PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24184599-3 2014 On the basis of the effect of OPs on the ECL signal of AChE-QDs-GNs modified glassy carbon electrode (GCE), a highly sensitive GNs-anchored-QDs-based signal-on ECL biosensor was developed for sensing OPs, combined with the enzymatic reactions and the dissolved oxygen as coreactant. Oxygen 261-267 acetylcholinesterase (Cartwright blood group) Homo sapiens 55-59 1692236-5 1990 Among all the organophosphates tested, the combination of a methyl group and a negatively charged oxygen attached to the P atom, CH3P(O)(O-)-AChE, conferred the greatest protection to the active site of aged or nonaged organophosphoryl conjugates of acetylcholinesterase. Oxygen 98-104 acetylcholinesterase (Cartwright blood group) Homo sapiens 250-270 93746-8 1979 Illumination of eosin-labeled ghosts causes a rapid loss of acetylcholinesterase activity but this can be prevented by prior displacement of oxygen in the sample by argon. Oxygen 141-147 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-80 28192982-4 2017 With the occurrence of the enzymatic reactions induced by the acetylcholinesterase (AChE) and choline oxidase (ChOx), the cathodic ECL signal from RGO-CdTe QDs was at "signal off" state due to the consumption of dissolved O2. Oxygen 222-224 acetylcholinesterase (Cartwright blood group) Homo sapiens 62-82 28192982-4 2017 With the occurrence of the enzymatic reactions induced by the acetylcholinesterase (AChE) and choline oxidase (ChOx), the cathodic ECL signal from RGO-CdTe QDs was at "signal off" state due to the consumption of dissolved O2. Oxygen 222-224 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-88 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. Oxygen 13-19 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. Oxygen 13-19 acetylcholinesterase (Cartwright blood group) Homo sapiens 113-117 21787634-0 2010 Reactivation of VX-inhibited AChE by novel oximes having two oxygen atoms in the linker. Oxygen 61-67 acetylcholinesterase (Cartwright blood group) Homo sapiens 29-33 16022504-9 2005 Conformations of enzyme-inhibitor tetrahedral intermediates for butyrylcholinesterase were different from those for acetylcholinesterase and cholesterol esterase; ortho substituents in the tetrahedral intermediates were located far from the negatively charged carbonyl oxygens in butyrylcholinesterase, but close to the negatively charged carbonyl oxygens in acetylcholinesterase and cholesterol esterase. Oxygen 269-276 acetylcholinesterase (Cartwright blood group) Homo sapiens 116-136 17384975-5 2008 We conclude that the photoinactivation of ACE with sequential 2-gamma irradiation involves reactive oxygen species produced by the interaction of the upper excited T(n) state of CuPcS(4) with molecular oxygen. Oxygen 100-106 acetylcholinesterase (Cartwright blood group) Homo sapiens 42-45 17467020-1 2007 For many decades it has been thought that oxygen analogs (oxons) of organophosphorus insecticides phosphorylate the catalytic site of acetylcholinesterase by a mechanism that follows simple Michaelis-Menten kinetics. Oxygen 42-48 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-154 19764241-2 2009 Two AChE immobilization strategies are proposed based on the composite film with hydrophobic and hydrophilic surface tailored by oxygen plasma. Oxygen 129-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 4-8 16245689-4 2005 AChE is shown to hydrolyze only those substrates that form equilibrium conformers compatible in the mutual arrangement of trimethylammonium group, carbonyl carbon, and carbonyl oxygen with the tt conformation of ACh; in this case, the rate of substrate hydrolysis depends on the total population of these conformers. Oxygen 177-183 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 16022504-9 2005 Conformations of enzyme-inhibitor tetrahedral intermediates for butyrylcholinesterase were different from those for acetylcholinesterase and cholesterol esterase; ortho substituents in the tetrahedral intermediates were located far from the negatively charged carbonyl oxygens in butyrylcholinesterase, but close to the negatively charged carbonyl oxygens in acetylcholinesterase and cholesterol esterase. Oxygen 348-355 acetylcholinesterase (Cartwright blood group) Homo sapiens 116-136 11959475-1 2002 In this study, acetylcholinesterase and choline oxidase were co-immobilized on poly(2-hydroxyethyl methacrylate) membranes and the change in oxygen consumption upon aldicarb introduction was measured. Oxygen 141-147 acetylcholinesterase (Cartwright blood group) Homo sapiens 15-35 12197759-6 2002 Our calculations indicate that, in the AChE-ACh Michaelis complex, only two hydrogen bonds are formed between the carbonyl oxygen of ACh and the peptidic NH groups of Gly121 and Gly122. Oxygen 123-129 acetylcholinesterase (Cartwright blood group) Homo sapiens 39-43 8768334-1 1996 The data of long-standing research allowed to establish correlation between oxygen consumption different at various age and catecholamine (CA) content and acetylcholinesterase (AChE) activity in blood. Oxygen 76-82 acetylcholinesterase (Cartwright blood group) Homo sapiens 177-181 9871590-2 1998 It was revealed that the methyl group at the three carbon bridge of (-)-huperzine A can form a weak hydrogen bond with the phenol hydroxyl oxygen of Tyr121 and the main-chain oxygen of Gly118 of AChE, respectively. Oxygen 139-145 acetylcholinesterase (Cartwright blood group) Homo sapiens 195-199 9871590-2 1998 It was revealed that the methyl group at the three carbon bridge of (-)-huperzine A can form a weak hydrogen bond with the phenol hydroxyl oxygen of Tyr121 and the main-chain oxygen of Gly118 of AChE, respectively. Oxygen 175-181 acetylcholinesterase (Cartwright blood group) Homo sapiens 195-199 8893840-2 1996 A new mode of binding of ACh to AChE was found which involves the carboxyl oxygen of ACh interacting with Gly 118 and 119. Oxygen 75-81 acetylcholinesterase (Cartwright blood group) Homo sapiens 32-36 10471290-7 1999 This agrees with our observation, using spin traps, that mainly singlet oxygen is produced by the complex of hypericin with the molten globule of acetylcholinesterase. Oxygen 72-78 acetylcholinesterase (Cartwright blood group) Homo sapiens 146-166 8117296-6 1994 These data show that oxygen radical treatment converts acetylcholinesterase to a partially unfolded state, which retains most of its secondary structure but lacks substantial tertiary structure, thus resembling a "molten globule" state. Oxygen 21-27 acetylcholinesterase (Cartwright blood group) Homo sapiens 55-75