PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. cupric ion 93-97 acetylcholinesterase (Cartwright blood group) Homo sapiens 245-265 34476614-3 2021 Acetylcholinesterase hydrolyzed acetylthiocholine to generate thiocholine that bound with Cu2+ strongly via S-Cu-S bond. cupric ion 90-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 8984476-1 1996 Acetylcholinesterase (AChE) was purified on columns with iminodiacetate Agarose charged with Cu2+, Zn2+, and Ni2+. cupric ion 93-97 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 8984476-1 1996 Acetylcholinesterase (AChE) was purified on columns with iminodiacetate Agarose charged with Cu2+, Zn2+, and Ni2+. cupric ion 93-97 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 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. cupric ion 93-97 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. cupric ion 193-197 acetylcholinesterase (Cartwright blood group) Homo sapiens 96-100 31816742-0 2020 Copper(II) complex as a turn on fluorescent sensing platform for acetylcholinesterase activity with high sensitivity. cupric ion 0-10 acetylcholinesterase (Cartwright blood group) Homo sapiens 65-85 32781220-6 2020 13b (most potent AChE inhibitor) also showed copper-induced Abeta1-42 aggregation inhibition (34.26 % at 50 muMu) and chelating properties for metal ions (Cu2+, Fe2+, and Zn2+) involved in AD pathogenesis along with DNA protective potential against degenerative actions of OH radicals. cupric ion 155-159 acetylcholinesterase (Cartwright blood group) Homo sapiens 17-21 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%. cupric ion 160-164 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 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%. cupric ion 160-164 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 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+. cupric ion 29-33 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+. cupric ion 195-199 acetylcholinesterase (Cartwright blood group) Homo sapiens 102-106 31816742-6 2020 Furthermore, both HBTP-Cu2+ and HBTP show little toxicity to live cells and is available in visualizing cellular AChE activity. cupric ion 23-27 acetylcholinesterase (Cartwright blood group) Homo sapiens 113-117 30888170-0 2019 Fabricating an Acetylcholinesterase Modulated UCNPs-Cu2+ Fluorescence Biosensor for Ultrasensitive Detection of Organophosphorus Pesticides-Diazinon in Food. cupric ion 52-56 acetylcholinesterase (Cartwright blood group) Homo sapiens 15-35 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. cupric ion 156-160 acetylcholinesterase (Cartwright blood group) Homo sapiens 4-8 30888170-3 2019 Upon addition of AChE and acetylthiocholine (ATCh), the enzymatic hydrolysate (thiocholine) could seize Cu2+ from UCNPs-Cu2+ mixture, resulting in the quenched FL triggered on. cupric ion 104-108 acetylcholinesterase (Cartwright blood group) Homo sapiens 17-21 30888170-3 2019 Upon addition of AChE and acetylthiocholine (ATCh), the enzymatic hydrolysate (thiocholine) could seize Cu2+ from UCNPs-Cu2+ mixture, resulting in the quenched FL triggered on. cupric ion 120-124 acetylcholinesterase (Cartwright blood group) Homo sapiens 17-21 25560517-6 2015 The assay was based on the reaction between Cu(2+) and thiocholine, the hydrolysis product of ATCh by AChE. cupric ion 44-50 acetylcholinesterase (Cartwright blood group) Homo sapiens 102-106 30568757-5 2018 Molecules 5g and 5a disaggregated AChE-induced (58.26%, 47.36%) Abeta aggregation more than two fold more than the standard drug-donepezil (23.66%) and inhibited Cu2+-induced Abeta aggregation. cupric ion 162-166 acetylcholinesterase (Cartwright blood group) Homo sapiens 34-38 25096900-5 2014 Therefore, we have studied in vitro how AChE catalytic activity and ACh levels are affected by the presence of metals (Fe(3+), Cu(2+), Cr(3+), Zn(2+), and Cd(2+)), H2O2 (without Abeta42), and ( ) OH radicals produced from FR and FLR. cupric ion 127-133 acetylcholinesterase (Cartwright blood group) Homo sapiens 40-44 19540550-9 2009 However, Cu(2+) release in Cu and Cu-C nanoparticle suspensions caused 40% and 45% of AChE activity reduction, respectively. cupric ion 9-15 acetylcholinesterase (Cartwright blood group) Homo sapiens 86-90