PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 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. Sulfur 208-209 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-148 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. Sulfur 101-102 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 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. Sulfur 208-209 acetylcholinesterase (Cartwright blood group) Homo sapiens 150-154 12449529-3 2002 Their oxons are converted further to the S-oxides, which either inhibit AChE or decompose, depending on the alkyl substituents on the sulfur atom. Sulfur 134-140 acetylcholinesterase (Cartwright blood group) Homo sapiens 72-76 12502352-4 2003 The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges. Sulfur 58-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 141-145 12449529-4 2002 It is also inferred in the case of prothiophos oxon that its S-oxide not only inhibits AChE but also conjugates with glutathione (GSH) by the action of glutathione S-transferase (GST), and the conjugate inhibits AChE. Sulfur 61-62 acetylcholinesterase (Cartwright blood group) Homo sapiens 87-91 12449529-4 2002 It is also inferred in the case of prothiophos oxon that its S-oxide not only inhibits AChE but also conjugates with glutathione (GSH) by the action of glutathione S-transferase (GST), and the conjugate inhibits AChE. Sulfur 61-62 acetylcholinesterase (Cartwright blood group) Homo sapiens 212-216 30851693-2 2019 Based on the in vitro biological profile, compound S-K1035 was found to be the most potent inhibitor of human acetylcholinesterase (hAChE) and human butyrylcholinesterase (hBChE), demonstrating balanced IC50 values of 6.3 and 9.1 nM, respectively. Sulfur 51-52 acetylcholinesterase (Cartwright blood group) Homo sapiens 132-137 34476614-3 2021 Acetylcholinesterase hydrolyzed acetylthiocholine to generate thiocholine that bound with Cu2+ strongly via S-Cu-S bond. Sulfur 113-114 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 6493583-4 1984 These results support the hypothesis that extracellular 16S AChE at mammalian skeletal muscle motor endplates is primarily derived from complete, previously assembled 16S molecules originating in myofibers. Sulfur 56-59 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-64 6493583-4 1984 These results support the hypothesis that extracellular 16S AChE at mammalian skeletal muscle motor endplates is primarily derived from complete, previously assembled 16S molecules originating in myofibers. Sulfur 167-170 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-64 2937928-3 1986 In order to prove the in vivo interaction between the 16S AChE and heparan sulfate residues, the binding of exogenously added 16S enzyme to intact cells rich in cell-surface heparan sulfate proteoglycans was examined; 16S AChE form was shown to bind to intact endothelial cells in a specific, time-dependent, saturable fashion. Sulfur 54-57 acetylcholinesterase (Cartwright blood group) Homo sapiens 58-62 7441241-8 1980 Our results suggest that some nerve soluble substance, other than serum contaminants or 16S AChE itself, affects the maintenance of 16S AChE at the neuromuscular junction. Sulfur 132-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 92-96 7441241-8 1980 Our results suggest that some nerve soluble substance, other than serum contaminants or 16S AChE itself, affects the maintenance of 16S AChE at the neuromuscular junction. Sulfur 132-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 136-140 32891857-0 2020 Synthesis of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds - Determination of their carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and alpha-glycosidase inhibition properties. Sulfur 48-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-154