Andrew P, Feng W, Calsbeek J, Antrobus S, Cherednychenko G, MacMahon J
Toxics. 2024; 12(4).
PMID: 38668486
PMC: 11054284.
DOI: 10.3390/toxics12040263.
Hrabinova M, Pejchal J, Hepnarova V, Muckova L, Junova L, Opravil J
Arch Toxicol. 2024; 98(4):1135-1149.
PMID: 38446233
PMC: 10944400.
DOI: 10.1007/s00204-024-03689-3.
Thompson C, Gerdes J, VanBrocklin H
Neurobiol Dis. 2019; 133:104455.
PMID: 31022458
PMC: 6810781.
DOI: 10.1016/j.nbd.2019.04.011.
Bester S, Adipietro K, Funk V, Myslinski J, Keul N, Cheung J
Protein Sci. 2019; 28(6):1106-1114.
PMID: 30993792
PMC: 6856767.
DOI: 10.1002/pro.3625.
Ramsay R, Tipton K
Molecules. 2017; 22(7).
PMID: 28714881
PMC: 6152246.
DOI: 10.3390/molecules22071192.
Novel Organophosphate Ligand O-(2-Fluoroethyl)-O-(p-Nitrophenyl)Methylphosphonate: Synthesis, Hydrolytic Stability and Analysis of the Inhibition and Reactivation of Cholinesterases.
Chao C, Ahmed S, Gerdes J, Thompson C
Chem Res Toxicol. 2016; 29(11):1810-1817.
PMID: 27551891
PMC: 5575788.
DOI: 10.1021/acs.chemrestox.6b00160.
Functional and structural characterization of a thermostable acetyl esterase from Thermotoga maritima.
Levisson M, Han G, Deller M, Xu Q, Biely P, Hendriks S
Proteins. 2012; 80(6):1545-59.
PMID: 22411095
PMC: 3348966.
DOI: 10.1002/prot.24041.
Entropy and Free Energy of a Mobile Loop Based on the Crystal Structures of the Free and Bound Proteins.
Mihailescu M, Meirovitch H
Entropy (Basel). 2011; 12(8):1946-1974.
PMID: 21448250
PMC: 3064000.
DOI: 10.3390/e12081946.
A new 3D mass diffusion-reaction model in the neuromuscular junction.
Khaliq A, Jenkins F, DeCoster M, Dai W
J Comput Neurosci. 2010; 30(3):729-45.
PMID: 21063761
DOI: 10.1007/s10827-010-0289-5.
Human carboxylesterase 1 stereoselectively binds the nerve agent cyclosarin and spontaneously hydrolyzes the nerve agent sarin.
Hemmert A, Otto T, Wierdl M, Edwards C, Fleming C, MacDonald M
Mol Pharmacol. 2010; 77(4):508-16.
PMID: 20051531
PMC: 2845941.
DOI: 10.1124/mol.109.062356.
Absolute free energy and entropy of a mobile loop of the enzyme acetylcholinesterase.
Mihailescu M, Meirovitch H
J Phys Chem B. 2009; 113(22):7950-64.
PMID: 19435302
PMC: 2747743.
DOI: 10.1021/jp900308y.
Irreversible inhibition of the thermophilic esterase EST2 from Alicyclobacillus acidocaldarius.
Febbraio F, DAndrea S, Mandrich L, Merone L, Rossi M, Nucci R
Extremophiles. 2008; 12(5):719-28.
PMID: 18622571
DOI: 10.1007/s00792-008-0179-1.
Inactivation of acetylcholinesterase by 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine hydrochloride.
Zang L, Misra H
Mol Cell Biochem. 2003; 254(1-2):131-6.
PMID: 14674691
DOI: 10.1023/a:1027376303043.
Acetylcholinesterase inhibition by 1-methyl-4-phenylpyridinium ion, a bioactivated metabolite of MPTP.
Zang L, Misra H
Mol Cell Biochem. 1993; 126(2):93-100.
PMID: 8302294
DOI: 10.1007/BF00925686.
Kinetic study of an enzyme-catalysed reaction in the presence of novel irreversible-type inhibitors that react with the product of enzymatic catalysis.
Valero E, Varon R, Garcia-Carmona F
Bull Math Biol. 1995; 57(1):157-68.
PMID: 7833851
DOI: 10.1007/BF02458321.
Analysis of kinetic data for irreversible enzyme inhibition.
Gray P, Duggleby R
Biochem J. 1989; 257(2):419-24.
PMID: 2930459
PMC: 1135596.
DOI: 10.1042/bj2570419.
The effects of systematic errors on the analysis of irreversible enzyme inhibition progress curves.
Gray P
Biochem J. 1991; 274 ( Pt 1):181-5.
PMID: 2001230
PMC: 1149936.
DOI: 10.1042/bj2740181.