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Volumn 155, Issue 3, 2011, Pages 219-230

Cholinesterases, a target of pharmacology and toxicology

Author keywords

Acetylcholinesterase; Alzheimer's disease; Butyrylcholinesterase; Donepezil; Galantamine; Huperzine; Myasthenia gravis; Rivastigmine

Indexed keywords

ACETYLCHOLINESTERASE; CHEMICAL WARFARE AGENT; CHOLINESTERASE; CHOLINESTERASE INHIBITOR;

EID: 80054096801     PISSN: 12138118     EISSN: 18047521     Source Type: Journal    
DOI: 10.5507/bp.2011.036     Document Type: Article
Times cited : (315)

References (126)
  • 1
    • 10444252700 scopus 로고
    • Uberhumerole ubertragbarkeit der herznervenwirkung
    • Loewi O. Uberhumerole ubertragbarkeit der herznervenwirkung. I Mitteilung Pflugers Arch 1921;189:239-42.
    • (1921) I Mitteilung Pflugers Arch , vol.189 , pp. 239-242
    • Loewi, O.1
  • 2
    • 49449094458 scopus 로고    scopus 로고
    • Acetylcholine beyond neurons: The non-neuronal cholinergic system in humans
    • Wessler I, Kirkpatrick CJ. Acetylcholine beyond neurons: the non-neuronal cholinergic system in humans. Br J Pharmacol 2008;154:1558-71.
    • (2008) Br J Pharmacol , vol.154 , pp. 1558-1571
    • Wessler, I.1    Kirkpatrick, C.J.2
  • 3
    • 10044275708 scopus 로고    scopus 로고
    • Organophosphates/nerve agent poisoning: Mechanism of action, diagnosis, prophylaxis, and treatment
    • Bajgar J. Organophosphates/nerve agent poisoning: mechanism of action, diagnosis, prophylaxis, and treatment. Adv Clin Chem 2004;38:151-216.
    • (2004) Adv Clin Chem , vol.38 , pp. 151-216
    • Bajgar, J.1
  • 4
    • 33846969163 scopus 로고    scopus 로고
    • A medial health report on individuals with silent butyrylcholinesterase in Vysya community of India
    • Manoharan I, Boopathy R, DArvesh S, Lockridge O. A medial health report on individuals with silent butyrylcholinesterase in Vysya community of India. Clin Chim Acta 2007;378:128-35.
    • (2007) Clin Chim Acta , vol.378 , pp. 128-135
    • Manoharan, I.1    Boopathy, R.2    Darvesh, S.3    Lockridge, O.4
  • 5
    • 40849102715 scopus 로고    scopus 로고
    • The butyrylcholinesterase knockout mouse as a model for human butyrylcholinesterase deficiency
    • Li B, Duysen EG, Carlson M, Lockridge O. The butyrylcholinesterase knockout mouse as a model for human butyrylcholinesterase deficiency. J Pharmacol Exp Ther 2008;324:1146-54.
    • (2008) J Pharmacol Exp Ther , vol.324 , pp. 1146-1154
    • Li, B.1    Duysen, E.G.2    Carlson, M.3    Lockridge, O.4
  • 6
    • 67649322217 scopus 로고    scopus 로고
    • The butyrylcholinesterase knock-out mouse a research tool in the study of drug sensitivity, biodistribution, obesity and Alzheimer's disease
    • Duysen EG, Li B, Lockridge O. The butyrylcholinesterase knock-out mouse a research tool in the study of drug sensitivity, biodistribution, obesity and Alzheimer's disease. Expert Opin Drug Metab Toxicol 2009;5:523-8.
    • (2009) Expert Opin Drug Metab Toxicol , vol.5 , pp. 523-528
    • Duysen, E.G.1    Li, B.2    Lockridge, O.3
  • 7
    • 0041866793 scopus 로고    scopus 로고
    • Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population
    • Yen T, Nightingale BN, Burns JC, Sullivan DR, Stewart PM. Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population. Clin Chem 2003;49:1297-1308.
    • (2003) Clin Chem , vol.49 , pp. 1297-1308
    • Yen, T.1    Nightingale, B.N.2    Burns, J.C.3    Sullivan, D.R.4    Stewart, P.M.5
  • 8
    • 0035672219 scopus 로고    scopus 로고
    • Butyrylcholinesterase K variant on chromosome 3 q is associated with Type II diabetes in white Caucasian subjects
    • Hashim Y, Shepherd D, Wiltshire S, Holman R, Levy JC, Clark A, Cull CA. Butyrylcholinesterase K variant on chromosome 3 q is associated with Type II diabetes in white Caucasian subjects. Diabetologia 2001;44:2227-30.
    • (2001) Diabetologia , vol.44 , pp. 2227-2230
    • Hashim, Y.1    Shepherd, D.2    Wiltshire, S.3    Holman, R.4    Levy, J.C.5    Clark, A.6    Cull, C.A.7
  • 10
    • 70449162191 scopus 로고
    • A method for the detection of human serum cholinesterase: Determnation of dibucaine numbers
    • Kallow W, Genest K. A method for the detection of human serum cholinesterase: determnation of dibucaine numbers. Can J Biochem 1957;35:339-46.
    • (1957) Can J Biochem , vol.35 , pp. 339-346
    • Kallow, W.1    Genest, K.2
  • 11
    • 35448969267 scopus 로고    scopus 로고
    • Serum butyrylcholinesterase is strongly associated with adiposity, the serum lipid profile and insulin resistance
    • Iwasaki T, Yoneda M, Nakajima A, Terauchi Y. Serum butyrylcholinesterase is strongly associated with adiposity, the serum lipid profile and insulin resistance. Intern Med 2007;46:1633-9.
    • (2007) Intern Med , vol.46 , pp. 1633-1639
    • Iwasaki, T.1    Yoneda, M.2    Nakajima, A.3    Terauchi, Y.4
  • 13
    • 34249655690 scopus 로고    scopus 로고
    • Characterization of procaine metabolism as probe for the butyrylcholinesterase enzyme investigation by simultaneous determination of procaine and its metabolite using capillary electrophoresis with electrochemiluminescence detection
    • Yuan J, Yin J, Wang E. Characterization of procaine metabolism as probe for the butyrylcholinesterase enzyme investigation by simultaneous determination of procaine and its metabolite using capillary electrophoresis with electrochemiluminescence detection. J Chromatogr A 2007;1154:368-72.
    • (2007) J Chromatogr A , vol.1154 , pp. 368-372
    • Yuan, J.1    Yin, J.2    Wang, E.3
  • 14
    • 33846379204 scopus 로고    scopus 로고
    • Molecular basis of succinylcholine sensitivity in a prairie Hutterite kindred and genetic characterization of the region containing the BCHE gene
    • Zelinski T, Coghlan G, Mauthe J, Triggs-Raine B. Molecular basis of succinylcholine sensitivity in a prairie Hutterite kindred and genetic characterization of the region containing the BCHE gene. Mol Genet Metab 2007;90:210-16.
    • (2007) Mol Genet Metab , vol.90 , pp. 210-216
    • Zelinski, T.1    Coghlan, G.2    Mauthe, J.3    Triggs-Raine, B.4
  • 19
    • 54049143783 scopus 로고    scopus 로고
    • Mechanism of hydrolysis of dicholine esters with long polymethylene chain by human butyrylcholinesterase
    • Grigoryan H, Halebyan G, Lefebvre B, Brasme B, Masson P. Mechanism of hydrolysis of dicholine esters with long polymethylene chain by human butyrylcholinesterase. Biochim Biophys Acta 2008;1784:1818-24.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1818-1824
    • Grigoryan, H.1    Halebyan, G.2    Lefebvre, B.3    Brasme, B.4    Masson, P.5
  • 20
    • 0019318905 scopus 로고
    • Hen's egg yolk cholinesterase. Purification, characterization and comparison with hen's liver and blood plasma cholinesterase
    • Saeed A, de Boeck S, Debruyne I, Wouters J, Stockx J. Hen's egg yolk cholinesterase. Purification, characterization and comparison with hen's liver and blood plasma cholinesterase. Biochim Biophys Acta 1980;614:389-99.
    • (1980) Biochim Biophys Acta , vol.614 , pp. 389-399
    • Saeed, A.1    de Boeck, S.2    Debruyne, I.3    Wouters, J.4    Stockx, J.5
  • 21
    • 0037375876 scopus 로고    scopus 로고
    • Cholinesterases: New roles in brain function and in Alzheimer's disease
    • Giacobini E. Cholinesterases: new roles in brain function and in Alzheimer's disease. Neurochem Res 2003;28:515-22.
    • (2003) Neurochem Res , vol.28 , pp. 515-522
    • Giacobini, E.1
  • 22
    • 36549071466 scopus 로고    scopus 로고
    • Alpha, beta-dehydrophenylalanine choline esters, a new class of reversible inhibitors of human acetylcholiensterse and butyrylcholinesterase
    • Grigoryan HA, Hambardzumyan AA, Mkrtchyan MV, Topuzyan VO, Halebyan GP, Asatryan RS. Alpha, beta-dehydrophenylalanine choline esters, a new class of reversible inhibitors of human acetylcholiensterse and butyrylcholinesterase. Chem Biol Interact 2008;171:108-16.
    • (2008) Chem Biol Interact , vol.171 , pp. 108-116
    • Grigoryan, H.A.1    Hambardzumyan, A.A.2    Mkrtchyan, M.V.3    Topuzyan, V.O.4    Halebyan, G.P.5    Asatryan, R.S.6
  • 23
    • 37549009507 scopus 로고    scopus 로고
    • Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates
    • Debord J, Laubarie C, Dantoine T. Microcalorimetric study of the inhibition of butyrylcholinesterase by carbamates. Anal Biochem 2008;373:247-52.
    • (2008) Anal Biochem , vol.373 , pp. 247-252
    • Debord, J.1    Laubarie, C.2    Dantoine, T.3
  • 24
    • 41049107851 scopus 로고    scopus 로고
    • Kinetics of human serum butyrylcholinesterase inhibition by a novel experimental Alzheimer therapeutic, dihydrobenzodioxepine cymserine
    • Kamal MA, Klein P, Luo W, Li Y, Holloway HW, Tweedie D, Greig NH. Kinetics of human serum butyrylcholinesterase inhibition by a novel experimental Alzheimer therapeutic, dihydrobenzodioxepine cymserine. Neurochem Res 2008;33:745-53.
    • (2008) Neurochem Res , vol.33 , pp. 745-753
    • Kamal, M.A.1    Klein, P.2    Luo, W.3    Li, Y.4    Holloway, H.W.5    Tweedie, D.6    Greig, N.H.7
  • 25
    • 0017129083 scopus 로고
    • Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor
    • Nagasawa T, Sugisaki H, Tani Y, Ogata K. Purification and characterization of butyrylcholine-hydrolyzing enzyme from Pseudomonas polycolor. Biochim Biophys Acta 1976;429:817-27.
    • (1976) Biochim Biophys Acta , vol.429 , pp. 817-827
    • Nagasawa, T.1    Sugisaki, H.2    Tani, Y.3    Ogata, K.4
  • 26
    • 26444498011 scopus 로고    scopus 로고
    • Characterization of the cholinesterases present in head tissues of the estuarine fish Pomatoschistus microps: Application to biomonitoring. Exotoxicol. Environ
    • Monteiro M, Quintaneiro C, Morgado F, Soares AM, Guilhermino L. Characterization of the cholinesterases present in head tissues of the estuarine fish Pomatoschistus microps: application to biomonitoring. Exotoxicol. Environ. Saf. 2005;62:341-7.
    • (2005) Saf , vol.62 , pp. 341-347
    • Monteiro, M.1    Quintaneiro, C.2    Morgado, F.3    Soares, A.M.4    Guilhermino, L.5
  • 28
    • 0142052989 scopus 로고    scopus 로고
    • On establishment of individuality of the choliensterase enzyme in the studied preparation
    • Zhukovskii YG. On establishment of individuality of the choliensterase enzyme in the studied preparation. J Evol Biochem Physiol 2003;39:281-90.
    • (2003) J Evol Biochem Physiol , vol.39 , pp. 281-290
    • Zhukovskii, Y.G.1
  • 29
    • 0030668464 scopus 로고    scopus 로고
    • Tetramerization domain of human butyrylcholinesterase is at the C-terminus
    • Blong RM, Bedows E, Lockridge O. Tetramerization domain of human butyrylcholinesterase is at the C-terminus. Biochem J 1997;327:747-57.
    • (1997) Biochem J , vol.327 , pp. 747-757
    • Blong, R.M.1    Bedows, E.2    Lockridge, O.3
  • 32
    • 0142039868 scopus 로고    scopus 로고
    • Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products
    • Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F. Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem 2003;278:41141-7.
    • (2003) J Biol Chem , vol.278 , pp. 41141-41147
    • Nicolet, Y.1    Lockridge, O.2    Masson, P.3    Fontecilla-Camps, J.C.4    Nachon, F.5
  • 33
    • 0030960299 scopus 로고    scopus 로고
    • Maintenance of constant blood acetylcholine content before and after feeding in young chimpanzees
    • Fujii T, Mori Y, Tominaga T, Hayasaka I, Kawashima K. Maintenance of constant blood acetylcholine content before and after feeding in young chimpanzees. Neurosci Lett 1997;227:21-4.
    • (1997) Neurosci Lett , vol.227 , pp. 21-24
    • Fujii, T.1    Mori, Y.2    Tominaga, T.3    Hayasaka, I.4    Kawashima, K.5
  • 34
    • 0025100471 scopus 로고
    • Mechanism of action of organophosphorus and carbamate insecticides
    • Fukuto TR. Mechanism of action of organophosphorus and carbamate insecticides. Environ Health Perspect 1990;87:245-54.
    • (1990) Environ Health Perspect , vol.87 , pp. 245-254
    • Fukuto, T.R.1
  • 36
    • 33846981174 scopus 로고    scopus 로고
    • Excessive hippocampal acetylcholine levels in acetylcholinesterase-deficient mice are moderated by butyrylcholinesterase activity
    • Hartmann J, Kiewert C, Duysen EG, Lockridge O, Greig NH, Klein J. Excessive hippocampal acetylcholine levels in acetylcholinesterase-deficient mice are moderated by butyrylcholinesterase activity. J Neurochem 2007;100:1421-9.
    • (2007) J Neurochem , vol.100 , pp. 1421-1429
    • Hartmann, J.1    Kiewert, C.2    Duysen, E.G.3    Lockridge, O.4    Greig, N.H.5    Klein, J.6
  • 37
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman JL, Harel M, Frolow F, Oefner C, Goldman A, Toker L, Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991;253:872-9.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Silman, I.7
  • 39
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
    • Cygler M, Schrag JD, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci 1993;2:366-82.
    • (1993) Protein Sci , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 40
    • 0023767035 scopus 로고
    • The molecular evolution of genes and proteins: A tale of two serines
    • Brenner S. The molecular evolution of genes and proteins: a tale of two serines. Nature 1988;334:528-30.
    • (1988) Nature , vol.334 , pp. 528-530
    • Brenner, S.1
  • 41
    • 50649087289 scopus 로고    scopus 로고
    • Acetylcholinesterase: How is structure related to function?
    • Silman I, Sussman JL. Acetylcholinesterase: how is structure related to function? Chem Biol Interact 2008;175:3-10.
    • (2008) Chem Biol Interact , vol.175 , pp. 3-10
    • Silman, I.1    Sussman, J.L.2
  • 42
    • 0038682446 scopus 로고    scopus 로고
    • Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates
    • Kovarik Z, Radic Z, Berman HA, Simeon-Rudolf V, Reiner E, Taylor P. Acetylcholinesterase active centre and gorge conformations analysed by combinatorial mutations and enantiomeric phosphonates. Biochem J 2003;373:33-40.
    • (2003) Biochem J , vol.373 , pp. 33-40
    • Kovarik, Z.1    Radic, Z.2    Berman, H.A.3    Simeon-Rudolf, V.4    Reiner, E.5    Taylor, P.6
  • 43
    • 77249107098 scopus 로고    scopus 로고
    • Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives
    • Bartolucci C, Haller LA, Jardis U, Fels G, Lamba D. Probing Torpedo californica acetylcholinesterase catalytic gorge with two novel bis-functional galanthamine derivatives. J Med Chem 2010;53:745-51.
    • (2010) J Med Chem , vol.53 , pp. 745-751
    • Bartolucci, C.1    Haller, L.A.2    Jardis, U.3    Fels, G.4    Lamba, D.5
  • 44
    • 0025871564 scopus 로고
    • Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom
    • Kreienkamp HJ, Weise C, Raba R., Aaviksaar A, Hucho F. Anionic subsites of the catalytic center of acetylcholinesterase from Torpedo and from cobra venom. Proc Natl Acad Sci USA 1991;88:6117-21.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6117-6121
    • Kreienkamp, H.J.1    Weise, C.2    Raba, R.3    Aaviksaar, A.4    Hucho, F.5
  • 45
    • 0027265211 scopus 로고
    • An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase
    • Ripoll DR, Faerman CH, Axelsen PH, Silman I, Sussman JL. An electrostatic mechanism for substrate guidance down the aromatic gorge of acetylcholinesterase. Proc Natl Acad Sci USA 1993;90:5128-32.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5128-5132
    • Ripoll, D.R.1    Faerman, C.H.2    Axelsen, P.H.3    Silman, I.4    Sussman, J.L.5
  • 46
    • 0036301326 scopus 로고    scopus 로고
    • A neutral molecule in a cation-binding site: Specific binding of a PEGSH to acetylcholinesterase from Torpedo californica
    • Koellner G, Steiner T, Millard CB, Silman I, Sussman JL. A neutral molecule in a cation-binding site: specific binding of a PEGSH to acetylcholinesterase from Torpedo californica. J Mol Biol 2002;320:721-5.
    • (2002) J Mol Biol , vol.320 , pp. 721-725
    • Koellner, G.1    Steiner, T.2    Millard, C.B.3    Silman, I.4    Sussman, J.L.5
  • 47
    • 0013945471 scopus 로고    scopus 로고
    • Responses of acetylcholinesterase from Torpedo marmarata to salts and curarizing drugs
    • Changeux JP. Responses of acetylcholinesterase from Torpedo marmarata to salts and curarizing drugs. Mol Pharmacol 1996;2:369-92.
    • (1996) Mol Pharmacol , vol.2 , pp. 369-392
    • Changeux, J.P.1
  • 48
    • 33644867844 scopus 로고    scopus 로고
    • The peripheral anionic site of acetylcholinesterase: Structure, functions and potential role in rational drug design
    • Johnson G, Moore SW. The peripheral anionic site of acetylcholinesterase: structure, functions and potential role in rational drug design. Curr Pharm Des 2006;12:217-25.
    • (2006) Curr Pharm Des , vol.12 , pp. 217-225
    • Johnson, G.1    Moore, S.W.2
  • 49
    • 33847671821 scopus 로고    scopus 로고
    • Bivalent ligands derived from Huperzine A as acetylcholinesterase inhibitors
    • Haviv H, Wong DM, Silman I, Sussman JL. Bivalent ligands derived from Huperzine A as acetylcholinesterase inhibitors. Curr Top Med Chem 2007;7:375-87.
    • (2007) Curr Top Med Chem , vol.7 , pp. 375-387
    • Haviv, H.1    Wong, D.M.2    Silman, I.3    Sussman, J.L.4
  • 50
    • 0028177161 scopus 로고
    • Differential effects of "peripheral"site ligands on Torpedo and chicken acetylcholinesterase
    • Eichler J, Anselment A, Sussman JL, Massoulie J, Silman I. Differential effects of "peripheral"site ligands on Torpedo and chicken acetylcholinesterase. Mol Pharmacol 1994;45:335-40.
    • (1994) Mol Pharmacol , vol.45 , pp. 335-340
    • Eichler, J.1    Anselment, A.2    Sussman, J.L.3    Massoulie, J.4    Silman, I.5
  • 51
    • 38549098085 scopus 로고    scopus 로고
    • Amyloid-cholinesterase interactions. Implications for Alzheimer's disease
    • Inestrosa NC, Dinamarca MC, Alvarez A. Amyloid-cholinesterase interactions. Implications for Alzheimer's disease. FEBS J 2008;275:625-32.
    • (2008) FEBS J , vol.275 , pp. 625-632
    • Inestrosa, N.C.1    Dinamarca, M.C.2    Alvarez, A.3
  • 52
    • 0024352019 scopus 로고
    • Comparison of butyrylcholinesterase and acetylcholinesterase
    • Chatonnet A, Lockridge O. Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem J 1989;260:625-34.
    • (1989) Biochem J , vol.260 , pp. 625-634
    • Chatonnet, A.1    Lockridge, O.2
  • 53
    • 0025636509 scopus 로고
    • Are soluble and membrane-bound rat brain acetlcholinesterase different?
    • Andres C, elMourabit M, Stutz C, Mark J, Waksman A. Are soluble and membrane-bound rat brain acetlcholinesterase different? Neurochem Res 1990;15:1065-72.
    • (1990) Neurochem Res , vol.15 , pp. 1065-1072
    • Andres, C.1    Elmourabit, M.2    Stutz, C.3    Mark, J.4    Waksman, A.5
  • 54
    • 0029670364 scopus 로고    scopus 로고
    • Tetrameric (G4) acetylcholinesterase: Structure, localization, and physiological regulation
    • Fernandez HL, Moreno RD, Inestrosa NC. Tetrameric (G4) acetylcholinesterase: structure, localization, and physiological regulation. J Neurochem 1996;66:1335-46.
    • (1996) J Neurochem , vol.66 , pp. 1335-1346
    • Fernandez, H.L.1    Moreno, R.D.2    Inestrosa, N.C.3
  • 55
    • 0023219731 scopus 로고
    • Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterases in other tissues
    • Inestrosa NC, Roberts WL, Marshall TL, Rosenberry TL. Acetylcholinesterase from bovine caudate nucleus is attached to membranes by a novel subunit distinct from those of acetylcholinesterases in other tissues. J Biol Chem 1987;262:4441-4.
    • (1987) J Biol Chem , vol.262 , pp. 4441-4444
    • Inestrosa, N.C.1    Roberts, W.L.2    Marshall, T.L.3    Rosenberry, T.L.4
  • 56
    • 0027376380 scopus 로고
    • Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica
    • Mehlert A, Varon L, Silman I, Homans SW, Ferguson MAJ. Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica. Biochem J 1993;296:473-9.
    • (1993) Biochem J , vol.296 , pp. 473-479
    • Mehlert, A.1    Varon, L.2    Silman, I.3    Homans, S.W.4    Ferguson, M.A.J.5
  • 57
    • 0022887783 scopus 로고
    • Glycolipid membrane-binding domain of human erythrocyte acetylcholinesterase
    • Rosenberry TL, Roberts WL, Haas R. Glycolipid membrane-binding domain of human erythrocyte acetylcholinesterase. Fed Proc 1986; 45:2970-5.
    • (1986) Fed Proc , vol.45 , pp. 2970-2975
    • Rosenberry, T.L.1    Roberts, W.L.2    Haas, R.3
  • 58
    • 0027228514 scopus 로고
    • Subunit association and glycosylation of acetylcholinesterase from monkey brain
    • Liao J, Norgaard-Pedersen B, Brodbeck U. Subunit association and glycosylation of acetylcholinesterase from monkey brain. J Neurochem 1993;61:1127-34.
    • (1993) J Neurochem , vol.61 , pp. 1127-1134
    • Liao, J.1    Norgaard-Pedersen, B.2    Brodbeck, U.3
  • 59
    • 0020021171 scopus 로고
    • The molecular forms of cholinesterse and acetylcholinesterase in verterbrates
    • Massoulie J, Bon S. The molecular forms of cholinesterse and acetylcholinesterase in verterbrates. Ann Rev Neurosci 1982;5:57-106.
    • (1982) Ann Rev Neurosci , vol.5 , pp. 57-106
    • Massoulie, J.1    Bon, S.2
  • 60
    • 0033594106 scopus 로고    scopus 로고
    • Genetic analysis of collagen Q: Roles in acetylcholinesterse and butyrylchoilnesterase assembly and in synaptic structure and function
    • Feng G, Krejci E, Molgo J, Cunningham JM, Massoulie J, Sanes JR. Genetic analysis of collagen Q: roles in acetylcholinesterse and butyrylchoilnesterase assembly and in synaptic structure and function. J Cell Biol 1999;144:1349-60.
    • (1999) J Cell Biol , vol.144 , pp. 1349-1360
    • Feng, G.1    Krejci, E.2    Molgo, J.3    Cunningham, J.M.4    Massoulie, J.5    Sanes, J.R.6
  • 62
    • 50649086147 scopus 로고    scopus 로고
    • Protection of red blood cell acetylcholinesterase by oral huperzine A against ex vivo soman exposure: Next generation prophylaxis and sequestering of acetylcholinesterase over butyrylcholinesterase
    • Haigh JR, Johnston SR, Peppernay A, Mattern PJ, Garcia GE, Doctor BP, Gordon RK, Aisen PS. Protection of red blood cell acetylcholinesterase by oral huperzine A against ex vivo soman exposure: next generation prophylaxis and sequestering of acetylcholinesterase over butyrylcholinesterase. Chem Biol Interact 2008;175:380-6.
    • (2008) Chem Biol Interact , vol.175 , pp. 380-386
    • Haigh, J.R.1    Johnston, S.R.2    Peppernay, A.3    Mattern, P.J.4    Garcia, G.E.5    Doctor, B.P.6    Gordon, R.K.7    Aisen, P.S.8
  • 64
    • 35648945420 scopus 로고    scopus 로고
    • Amperometric biosensor for evaluation of competitive cholinesterase inhibition by the reactivator HI-6
    • Pohanka M, Jun D, Kuca K. Amperometric biosensor for evaluation of competitive cholinesterase inhibition by the reactivator HI-6. Anal Lett 2007;40:2351-9.
    • (2007) Anal Lett , vol.40 , pp. 2351-2359
    • Pohanka, M.1    Jun, D.2    Kuca, K.3
  • 65
    • 67651009572 scopus 로고    scopus 로고
    • Progress of biosensors based on cholinesterase inhibition
    • Pohanka M, Musilek K, Kuca K. Progress of biosensors based on cholinesterase inhibition. Curr Med Chem 2009;16:1790-8.
    • (2009) Curr Med Chem , vol.16 , pp. 1790-1798
    • Pohanka, M.1    Musilek, K.2    Kuca, K.3
  • 66
    • 33947685552 scopus 로고    scopus 로고
    • Enzyme-kinetic investigation of different sarin analogues reacting with human acetylcholinesterase and butyrylcholinesterase
    • Bartling A, Worek F, Szinicz L, Thiermann H. Enzyme-kinetic investigation of different sarin analogues reacting with human acetylcholinesterase and butyrylcholinesterase. Toxicology 2007;233:166-72.
    • (2007) Toxicology , vol.233 , pp. 166-172
    • Bartling, A.1    Worek, F.2    Szinicz, L.3    Thiermann, H.4
  • 67
    • 0035380641 scopus 로고    scopus 로고
    • Determination of whole blood cholinesterase in different animal species using specific substrates
    • Tecles F, Ceron JJ. Determination of whole blood cholinesterase in different animal species using specific substrates. Res Vet Sci 2001;70:233-8.
    • (2001) Res Vet Sci , vol.70 , pp. 233-238
    • Tecles, F.1    Ceron, J.J.2
  • 68
    • 1542555313 scopus 로고
    • Catalysis by acetylcholinesterase: Evidence that the rate-limitng step for acylation with certain substrates general acid-base catalysis
    • Rosenberry TL. Catalysis by acetylcholinesterase: evidence that the rate-limitng step for acylation with certain substrates general acid-base catalysis. Proc Natl Acad Sci USA 1975;72:3834-8.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3834-3838
    • Rosenberry, T.L.1
  • 69
    • 0040920320 scopus 로고
    • The mechanism of action of acetylcholinesterase: Substrate inhibition and the binding of inhibitors
    • Krupka RM. The mechanism of action of acetylcholinesterase: substrate inhibition and the binding of inhibitors. Biochemistry 1963;2:76-82.
    • (1963) Biochemistry , vol.2 , pp. 76-82
    • Krupka, R.M.1
  • 70
    • 77951761289 scopus 로고    scopus 로고
    • The biological significance of substrate inhibition: A mechanism with diverse functions
    • Reed MC, Lieb A, Nijhout HF. The biological significance of substrate inhibition: a mechanism with diverse functions. Bioassays 2010;32:422-9.
    • (2010) Bioassays , vol.32 , pp. 422-429
    • Reed, M.C.1    Lieb, A.2    Nijhout, H.F.3
  • 71
    • 0032006409 scopus 로고    scopus 로고
    • Characterization of acetylcholinesterase purified from the lesser grain borer, Rhyzopertha dominica (Coleoptera: Bostrichidae)
    • Guedes RN, Zhu KY, Kambhampati S, Dover BA. Characterization of acetylcholinesterase purified from the lesser grain borer, Rhyzopertha dominica (Coleoptera: Bostrichidae). Comp Biochem Physiol C Pharmacol Toxicol Endocrinol 1998;119:205-10.
    • (1998) Comp Biochem Physiol C Pharmacol Toxicol Endocrinol , vol.119 , pp. 205-210
    • Guedes, R.N.1    Zhu, K.Y.2    Kambhampati, S.3    Dover, B.A.4
  • 72
    • 0034808451 scopus 로고    scopus 로고
    • An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics
    • Gao JR, Zhu KY. An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics. Insect Biochem Mol Biol 2001;31:1095-104.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 1095-1104
    • Gao, J.R.1    Zhu, K.Y.2
  • 73
    • 38549176068 scopus 로고    scopus 로고
    • Acetylcholinesterase in cell adhesion, neurite growth and network formation
    • Paraoanu LE, Layer PG. Acetylcholinesterase in cell adhesion, neurite growth and network formation. FEBS J 2008;275:618-24.
    • (2008) FEBS J , vol.275 , pp. 618-624
    • Paraoanu, L.E.1    Layer, P.G.2
  • 74
    • 52449122884 scopus 로고    scopus 로고
    • Non-enzymatic developmental functions of acetylcholiensterase-the question of redundancy
    • Johnson G, Swart C, Moore SW. Non-enzymatic developmental functions of acetylcholiensterase-the question of redundancy. FEBS J 2008;275:519-38.
    • (2008) FEBS J , vol.275 , pp. 519-538
    • Johnson, G.1    Swart, C.2    Moore, S.W.3
  • 75
    • 0025354508 scopus 로고
    • Role of butyrylcholinesterase in canine tracheal smooth muscle function
    • Adler M, Filbert MG. Role of butyrylcholinesterase in canine tracheal smooth muscle function. FEBS Lett 1990;267:107-10.
    • (1990) FEBS Lett , vol.267 , pp. 107-110
    • Adler, M.1    Filbert, M.G.2
  • 76
    • 4544247386 scopus 로고    scopus 로고
    • New classes of AChE inhibitors with additional pharmacological effects of interests for the treatment of Alzheimer's disease
    • Villarroya M, Garcia AG, Marco JL. New classes of AChE inhibitors with additional pharmacological effects of interests for the treatment of Alzheimer's disease. Curr Pharm Des 2004;10:3177-84.
    • (2004) Curr Pharm Des , vol.10 , pp. 3177-3184
    • Villarroya, M.1    Garcia, A.G.2    Marco, J.L.3
  • 77
    • 0035727527 scopus 로고    scopus 로고
    • Selective inhibitors of butyrylcholinesterase: A valid alternative for therapy of Alzheimer's disease?
    • Giacobini E. Selective inhibitors of butyrylcholinesterase: a valid alternative for therapy of Alzheimer's disease? Drugs Aging 2001;18:891-8.
    • (2001) Drugs Aging , vol.18 , pp. 891-898
    • Giacobini, E.1
  • 78
    • 4043074138 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: New roles and therapeutic alternatives
    • Giacobini E. Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacol Res 2004;50:433-40.
    • (2004) Pharmacol Res , vol.50 , pp. 433-440
    • Giacobini, E.1
  • 81
    • 58249088265 scopus 로고    scopus 로고
    • Accomodation of physostigmine and its analogues by acetylchoilnesterase is dominated by hydrophobic interactions
    • Barak D, Ordentlich A, Stein D, Yu QS, Greig NH, Shafferman A. Accomodation of physostigmine and its analogues by acetylchoilnesterase is dominated by hydrophobic interactions. Biochem J 2009;417:213-22.
    • (2009) Biochem J , vol.417 , pp. 213-222
    • Barak, D.1    Ordentlich, A.2    Stein, D.3    Yu, Q.S.4    Greig, N.H.5    Shafferman, A.6
  • 82
    • 33746843949 scopus 로고    scopus 로고
    • Neurosciences and research on chemical weapons of mass destruction in Nazi Germany
    • Schaltz F. Neurosciences and research on chemical weapons of mass destruction in Nazi Germany. J Hist Neurosci 2006;15:186-209.
    • (2006) J Hist Neurosci , vol.15 , pp. 186-209
    • Schaltz, F.1
  • 83
    • 77950872713 scopus 로고    scopus 로고
    • Chemcial warfare agents
    • Kuca K, Pohanka M. Chemcial warfare agents. EXS 2010; 100:543-58.
    • (2010) EXS , vol.100 , pp. 543-558
    • Kuca, K.1    Pohanka, M.2
  • 84
    • 0020530435 scopus 로고
    • The effect of bispyridinium oximes on neuromuscular blockade induced by highly toxic organohposhates in rat
    • Jovanovic D. The effect of bispyridinium oximes on neuromuscular blockade induced by highly toxic organohposhates in rat. Archives Internationales de Pharmacodynamie et de Therapie 1983;262:231-41.
    • (1983) Archives Internationales De Pharmacodynamie Et De Therapie , vol.262 , pp. 231-241
    • Jovanovic, D.1
  • 86
    • 0021150638 scopus 로고
    • 2-PAM chloride HI6 and HGG12 in soman and tabun poisoning
    • Boskovic B, Kovacevic V, Jovanovic D. 2-PAM chloride HI6 and HGG12 in soman and tabun poisoning. Fund Appl Toxicol 1984;4:106-15.
    • (1984) Fund Appl Toxicol , vol.4 , pp. 106-115
    • Boskovic, B.1    Kovacevic, V.2    Jovanovic, D.3
  • 87
    • 0021744292 scopus 로고
    • Accidental exposure to sarin: Vision effects
    • Rengstorff RH. Accidental exposure to sarin: vision effects. Arch Toxicol 1985;56:201-3.
    • (1985) Arch Toxicol , vol.56 , pp. 201-203
    • Rengstorff, R.H.1
  • 88
    • 23744504223 scopus 로고    scopus 로고
    • In vivo skin absorption and distribution of the nerve agent VX (O-ethyl-S-[2(diisopropylamino)ethyl] methyl-phosphonothioate) in the domestic white pig
    • Chilcott RP, Dalton CH, Hill I, Davison CM, Blohm KL, Clarkson ED, Hamilton MG. In vivo skin absorption and distribution of the nerve agent VX (O-ethyl-S-[2(diisopropylamino)ethyl] methyl-phosphonothioate) in the domestic white pig. Hum Exp Toxicol 2005;24:347-52.
    • (2005) Hum Exp Toxicol , vol.24 , pp. 347-352
    • Chilcott, R.P.1    Dalton, C.H.2    Hill, I.3    Davison, C.M.4    Blohm, K.L.5    Clarkson, E.D.6    Hamilton, M.G.7
  • 90
    • 57749179505 scopus 로고    scopus 로고
    • Paraoxonase activity against nerve gases measured by capillary electrophoresis and characterization of human serum paraoxonase (PON1) polymorphism in the coding region (Q192R)
    • Kanamori-Kataoka M, Seto Y. Paraoxonase activity against nerve gases measured by capillary electrophoresis and characterization of human serum paraoxonase (PON1) polymorphism in the coding region (Q192R). Anal Biochem 2009;385:94-100.
    • (2009) Anal Biochem , vol.385 , pp. 94-100
    • Kanamori-Kataoka, M.1    Seto, Y.2
  • 91
    • 0036830397 scopus 로고    scopus 로고
    • Activated transformations of organophoshorus insecticides in the case of non-AChE inhibitory oxons
    • Kasagami T, Miyamoto T, Yamamoto I. Activated transformations of organophoshorus insecticides in the case of non-AChE inhibitory oxons. Pest Manag Sci 2002;58:1107-17.
    • (2002) Pest Manag Sci , vol.58 , pp. 1107-1117
    • Kasagami, T.1    Miyamoto, T.2    Yamamoto, I.3
  • 93
    • 78649610526 scopus 로고    scopus 로고
    • Myasthenia gravis requiring pyridostigmine treatment in a national population cohort
    • In press
    • Andersen JB, Engeland A, Owe JF, Gilhus NE. Myasthenia gravis requiring pyridostigmine treatment in a national population cohort. Eur J Neurol, In press.
    • Eur J Neurol
    • Andersen, J.B.1    Engeland, A.2    Owe, J.F.3    Gilhus, N.E.4
  • 95
    • 0029850424 scopus 로고    scopus 로고
    • Pyridostigmine brain penetration under stress enhances neuronal excitability and induces early immediate transcriptional response
    • Friedman A, Kaufer D, Shemer J, Hendler I, Soreq H, Tur-Kaspa I. Pyridostigmine brain penetration under stress enhances neuronal excitability and induces early immediate transcriptional response. Nat Med 1996;2:1382-5.
    • (1996) Nat Med , vol.2 , pp. 1382-1385
    • Friedman, A.1    Kaufer, D.2    Shemer, J.3    Hendler, I.4    Soreq, H.5    Tur-Kaspa, I.6
  • 96
    • 68149100645 scopus 로고    scopus 로고
    • Rivastigmine in Parkinson's disease dementia
    • Chitnis S, Rao J. Rivastigmine in Parkinson's disease dementia. Expert Opin Drug Metab Toxicol 2009;5:941-55.
    • (2009) Expert Opin Drug Metab Toxicol , vol.5 , pp. 941-955
    • Chitnis, S.1    Rao, J.2
  • 97
    • 0034965634 scopus 로고    scopus 로고
    • Efficacy of metrifonate in imporving the psychiatric and behavioral disturbances of patients with Alzheimer's disease
    • Cummings JL, Nadel A, Masterman D, Cyrus PA. Efficacy of metrifonate in imporving the psychiatric and behavioral disturbances of patients with Alzheimer's disease. J Geriatr Psychiatry Neurol 2001;14:101-8.
    • (2001) J Geriatr Psychiatry Neurol , vol.14 , pp. 101-108
    • Cummings, J.L.1    Nadel, A.2    Masterman, D.3    Cyrus, P.A.4
  • 100
    • 0028842771 scopus 로고
    • Differential inhibition of rat brain acetylcholinesterase molecular forms by 7-methoxytacrine in vitro
    • Bajgar J, Bisso GM, Michalek H. Differential inhibition of rat brain acetylcholinesterase molecular forms by 7-methoxytacrine in vitro. Toxicol Lett 1995;80:109-14.
    • (1995) Toxicol Lett , vol.80 , pp. 109-114
    • Bajgar, J.1    Bisso, G.M.2    Michalek, H.3
  • 101
    • 57149134942 scopus 로고    scopus 로고
    • New performance of biosensor technology for Alzheimer's disease drugs: In vitro comparison of tacrine and 7-methoxytacrine
    • Pohanka M, Kuca K, Kassa J. New performance of biosensor technology for Alzheimer's disease drugs: in vitro comparison of tacrine and 7-methoxytacrine. Neuroendocrinol Lett 2008;29:755-8.
    • (2008) Neuroendocrinol Lett , vol.29 , pp. 755-758
    • Pohanka, M.1    Kuca, K.2    Kassa, J.3
  • 104
    • 0035254937 scopus 로고    scopus 로고
    • Threedimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: Implications for the design of new anti-Alzheimer drugs
    • Bartolucci C, Perola E, Pilger C, Fels G, Lamba D. Threedimensional structure of a complex of galanthamine (Nivalin) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-Alzheimer drugs. Proteins 2001;42:182-91.
    • (2001) Proteins , vol.42 , pp. 182-191
    • Bartolucci, C.1    Perola, E.2    Pilger, C.3    Fels, G.4    Lamba, D.5
  • 105
    • 0034966268 scopus 로고    scopus 로고
    • Accurate prediction fo the bound conformation of galanthamine in the active site of Torpedo californica acetylcholinesterase using molecular docking
    • Pilger C, Bartolucci C, Lamba D, Tropsha A, Fels G. Accurate prediction fo the bound conformation of galanthamine in the active site of Torpedo californica acetylcholinesterase using molecular docking. J Mol Graph Model 2001;19:288-96.
    • (2001) J Mol Graph Model , vol.19 , pp. 288-296
    • Pilger, C.1    Bartolucci, C.2    Lamba, D.3    Tropsha, A.4    Fels, G.5
  • 106
    • 0028230038 scopus 로고
    • Structure and dynamics of the active site gorge of acetylcholinesterase: Synergistic use of molecular dynamics simulation and X-ray crystallography
    • Axelsen PH, Harel M, Silman I, Sussman JL. Structure and dynamics of the active site gorge of acetylcholinesterase: synergistic use of molecular dynamics simulation and X-ray crystallography. Protein Sci 1994;3:188-97.
    • (1994) Protein Sci , vol.3 , pp. 188-197
    • Axelsen, P.H.1    Harel, M.2    Silman, I.3    Sussman, J.L.4
  • 108
    • 33750883640 scopus 로고    scopus 로고
    • Targeting beta-amyloid pathogenesis through acetylchoinesterase inhibitors
    • Castro A, Martinez A. Targeting beta-amyloid pathogenesis through acetylchoinesterase inhibitors. Curr Pharm Des 2006;12:4377-87.
    • (2006) Curr Pharm Des , vol.12 , pp. 4377-4387
    • Castro, A.1    Martinez, A.2
  • 109
    • 60349086982 scopus 로고    scopus 로고
    • Kinetic insight into the mechanism of cholinesterase inhibition by aflatoxin B1 to develop biosensors
    • Hansmann T, Sanson B, Stojan J, Weik M, Marty JL, Fournier D. Kinetic insight into the mechanism of cholinesterase inhibition by aflatoxin B1 to develop biosensors. Biosens Bioelectron 2009;24:2119-24.
    • (2009) Biosens Bioelectron , vol.24 , pp. 2119-2124
    • Hansmann, T.1    Sanson, B.2    Stojan, J.3    Weik, M.4    Marty, J.L.5    Fournier, D.6
  • 110
    • 77949948148 scopus 로고    scopus 로고
    • Evaluation of aflatoxin B1 - acetylcholinesterase dissociation kinetic using the amperometric biosensor technology: Prospect for toxicity mechanism
    • Pohanka M, Musilek K, Kuca K. Evaluation of aflatoxin B1 - acetylcholinesterase dissociation kinetic using the amperometric biosensor technology: prospect for toxicity mechanism. Protein Pept Lett 2010;17:340-2.
    • (2010) Protein Pept Lett , vol.17 , pp. 340-342
    • Pohanka, M.1    Musilek, K.2    Kuca, K.3
  • 111
    • 53349132129 scopus 로고    scopus 로고
    • Aflatoxin assay using an amerometric sensor strip and acetylcholinesterase as recognition element
    • Pohanka, M, Kuca K, Jun D. Aflatoxin assay using an amerometric sensor strip and acetylcholinesterase as recognition element. Sens Lett 2008;6:450-3.
    • (2008) Sens Lett , vol.6 , pp. 450-453
    • Pohanka, M.1    Kuca, K.2    Jun, D.3
  • 112
    • 0021744267 scopus 로고
    • Effect of aflatoxicosis on acetylcholinesterse activity in the brain and adenohypophysis of the male rat
    • Egbunike GN, Ikegwuonu FI. Effect of aflatoxicosis on acetylcholinesterse activity in the brain and adenohypophysis of the male rat. Neurosci Lett 1984;52:171-4.
    • (1984) Neurosci Lett , vol.52 , pp. 171-174
    • Egbunike, G.N.1    Ikegwuonu, F.I.2
  • 113
    • 3242794237 scopus 로고    scopus 로고
    • A computational study of the binding of propidium to the peripheral anionic site of human acetylcholinesterase
    • Cavalli A, Bottegoni G, Raco C, De Vivo M, Recanatini M. A computational study of the binding of propidium to the peripheral anionic site of human acetylcholinesterase. J Med Chem 2004;47:3991-9.
    • (2004) J Med Chem , vol.47 , pp. 3991-3999
    • Cavalli, A.1    Bottegoni, G.2    Raco, C.3    de Vivo, M.4    Recanatini, M.5
  • 115
    • 58049209924 scopus 로고    scopus 로고
    • Role of metalions in the abeta oligomerization in Alzheimer's disease and in other neurological disorders
    • Drago D, Bolognin S, Zatta P. Role of metalions in the abeta oligomerization in Alzheimer's disease and in other neurological disorders. Curr Alzheimer Res 2008;5:500-7.
    • (2008) Curr Alzheimer Res , vol.5 , pp. 500-507
    • Drago, D.1    Bolognin, S.2    Zatta, P.3
  • 116
    • 0035652227 scopus 로고    scopus 로고
    • Aluminum exposure and Alzheimer's disease
    • Jansson ET. Aluminum exposure and Alzheimer's disease. J Alzheimers Dis 2001;3:541-9.
    • (2001) J Alzheimers Dis , vol.3 , pp. 541-549
    • Jansson, E.T.1
  • 117
    • 24344442031 scopus 로고    scopus 로고
    • Acetylcholinesterase activation and enhanced lipid peroxidation after long-term exposure to low levels of aluminum on different mouse brain regions
    • Kaizer RR, Correa MC, Spanevello RM, Morsch VM, Mazzanti CM, Goncalves JF, Schetinger MR. Acetylcholinesterase activation and enhanced lipid peroxidation after long-term exposure to low levels of aluminum on different mouse brain regions. J Inorg Biochem 2005;99:1865-70.
    • (2005) J Inorg Biochem , vol.99 , pp. 1865-1870
    • Kaizer, R.R.1    Correa, M.C.2    Spanevello, R.M.3    Morsch, V.M.4    Mazzanti, C.M.5    Goncalves, J.F.6    Schetinger, M.R.7
  • 118
    • 52549116539 scopus 로고    scopus 로고
    • Effect of long-term exposure to aluminum on the acetylcholinesterase activity in the central nervous system and erythrocytes
    • Kaizer RR, Correa MC, Gris LR, da Rosa CS, Bohrer D, Morsch VM, Schetinger MR. Effect of long-term exposure to aluminum on the acetylcholinesterase activity in the central nervous system and erythrocytes. Neurochem Res 2008;33:2294-2301.
    • (2008) Neurochem Res , vol.33 , pp. 2294-2301
    • Kaizer, R.R.1    Correa, M.C.2    Gris, L.R.3    da Rosa, C.S.4    Bohrer, D.5    Morsch, V.M.6    Schetinger, M.R.7
  • 122
    • 77649234636 scopus 로고    scopus 로고
    • Effects of cholinesterse inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzheimer's disease: A review of recent clinical studies
    • Darreh-Shori T, Soininen H. Effects of cholinesterse inhibitors on the activities and protein levels of cholinesterases in the cerebrospinal fluid of patients with Alzheimer's disease: a review of recent clinical studies. Curr Alzheimer Res 2010;7:67-73.
    • (2010) Curr Alzheimer Res , vol.7 , pp. 67-73
    • Darreh-Shori, T.1    Soininen, H.2
  • 123
    • 67349281227 scopus 로고    scopus 로고
    • Huperzine a protects isolated rat brain mitochondria against beta-amyloid peptide
    • Gao X, Zheng CY, Yang L, Tang XC, Zhang HY. Huperzine A protects isolated rat brain mitochondria against beta-amyloid peptide. Free Radic Biol Med 2009; 46:1454-62.
    • (2009) Free Radic Biol Med , vol.46 , pp. 1454-1462
    • Gao, X.1    Zheng, C.Y.2    Yang, L.3    Tang, X.C.4    Zhang, H.Y.5
  • 124
    • 0342409367 scopus 로고    scopus 로고
    • A novel acetylcholinesterase inhibitor, attenuates hydrogen peroxide induced injury in PC12 cells
    • Zhang HY, Tang XC. Huperzine B, a novel acetylcholinesterase inhibitor, attenuates hydrogen peroxide induced injury in PC12 cells. Neurosci Lett 2000;292:41-44.
    • (2000) Neurosci Lett , vol.292 , pp. 41-44
    • Zhang, H.Y.1    Tang, X.C.2    Huperzine, B.3
  • 125
    • 34247581682 scopus 로고    scopus 로고
    • Development of huperzine A and B for treatment of Alzheimer's disease
    • Bai D. Development of huperzine A and B for treatment of Alzheimer's disease. Pure Appl Chem 2007;79:469-79.
    • (2007) Pure Appl Chem , vol.79 , pp. 469-479
    • Bai, D.1
  • 126
    • 0032458505 scopus 로고    scopus 로고
    • Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica
    • Kryger G, Silman I, Sussman JL. Three-dimensional structure of a complex of E2020 with acetylcholinesterase from Torpedo californica. J Physiol Paris 1998;92:191-4.
    • (1998) J Physiol Paris , vol.92 , pp. 191-194
    • Kryger, G.1    Silman, I.2    Sussman, J.L.3


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