PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10779503-0 2000 Probing the active center gorge of acetylcholinesterase by fluorophores linked to substituted cysteines. Cysteine 94-103 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-55 19194505-3 2009 We previously reported that a cysteine residue (Cys), found at the AChE active site in aphids and other insects but not mammals, might serve as a target for insect-selective pesticides. Cysteine 30-38 acetylcholinesterase (Cartwright blood group) Homo sapiens 67-71 19194505-3 2009 We previously reported that a cysteine residue (Cys), found at the AChE active site in aphids and other insects but not mammals, might serve as a target for insect-selective pesticides. Cysteine 48-51 acetylcholinesterase (Cartwright blood group) Homo sapiens 67-71 19194505-5 2009 The absence of the active-site Cys in AO-AChE might raise concerns about the utility of targeting that residue. Cysteine 31-34 acetylcholinesterase (Cartwright blood group) Homo sapiens 41-45 19194505-9 2009 More importantly, by demonstrating that the Cys-targeting inhibitor can abolish AChE activity in aphids, we can conclude that the unique Cys may be a viable target for species-selective agents to control aphids without causing human toxicity and resistance problems. Cysteine 44-47 acetylcholinesterase (Cartwright blood group) Homo sapiens 80-84 19194505-9 2009 More importantly, by demonstrating that the Cys-targeting inhibitor can abolish AChE activity in aphids, we can conclude that the unique Cys may be a viable target for species-selective agents to control aphids without causing human toxicity and resistance problems. Cysteine 137-140 acetylcholinesterase (Cartwright blood group) Homo sapiens 80-84 18555979-6 2008 To examine whether the introduction of a Cys in the C-terminal region of other alpha/beta-hydrolase fold proteins could promote the same cellular phenotype, we made homologous mutations in acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) and found a similar processing deficiency and intracellular retention (De Jaco et al., J Biol Chem. Cysteine 41-44 acetylcholinesterase (Cartwright blood group) Homo sapiens 189-209 18555979-6 2008 To examine whether the introduction of a Cys in the C-terminal region of other alpha/beta-hydrolase fold proteins could promote the same cellular phenotype, we made homologous mutations in acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) and found a similar processing deficiency and intracellular retention (De Jaco et al., J Biol Chem. Cysteine 41-44 acetylcholinesterase (Cartwright blood group) Homo sapiens 211-215 17243918-0 2007 L-cysteine supplementation prevents exercise-induced alterations in human erythrocyte membrane acetylcholinesterase and Na+,K+-ATPase activities. Cysteine 0-10 acetylcholinesterase (Cartwright blood group) Homo sapiens 95-115 17243918-2 2007 The aim of this study was to investigate whether L-Cys supplementation prevents modulation of the activities of erythrocyte membrane acetylcholinesterase (AChE), Na(+),K(+)-ATPase and Mg(2+)-ATPase induced by free radicals in basketball players during training. Cysteine 49-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 133-153 17243918-2 2007 The aim of this study was to investigate whether L-Cys supplementation prevents modulation of the activities of erythrocyte membrane acetylcholinesterase (AChE), Na(+),K(+)-ATPase and Mg(2+)-ATPase induced by free radicals in basketball players during training. Cysteine 49-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 155-159 17243918-9 2007 When the players were supplemented with L-Cys, both AChE and Na(+),K(+)-ATPase activities remained unaltered post-exercise. Cysteine 40-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 11979423-0 2002 Inhibition of acetylcholinesterase by physostigmine analogs: conformational mobility of cysteine loop due to the steric effect of the alkyl chain. Cysteine 88-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 14-34 19714254-2 2009 We previously reported the finding of a free cysteine (Cys) residue at the entrance of the active site of acetylcholinesterase (AChE) in some insects but not in mammals, birds, and fish. Cysteine 45-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 19714254-2 2009 We previously reported the finding of a free cysteine (Cys) residue at the entrance of the active site of acetylcholinesterase (AChE) in some insects but not in mammals, birds, and fish. Cysteine 55-58 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 19714254-3 2009 These insects have two AChE genes (AP and AO), and only AP-AChE carries the Cys residue. Cysteine 76-79 acetylcholinesterase (Cartwright blood group) Homo sapiens 59-63 19714254-5 2009 Recently we reported a Cys-targeting small molecule that irreversibly inhibited all AChE activity extracted from aphids while an identical exposure caused no effect on the human AChE. Cysteine 23-26 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-88 19714254-6 2009 Full inhibition of AChE in aphids indicates that AP-AChE contributes most of the enzymatic activity and suggests that the Cys residue might serve as a target for developing better aphicides. Cysteine 122-125 acetylcholinesterase (Cartwright blood group) Homo sapiens 19-23 19714254-6 2009 Full inhibition of AChE in aphids indicates that AP-AChE contributes most of the enzymatic activity and suggests that the Cys residue might serve as a target for developing better aphicides. Cysteine 122-125 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 19714254-11 2009 This type of inhibition is fast ( approximately 30 min) and due to conjugation of the inhibitor to the active-site Cys of mosquito AP-AChE, according to our observed reactivation of the methanethiosulfonate-inhibited AChE by 2-mercaptoethanol. Cysteine 115-118 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-138 19714254-11 2009 This type of inhibition is fast ( approximately 30 min) and due to conjugation of the inhibitor to the active-site Cys of mosquito AP-AChE, according to our observed reactivation of the methanethiosulfonate-inhibited AChE by 2-mercaptoethanol. Cysteine 115-118 acetylcholinesterase (Cartwright blood group) Homo sapiens 217-221 17913689-7 2007 Finally, acetylcholinesterase can be modified through cysteine substitution mutagenesis and attachment of fluorophores at the substitution positions. Cysteine 54-62 acetylcholinesterase (Cartwright blood group) Homo sapiens 9-29 12851386-4 2003 To accelerate the process of identifying cyclic compounds with high affinity for the AChE P-site, we introduced a cysteine residue near the rim of the P-site by site-specific mutagenesis to generate recombinant human H287C AChE. Cysteine 114-122 acetylcholinesterase (Cartwright blood group) Homo sapiens 85-89 12851386-4 2003 To accelerate the process of identifying cyclic compounds with high affinity for the AChE P-site, we introduced a cysteine residue near the rim of the P-site by site-specific mutagenesis to generate recombinant human H287C AChE. Cysteine 114-122 acetylcholinesterase (Cartwright blood group) Homo sapiens 223-227 10347238-1 1999 Torpedo acetylcholinesterase is irreversibly inactivated by modifying a buried free cysteine, Cys231, with sulfhydryl reagents. Cysteine 84-92 acetylcholinesterase (Cartwright blood group) Homo sapiens 8-28 9545588-9 1998 Removing the cysteine residue near the C-terminus (truncated AChE, delta TAChE) assuming to affect the refolding, did not increase the amount of active enzyme obtained after refolding. Cysteine 13-21 acetylcholinesterase (Cartwright blood group) Homo sapiens 61-65 8615775-8 1996 Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a ...CTC... motif, in contrast with human AChE which contains only a single cysteine in this segment. Cysteine 143-151 acetylcholinesterase (Cartwright blood group) Homo sapiens 124-128 8849682-1 1996 Conformational mobility of the surface omega loop (Cys-69-Cys-96) in human acetylcholinesterase (HuAChE) was recently implicated in substrate accessibility to the active center and in the mechanism of allosteric modulation of enzymatic activity. Cysteine 51-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-95 8849682-1 1996 Conformational mobility of the surface omega loop (Cys-69-Cys-96) in human acetylcholinesterase (HuAChE) was recently implicated in substrate accessibility to the active center and in the mechanism of allosteric modulation of enzymatic activity. Cysteine 58-61 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-95 8615775-8 1996 Dimerization of AChE polypeptides is mediated by intersubunit disulphide bonding in this C-terminal segment, but the bovine AChE contained two cysteine residues in a ...CTC... motif, in contrast with human AChE which contains only a single cysteine in this segment. Cysteine 240-248 acetylcholinesterase (Cartwright blood group) Homo sapiens 124-128 29567174-1 2018 A highly sensitive electrochemical biosensor based on the synthetized L-Cysteine-Ag(I) coordination polymer (L-Cys-Ag(I) CP), which looks like a protein-mimicking nanowire, was constructed to detect acetylcholinesterase (AChE) activity and screen its inhibitors. Cysteine 72-75 acetylcholinesterase (Cartwright blood group) Homo sapiens 199-219 8077224-10 1994 Taken together, these results indicate (alpha) that sub-unit dimerization mediated by the COOH-terminal cysteine of HuAChE can reverse the signal-mediated retention by masking recognition of KDEL by its cognate receptor and (b) that the native sequences of the acetylcholinesterase subunit polypeptide do not appear to function as a coupled retention/dimerization signal in the control of secretion of assembled enzyme molecules. Cysteine 104-112 acetylcholinesterase (Cartwright blood group) Homo sapiens 261-281 31938465-0 2020 Cysteine-Targeted Insecticides against A. gambiae Acetylcholinesterase Are Neither Selective nor Reversible Inhibitors. Cysteine 0-8 acetylcholinesterase (Cartwright blood group) Homo sapiens 50-70 31938465-1 2020 Acetylcholinesterase cysteine-targeted insecticides against malaria vector Anopheles gambia and other mosquitos have already been introduced. Cysteine 21-29 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 1748670-2 1991 Site-directed mutagenesis was used to study the cysteine residue involved in the assembly of human acetylcholinesterase (HuAChE) catalytic subunits. Cysteine 48-56 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-119 29567174-1 2018 A highly sensitive electrochemical biosensor based on the synthetized L-Cysteine-Ag(I) coordination polymer (L-Cys-Ag(I) CP), which looks like a protein-mimicking nanowire, was constructed to detect acetylcholinesterase (AChE) activity and screen its inhibitors. Cysteine 72-75 acetylcholinesterase (Cartwright blood group) Homo sapiens 221-225 29567174-2 2018 This sensing strategy involves the reaction of acetylcholine chloride (ACh) with acetylcholinesterase (AChE) to form choline that is in turn catalytically oxidized by choline oxidase (ChOx) to produce hydrogen peroxide (H2O2), thus L-Cys-Ag(I) CP possesses the electro-catalytic property to H2O2 reduction. Cysteine 232-237 acetylcholinesterase (Cartwright blood group) Homo sapiens 81-101 29567174-2 2018 This sensing strategy involves the reaction of acetylcholine chloride (ACh) with acetylcholinesterase (AChE) to form choline that is in turn catalytically oxidized by choline oxidase (ChOx) to produce hydrogen peroxide (H2O2), thus L-Cys-Ag(I) CP possesses the electro-catalytic property to H2O2 reduction. Cysteine 232-237 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-107 28058724-5 2017 AChE is transported through the other inlet channel and mixes with the ATC (or Cys) as they travel up to the analysis sites. Cysteine 79-82 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 28008633-6 2017 DTNB and AChE/ATC (or Cys) flow towards each other where a reaction occurs to form the yellow colored 2-nitro-5-thiobenzoic acid anion (TNB2- ). Cysteine 22-25 acetylcholinesterase (Cartwright blood group) Homo sapiens 9-13 23323211-5 2013 These results further support our hypothesis that the insect-specific AChE cysteine is a unique and unexplored target to develop new insecticides with reduced insecticide resistance and low toxicity to mammals, fish, and birds for the control of mosquito-borne diseases. Cysteine 75-83 acetylcholinesterase (Cartwright blood group) Homo sapiens 70-74 23829431-4 2013 As the GOx-biocatalyzed oxidation of glucose yields H2O2, and the AChE/ChOx cascade leads to the formation of H2O2, the two biocatalytic processes could be probed by the cysteine-stimulated aggregation of the Au NPs. Cysteine 170-178 acetylcholinesterase (Cartwright blood group) Homo sapiens 66-70 23829431-5 2013 Since AChE is inhibited by 1,5-bis(4-allyldimethylammonium phenyl)pentane-3-one dibromide, the biocatalytic AChE/ChOx cascade is inhibited by the inhibitor, thus leading to the enhanced cysteine-mediated aggregation of the NPs. Cysteine 186-194 acetylcholinesterase (Cartwright blood group) Homo sapiens 6-10 23829431-5 2013 Since AChE is inhibited by 1,5-bis(4-allyldimethylammonium phenyl)pentane-3-one dibromide, the biocatalytic AChE/ChOx cascade is inhibited by the inhibitor, thus leading to the enhanced cysteine-mediated aggregation of the NPs. Cysteine 186-194 acetylcholinesterase (Cartwright blood group) Homo sapiens 108-112 23829431-6 2013 The results suggest the potential implementation of the cysteine-mediated aggregation of Au NPs in the presence of AChE/ChOx as a sensing platform for the optical detection of chemical warfare agents. Cysteine 56-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 115-119 22829062-6 2013 Finally, AChE was immobilized with covalent binding via -COOH groups of L-cysteine onto the modified GCE. Cysteine 72-82 acetylcholinesterase (Cartwright blood group) Homo sapiens 9-13 28176636-8 2017 Since AgAChE possesses an unpaired Cys residue not present in mammalian AChE, a logical strategy to achieve selective inhibition involves design of compounds that could ligate that Cys. Cysteine 35-38 acetylcholinesterase (Cartwright blood group) Homo sapiens 8-12 28176636-8 2017 Since AgAChE possesses an unpaired Cys residue not present in mammalian AChE, a logical strategy to achieve selective inhibition involves design of compounds that could ligate that Cys. Cysteine 181-184 acetylcholinesterase (Cartwright blood group) Homo sapiens 8-12 22280344-5 2012 This review summarizes the literature data that support the hypothesis that an insect-specific cysteine residue located at the opening of the acetylcholinesterase active site is a promising target site for developing new insecticides with reduced off-target toxicity and low propensity for insect resistance. Cysteine 95-103 acetylcholinesterase (Cartwright blood group) Homo sapiens 142-162 20109441-3 2010 We previously reported a free cysteine (Cys) residue at the entrance to the AChE active site in some insects but not higher vertebrates. Cysteine 30-38 acetylcholinesterase (Cartwright blood group) Homo sapiens 76-80 20109441-3 2010 We previously reported a free cysteine (Cys) residue at the entrance to the AChE active site in some insects but not higher vertebrates. Cysteine 40-43 acetylcholinesterase (Cartwright blood group) Homo sapiens 76-80 20109441-4 2010 We also reported Cys-targeting methanethiosulfonate molecules (AMTSn), which, under conditions that spared human AChE, caused total irreversible inhibition of aphid AChE, 95% inhibition of AChE from the malaria vector mosquito (Anopheles gambia), and >80% inhibition of activity from the yellow fever mosquito (Aedes aegypti) and northern house mosquito (Culex pipiens). Cysteine 17-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 113-117 20109441-4 2010 We also reported Cys-targeting methanethiosulfonate molecules (AMTSn), which, under conditions that spared human AChE, caused total irreversible inhibition of aphid AChE, 95% inhibition of AChE from the malaria vector mosquito (Anopheles gambia), and >80% inhibition of activity from the yellow fever mosquito (Aedes aegypti) and northern house mosquito (Culex pipiens). Cysteine 17-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 165-169 20109441-4 2010 We also reported Cys-targeting methanethiosulfonate molecules (AMTSn), which, under conditions that spared human AChE, caused total irreversible inhibition of aphid AChE, 95% inhibition of AChE from the malaria vector mosquito (Anopheles gambia), and >80% inhibition of activity from the yellow fever mosquito (Aedes aegypti) and northern house mosquito (Culex pipiens). Cysteine 17-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 165-169