine, ACh) and inhibitor (velnacrine maleate, VM). Sulfhydryl Compounds 22-27 acetylcholinesterase (Cartwright blood group) Homo sapiens 120-140 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). Sulfhydryl Compounds 41-46 acetylcholinesterase (Cartwright blood group) Homo sapiens 168-188 19238297-4 2009 The PQQ electrode was then utilized as a thiol-specific sensor for the real-time monitoring of thiocholine generated from the hydrolysis of acetylthiocholine (ASCh) by acetylcholinesterase (AChE). Sulfhydryl Compounds 41-46 acetylcholinesterase (Cartwright blood group) Homo sapiens 190-194 19238297-6 2009 These measurements demonstrated the versatility of this sensor for the detection of thiols and potentially for the development of assays to evaluate the enzymatic activity of acetylcholinesterase. Sulfhydryl Compounds 84-90 acetylcholinesterase (Cartwright blood group) Homo sapiens 175-195 18781015-4 2008 The FET-based immunoassay was constructed by combining the 11-FUT modified-FET sensor with the enzyme-linked immunosorbent assay (ELISA), in which the enzyme chemistry of acetylcholinesterase (AChE) was used to generate a thiol compound. Sulfhydryl Compounds 222-227 acetylcholinesterase (Cartwright blood group) Homo sapiens 171-191 18781015-4 2008 The FET-based immunoassay was constructed by combining the 11-FUT modified-FET sensor with the enzyme-linked immunosorbent assay (ELISA), in which the enzyme chemistry of acetylcholinesterase (AChE) was used to generate a thiol compound. Sulfhydryl Compounds 222-227 acetylcholinesterase (Cartwright blood group) Homo sapiens 193-197 34170111-7 2021 As a proof-of-concept application, the free-standing POD-like membranes were applied as a label-free assay in sensing cysteine, as well as monitoring acetylcholinesterase (AChE) activity through the generated thiol-containing product. Sulfhydryl Compounds 209-214 acetylcholinesterase (Cartwright blood group) Homo sapiens 150-170 19029635-8 2008 Upon intracellular thiol stimulation, the presence of AChE effectors (either acetylcholine or velnacrine) decreases erythrocyte aggregation and elongation indexes. Sulfhydryl Compounds 19-24 acetylcholinesterase (Cartwright blood group) Homo sapiens 54-58 17324568-3 2007 To construct an electrochemical enzyme immunoassay system by using the sensor, the enzyme chemistry of acetylcholinesterase (AChE) to generate a thiol compound was used and combined with the enzyme-linked immunosorbent assays (ELISA). Sulfhydryl Compounds 145-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-123 17324568-3 2007 To construct an electrochemical enzyme immunoassay system by using the sensor, the enzyme chemistry of acetylcholinesterase (AChE) to generate a thiol compound was used and combined with the enzyme-linked immunosorbent assays (ELISA). Sulfhydryl Compounds 145-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-129 17324568-4 2007 After the AChE-catalyzed reaction, the amount of the antigen was obtained by detecting the adsorbing rate of the generated thiol compound on the gold electrode using the FET sensor. Sulfhydryl Compounds 123-128 acetylcholinesterase (Cartwright blood group) Homo sapiens 10-14 1906943-3 1991 Optimum conditions for the cerebellar AChE activity were determined with respect to molarity of the buffer, pH, temperature, and concentrations of substrate (acetylthiocholine iodide), activators (NaCl, MgCl2), and thiol indicator (dithiobisnitrobenzoic acid). Sulfhydryl Compounds 215-220 acetylcholinesterase (Cartwright blood group) Homo sapiens 38-42 34170111-7 2021 As a proof-of-concept application, the free-standing POD-like membranes were applied as a label-free assay in sensing cysteine, as well as monitoring acetylcholinesterase (AChE) activity through the generated thiol-containing product. Sulfhydryl Compounds 209-214 acetylcholinesterase (Cartwright blood group) Homo sapiens 172-176 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%. Sulfhydryl Compounds 168-173 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 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. Sulfhydryl Compounds 56-61 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. Sulfhydryl Compounds 56-61 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. Sulfhydryl Compounds 56-61 acetylcholinesterase (Cartwright blood group) Homo sapiens 279-283 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. Sulfhydryl Compounds 91-96 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. Sulfhydryl Compounds 91-96 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. Sulfhydryl Compounds 91-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 326-330 33839958-0 2021 Colorimetric detection of acetylcholinesterase and its inhibitor based on thiol-regulated oxidase-like activity of 2D palladium square nanoplates on reduced graphene oxide. Sulfhydryl Compounds 74-79 acetylcholinesterase (Cartwright blood group) Homo sapiens 26-46 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. Sulfhydryl Compounds 0-5 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. Sulfhydryl Compounds 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 123-127 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%. Sulfhydryl Compounds 168-173 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 31482681-5 2019 Besides, the Fe-N-C SAzymes are applied in biosensor areas to evaluate the activity of acetylcholinesterase based on the inhibition toward nanozyme activity by thiols. Sulfhydryl Compounds 160-166 acetylcholinesterase (Cartwright blood group) Homo sapiens 87-107 26839920-3 2016 The competitive binding by a thiol group (-SH), produced in the hydrolysis reaction of acetylthiocholine (ACh) chloride with acetylcholinesterase (AChE), removes mercury ions from the base pairs, causing a nuclease-catalyzed digestion, and the subsequent electrochemical response increase due to the weak electrostatic repulsion between the product-mononucleotides and the ITO electrode. Sulfhydryl Compounds 29-34 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-145 26492468-6 2016 In the presence of carbamate pesticide, the activity of AChE is inhibited, and the amount of the product containing the thiol group generated by the hydrolysis reaction of acetylthiocholine chloride (ACh) decreases, resulting in the release of a low concentration of Hg(2+). Sulfhydryl Compounds 120-125 acetylcholinesterase (Cartwright blood group) Homo sapiens 56-60 31020297-4 2019 AChE can hydrolyze acetylthiocholine (ATCh) to form thiocholine (TCh) which contains a thiol group. Sulfhydryl Compounds 87-92 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 26839920-3 2016 The competitive binding by a thiol group (-SH), produced in the hydrolysis reaction of acetylthiocholine (ACh) chloride with acetylcholinesterase (AChE), removes mercury ions from the base pairs, causing a nuclease-catalyzed digestion, and the subsequent electrochemical response increase due to the weak electrostatic repulsion between the product-mononucleotides and the ITO electrode. Sulfhydryl Compounds 29-34 acetylcholinesterase (Cartwright blood group) Homo sapiens 147-151 26494253-0 2016 A novel fluorogenic probe for the investigation of free thiols: Application to kinetic measurements of acetylcholinesterase activity. Sulfhydryl Compounds 56-62 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-123 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. Sulfhydryl Compounds 215-220 acetylcholinesterase (Cartwright blood group) Homo sapiens 20-24 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). Sulfhydryl Compounds 112-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 89-93 24299064-9 2013 The AChE-catalyzed hydrolysis of acetylthiocholine to the thiol-functionalized thiocholine enabled the probing of the enzymatic activity of AChE through the hemin/G-quadruplex-catalyzed aerobic oxidation of thiocholine to the respective disulfide and the concomitant generation of the fluorescent resorufin product. Sulfhydryl Compounds 58-63 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. Sulfhydryl Compounds 58-63 acetylcholinesterase (Cartwright blood group) Homo sapiens 140-144 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. Sulfhydryl Compounds 215-220 acetylcholinesterase (Cartwright blood group) Homo sapiens 351-355 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. Sulfhydryl Compounds 34-39 acetylcholinesterase (Cartwright blood group) Homo sapiens 164-168