PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 26620258-0 2016 Involvement of acetylcholinesterase and protein kinase C in the protective effect of caffeine against beta-amyloid-induced alterations in red blood cells. Caffeine 85-93 acetylcholinesterase (Cartwright blood group) Homo sapiens 15-35 11453726-2 2001 Recent kinetic and mass spectral data demonstrated that a difference in mechanism of inactivation exists for AChE treated with (1R)- versus (1S,3S)-stereoisomers. Caffeine 140-146 acetylcholinesterase (Cartwright blood group) Homo sapiens 109-113 24475784-1 2014 Many previous works have demonstrated that acetylcholinesterase (AChE) was enantioselectively inhibited by chiral organophosphorus insecticides (OPs) and that a significant difference in reactivation existed for AChE inactivated by (1R)- versus (1S,3S)-stereoisomers of isomalathion. Caffeine 245-251 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-63 24475784-1 2014 Many previous works have demonstrated that acetylcholinesterase (AChE) was enantioselectively inhibited by chiral organophosphorus insecticides (OPs) and that a significant difference in reactivation existed for AChE inactivated by (1R)- versus (1S,3S)-stereoisomers of isomalathion. Caffeine 245-251 acetylcholinesterase (Cartwright blood group) Homo sapiens 65-69 24475784-1 2014 Many previous works have demonstrated that acetylcholinesterase (AChE) was enantioselectively inhibited by chiral organophosphorus insecticides (OPs) and that a significant difference in reactivation existed for AChE inactivated by (1R)- versus (1S,3S)-stereoisomers of isomalathion. Caffeine 245-251 acetylcholinesterase (Cartwright blood group) Homo sapiens 212-216 23791077-1 2013 The commonly used beverage and psychostimulant caffeine is known to inhibit human acetylcholinesterase enzyme. Caffeine 47-55 acetylcholinesterase (Cartwright blood group) Homo sapiens 82-102 23791077-9 2013 Molecular modeling investigations indicate that caffeine binds primarily in the catalytic site (Ser203, Glu334 and His447) region of hAChE whereas pentoxifylline and propentofylline are able to bind to both the catalytic site and peripheral anionic site due to their increased bulk/size, thereby exhibiting superior AChE inhibition relative to caffeine. Caffeine 48-56 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-138 23791077-9 2013 Molecular modeling investigations indicate that caffeine binds primarily in the catalytic site (Ser203, Glu334 and His447) region of hAChE whereas pentoxifylline and propentofylline are able to bind to both the catalytic site and peripheral anionic site due to their increased bulk/size, thereby exhibiting superior AChE inhibition relative to caffeine. Caffeine 344-352 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-138 23791077-11 2013 In summary, our study has important implications in the development of novel caffeine derivatives as selective AChE inhibitors with potential application as cognitive enhancers and to treat various forms of dementia. Caffeine 77-85 acetylcholinesterase (Cartwright blood group) Homo sapiens 111-115 23698772-0 2013 Caffeine inhibits acetylcholinesterase, but not butyrylcholinesterase. Caffeine 0-8 acetylcholinesterase (Cartwright blood group) Homo sapiens 18-38 23698772-5 2013 In the present work, we focused on the question whether caffeine can inhibit acetylcholinesterase (AChE) and/or, butyrylcholinesterase (BChE), the two enzymes participating in cholinergic neurotransmission. Caffeine 56-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 77-97 23698772-5 2013 In the present work, we focused on the question whether caffeine can inhibit acetylcholinesterase (AChE) and/or, butyrylcholinesterase (BChE), the two enzymes participating in cholinergic neurotransmission. Caffeine 56-64 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-103 23698772-6 2013 A standard Ellman test with human AChE and BChE was done for altering concentrations of caffeine. Caffeine 88-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 34-38 23698772-9 2013 In compliance with Dixon"s plot, caffeine was proved to be a non-competitive inhibitor of AChE and BChE. Caffeine 33-41 acetylcholinesterase (Cartwright blood group) Homo sapiens 90-94 23698772-13 2013 The proposed binding orientation of caffeine can interact with Trp86, and it can be stabilize by Tyr337 in comparison to the smaller Ala328 in the case of human BChE; thus, it can explain the lower binding affinity of caffeine for BChE with reference to AChE. Caffeine 36-44 acetylcholinesterase (Cartwright blood group) Homo sapiens 254-258 23698772-13 2013 The proposed binding orientation of caffeine can interact with Trp86, and it can be stabilize by Tyr337 in comparison to the smaller Ala328 in the case of human BChE; thus, it can explain the lower binding affinity of caffeine for BChE with reference to AChE. Caffeine 218-226 acetylcholinesterase (Cartwright blood group) Homo sapiens 254-258 11453726-13 2001 Furthermore, the results suggest that the mechanistic shift demonstrated to occur for inhibition of AChE by (1R)- versus (1S,3S)-isomers is conserved for butyrylcholinesterase and cholesterol esterase. Caffeine 121-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 100-104 11123973-0 2000 Inhibition of acetylcholinesterase by (1S,3S)-isomalathion proceeds with loss of thiomethyl: kinetic and mass spectral evidence for an unexpected primary leaving group. Caffeine 38-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 14-34 11123973-2 2000 This study sought to identify the adduct that renders AChE refractory toward reactivation after inhibition with the (1S, 3S)-stereoisomer. Caffeine 116-123 acetylcholinesterase (Cartwright blood group) Homo sapiens 54-58 2003276-0 1991 Inhibition of acetylcholinesterase by caffeine, anabasine, methyl pyrrolidine and their derivatives. Caffeine 38-46 acetylcholinesterase (Cartwright blood group) Homo sapiens 14-34 2003276-1 1991 The inhibition of acetylcholinesterase (AChE) by caffeine, anabasine, methylpyrrolidine and several derivatives was examined. Caffeine 49-57 acetylcholinesterase (Cartwright blood group) Homo sapiens 18-38 2003276-1 1991 The inhibition of acetylcholinesterase (AChE) by caffeine, anabasine, methylpyrrolidine and several derivatives was examined. Caffeine 49-57 acetylcholinesterase (Cartwright blood group) Homo sapiens 40-44 34969831-3 2022 Given that caffeine is a natural compound that behaves as an AChE inhibitor and as a partial agonist of nAChRs, the aim of this work was to synthetize more potent bifunctional caffeine analogs that modulate these two molecular targets. Caffeine 11-19 acetylcholinesterase (Cartwright blood group) Homo sapiens 61-65 34969831-3 2022 Given that caffeine is a natural compound that behaves as an AChE inhibitor and as a partial agonist of nAChRs, the aim of this work was to synthetize more potent bifunctional caffeine analogs that modulate these two molecular targets. Caffeine 176-184 acetylcholinesterase (Cartwright blood group) Homo sapiens 61-65 34969831-4 2022 To this end, a theophylline structure was connected to a pyrrolidine structure through a methylene chain of different lengths (3 to 7 carbon atoms) to give compounds 7-11 All caffeine derivatives inhibited the AChE, of which compound 11 showed the strongest effect. Caffeine 175-183 acetylcholinesterase (Cartwright blood group) Homo sapiens 210-214 34969831-9 2022 Thus, the new synthetized compounds can inhibit the AChE and activate muscle and alpha7 nAChRs with greater potency than caffeine, which suggests that they could be useful leaders for the development of new therapies for the treatment of different neurological diseases. Caffeine 121-129 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 34969831-10 2022 Significance Statement In this work we synthetized caffeine derivatives which can inhibit the AChE and activate both muscle and alpha7 nAChRs with higher potency than caffeine. Caffeine 51-59 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 34969831-10 2022 Significance Statement In this work we synthetized caffeine derivatives which can inhibit the AChE and activate both muscle and alpha7 nAChRs with higher potency than caffeine. Caffeine 167-175 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 30543170-5 2019 RESULTS: Based on in-silico AChE interaction studies, we predicted quercetin, caffeine, ascorbic acid and gallic acid to be potential AChE inhibitors. Caffeine 78-86 acetylcholinesterase (Cartwright blood group) Homo sapiens 28-32 30543170-5 2019 RESULTS: Based on in-silico AChE interaction studies, we predicted quercetin, caffeine, ascorbic acid and gallic acid to be potential AChE inhibitors. Caffeine 78-86 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-138