PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 3566286-1 1987 The aim of the work was to elucidate the role of water in the reaction between acetylcholinesterase (acetylcholine hydrolase, EC 3.1.1.7) and methanesulfonyl fluoride, accelerated by accelerators. Water 49-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 79-99 3566286-6 1987 These findings, together with others, led to the following model of the role of hydration water in acylation of acetylcholinesterase. Water 90-95 acetylcholinesterase (Cartwright blood group) Homo sapiens 112-132 1029908-1 1976 Water, saline and ethanol extracts of Eugenia caryophyllus inhibited brain acetylcholinesterase (AchE) activity. Water 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-95 4005268-6 1985 The beta-sheet content is slightly higher for 5.6 S than 11 S acetylcholinesterase in water. Water 86-91 acetylcholinesterase (Cartwright blood group) Homo sapiens 62-82 3867447-0 1985 [Acetylcholinesterase activity in the mixed saliva of subjects living in areas of differing fluoride content in the drinking water]. Water 125-130 acetylcholinesterase (Cartwright blood group) Homo sapiens 1-21 1029908-1 1976 Water, saline and ethanol extracts of Eugenia caryophyllus inhibited brain acetylcholinesterase (AchE) activity. Water 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 97-101 32739347-1 2020 A reversible fluorescence probe for acetylcholinesterase activity detection was developed based on water soluble perylene derivative, N,N"-di(2-aspartic acid)-perylene-3,4,9,10-tetracarboxylic diimide (PASP). Water 99-104 acetylcholinesterase (Cartwright blood group) Homo sapiens 36-56 6070259-0 1967 Acetylcholinesterase inhibition by micropollutants in drinking water. Water 63-68 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 31360962-0 2019 Molecular recognition of organophosphorus compounds in water and inhibition of their toxicity to acetylcholinesterase. Water 55-60 acetylcholinesterase (Cartwright blood group) Homo sapiens 97-117 32731540-6 2020 Overall, the most active extracts in inhibiting both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes were ethanol/water and ethanol extracts from seeds (between 31.11 and 53.90%). Water 135-140 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-73 32731540-6 2020 Overall, the most active extracts in inhibiting both acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes were ethanol/water and ethanol extracts from seeds (between 31.11 and 53.90%). Water 135-140 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-79 32053129-5 2020 Under the catalysis of acetylcholinesterase (AChE) and choline oxidase (CHO), H2O2 was produced by using acetylcholine chloride (ACh) as a substrate, which was sensitive to the proposed CL system. Water 78-82 acetylcholinesterase (Cartwright blood group) Homo sapiens 23-43 32053129-5 2020 Under the catalysis of acetylcholinesterase (AChE) and choline oxidase (CHO), H2O2 was produced by using acetylcholine chloride (ACh) as a substrate, which was sensitive to the proposed CL system. Water 78-82 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-49 32540077-0 2020 Identification of acetylcholinesterase inhibitors in water by combining two-dimensional thin-layer chromatography and high-resolution mass spectrometry. Water 53-58 acetylcholinesterase (Cartwright blood group) Homo sapiens 18-38 32765630-8 2020 Results: The acetylcholinesterase inhibitory activity from Q. suber cork and corkback ethanol-water extracts was as follows: 62% inhibition with corkback extracts over 0.5 mg/mL and around 49% inhibition in cork extracts over 1.0 mg/mL extracts" concentration. Water 94-99 acetylcholinesterase (Cartwright blood group) Homo sapiens 13-33 30529825-2 2019 The water extracts had the highest antioxidant activity, especially those from roots and flowers, and were further appraised for in vitro inhibition of enzymes implicated on the onset of human ailments, namely acetyl- (AChE) and butyrylcholinesterase (BuChE) for Alzheimer"s disease, alpha-glucosidase and alpha-amylase for diabetes, and tyrosinase for skin hyperpigmentation disorders. Water 4-9 acetylcholinesterase (Cartwright blood group) Homo sapiens 219-223 31173012-8 2019 The WTMtD simulations further reveal that the bridged water molecules are more ordered near the catalytic triad of AChE to deter the nucleophilicity of Ser203 through intermolecular hydrogen bonding when donepezil approaches near to the active site gorge of AChE. Water 54-59 acetylcholinesterase (Cartwright blood group) Homo sapiens 115-119 31173012-8 2019 The WTMtD simulations further reveal that the bridged water molecules are more ordered near the catalytic triad of AChE to deter the nucleophilicity of Ser203 through intermolecular hydrogen bonding when donepezil approaches near to the active site gorge of AChE. Water 54-59 acetylcholinesterase (Cartwright blood group) Homo sapiens 258-262 29773682-0 2018 Water structure changes in oxime-mediated reactivation process of phosphorylated human acetylcholinesterase. Water 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 87-107 29773682-2 2018 To investigate oximate water structure changes in this reaction, reactivation of paraoxon-inhibited human acetylcholinesterase (AChE) was performed by the oxime asoxime (HI-6) at different pH in the presence and absence of lyotropic salts: a neutral salt (NaCl), a strong chaotropic salt (LiSCN) and strong kosmotropic salts (ammonium sulphate and phosphate HPO42-). Water 23-28 acetylcholinesterase (Cartwright blood group) Homo sapiens 106-126 29773682-2 2018 To investigate oximate water structure changes in this reaction, reactivation of paraoxon-inhibited human acetylcholinesterase (AChE) was performed by the oxime asoxime (HI-6) at different pH in the presence and absence of lyotropic salts: a neutral salt (NaCl), a strong chaotropic salt (LiSCN) and strong kosmotropic salts (ammonium sulphate and phosphate HPO42-). Water 23-28 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 29977295-0 2018 Fabrication of AChE/SnO2-cMWCNTs/Cu Nanocomposite-Based Sensor Electrode for Detection of Methyl Parathion in Water. Water 110-115 acetylcholinesterase (Cartwright blood group) Homo sapiens 15-19 29977295-1 2018 The work highlights inhibition-based Acetylcholinesterase (AChE) fabrication using composite nanomaterial comprising tin oxide nanoparticles (SnO2) and carboxylated multiwalled carbon nanotubes (cMWCNTs) for detection of pesticide methyl parathion (MP) in water samples. Water 256-261 acetylcholinesterase (Cartwright blood group) Homo sapiens 37-57 29977295-1 2018 The work highlights inhibition-based Acetylcholinesterase (AChE) fabrication using composite nanomaterial comprising tin oxide nanoparticles (SnO2) and carboxylated multiwalled carbon nanotubes (cMWCNTs) for detection of pesticide methyl parathion (MP) in water samples. Water 256-261 acetylcholinesterase (Cartwright blood group) Homo sapiens 59-63 29977295-2 2018 Working electrode AChE/SnO2-cMWCNTs/Cu exhibited high sensitivity with a linearity range of 1.0 muM to 160 muM and a minimum detection limit of 0.1 muM for MP in water. Water 162-167 acetylcholinesterase (Cartwright blood group) Homo sapiens 18-22 29272792-8 2018 Molecular dynamic simulation (GROMACS 4.5.5) of hAChE-PEP complex for 4 x 104 pico-second with SPC16 water system at 310 K temperature explained the evident role of Trp86 in stabilizing the ligand at P-site of the enzyme. Water 101-106 acetylcholinesterase (Cartwright blood group) Homo sapiens 48-53 29553731-0 2018 Dynamic Mechanism of a Fluorinated Oxime Reactivator Unbinding from AChE Gorge in Polarizable Water. Water 94-99 acetylcholinesterase (Cartwright blood group) Homo sapiens 68-72 27347731-0 2016 Exploring Basic Tail Modifications of Coumarin-Based Dual Acetylcholinesterase-Monoamine Oxidase B Inhibitors: Identification of Water-Soluble, Brain-Permeant Neuroprotective Multitarget Agents. Water 129-134 acetylcholinesterase (Cartwright blood group) Homo sapiens 58-78 28406297-7 2017 This behavior can be accounted for by the special features of AChE, such as the presence of several subsites of different natures in the gorge or the existence of several water molecules that act as bridges in the electrostatic interactions. Water 171-176 acetylcholinesterase (Cartwright blood group) Homo sapiens 62-66 28165084-0 2017 Unbinding of fluorinated oxime drug from the AChE gorge in polarizable water: a well-tempered metadynamics study. Water 71-76 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-49 28165084-3 2017 We systematically studied the unbinding of fluorinated obidoxime (FOBI) and non-fluorinated obidoxime (OBI) from the active site gorge of the serine hydrolase AChE in mean field polarizable water by employing all atom molecular dynamics simulations. Water 190-195 acetylcholinesterase (Cartwright blood group) Homo sapiens 159-163 27611473-9 2017 The small molecules regulated dual-functional platform based on UCNPs/AuNPs is a simple, label-free method and can be applied for the turn-on fluorescence detection of AChE activity in human serum and Cd2+ in real water samples. Water 214-219 acetylcholinesterase (Cartwright blood group) Homo sapiens 168-172 29842826-3 2018 It was speculated that higher electronic cloud density and lower water solubility of beta-CD than alpha-CD and RAMEB might favor to combination between acetylcholinesterase (AChE) and isomalathion included by beta-CD. Water 65-70 acetylcholinesterase (Cartwright blood group) Homo sapiens 152-172 29842826-3 2018 It was speculated that higher electronic cloud density and lower water solubility of beta-CD than alpha-CD and RAMEB might favor to combination between acetylcholinesterase (AChE) and isomalathion included by beta-CD. Water 65-70 acetylcholinesterase (Cartwright blood group) Homo sapiens 174-178 27109895-0 2016 Dynamics of human acetylcholinesterase bound to non-covalent and covalent inhibitors shedding light on changes to the water network structure. Water 118-123 acetylcholinesterase (Cartwright blood group) Homo sapiens 18-38 25096900-0 2014 In vitro effect of H2O 2, some transition metals and hydroxyl radical produced via fenton and fenton-like reactions, on the catalytic activity of AChE and the hydrolysis of ACh. Water 19-22 acetylcholinesterase (Cartwright blood group) Homo sapiens 146-150 26468911-0 2015 Protein-Drug Interactions with Effective Polarization in Polarizable Water: Oxime Unbinding from AChE Gorge. Water 69-74 acetylcholinesterase (Cartwright blood group) Homo sapiens 97-101 26468911-2 2015 We present oxime (HI-6) unbinding from the active site gorge of AChE, known to be strongly influenced by intermolecular cation-pi, hydrogen bridge (HB) and water bridge (WB) interactions and by molecular simulations with effective polarization in polarizable mean-field model of TIP3P water. Water 156-161 acetylcholinesterase (Cartwright blood group) Homo sapiens 64-68 26468911-2 2015 We present oxime (HI-6) unbinding from the active site gorge of AChE, known to be strongly influenced by intermolecular cation-pi, hydrogen bridge (HB) and water bridge (WB) interactions and by molecular simulations with effective polarization in polarizable mean-field model of TIP3P water. Water 285-290 acetylcholinesterase (Cartwright blood group) Homo sapiens 64-68 22972560-1 2012 A quantitative analysis of the interaction sites of the anti-Alzheimer drug galanthamine with molecular probes (water and benzene molecules) representative of its surroundings in the binding site of acetylcholinesterase (AChE) has been realized through pairwise potentials calculations and quantum chemistry. Water 112-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 199-219 24479585-2 2014 We present here a comparison of the reorientation dynamics of individual water molecules within the hydration shell of a series of globular proteins: acetylcholinesterase, subtilisin Carlsberg, lysozyme, and ubiquitin. Water 73-78 acetylcholinesterase (Cartwright blood group) Homo sapiens 150-170 24020636-0 2013 Analysis of the activation of acetylcholinesterase by carbon nanoparticles using a monolithic immobilized enzyme microreactor: role of the water molecules in the active site gorge. Water 139-144 acetylcholinesterase (Cartwright blood group) Homo sapiens 30-50 23262302-6 2013 Molecular docking revealed that two "water bridges" located at the two wings of Bis-Mep stabilized its interaction with both catalytic and peripheral anionic sites of AChE. Water 37-42 acetylcholinesterase (Cartwright blood group) Homo sapiens 167-171 23863115-2 2013 The MD simulation was performed on AChE to obtain enzyme conformation in a water environment. Water 75-80 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-39 22972560-1 2012 A quantitative analysis of the interaction sites of the anti-Alzheimer drug galanthamine with molecular probes (water and benzene molecules) representative of its surroundings in the binding site of acetylcholinesterase (AChE) has been realized through pairwise potentials calculations and quantum chemistry. Water 112-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 221-225 22972560-10 2012 In particular, the positions of several water molecules appearing as strongly conserved in galanthamine-AChE co-crystals are predicted by the calculations. Water 40-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 104-108 22419270-7 2012 The suppressive effect of "Sunrouge" water extract on AChE activity in human neuroblastoma SK-N-SH cells was the strongest among the three tea cultivars ("Sunrouge", "Yabukita" and "Benifuuki"). Water 37-42 acetylcholinesterase (Cartwright blood group) Homo sapiens 54-58 22732728-12 2012 The methanolic and water extracts of the same plant exhibited high inhibitory effects towards AChE with IC(50) values of 0.22 and 0.26mg/ml, respectively. Water 19-24 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 21438627-0 2011 Colorimetric assays for acetylcholinesterase activity and inhibitor screening based on the disassembly-assembly of a water-soluble polythiophene derivative. Water 117-122 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-44 21916483-0 2011 Novel water-soluble red-emitting poly(p-phenylenevinylene) derivative: synthesis, characterization, and fluorescent acetylcholinesterase assays. Water 6-11 acetylcholinesterase (Cartwright blood group) Homo sapiens 116-136 21682268-2 2011 In this study we compared the active sites of monomers and tetramers of human BChE and human AChE after performing molecular dynamics (MD) simulations in water-solvated systems. Water 154-159 acetylcholinesterase (Cartwright blood group) Homo sapiens 93-97 21838142-3 2011 Results show harmine in form of base and salt in water and in mixture of DMSO and water has the hightest inhibition activity on ACHE using eserine as reference substance. Water 49-54 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 21838142-3 2011 Results show harmine in form of base and salt in water and in mixture of DMSO and water has the hightest inhibition activity on ACHE using eserine as reference substance. Water 82-87 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 19650071-9 2010 Subsequently, HSMD was applied to mobile loops of the enzymes porcine pancreatic alpha-amylase and acetylcholinesterase in explicit water, where the difference in F between the bound and free states of the loop was calculated. Water 132-137 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-119 12706567-1 2003 The optical biosensor consisting of GST and acetylcholinesterase (AChE)-immobilized gel film was developed to detect captan and organophosphorus compounds simultaneously in contaminated water. Water 186-191 acetylcholinesterase (Cartwright blood group) Homo sapiens 44-64 18508040-17 2008 According to the putative water-activation mechanism of G117H BChE, a new histidine/aspartate dyad was introduced into the active center of human AChE at the optimum location for hydrolysis of the OP adduct. Water 26-31 acetylcholinesterase (Cartwright blood group) Homo sapiens 146-150 15994894-0 2005 Influence of the water structure on the acetylcholinesterase efficiency. Water 17-22 acetylcholinesterase (Cartwright blood group) Homo sapiens 40-60 15994894-1 2005 We have studied the catalytic efficiency of acetylcholinesterase (AChE) in various solutions with ion-disturbed water structure to explore the role that the water structure plays in the substrate-enzyme encounter. Water 112-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 44-64 15994894-1 2005 We have studied the catalytic efficiency of acetylcholinesterase (AChE) in various solutions with ion-disturbed water structure to explore the role that the water structure plays in the substrate-enzyme encounter. Water 112-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 66-70 15994894-1 2005 We have studied the catalytic efficiency of acetylcholinesterase (AChE) in various solutions with ion-disturbed water structure to explore the role that the water structure plays in the substrate-enzyme encounter. Water 157-162 acetylcholinesterase (Cartwright blood group) Homo sapiens 44-64 15994894-1 2005 We have studied the catalytic efficiency of acetylcholinesterase (AChE) in various solutions with ion-disturbed water structure to explore the role that the water structure plays in the substrate-enzyme encounter. Water 157-162 acetylcholinesterase (Cartwright blood group) Homo sapiens 66-70 15994894-3 2005 The influence of water structure on the degree of solvation and on the intramolecular mobility of AChE was investigated for different aqueous ionic solutions by small-angle x-ray scattering technique and depolarization fluorescence spectroscopy. Water 17-22 acetylcholinesterase (Cartwright blood group) Homo sapiens 98-102 15994894-4 2005 It was found that the encounter process between AChE and acetylthiocholine was promoted in solutions with less structured water. Water 122-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 48-52 15994894-6 2005 The found experimental results suggest that the water structure may influence the substrate-enzyme encounter process by diminishing the AChE solvation shell and may help diffusion of the substrate through the gorge by enhancing the intramolecular mobility of AChE. Water 48-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 136-140 15994894-6 2005 The found experimental results suggest that the water structure may influence the substrate-enzyme encounter process by diminishing the AChE solvation shell and may help diffusion of the substrate through the gorge by enhancing the intramolecular mobility of AChE. Water 48-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 259-263 17508773-3 2007 We have focused in this work on the usage of computer-aided molecular design by virtual screening, molecular dynamics with implicit and explicit water solvation, density functional, molecular interaction field studies, docking procedures, ADMET predictions in order to propose novel potential AChE inhibitor for the treatment of Alzheimer"s disease. Water 145-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 293-297 12706567-1 2003 The optical biosensor consisting of GST and acetylcholinesterase (AChE)-immobilized gel film was developed to detect captan and organophosphorus compounds simultaneously in contaminated water. Water 186-191 acetylcholinesterase (Cartwright blood group) Homo sapiens 66-70 2048762-9 1991 In humans, exposure to the acetylcholinesterase inhibitor, Aldicarb, was received through contaminated well water. Water 108-113 acetylcholinesterase (Cartwright blood group) Homo sapiens 27-47 12373455-1 2002 The well-documented efficacy of HI 6 dichloride in reactivating acetylcholinesterase (AChE) inhibited by nerve agents is curtailed by its poor water-solubility at temperatures below 10 degrees C. This drawback can be circumvented by using HI 6 dimethanesulfonate, which has been developed in our laboratory. Water 143-148 acetylcholinesterase (Cartwright blood group) Homo sapiens 86-90 11964254-0 2002 Properties of water molecules in the active site gorge of acetylcholinesterase from computer simulation. Water 14-19 acetylcholinesterase (Cartwright blood group) Homo sapiens 58-78 11964254-1 2002 A 10-ns trajectory from a molecular dynamics simulation is used to examine the structure and dynamics of water in the active site gorge of acetylcholinesterase to determine what influence water may have on its function. Water 105-110 acetylcholinesterase (Cartwright blood group) Homo sapiens 139-159 11964254-1 2002 A 10-ns trajectory from a molecular dynamics simulation is used to examine the structure and dynamics of water in the active site gorge of acetylcholinesterase to determine what influence water may have on its function. Water 188-193 acetylcholinesterase (Cartwright blood group) Homo sapiens 139-159 18968616-1 2002 A screen-printed biosensor for the detection of pesticides in water miscible organic solvents is described based on the use of p-aminophenyl acetate as acetylcholinesterase substrate. Water 62-67 acetylcholinesterase (Cartwright blood group) Homo sapiens 152-172 8122110-3 1994 A molecular dynamics simulation of acetylcholinesterase in water reveals the transient opening of a short channel, large enough to pass a water molecule, through a thin wall of the active site near tryptophan-84. Water 59-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-55 8122110-3 1994 A molecular dynamics simulation of acetylcholinesterase in water reveals the transient opening of a short channel, large enough to pass a water molecule, through a thin wall of the active site near tryptophan-84. Water 138-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-55 1447418-3 1992 The comparative study of the inhibitory action of water-soluble derivatives of hindered phenols and fatty-soluble ionol made it possible to reveal possible contributions to the inhibition of both direct and mediated (by the membrane microsurroundings) effects on the membrane-bound AChE by the studied synthetic bioantioxidants. Water 50-55 acetylcholinesterase (Cartwright blood group) Homo sapiens 282-286 12192064-0 2002 Structural and dynamic properties of water around acetylcholinesterase. Water 37-42 acetylcholinesterase (Cartwright blood group) Homo sapiens 50-70 12192064-1 2002 Structural and dynamic properties of water molecules around acetylcholinesterase are examined from a 10-nsec molecular dynamics simulation to help understand how the protein alters water properties. Water 37-42 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-80 12192064-1 2002 Structural and dynamic properties of water molecules around acetylcholinesterase are examined from a 10-nsec molecular dynamics simulation to help understand how the protein alters water properties. Water 181-186 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-80 11679273-1 2001 The fiber-optic biosensor consisting of an acetylcholinesterase (AChE)-immobilized Langmuir-Blodgett (LB) film was developed to detect organophosphorus compounds in contaminated water. Water 178-183 acetylcholinesterase (Cartwright blood group) Homo sapiens 65-69 9367582-0 1997 Surface and Spectroscopic Properties of Acetylcholinesterase Monolayer at the Air/Water Interface The behavior of the enzyme acetylcholinesterase was studied at the air/water interface. Water 82-87 acetylcholinesterase (Cartwright blood group) Homo sapiens 40-60 9367582-0 1997 Surface and Spectroscopic Properties of Acetylcholinesterase Monolayer at the Air/Water Interface The behavior of the enzyme acetylcholinesterase was studied at the air/water interface. Water 169-174 acetylcholinesterase (Cartwright blood group) Homo sapiens 40-60 9367582-0 1997 Surface and Spectroscopic Properties of Acetylcholinesterase Monolayer at the Air/Water Interface The behavior of the enzyme acetylcholinesterase was studied at the air/water interface. Water 169-174 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-145 9367582-5 1997 The long-term stability of acetylcholinesterase at the air/water interface was demonstrated for pH 6.5 and a salt concentration of 10(-2) M (KCl). Water 59-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 27-47 34865979-1 2022 A colorimetric gold nanoparticles (AuNPs)-based acetylcholinesterase (AChE) assay was designed for the first time to measure the concentration of parathion-methyl (PM) in lake water samples. Water 176-181 acetylcholinesterase (Cartwright blood group) Homo sapiens 70-74 35424765-0 2022 Facile preparation of fluorescent water-soluble non-conjugated polymer dots and fabricating an acetylcholinesterase biosensor. Water 34-39 acetylcholinesterase (Cartwright blood group) Homo sapiens 95-115 34808511-8 2021 Water fluoride concentrations were positively associated with AChE and negatively associated with ChAT and ACh, trends were same for urinary fluoride except for ACh. Water 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 62-66 34808511-10 2021 The mediation proportion by AChE between water fluoride and either developing DF or IQ < 120 was 15.7%. Water 41-46 acetylcholinesterase (Cartwright blood group) Homo sapiens 28-32 35195417-4 2022 Compound 15 bearing a -CF2H motif emerged as a water-soluble, orally bioavailable CNS-permeant potent inhibitor of both human AChE (IC50 = 550 nM) and MAO B (IC50 = 8.2 nM, B/A selectivity > 1200). Water 47-52 acetylcholinesterase (Cartwright blood group) Homo sapiens 126-130 3337547-1 1988 Water-induced activation of acetylcholinesterase. Water 0-5 acetylcholinesterase (Cartwright blood group) Homo sapiens 28-48 3337547-5 1988 In AP and polycythemia rubra vera after water exposure a significantly increased AChE activity suggesting acetylcholine release was observed, whereas in the patient with cold urticaria and the controls, a significant decrease was noted. Water 40-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 81-85