PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22425525-2 2012 CPO is also responsible for the acetylcholinesterase (AChE) inhibition associated with CPF exposures; CPF is converted by liver CYP450 enzymes to CPO, which binds to and inhibits AChE and other serine active-site esterases, lipases and proteases. Serine 194-200 acetylcholinesterase Mus musculus 54-58 22425525-2 2012 CPO is also responsible for the acetylcholinesterase (AChE) inhibition associated with CPF exposures; CPF is converted by liver CYP450 enzymes to CPO, which binds to and inhibits AChE and other serine active-site esterases, lipases and proteases. Serine 194-200 acetylcholinesterase Mus musculus 32-52 19732756-1 2010 Organophosphorus insecticides and nerve agents inhibit the vital enzyme acetylcholinesterase by covalently bonding to the catalytic serine residue of the enzyme. Serine 132-138 acetylcholinesterase Mus musculus 72-92 20408548-1 2010 Tabun is a warfare agent that inhibits human acetylcholinesterase (hAChE) by rapid phosphylation of the catalytic serine. Serine 114-120 acetylcholinesterase Mus musculus 45-65 18215127-8 2008 Docking showed the major component of the interaction site on AChE to be the acidic sequence Arg(90)-Glu-Leu-Ser-Glu-Asp(95) on the omega loop, and also the involvement of Pro(40)-Pro-Val(42), Arg(46) (linked to Glu(94) by a salt bridge) and the hexapeptide Asp(61)-Ala-Thr-Thr-Phe-Gln(66). Serine 109-112 acetylcholinesterase Mus musculus 62-66 16388582-1 2006 Organophosphorus compounds (OPs) interfere with the catalytic mechanism of acetylcholinesterase (AChE) by rapidly phosphorylating the catalytic serine residue. Serine 144-150 acetylcholinesterase Mus musculus 75-95 16388582-1 2006 Organophosphorus compounds (OPs) interfere with the catalytic mechanism of acetylcholinesterase (AChE) by rapidly phosphorylating the catalytic serine residue. Serine 144-150 acetylcholinesterase Mus musculus 97-101 17192653-1 2006 The progressive inhibition of acetylcholinesterase (AChE [EC 3.1.1.7]) by organophosphates (OPs), such as the nerve agents tabun and soman, is due to phosphorylation of the active center serine characterized by the formation of conjugates and inactivation of this essential enzyme involved in neurotransmission. Serine 187-193 acetylcholinesterase Mus musculus 30-50 17192653-1 2006 The progressive inhibition of acetylcholinesterase (AChE [EC 3.1.1.7]) by organophosphates (OPs), such as the nerve agents tabun and soman, is due to phosphorylation of the active center serine characterized by the formation of conjugates and inactivation of this essential enzyme involved in neurotransmission. Serine 187-193 acetylcholinesterase Mus musculus 52-56 26494532-5 2015 The SMD simulations showed that the active pyridinium ring of K048 is directed towards the phosphorus atom conjugated to the active serine (SUN203) of tabun-mAChE(wild-type). Serine 132-138 acetylcholinesterase Mus musculus 157-162 9271331-5 1997 Substitution of glutamine for glutamate (E199) located at the amino-terminal to the active-site serine (S200) in Torpedo AChE generated an enzyme largely resistant to aging. Serine 96-102 acetylcholinesterase Mus musculus 121-125 8530502-7 1995 The time course analysis reveals that the increase in serine/threonine activity precedes the effect of T3 on AChE mRNAs. Serine 54-60 acetylcholinesterase Mus musculus 109-113 31226285-7 2019 Whereas benzenesulfonyl fluoride closely approaches the active-site serine in both mouse and Torpedo acetylcholinesterase in such simulations, phenylmethylsulfonyl fluoride is able to approach the active-site serine of mouse acetylcholinesterase, but remains trapped above the bottleneck in the Torpedo enzyme. Serine 68-74 acetylcholinesterase Mus musculus 101-121 12933813-1 2003 Two types of polyclonal antibodies were generated from (a) a decapeptide sequence that includes the active site serine of acetylcholinesterase (anti-AChE10S) and (b) the identical decapeptide sequence phosphorylated at the active site serine of acetylcholinesterase (anti-AChE10SP). Serine 112-118 acetylcholinesterase Mus musculus 122-142 12974645-3 2003 The tryptic peptide of mAChE that contains the active center serine residue resolves to a molecular mass of 4331.0 Da. Serine 61-67 acetylcholinesterase Mus musculus 23-28 12974645-5 2003 The relative abundance of AChE peptides containing a modified active center serine strongly correlates with the fractional inhibition of the enzyme, achieving a detection range of phosphorylated to nonphosphorylated enzyme of 5-95%. Serine 76-82 acetylcholinesterase Mus musculus 26-30 12974645-8 2003 Further, the tryptic peptide containing the active center serine of AChE, isolated from mouse brain by anion-exchange and affinity chromatography, has been monitored by mass spectrometry. Serine 58-64 acetylcholinesterase Mus musculus 68-72 10898598-7 2000 Most importantly, POCl(3)-induced electric eel AChE inhibition prevents postlabeling with [(3)H]diisopropyl phosphorofluoridate; i.e., both compounds phosphorylate at Ser-200 in the catalytic triad. Serine 167-170 acetylcholinesterase Mus musculus 47-51 26494532-9 2015 Such displacement is causing the inaccessibility of the drug towards the phosphorus atom conjugated to the active serine (SUN203) of tabun-mutant mAChE(Y337A). Serine 114-120 acetylcholinesterase Mus musculus 146-151 26494532-10 2015 Furthermore, the unbinding of the K048 with SMD studies showed that the active pyridinium ring of the drug undergoes a complete turn along the gorge axis and is directed away from the phosphorus atom conjugated to the active serine of the tabun-mutant mAChE(Y337A). Serine 225-231 acetylcholinesterase Mus musculus 252-257