PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 6639987-8 1983 During the interaction of the enanthiomers with the asymmetric phosphorus the stereospecificity of acetylcholinesterase is much higher than that of carboxylesterase. Phosphorus 63-73 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-119 11453739-7 2001 For methamidophos, we show that phosphylation of AChE involves elimination of the thiomethyl moiety and that the spontaneous reactivation of the resulting organophosphate adduct generates the phosphorus free AChE active site Ser-peptide. Phosphorus 192-202 acetylcholinesterase (Cartwright blood group) Homo sapiens 208-212 8718893-7 1996 Docking of Sp and Rp cycloheptyl methylphosphonyl thiocholines and thioethylates in AChE as models of the reversible complex and transition state using molecular dynamics affords structural insight into the spatial arrangement of the substituents surrounding phosphorus prior to and during reaction. Phosphorus 259-269 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-88 3954784-6 1986 From results with O-ethyl methylphosphonylated AChE prepared from two pairs of enantiomers as well as from the racemic fluoridate it was concluded that phosphonylation of AChE may not always occur via a mechanism involving inversion of configuration at phosphorus but can also occur with retention of configuration. Phosphorus 253-263 acetylcholinesterase (Cartwright blood group) Homo sapiens 171-175 2917983-7 1989 These studies reveal that chiral reactions with acetylcholinesterase are dependent more on the nature of the groups surrounding the tetrahedral phosphorus than on the absolute configuration about the phosphorus atom and indicate that the active center comprises partially overlapping subsites that can accommodate the -OR and -SR" groups. Phosphorus 144-154 acetylcholinesterase (Cartwright blood group) Homo sapiens 48-68 2917983-7 1989 These studies reveal that chiral reactions with acetylcholinesterase are dependent more on the nature of the groups surrounding the tetrahedral phosphorus than on the absolute configuration about the phosphorus atom and indicate that the active center comprises partially overlapping subsites that can accommodate the -OR and -SR" groups. Phosphorus 200-210 acetylcholinesterase (Cartwright blood group) Homo sapiens 48-68 30427781-13 2018 There were significant relationships between AChE activity with P and PTH. Phosphorus 64-65 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-49 33057486-0 2021 Light-accelerating oxidase-mimicking activity of black phosphorus quantum dots for colorimetric detection of acetylcholinesterase activity and inhibitor screening. Phosphorus 55-65 acetylcholinesterase (Cartwright blood group) Homo sapiens 109-129 33057486-1 2021 A feasible and sensitive colorimetric platform was established for the assay of acetylcholinesterase (AChE) activity and evaluation of its inhibitor screening, based upon the light-accelerating oxidase-mimicking activity of black phosphorus quantum dots (BP QDs). Phosphorus 230-240 acetylcholinesterase (Cartwright blood group) Homo sapiens 80-100 33057486-1 2021 A feasible and sensitive colorimetric platform was established for the assay of acetylcholinesterase (AChE) activity and evaluation of its inhibitor screening, based upon the light-accelerating oxidase-mimicking activity of black phosphorus quantum dots (BP QDs). Phosphorus 230-240 acetylcholinesterase (Cartwright blood group) Homo sapiens 102-106 31309898-8 2020 RESULTS: The results of the docking studies showed that the newly designed phosphorus and thiophosphorus tacrine analogs, theoretically possess AChE and BChE-binding ability. Phosphorus 75-85 acetylcholinesterase (Cartwright blood group) Homo sapiens 144-148 30230960-3 2019 Variability between organophosphorus insecticides-in lipophilicity, speed of activation, speed and potency of acetylcholinesterase inhibition, and in the chemical groups attached to the phosphorus-results in variable speed of poisoning onset, severity, clinical toxidrome, and case fatality. Phosphorus 26-36 acetylcholinesterase (Cartwright blood group) Homo sapiens 110-130 27062893-2 2016 2PAM reactivates nerve agent-inhibited AChE via direct nucleophilic attack by the oxime moiety on the phosphorus center of the bound nerve agent. Phosphorus 102-112 acetylcholinesterase (Cartwright blood group) Homo sapiens 39-43 23376121-6 2013 Our findings show that HI-6 binds to tabun inhibited Homo sapiens AChE (hAChE) with an IC50 value of 300muM and suggest that the reactive nucleophilic moiety of HI-6 is excluded from the phosphorus atom of tabun. Phosphorus 187-197 acetylcholinesterase (Cartwright blood group) Homo sapiens 66-70 27371941-2 2016 Catalytically inactive OP-AChE conjugates formed between the active-center serine and phosphorus of OPs can, in principle, be reactivated by nucleophilic oxime antidotes. Phosphorus 86-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 26-30 27371941-5 2016 We outline here the potential limitations of available AChE X-ray structures that preclude an accurate prediction of oxime structures, which are necessary for association in the OP-AChE gorge and nucleophilic attack of the OP-conjugated phosphorus. Phosphorus 237-247 acetylcholinesterase (Cartwright blood group) Homo sapiens 181-185 25743373-1 2016 The hydroxyl oxygen of the catalytic triad serine in the active center of serine hydrolase acetylcholinesterase (AChE) attacks organophosphorus compounds (OPs) at the phosphorus atom to displace the primary leaving group and to form a covalent bond. Phosphorus 133-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 91-111 25743373-1 2016 The hydroxyl oxygen of the catalytic triad serine in the active center of serine hydrolase acetylcholinesterase (AChE) attacks organophosphorus compounds (OPs) at the phosphorus atom to displace the primary leaving group and to form a covalent bond. Phosphorus 133-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 113-117 25743373-2 2016 Inhibited AChE can be reactivated by cleavage of the Ser-phosphorus bond either spontaneously or through a reaction with nucleophilic agents, such as oximes. Phosphorus 57-67 acetylcholinesterase (Cartwright blood group) Homo sapiens 10-14 23376121-6 2013 Our findings show that HI-6 binds to tabun inhibited Homo sapiens AChE (hAChE) with an IC50 value of 300muM and suggest that the reactive nucleophilic moiety of HI-6 is excluded from the phosphorus atom of tabun. Phosphorus 187-197 acetylcholinesterase (Cartwright blood group) Homo sapiens 72-77 16962227-9 2007 Final docked energies predicted correctly the relative order of the inhibition potency of compounds (except in the case of Py-4-CH(3)) as well as the most probable orientation of the best reactivator, Py-4-Br, which can result in an attack on the phosphorus atom of the tabun-phosphorylated human AChE. Phosphorus 247-257 acetylcholinesterase (Cartwright blood group) Homo sapiens 297-301 17298091-5 2007 Through the nucleophilic attack, the oximate first binds to the sarin-AChE adduct to form a relatively stable phosphorus complex. Phosphorus 110-120 acetylcholinesterase (Cartwright blood group) Homo sapiens 70-74