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Volumn 12, Issue 2, 2006, Pages 217-225

The peripheral anionic site of acetylcholinesterase: Structure, functions and potential role in rational drug design

Author keywords

Acetylcholinesterase; Allosterism; Inhibitors; Non cholinergic; Peripheral anionic site; Rational drug design

Indexed keywords

1,5 BIS(4 ALLYLDIMETHYLAMMONIUMPHENYL)PENTAN 3 ONE DIBROMIDE; ACETYLCHOLINESTERASE; AMYLOID BETA PROTEIN; ASPARTIC ACID; CARBAMIC ACID DERIVATIVE; CELL ADHESION MOLECULE; CHOLINESTERASE INHIBITOR; COLLAGEN TYPE 4; DECAMETHONIUM; DONEPEZIL; FASCICULIN; GALLAMINE; HUPERZINE A; LAMININ; ORGANOPHOSPHATE; ORGANOPHOSPHATE PESTICIDE; PROPIDIUM IODIDE; RETINOID; SERINE; SNAKE VENOM; TRYPTOPHAN; TYROSINE; ANION;

EID: 33644867844     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161206775193127     Document Type: Review
Times cited : (253)

References (106)
  • 1
    • 0034285515 scopus 로고    scopus 로고
    • Alpha/Beta hydrolase fold enzymes: Structures, functions and mechanisms
    • Holmquist M. Alpha/Beta hydrolase fold enzymes: structures, functions and mechanisms. Curr Protein Pept Sci 2000; 1: 209-235.
    • (2000) Curr Protein Pept Sci , vol.1 , pp. 209-235
    • Holmquist, M.1
  • 2
    • 0025606148 scopus 로고
    • Drosophila neurotactin, a surface glycorprotein with homology to serine esterases is dynamically expressed dyring embryogenesis
    • Hortsch M, Patel NH, Bieber AJ, Traquina ZR, Goodman CS. Drosophila neurotactin, a surface glycorprotein with homology to serine esterases is dynamically expressed dyring embryogenesis. Development 1990; 110: 1327-1340.
    • (1990) Development , vol.110 , pp. 1327-1340
    • Hortsch, M.1    Patel, N.H.2    Bieber, A.J.3    Traquina, Z.R.4    Goodman, C.S.5
  • 3
    • 0025270460 scopus 로고
    • Glutactin, a novel Drosophila basement membrane-related glycoprotein with sequence similarity to serine esterases
    • Olson PR, Fessler LI, Nelson RE, Sterne RE, Campbell AG, Fessler JH. Glutactin, a novel Drosophila basement membrane-related glycoprotein with sequence similarity to serine esterases. EMBO J 1990; 9: 1219-1227.
    • (1990) EMBO J , vol.9 , pp. 1219-1227
    • Olson, P.R.1    Fessler, L.I.2    Nelson, R.E.3    Sterne, R.E.4    Campbell, A.G.5    Fessler, J.H.6
  • 4
    • 0029055716 scopus 로고
    • Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-brain barrier in Drosophila
    • Auld VJ, Fetter RD, Broadie K, Goodman CS. Gliotactin, a novel transmembrane protein on peripheral glia, is required to form the blood-brain barrier in Drosophila. Cell 1995; 81: 757-767.
    • (1995) Cell , vol.81 , pp. 757-767
    • Auld, V.J.1    Fetter, R.D.2    Broadie, K.3    Goodman, C.S.4
  • 5
    • 0030026657 scopus 로고    scopus 로고
    • Structures, alternative splicing and neurexin binding of multiple neuroligins
    • Ichtchenko K, Nguyen T, Sudhof TC. Structures, alternative splicing and neurexin binding of multiple neuroligins. J Biol Chem 1996: 271: 2676-2682.
    • (1996) J Biol Chem , vol.271 , pp. 2676-2682
    • Ichtchenko, K.1    Nguyen, T.2    Sudhof, T.C.3
  • 6
    • 0025305481 scopus 로고
    • Humbel BM.Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases
    • Bomblies L, Biegelmann E, During V, Gerisch G, Kraft-Czepa H, Noegel AA, et al. Humbel BM.Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases. J Cell Biol 1990; 110: 669-679.
    • (1990) J Cell Biol , vol.110 , pp. 669-679
    • Bomblies, L.1    Biegelmann, E.2    During, V.3    Gerisch, G.4    Kraft-Czepa, H.5    Noegel, A.A.6
  • 7
    • 0022988692 scopus 로고
    • Primary structure of acetylcholinesterase; implications for regulation and function
    • Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K, Taylor SS, et al. Primary structure of acetylcholinesterase; implications for regulation and function. Fed Proc 1986; 45: 2976-2981.
    • (1986) Fed Proc , vol.45 , pp. 2976-2981
    • Schumacher, M.1    Camp, S.2    Maulet, Y.3    Newton, M.4    MacPhee-Quigley, K.5    Taylor, S.S.6
  • 8
    • 0022870262 scopus 로고
    • Preliminary evidence for a cholinergic-like system in lichen morphogenesis
    • Raineri M, Modenisi P. Preliminary evidence for a cholinergic-like system in lichen morphogenesis. Histochem J 1986; 18: 647-657.
    • (1986) Histochem J , vol.18 , pp. 647-657
    • Raineri, M.1    Modenisi, P.2
  • 9
    • 0345004812 scopus 로고    scopus 로고
    • Evidence for the presence of a mammalian-like cholinesterase in Paramecium primaurelia (Protista, Ciliophora) developmental cycle
    • Delmonte Corrado MU, Politi H, Trielli F, Angelini C, Falugi C. Evidence for the presence of a mammalian-like cholinesterase in Paramecium primaurelia (Protista, Ciliophora) developmental cycle. J Exp Zool 1999; 283: 102-105.
    • (1999) J Exp Zool , vol.283 , pp. 102-105
    • Delmonte Corrado, M.U.1    Politi, H.2    Trielli, F.3    Angelini, C.4    Falugi, C.5
  • 10
    • 0024595550 scopus 로고
    • Molecular analysis of a developmentally regulated gene required for Dictyostelium aggregation
    • Rubino S, Mann SK, Hori RT, Pinko C, Firtel RA. Molecular analysis of a developmentally regulated gene required for Dictyostelium aggregation. Dev Biol 1989; 131: 27-36.
    • (1989) Dev Biol , vol.131 , pp. 27-36
    • Rubino, S.1    Mann, S.K.2    Hori, R.T.3    Pinko, C.4    Firtel, R.A.5
  • 12
    • 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, et al. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991; 253: 872-879.
    • (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
  • 13
    • 0034604236 scopus 로고    scopus 로고
    • Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway
    • Mallender WD, Szegletes T, Rosenberry TL. Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway. Biochemistry 2000; 39: 7753-7763.
    • (2000) Biochemistry , vol.39 , pp. 7753-7763
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 14
    • 0029781839 scopus 로고    scopus 로고
    • Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates
    • Hosea NA, Radic Z, Tsigelny I, Berman HA, Quinn DM, Taylor P. Aspartate 74 as a primary determinant in acetylcholinesterase governing specificity to cationic organophosphonates. Biochemistry 1996; 35: 10995-11004.
    • (1996) Biochemistry , vol.35 , pp. 10995-11004
    • Hosea, N.A.1    Radic, Z.2    Tsigelny, I.3    Berman, H.A.4    Quinn, D.M.5    Taylor, P.6
  • 15
    • 0026031111 scopus 로고
    • Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
    • Radic Z, Reiner E, Taylor P. Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives. Mol Pharmacol 1991; 39: 98-104.
    • (1991) Mol Pharmacol , vol.39 , pp. 98-104
    • Radic, Z.1    Reiner, E.2    Taylor, P.3
  • 16
    • 0033583819 scopus 로고    scopus 로고
    • The adhesion function of acetylcholinesterase is located at the peripheral anionic site
    • Johnson G, Moore SW. The adhesion function of acetylcholinesterase is located at the peripheral anionic site. Biochem Biophys Res Commun 1999; 258: 758-762.
    • (1999) Biochem Biophys Res Commun , vol.258 , pp. 758-762
    • Johnson, G.1    Moore, S.W.2
  • 17
    • 0033607448 scopus 로고    scopus 로고
    • Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase
    • Munoz FJ, Aldunate R, Inestrosa NC. Peripheral binding site is involved in the neurotrophic activity of acetylcholinesterase. Neuroreport 1999; 10: 3621-3625.
    • (1999) Neuroreport , vol.10 , pp. 3621-3625
    • Munoz, F.J.1    Aldunate, R.2    Inestrosa, N.C.3
  • 18
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase acceleerates assembly of amyloid beta-peptides into Alzheimer's fibrils; possible role of the peripheral site of the enzyme
    • Inestrosa NC, Alvarez A, Perez CA, Moreno RD, Vicente M, Linker C, et al. Acetylcholinesterase acceleerates assembly of amyloid beta-peptides into Alzheimer's fibrils; possible role of the peripheral site of the enzyme. Neuron 1996; 16: 881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Perez, C.A.3    Moreno, R.D.4    Vicente, M.5    Linker, C.6
  • 19
    • 0032440687 scopus 로고    scopus 로고
    • Molecular interactions of acetylcholinesterase with senile plaques
    • Inestrosa NC, Alarcon R. Molecular interactions of acetylcholinesterase with senile plaques. J Physiol Paris 1998; 92: 341-344.
    • (1998) J Physiol Paris , vol.92 , pp. 341-344
    • Inestrosa, N.C.1    Alarcon, R.2
  • 20
    • 0033613931 scopus 로고    scopus 로고
    • Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly
    • Bourne Y, Taylor P, Bougis PE, Marchot P. Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly. J Biol Chem 1999; 274: 2963-2970.
    • (1999) J Biol Chem , vol.274 , pp. 2963-2970
    • Bourne, Y.1    Taylor, P.2    Bougis, P.E.3    Marchot, P.4
  • 21
    • 0037472358 scopus 로고    scopus 로고
    • Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site
    • Johnson G, Moore SW. Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site. Neurosci Lett 2003; 337: 37-40.
    • (2003) Neurosci Lett , vol.337 , pp. 37-40
    • Johnson, G.1    Moore, S.W.2
  • 22
    • 0027401977 scopus 로고
    • Tissue-specific expression and alternative mRNA processing of the mammalian acetylcholinesterase gene
    • Li Y, Camp S, Taylor P. Tissue-specific expression and alternative mRNA processing of the mammalian acetylcholinesterase gene. J Biol Chem 1993; 268: 5790-5797.
    • (1993) J Biol Chem , vol.268 , pp. 5790-5797
    • Li, Y.1    Camp, S.2    Taylor, P.3
  • 23
    • 0036560908 scopus 로고    scopus 로고
    • The origin of the molecular diversity and functional anchoring of cholinesterases
    • Massoulie J. The origin of the molecular diversity and functional anchoring of cholinesterases. Neurosignals 2002; 11: 130-143.
    • (2002) Neurosignals , vol.11 , pp. 130-143
    • Massoulie, J.1
  • 24
    • 0027217179 scopus 로고
    • Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the active site, the hydrophobic site and the acyl pocket
    • Ordentlich A, Kronman C, Flashner Y, Leitner M, Segall Y, Ariel N, et al. Dissection of the human acetylcholinesterase active center determinants of substrate specificity. Identification of residues constituting the active site, the hydrophobic site and the acyl pocket. J Biol Chem 1993; 268: 17083-17095.
    • (1993) J Biol Chem , vol.268 , pp. 17083-17095
    • Ordentlich, A.1    Kronman, C.2    Flashner, Y.3    Leitner, M.4    Segall, Y.5    Ariel, N.6
  • 25
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors
    • Radic Z, Pickering NA, Vellom DC, Camp S, Taylor P. Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors. Biochemistry 1993; 32: 12074-12084.
    • (1993) Biochemistry , vol.32 , pp. 12074-12084
    • Radic, Z.1    Pickering, N.A.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 27
    • 0032584583 scopus 로고    scopus 로고
    • Functional characteristics of the oxyanion hole in human acetycholinesterase
    • Ordentlich A, Barak D, Kronman C, Ariel N, Segall Y, Velan B, et al. Functional characteristics of the oxyanion hole in human acetycholinesterase. J Biol Chem 1998; 273: 19509-19517.
    • (1998) J Biol Chem , vol.273 , pp. 19509-19517
    • Ordentlich, A.1    Barak, D.2    Kronman, C.3    Ariel, N.4    Segall, Y.5    Velan, B.6
  • 28
    • 0025132889 scopus 로고
    • Anionic subsites of the acetylcholinesterase from Torpedo californica: Affinity labelling with the cationic reagent N, N-dimethyl-2-phenyl-aziridinium
    • Weise C, Kreienkamp HJ, Raba R, Pedak A, Aaviksaar A. Anionic subsites of the acetylcholinesterase from Torpedo californica: affinity labelling with the cationic reagent N, N-dimethyl-2-phenyl-aziridinium. EMBO J 1990; 9: 3885-8.
    • (1990) EMBO J , vol.9 , pp. 3885-3888
    • Weise, C.1    Kreienkamp, H.J.2    Raba, R.3    Pedak, A.4    Aaviksaar, A.5
  • 29
    • 0026733022 scopus 로고
    • Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding
    • Shafferman A, Kronman C, Flashner Y, Leitner M, Ordentlich A, Gozes Y, et al. Mutagenesis of human acetylcholinesterase. Identification of residues involved in catalytic activity and in polypeptide folding. J Biol Chem 1992; 261: 17640-17648.
    • (1992) J Biol Chem , vol.261 , pp. 17640-17648
    • Shafferman, A.1    Kronman, C.2    Flashner, Y.3    Leitner, M.4    Ordentlich, A.5    Gozes, Y.6
  • 30
    • 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, et al. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci 1993; 2: 366-382.
    • (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
  • 31
    • 0030583585 scopus 로고    scopus 로고
    • Structural modifications of the omega loop in human acetylcholinesterase
    • Velan B, Barak D, Ariel N, Leitner M, Bino T, Ordentlich A, et al. Structural modifications of the omega loop in human acetylcholinesterase. FEBS Lett 1996; 395: 22-28.
    • (1996) FEBS Lett , vol.395 , pp. 22-28
    • Velan, B.1    Barak, D.2    Ariel, N.3    Leitner, M.4    Bino, T.5    Ordentlich, A.6
  • 32
    • 0029911582 scopus 로고    scopus 로고
    • Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function
    • Faerman C, Ripoll D, Bon S, Le Feuvre Y, Morel N, Massoulie J, et al. Site-directed mutants designed to test back-door hypotheses of acetylcholinesterase function. FEBS Lett 1996; 386: 65-71.
    • (1996) FEBS Lett , vol.386 , pp. 65-71
    • Faerman, C.1    Ripoll, D.2    Bon, S.3    Le Feuvre, Y.4    Morel, N.5    Massoulie, J.6
  • 33
    • 0041731891 scopus 로고    scopus 로고
    • Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop
    • Shi J, Tai K, McCammon JA, Taylor P, Johnson DA. Nanosecond dynamics of the mouse acetylcholinesterase cys69-cys96 omega loop. J Biol Chem 2003; 278: 30905-30911.
    • (2003) J Biol Chem , vol.278 , pp. 30905-30911
    • Shi, J.1    Tai, K.2    McCammon, J.A.3    Taylor, P.4    Johnson, D.A.5
  • 34
    • 2942593807 scopus 로고    scopus 로고
    • Acetylcholinesterase: Enhanced fluctuations and alternative routes to the active site in the complex with fasciculin-2
    • Bui JM, Tai Y, McCammon JA. Acetylcholinesterase: enhanced fluctuations and alternative routes to the active site in the complex with fasciculin-2. J Am Chem Soc 2004; 126: 7198-7205.
    • (2004) J Am Chem Soc , vol.126 , pp. 7198-7205
    • Bui, J.M.1    Tai, Y.2    McCammon, J.A.3
  • 35
    • 0031820915 scopus 로고    scopus 로고
    • Electrotactins: A class of adhesion proteins with conserved electrostatic and structural motifs
    • Botti SA, Felder CE, Silman I. Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs. Protein Eng 1998; 11: 415-420.
    • (1998) Protein Eng , vol.11 , pp. 415-420
    • Botti, S.A.1    Felder, C.E.2    Silman, I.3
  • 37
    • 0028270692 scopus 로고
    • Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core
    • Barak D, Kronman C, Ordentlich A, Ariel N, Bromberg A, Marcus D, et al. Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core. J Biol Chem 1994; 269: 6296-6305.
    • (1994) J Biol Chem , vol.269 , pp. 6296-6305
    • Barak, D.1    Kronman, C.2    Ordentlich, A.3    Ariel, N.4    Bromberg, A.5    Marcus, D.6
  • 38
    • 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: 6117-6121.
    • (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
  • 40
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • Bourne Y, Taylor P, Marchot P. Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell 1995; 83: 503-512.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 41
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect
    • Szegletes T, Mallender WD, Thomas PJ, Rosenberry TL. Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 1999; 38: 122-133.
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 42
    • 0014597797 scopus 로고
    • Two types of inhibition by an organophosphorus compound: One the formation of phosphorylated enzyme and the other analogous to inhibition by substrate
    • Aldridge WN, Reiner E. Two types of inhibition by an organophosphorus compound: one the formation of phosphorylated enzyme and the other analogous to inhibition by substrate. Biochem J 1969; 115: 147-162.
    • (1969) Biochem J , vol.115 , pp. 147-162
    • Aldridge, W.N.1    Reiner, E.2
  • 43
    • 0027955949 scopus 로고
    • Expression and ligand specificity of acetylcholinesterase and the nicotinic receptor: A tale of two cholinergic sites
    • Taylor P, Radic Z, Kreienkamp HJ, Maeda R, Luo Z, Fuentes ME, et al. Expression and ligand specificity of acetylcholinesterase and the nicotinic receptor: a tale of two cholinergic sites. Biochem Soc Trans 1994; 22: 740-745.
    • (1994) Biochem Soc Trans , vol.22 , pp. 740-745
    • Taylor, P.1    Radic, Z.2    Kreienkamp, H.J.3    Maeda, R.4    Luo, Z.5    Fuentes, M.E.6
  • 44
    • 0014750669 scopus 로고
    • On the question: Is acetylcholinesterase an allosteric protein?
    • Kitz RJ, Braswell LM, Ginsburg S. On the question: is acetylcholinesterase an allosteric protein? Mol Pharmacol 1970; 6: 108-121.
    • (1970) Mol Pharmacol , vol.6 , pp. 108-121
    • Kitz, R.J.1    Braswell, L.M.2    Ginsburg, S.3
  • 45
    • 0014272825 scopus 로고
    • The reaction of acetylcholinesterase (AChE) with some quaternary hydroxy aminophenols
    • Kitz RJ, Ginsburg S. The reaction of acetylcholinesterase (AChE) with some quaternary hydroxy aminophenols. Biochem Pharmacol 1968; 17: 525-532.
    • (1968) Biochem Pharmacol , vol.17 , pp. 525-532
    • Kitz, R.J.1    Ginsburg, S.2
  • 46
    • 0014879409 scopus 로고
    • Nuclear magnetic resonance studies on acetylcholinesterase. The use of atropine and eserine to probe binding sites
    • Kato G, Yung J, Ihnat M. Nuclear magnetic resonance studies on acetylcholinesterase. The use of atropine and eserine to probe binding sites. Mol Pharmacol 1970; 6: 588-596.
    • (1970) Mol Pharmacol , vol.6 , pp. 588-596
    • Kato, G.1    Yung, J.2    Ihnat, M.3
  • 47
    • 0013945471 scopus 로고
    • Responses of acetylcholinesterase from Torpedo marmorata to salts curarizing agents
    • Changeux JP. Responses of acetylcholinesterase from Torpedo marmorata to salts curarizing agents. Mol Pharmacol 1966; 2: 369-392.
    • (1966) Mol Pharmacol , vol.2 , pp. 369-392
    • Changeux, J.P.1
  • 48
    • 0028845803 scopus 로고
    • Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite
    • Barak D, Ordentlick A, Bromberg A, Kronman C, Marcus D, Lazar A, et al. Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite. Biochemistry 1995; 34: 15444-15452.
    • (1995) Biochemistry , vol.34 , pp. 15444-15452
    • Barak, D.1    Ordentlick, A.2    Bromberg, A.3    Kronman, C.4    Marcus, D.5    Lazar, A.6
  • 49
    • 0029133139 scopus 로고
    • Allosteric control of acetylcholinesterase by fasciculin
    • Radic Z, Quinn DM, Vellom DC, Camp S, Taylor P. Allosteric control of acetylcholinesterase by fasciculin. J Biol Chem 1995; 270: 20391-20399.
    • (1995) J Biol Chem , vol.270 , pp. 20391-20399
    • Radic, Z.1    Quinn, D.M.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 50
    • 0026794595 scopus 로고
    • Expression of recombinant acetylcholinesterase in a baculovirus system: Kinetic properties of glutamate 199 mutants
    • Radic Z, Gibney G, Kawamoto S, MacPhee-Quigley K, Bongiorno C, Taylor P. Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants. Biochemistry 1992; 31: 9760-9767.
    • (1992) Biochemistry , vol.31 , pp. 9760-9767
    • Radic, Z.1    Gibney, G.2    Kawamoto, S.3    MacPhee-Quigley, K.4    Bongiorno, C.5    Taylor, P.6
  • 51
    • 0029067038 scopus 로고
    • Different effects of two peripheral anionic site-binding ligands on acetylcholinesterase active-site gorge topography revealed by electron paramagnetic resonance
    • Grubic Z, Stalc A, Sentjuro M, Pecar S, Gentry MK, Doctor BP. Different effects of two peripheral anionic site-binding ligands on acetylcholinesterase active-site gorge topography revealed by electron paramagnetic resonance. Biochim Biophys Acta 1995; 1249: 155-160.
    • (1995) Biochim Biophys Acta , vol.1249 , pp. 155-160
    • Grubic, Z.1    Stalc, A.2    Sentjuro, M.3    Pecar, S.4    Gentry, M.K.5    Doctor, B.P.6
  • 52
    • 0346355503 scopus 로고    scopus 로고
    • Reversibly bound and covalently attached ligands induce conformational changes in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase
    • Shi J, Boyd AE, Radic Z, Taylor P. Reversibly bound and covalently attached ligands induce conformational changes in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase. J Biol Chem 2001, 276: 42196-42204.
    • (2001) J Biol Chem , vol.276 , pp. 42196-42204
    • Shi, J.1    Boyd, A.E.2    Radic, Z.3    Taylor, P.4
  • 53
    • 0037044841 scopus 로고    scopus 로고
    • Inhibitors of different structure induce distinguishing conformations in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase
    • Shi J, Radic, Z, Taylor P. Inhibitors of different structure induce distinguishing conformations in the omega loop, Cys69-Cys96, of mouse acetylcholinesterase. J Biol Chem 2002, 277: 43301-43308.
    • (2002) J Biol Chem , vol.277 , pp. 43301-43308
    • Shi, J.1    Radic, Z.2    Taylor, P.3
  • 54
    • 0027336819 scopus 로고
    • 125I-fasciculin to rat brain acetylcholinesterase: The complex still binds diisopropyl fluorophosphate
    • 125I-fasciculin to rat brain acetylcholinesterase: the complex still binds diisopropyl fluorophosphate. J Biol Chem 1993; 268: 12458-12467.
    • (1993) J Biol Chem , vol.268 , pp. 12458-12467
    • Marchot, P.1    Khelif, A.2    Ji, Y.H.3    Mansuelle, P.4    Bougis, P.E.5
  • 55
    • 0027459560 scopus 로고
    • Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity
    • Vellom DC, Radic Z, Li Y, Pickering NA, Camp S, Taylor P. Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity. Biochemistry 1993; 32: 12-17.
    • (1993) Biochemistry , vol.32 , pp. 12-17
    • Vellom, D.C.1    Radic, Z.2    Li, Y.3    Pickering, N.A.4    Camp, S.5    Taylor, P.6
  • 56
    • 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: 191-194.
    • (1998) J Physiol Paris , vol.92 , pp. 191-194
    • Kryger, G.1    Silman, I.2    Sussman, J.L.3
  • 57
    • 0036793068 scopus 로고    scopus 로고
    • Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase
    • Felder CE, Harel M, Silman I, Sussman JL. Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase. Acta Crystallogr D Biol Crystallogr 2002; 58: 1765-1771.
    • (2002) Acta Crystallogr D Biol Crystallogr , vol.58 , pp. 1765-1771
    • Felder, C.E.1    Harel, M.2    Silman, I.3    Sussman, J.L.4
  • 58
    • 0037015151 scopus 로고    scopus 로고
    • X-ray structure of Torpedo californica acetylcholinesterase complexed with (-)-huperzine A (-)-huperzine B: Structural evidence for an active site rearrangement
    • Dvir H, Jiang HL, Wong DM, Harel M, Chetrit M, He XC, et al. X-ray structure of Torpedo californica acetylcholinesterase complexed with (-)-huperzine A (-)-huperzine B: Structural evidence for an active site rearrangement. Biochemistry 2002; 41: 10810-10818.
    • (2002) Biochemistry , vol.41 , pp. 10810-10818
    • Dvir, H.1    Jiang, H.L.2    Wong, D.M.3    Harel, M.4    Chetrit, M.5    He, X.C.6
  • 59
    • 0000140355 scopus 로고    scopus 로고
    • Nonequilibrium analysis alters the mechamistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands
    • Szegletes T, Mallender WD, Rosenberry TL. Nonequilibrium analysis alters the mechamistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands. Biochemistry 1998, 37: 4206-4216.
    • (1998) Biochemistry , vol.37 , pp. 4206-4216
    • Szegletes, T.1    Mallender, W.D.2    Rosenberry, T.L.3
  • 60
    • 0035968202 scopus 로고    scopus 로고
    • Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites
    • De Ferrari GV, Mallender WD, Inestrosa NC, Rosenberry TL. Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. J Biol Chem 2001; 276: 23282-23287.
    • (2001) J Biol Chem , vol.276 , pp. 23282-23287
    • De Ferrari, G.V.1    Mallender, W.D.2    Inestrosa, N.C.3    Rosenberry, T.L.4
  • 62
    • 0029646114 scopus 로고
    • Crystal structure of an acetylcholinesterase-fasciculin complex: Interaction of a three-fingered toxin from snake venom with its target
    • Harel M, Kleywegt GJ, Ravelli RB, Silman I, Sussman JL. Crystal structure of an acetylcholinesterase-fasciculin complex: interaction of a three-fingered toxin from snake venom with its target. Structure 1995; 3: 1355-1366.
    • (1995) Structure , vol.3 , pp. 1355-1366
    • Harel, M.1    Kleywegt, G.J.2    Ravelli, R.B.3    Silman, I.4    Sussman, J.L.5
  • 63
    • 0027934296 scopus 로고
    • Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase
    • Shafferman A, Ordentlich A, Barak D, Kronman C, Ber R, Bino T, et al. Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase. EMBO J 1994; 13: 3448-3455.
    • (1994) EMBO J , vol.13 , pp. 3448-3455
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Kronman, C.4    Ber, R.5    Bino, T.6
  • 65
    • 0027386759 scopus 로고
    • Acetylcholinesterase: Electrostatic steering increases the rate of ligand binding
    • Tan RC, Truong TN, McCammon JA, Sussman JL. Acetylcholinesterase: electrostatic steering increases the rate of ligand binding. Biochemistry 1993; 32: 401-403.
    • (1993) Biochemistry , vol.32 , pp. 401-403
    • Tan, R.C.1    Truong, T.N.2    McCammon, J.A.3    Sussman, J.L.4
  • 66
    • 0029665127 scopus 로고    scopus 로고
    • Asp7O in the peripheral anionic site of human butyrlcholinesterase
    • Masson P, Froment MT, Bartels CF, Lockridge O. Asp7O in the peripheral anionic site of human butyrlcholinesterase. Eur J Biochem 1996; 235: 36-48.
    • (1996) Eur J Biochem , vol.235 , pp. 36-48
    • Masson, P.1    Froment, M.T.2    Bartels, C.F.3    Lockridge, O.4
  • 67
    • 0015549413 scopus 로고
    • The influence of ionic strength on the interaction of quaternary drugs with mammalian acetylcholinesterase in relation to possible regulatory effects
    • Crone HD. The influence of ionic strength on the interaction of quaternary drugs with mammalian acetylcholinesterase in relation to possible regulatory effects. J Neurochem 1973; 20: 225-236.
    • (1973) J Neurochem , vol.20 , pp. 225-236
    • Crone, H.D.1
  • 68
    • 0030828982 scopus 로고    scopus 로고
    • Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin
    • Radic Z, Kirchhoff PD, Quinn DM, McCammon JA, Taylor P. Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin. J Biol Chem 1997; 272: 23265-23267.
    • (1997) J Biol Chem , vol.272 , pp. 23265-23267
    • Radic, Z.1    Kirchhoff, P.D.2    Quinn, D.M.3    McCammon, J.A.4    Taylor, P.5
  • 69
    • 0029163984 scopus 로고
    • Novel functions of cholinesterases in development, physiology and disease
    • Layer PG, Willbold E. Novel functions of cholinesterases in development, physiology and disease. Prog Histochem Cytochem 1995; 29: 1-94.
    • (1995) Prog Histochem Cytochem , vol.29 , pp. 1-94
    • Layer, P.G.1    Willbold, E.2
  • 70
    • 0037008862 scopus 로고    scopus 로고
    • Parkinson's disease, Alzheimer's disease and motor neurone disease: Identifying a common mechanism
    • Greenfield S, Vaux DJ. Parkinson's disease, Alzheimer's disease and motor neurone disease: identifying a common mechanism. Neuroscience 2002; 113: 485-492.
    • (2002) Neuroscience , vol.113 , pp. 485-492
    • Greenfield, S.1    Vaux, D.J.2
  • 71
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism
    • Layer PG, Weikert T, Alber R. Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism. Cell Tissue Res 1993; 272: 219-226.
    • (1993) Cell Tissue Res , vol.272 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 72
    • 0028819272 scopus 로고
    • Cholinergic regulation of neurite outgrowth from isolated chick sympathetic neurons in culture
    • Small DH, Reed G, Whitefield B, Nurcombe V. Cholinergic regulation of neurite outgrowth from isolated chick sympathetic neurons in culture. J Neurosci 1995; 15: 144-151.
    • (1995) J Neurosci , vol.15 , pp. 144-151
    • Small, D.H.1    Reed, G.2    Whitefield, B.3    Nurcombe, V.4
  • 73
    • 0034647050 scopus 로고    scopus 로고
    • Evidence for the direct role of acetylcholinesteras in neurite outgrowth in primary dorsal root ganglion neurons
    • Bigbee JW, Sharma KV, Chan EL, Bogler O. Evidence for the direct role of acetylcholinesteras in neurite outgrowth in primary dorsal root ganglion neurons. Brain Res 2000; 861: 354-362.
    • (2000) Brain Res , vol.861 , pp. 354-362
    • Bigbee, J.W.1    Sharma, K.V.2    Chan, E.L.3    Bogler, O.4
  • 74
    • 0030045560 scopus 로고    scopus 로고
    • Overexpression of laternative human acetylcholinesterase forms modulates process extensions in cultured glioma cells
    • Karpel R, Sternfeld M, Ginzberg D, Guhl E, Graessmann A, Soreq H. Overexpression of laternative human acetylcholinesterase forms modulates process extensions in cultured glioma cells. J Neurochem 1996; 66: 114-123.
    • (1996) J Neurochem , vol.66 , pp. 114-123
    • Karpel, R.1    Sternfeld, M.2    Ginzberg, D.3    Guhl, E.4    Graessmann, A.5    Soreq, H.6
  • 75
    • 0030985407 scopus 로고    scopus 로고
    • Neurite differentiation is modulated in neuroblastoma cells engineered for altered acetylcholinesterase expression
    • Koenigsberger C, Chiappa S, Brimijoin S. Neurite differentiation is modulated in neuroblastoma cells engineered for altered acetylcholinesterase expression. J Neurochem 1997: 69: 1389-1397.
    • (1997) J Neurochem , vol.69 , pp. 1389-1397
    • Koenigsberger, C.1    Chiappa, S.2    Brimijoin, S.3
  • 76
    • 0034525702 scopus 로고    scopus 로고
    • Cholinesterases modulate cell adhesion in human neuroblastoma cells in vitro
    • Johnson G, Moore SW. Cholinesterases modulate cell adhesion in human neuroblastoma cells in vitro. Int J Dev Neurosci 2000; 18: 781-790.
    • (2000) Int J Dev Neurosci , vol.18 , pp. 781-790
    • Johnson, G.1    Moore, S.W.2
  • 77
    • 0032520131 scopus 로고    scopus 로고
    • Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein and variable C termini
    • Sternfeld M, Ming G, Song H, Sela K, Timberg R, Poo M, et al. Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein and variable C termini. J Neurosci 1998; 18: 1240-1249.
    • (1998) J Neurosci , vol.18 , pp. 1240-1249
    • Sternfeld, M.1    Ming, G.2    Song, H.3    Sela, K.4    Timberg, R.5    Poo, M.6
  • 78
    • 0030750402 scopus 로고    scopus 로고
    • Non-cholinergic trophic action of recombinant acetylcholinesterase on mid-brain dopaminergic neurons
    • Holmes C, Jones SA, Budd TC, Greenfield SA. Non-cholinergic trophic action of recombinant acetylcholinesterase on mid-brain dopaminergic neurons. J Neurosci Res 2000; 49: 207-218.
    • (2000) J Neurosci Res , vol.49 , pp. 207-218
    • Holmes, C.1    Jones, S.A.2    Budd, T.C.3    Greenfield, S.A.4
  • 79
    • 0036237097 scopus 로고    scopus 로고
    • Increased expression of intranuclear acetylcholinesterase involved in apoptosis of SK-N-SH cells
    • Yang L, He HY, Zhang XJ. Increased expression of intranuclear acetylcholinesterase involved in apoptosis of SK-N-SH cells. Neurosci Res 2002; 42: 261-268.
    • (2002) Neurosci Res , vol.42 , pp. 261-268
    • Yang, L.1    He, H.Y.2    Zhang, X.J.3
  • 80
    • 0036024019 scopus 로고    scopus 로고
    • Induction of acetylcholinesterase expression during apoptosis in various cell types
    • Zhang XJ, Yang L, Zhao Q, Caen JP, He HY, Jin QH, et al. Induction of acetylcholinesterase expression during apoptosis in various cell types. Cell Death Differ 2002; 9: 790-800.
    • (2002) Cell Death Differ , vol.9 , pp. 790-800
    • Zhang, X.J.1    Yang, L.2    Zhao, Q.3    Caen, J.P.4    He, H.Y.5    Jin, Q.H.6
  • 81
    • 0031550623 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes regeneration of neurites in cultured adult neurons of Aplysia
    • Srivatsan M, Peretz B. Acetylcholinesterase promotes regeneration of neurites in cultured adult neurons of Aplysia. Neuroscience 1997; 77: 9211-9231.
    • (1997) Neuroscience , vol.77 , pp. 9211-9231
    • Srivatsan, M.1    Peretz, B.2
  • 82
    • 0028027279 scopus 로고
    • Antisense oligonucleotide inhibition of acetylcholinesterase gene expression induces progenitor cell expansion and suppresses hematopoietic apoptosis ex vivo
    • Soreq H, Patinkin D, Lev-Lehman E, Grifman M, Girzberg D, Eckstein F, et al. Antisense oligonucleotide inhibition of acetylcholinesterase gene expression induces progenitor cell expansion and suppresses hematopoietic apoptosis ex vivo. Proc Natl Acad Sci USA 1994; 91: 7907-7911.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 7907-7911
    • Soreq, H.1    Patinkin, D.2    Lev-Lehman, E.3    Grifman, M.4    Girzberg, D.5    Eckstein, F.6
  • 83
    • 0034104866 scopus 로고    scopus 로고
    • Extraneuronal cholinergic system in lymphocytes
    • Kawashima K, Fujii T. Extraneuronal cholinergic system in lymphocytes. Pharmacol Ther 2000; 86: 29-48.
    • (2000) Pharmacol Ther , vol.86 , pp. 29-48
    • Kawashima, K.1    Fujii, T.2
  • 84
    • 2642554616 scopus 로고    scopus 로고
    • Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV
    • Johnson G, Moore SW. Identification of a structural site on acetylcholinesterase that promotes neurite outgrowth and binds laminin-1 and collagen IV. Biochem Biophys Res Commun 2004; 319: 448-455.
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 448-455
    • Johnson, G.1    Moore, S.W.2
  • 85
    • 0035807054 scopus 로고    scopus 로고
    • A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation
    • De Ferrari GV, Canales MA, Shin I, Weiner LM, Silman I, Inestrosa NC. A structural motif of acetylcholinesterase that promotes amyloid beta-peptide fibril formation. Biochemistry 2001; 40: 10447-10457.
    • (2001) Biochemistry , vol.40 , pp. 10447-10457
    • De Ferrari, G.V.1    Canales, M.A.2    Shin, I.3    Weiner, L.M.4    Silman, I.5    Inestrosa, N.C.6
  • 86
    • 0034119973 scopus 로고    scopus 로고
    • Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase
    • Xie W, Stribley JA, Chatonnet A, Wilder PJ, Rizzino A, McComb RD, et al. Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase. J Pharmacol Exp Ther 2000; 29: 896-902.
    • (2000) J Pharmacol Exp Ther , vol.29 , pp. 896-902
    • Xie, W.1    Stribley, J.A.2    Chatonnet, A.3    Wilder, P.J.4    Rizzino, A.5    McComb, R.D.6
  • 87
    • 0036837162 scopus 로고    scopus 로고
    • Catalytic antibodies with acetylcholinesterase activity
    • Johnson G, Moore SW. Catalytic antibodies with acetylcholinesterase activity. J Immumol Methods 2002; 269: 13-28.
    • (2002) J Immumol Methods , vol.269 , pp. 13-28
    • Johnson, G.1    Moore, S.W.2
  • 88
    • 0032506149 scopus 로고    scopus 로고
    • Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis
    • Grifman M, Galyam N Seidman S, Soreq H. Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis. Proc Natl Acad Sci USA 1999; 95: 13935-13940.
    • (1999) Proc Natl Acad Sci USA , vol.95 , pp. 13935-13940
    • Grifman, M.1    Galyam, N.2    Seidman, S.3    Soreq, H.4
  • 89
    • 0037413712 scopus 로고    scopus 로고
    • Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site
    • Bourne Y, Taylor P, Radic, Z, Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J 2003; 22: 1-12.
    • (2003) EMBO J , vol.22 , pp. 1-12
    • Bourne, Y.1    Taylor, P.2    Radic, Z.3    Marchot, P.4
  • 90
    • 2942720656 scopus 로고    scopus 로고
    • Nanosecond dynamics of acetylcholinesterase near the active center gorge
    • Boyd AE, Dunlop CS, Wong L, Radic Z, Taylor P, Johnson DA. Nanosecond dynamics of acetylcholinesterase near the active center gorge. J Biol Chem 2004; 279: 26612-26618.
    • (2004) J Biol Chem , vol.279 , pp. 26612-26618
    • Boyd, A.E.1    Dunlop, C.S.2    Wong, L.3    Radic, Z.4    Taylor, P.5    Johnson, D.A.6
  • 91
    • 0029070171 scopus 로고
    • Omega loops: Nonregular secondary structures signficant in protein function and stability
    • Fetrow JS. Omega loops: nonregular secondary structures signficant in protein function and stability. FASEB J 1995; 9: 708-717.
    • (1995) FASEB J , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 92
    • 0037413568 scopus 로고    scopus 로고
    • Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective and highly potent cholinesterase inhibitors
    • Savini L, Gaeta A, Fatturusso C, Catalanotti B, Campiani G, Chiasserini L, et al. Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective and highly potent cholinesterase inhibitors. J Med Chem 2003; 46: 1-4.
    • (2003) J Med Chem , vol.46 , pp. 1-4
    • Savini, L.1    Gaeta, A.2    Fatturusso, C.3    Catalanotti, B.4    Campiani, G.5    Chiasserini, L.6
  • 95
    • 0036480510 scopus 로고    scopus 로고
    • Rational design of reversible acetylcholinesterase inhibitors
    • Barril X, Kalko SG, Orozco M, Luque FJ. Rational design of reversible acetylcholinesterase inhibitors. Mini Rev Med Chem 2002; 2: 27-36.
    • (2002) Mini Rev Med Chem , vol.2 , pp. 27-36
    • Barril, X.1    Kalko, S.G.2    Orozco, M.3    Luque, F.J.4
  • 96
    • 0035468115 scopus 로고    scopus 로고
    • Peripheral and dual binding site acetylcholinesterase inhibitors: Implications in treatment of Alzheimer's disease
    • Castro A, Martinez A. Peripheral and dual binding site acetylcholinesterase inhibitors: implications in treatment of Alzheimer's disease. Mini Rev Med Chem 2001; 1: 267-272.
    • (2001) Mini Rev Med Chem , vol.1 , pp. 267-272
    • Castro, A.1    Martinez, A.2
  • 97
    • 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: 515-522.
    • (2003) Neurochem Res , vol.28 , pp. 515-522
    • Giacobini, E.1
  • 98
    • 0037492336 scopus 로고    scopus 로고
    • Rational design of alkylene-linked bis-pyridiniumal-doximes as improved acetylcholinesterase reactivators
    • Pang YP, Kollmeyer TM, Hong F, Lee JC, Hammond PI, Haugabouk SP, et al. Rational design of alkylene-linked bis-pyridiniumal-doximes as improved acetylcholinesterase reactivators. Chem Biol 2002; 10: 491-502.
    • (2002) Chem Biol , vol.10 , pp. 491-502
    • Pang, Y.P.1    Kollmeyer, T.M.2    Hong, F.3    Lee, J.C.4    Hammond, P.I.5    Haugabouk, S.P.6
  • 99
    • 0037313656 scopus 로고    scopus 로고
    • Current targets for anticancer drug discovery
    • Nam NH, Parang K. Current targets for anticancer drug discovery. Curr Drug Targets 2003; 4: 159-179.
    • (2003) Curr Drug Targets , vol.4 , pp. 159-179
    • Nam, N.H.1    Parang, K.2
  • 100
    • 0344394175 scopus 로고    scopus 로고
    • Retinoids in cancer therapy and chemoprevention: Promise meets resistance
    • Freemantle SJ, Spinella MJ, Dmitrovsky R. Retinoids in cancer therapy and chemoprevention: promise meets resistance. Oncogene 2003; 22: 7305-7315.
    • (2003) Oncogene , vol.22 , pp. 7305-7315
    • Freemantle, S.J.1    Spinella, M.J.2    Dmitrovsky, R.3
  • 101
    • 0036618860 scopus 로고    scopus 로고
    • Retinoids in combination therapies for the treatment of cancer: Mechanisms and perspectives
    • Ortiz MA, Bayar Y, Lopez-Hernandez FJ, Piedrafita FJ. Retinoids in combination therapies for the treatment of cancer: mechanisms and perspectives. Drug Resist Updat 2002; 5: 162-175.
    • (2002) Drug Resist Updat , vol.5 , pp. 162-175
    • Ortiz, M.A.1    Bayar, Y.2    Lopez-Hernandez, F.J.3    Piedrafita, F.J.4
  • 102
    • 2442545500 scopus 로고    scopus 로고
    • Anti-acetylcholinesterase antibody in myasthenic syndrome
    • Tang J, Yuan J, Hao H. Anti-acetylcholinesterase antibody in myasthenic syndrome. Chin Med J (Engl) 1997; 110: 698-700.
    • (1997) Chin Med J (Engl) , vol.110 , pp. 698-700
    • Tang, J.1    Yuan, J.2    Hao, H.3
  • 103
    • 0030971991 scopus 로고    scopus 로고
    • Clinically insignificant (natural) autoantibodies against acetyl cholinesterase in the sera of patients with a variety of neurologic, muscular and autoimmune diseases
    • Lidar T, Christian A, Yakar S, Langevitz P, Zeilig G, Ohry A, et al. Clinically insignificant (natural) autoantibodies against acetyl cholinesterase in the sera of patients with a variety of neurologic, muscular and autoimmune diseases. Immunol Left 1997; 55: 79-84.
    • (1997) Immunol Left , vol.55 , pp. 79-84
    • Lidar, T.1    Christian, A.2    Yakar, S.3    Langevitz, P.4    Zeilig, G.5    Ohry, A.6
  • 104
    • 0029074656 scopus 로고
    • Antibodies to acetylcholinesterase cross-reacting with thyroglobulin in myasthenia gravis and Graves's disease
    • Mappouras DG, Philippou G, Haralambous S. Antibodies to acetylcholinesterase cross-reacting with thyroglobulin in myasthenia gravis and Graves's disease. Clin Exp Immunol 1995; 100: 336-343.
    • (1995) Clin Exp Immunol , vol.100 , pp. 336-343
    • Mappouras, D.G.1    Philippou, G.2    Haralambous, S.3
  • 105
    • 0027517150 scopus 로고
    • Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polyrmorphism
    • Bartels CF, Zelinski T, Lockridge O. Mutation at codon 322 in the human acetylcholinesterase (ACHE) gene accounts for YT blood group polyrmorphism. Am J Hum Genet 1993; 52: 928-936.
    • (1993) Am J Hum Genet , vol.52 , pp. 928-936
    • Bartels, C.F.1    Zelinski, T.2    Lockridge, O.3
  • 106
    • 0027489204 scopus 로고
    • Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: Production of a catalytic antibody with a cholinesterase activity
    • Izadyar L, Friboulet A, Remy M-H, Roseto A, Thomas D. Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: production of a catalytic antibody with a cholinesterase activity. Proc Natl Acad Sci USA 1993; 90: 8876-8880.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 8876-8880
    • Izadyar, L.1    Friboulet, A.2    Remy, M.-H.3    Roseto, A.4    Thomas, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.