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Volumn 175, Issue 1-3, 2008, Pages 30-44

Old and new questions about cholinesterases

Author keywords

Cholinesterase; Evolution; Folding; Post translational modifications; Secretion

Indexed keywords

CHOLINESTERASE; COLLAGEN; COLLAGEN Q; PROTEIN PRIMA; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

EID: 50649089387     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.04.039     Document Type: Article
Times cited : (78)

References (175)
  • 1
    • 0000905202 scopus 로고
    • Über humorale Übertragarbeit der Herznervenwirkung. XI Über den Mechanismus der Vaguswirkung von Physostoigmin und Ergotamin
    • Loewi O., and Navratil E. Über humorale Übertragarbeit der Herznervenwirkung. XI Über den Mechanismus der Vaguswirkung von Physostoigmin und Ergotamin. Pflügers Arch. 214 (1926) 689-696
    • (1926) Pflügers Arch. , vol.214 , pp. 689-696
    • Loewi, O.1    Navratil, E.2
  • 2
    • 0000162994 scopus 로고
    • Choline-esterase. An enzyme present in the blood serum of the horse
    • Stedman E., and Easson L.H. Choline-esterase. An enzyme present in the blood serum of the horse. Biochem. J. 26 (1932) 2056-2066
    • (1932) Biochem. J. , vol.26 , pp. 2056-2066
    • Stedman, E.1    Easson, L.H.2
  • 3
    • 0001488498 scopus 로고
    • Cholinesterase in the blood of man
    • Alles G.A., and Hawes R.C. Cholinesterase in the blood of man. J. Biol. Chem. 133 (1940) 375-390
    • (1940) J. Biol. Chem. , vol.133 , pp. 375-390
    • Alles, G.A.1    Hawes, R.C.2
  • 4
    • 0343899610 scopus 로고
    • Specific tests for true cholinesterase and pseudo-cholinesterase
    • Mendel B., and Rudney H. Specific tests for true cholinesterase and pseudo-cholinesterase. Biochem. J. 37 (1943) 473-476
    • (1943) Biochem. J. , vol.37 , pp. 473-476
    • Mendel, B.1    Rudney, H.2
  • 5
    • 0002503613 scopus 로고
    • Distinction between acetylcholine-esterase and other choline ester-splitting enzymes
    • Augustinsson K.B., and Nachmansohn D. Distinction between acetylcholine-esterase and other choline ester-splitting enzymes. Science 110 (1949) 98-99
    • (1949) Science , vol.110 , pp. 98-99
    • Augustinsson, K.B.1    Nachmansohn, D.2
  • 6
    • 50649119070 scopus 로고    scopus 로고
    • G.B. Koelle, Cholinesterases and anticholinesterase agents, Handbuch der experimentellen Pharmakologie, 1963.
    • G.B. Koelle, Cholinesterases and anticholinesterase agents, Handbuch der experimentellen Pharmakologie, 1963.
  • 7
    • 0012119061 scopus 로고
    • Chemical nature of DFP-binding site of pseudocholinesterase
    • Jansz H.J., Brons D., and Warringa M.G.P.J. Chemical nature of DFP-binding site of pseudocholinesterase. Biochem. Biophys. Acta 34 (1959) 573-575
    • (1959) Biochem. Biophys. Acta , vol.34 , pp. 573-575
    • Jansz, H.J.1    Brons, D.2    Warringa, M.G.P.J.3
  • 8
    • 0006910255 scopus 로고
    • Sur la biochimie de la cholinestérase. Préparation de l'enzyme, rôle de groupements SH
    • Nachmansohn D., and Lederer E. Sur la biochimie de la cholinestérase. Préparation de l'enzyme, rôle de groupements SH. Bull. Soc. Chim. Biol. 21 (1939) 797-808
    • (1939) Bull. Soc. Chim. Biol. , vol.21 , pp. 797-808
    • Nachmansohn, D.1    Lederer, E.2
  • 9
    • 0014877189 scopus 로고
    • Use of a snake venom toxin to characterize the cholinergic receptor protein
    • Changeux J.-P., Kasai M., and Lee C.Y. Use of a snake venom toxin to characterize the cholinergic receptor protein. Proc. Natl. Acad. Sci. U.S.A. 67 (1970) 1241-1247
    • (1970) Proc. Natl. Acad. Sci. U.S.A. , vol.67 , pp. 1241-1247
    • Changeux, J.-P.1    Kasai, M.2    Lee, C.Y.3
  • 10
    • 28744432658 scopus 로고    scopus 로고
    • The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring
    • Massoulié J., Bon S., Perrier N., and Falasca C. The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring. Chem. Biol. Interact. 157/158 (2005) 3-14
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 3-14
    • Massoulié, J.1    Bon, S.2    Perrier, N.3    Falasca, C.4
  • 11
    • 0036560908 scopus 로고    scopus 로고
    • The origin of the molecular diversity and functional anchoring of cholinesterases
    • Massoulié J. The origin of the molecular diversity and functional anchoring of cholinesterases. NeuroSignals 11 (2002) 130-143
    • (2002) NeuroSignals , vol.11 , pp. 130-143
    • Massoulié, J.1
  • 14
    • 0023371687 scopus 로고
    • cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5′-untranslated regions
    • Sikorav J.L., Krejci E., and Massoulié J. cDNA sequences of Torpedo marmorata acetylcholinesterase: primary structure of the precursor of a catalytic subunit; existence of multiple 5′-untranslated regions. EMBO J. 6 7 (1987) 1865-1873
    • (1987) EMBO J. , vol.6 , Issue.7 , pp. 1865-1873
    • Sikorav, J.L.1    Krejci, E.2    Massoulié, J.3
  • 15
    • 0025735608 scopus 로고
    • Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells
    • Krejci E., Coussen F., Duval N., Chatel J.M., Legay C., Puype M., Vandekerckhove J., Cartaud J., Bon S., and Massoulié J. Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells. EMBO J. 10 5 (1991) 1285-1293
    • (1991) EMBO J. , vol.10 , Issue.5 , pp. 1285-1293
    • Krejci, E.1    Coussen, F.2    Duval, N.3    Chatel, J.M.4    Legay, C.5    Puype, M.6    Vandekerckhove, J.7    Cartaud, J.8    Bon, S.9    Massoulié, J.10
  • 17
    • 0037122918 scopus 로고    scopus 로고
    • PRiMA, the membrane anchor of acetylcholinesterase in brain
    • Perrier A.L., Massoulié J., and Krejci E. PRiMA, the membrane anchor of acetylcholinesterase in brain. Neuron 33 (2002) 275-285
    • (2002) Neuron , vol.33 , pp. 275-285
    • Perrier, A.L.1    Massoulié, J.2    Krejci, E.3
  • 18
    • 0031016694 scopus 로고    scopus 로고
    • Quaternary associations of acetylcholinesterase. II. The polyproline attachment domain of the collagen tail
    • Bon S., Coussen F., and Massoulié J. Quaternary associations of acetylcholinesterase. II. The polyproline attachment domain of the collagen tail. J. Biol. Chem. 272 (1997) 3016-3021
    • (1997) J. Biol. Chem. , vol.272 , pp. 3016-3021
    • Bon, S.1    Coussen, F.2    Massoulié, J.3
  • 19
    • 1642458122 scopus 로고    scopus 로고
    • The C-terminal t peptide of acetylcholinesterase forms an alpha helix that supports homomeric and heteromeric interactions
    • Bon S., Dufourcq J., Leroy J., Cornut I., and Massoulié J. The C-terminal t peptide of acetylcholinesterase forms an alpha helix that supports homomeric and heteromeric interactions. Eur. J. Biochem. 271 (2004) 33-47
    • (2004) Eur. J. Biochem. , vol.271 , pp. 33-47
    • Bon, S.1    Dufourcq, J.2    Leroy, J.3    Cornut, I.4    Massoulié, J.5
  • 20
    • 10044230413 scopus 로고    scopus 로고
    • Structural insight into tetramerization of the synaptic form of acetylcholinesterase: interaction of a polyproline II helix with four WWW motifs
    • Dvir H., Harel M., Bon S., Liu W.Q., Vidal M., Garbay C., Sussman J.L., Massoulié J., and Silman I. Structural insight into tetramerization of the synaptic form of acetylcholinesterase: interaction of a polyproline II helix with four WWW motifs. EMBO J. 23 (2004) 4394-4405
    • (2004) EMBO J. , vol.23 , pp. 4394-4405
    • Dvir, H.1    Harel, M.2    Bon, S.3    Liu, W.Q.4    Vidal, M.5    Garbay, C.6    Sussman, J.L.7    Massoulié, J.8    Silman, I.9
  • 21
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein
    • Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., and Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253 (1991) 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    Silman, I.7
  • 22
    • 0033573373 scopus 로고    scopus 로고
    • Differences in expression of acetylcholinesterase and collagen Q control the distribution and oligomerization of the collagen-tailed forms in fast and slow muscles
    • Krejci E., Legay C., Thomine S., Sketelj J., and Massoulié J. Differences in expression of acetylcholinesterase and collagen Q control the distribution and oligomerization of the collagen-tailed forms in fast and slow muscles. J. Neurosci. 19 (1999) 10672-10679
    • (1999) J. Neurosci. , vol.19 , pp. 10672-10679
    • Krejci, E.1    Legay, C.2    Thomine, S.3    Sketelj, J.4    Massoulié, J.5
  • 23
    • 3042602304 scopus 로고    scopus 로고
    • Transcriptional regulation of acetylcholinesterase-associated collagen ColQ: differential expression in fast and slow twitch muscle fibers is driven by distinct promoters
    • Lee H.H., Choi R.C., Ting A., Siow N.L., Jiang J.X., Massoulié J., and Tsim K.W. Transcriptional regulation of acetylcholinesterase-associated collagen ColQ: differential expression in fast and slow twitch muscle fibers is driven by distinct promoters. J. Biol. Chem. 279 (2004) 27098-27107
    • (2004) J. Biol. Chem. , vol.279 , pp. 27098-27107
    • Lee, H.H.1    Choi, R.C.2    Ting, A.3    Siow, N.L.4    Jiang, J.X.5    Massoulié, J.6    Tsim, K.W.7
  • 24
    • 28744453214 scopus 로고    scopus 로고
    • Junctional and extrajunctional acetylcholinesterase in skeletal muscle fibers
    • Çrne-Finderle N., Pregelj P., and Sketelj J. Junctional and extrajunctional acetylcholinesterase in skeletal muscle fibers. Chem. Biol. Interact. 157/158 (2005) 23-27
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 23-27
    • Çrne-Finderle, N.1    Pregelj, P.2    Sketelj, J.3
  • 25
    • 34547397458 scopus 로고    scopus 로고
    • Calcitonin gene-related peptide induces the expression of acetylcholinesterase-associated collagen ColQ in muscle: a distinction in driving two different promoters between fast- and slow-twitch muscle fibers
    • Choi R.C., Ting A.K., Lau F.T., Xie H.Q., Leung K.W., Chen V.P., Siow N.L., and Tsim K.W. Calcitonin gene-related peptide induces the expression of acetylcholinesterase-associated collagen ColQ in muscle: a distinction in driving two different promoters between fast- and slow-twitch muscle fibers. J. Neurochem. 102 (2007) 1316-1328
    • (2007) J. Neurochem. , vol.102 , pp. 1316-1328
    • Choi, R.C.1    Ting, A.K.2    Lau, F.T.3    Xie, H.Q.4    Leung, K.W.5    Chen, V.P.6    Siow, N.L.7    Tsim, K.W.8
  • 27
    • 0033594106 scopus 로고    scopus 로고
    • Genetic analysis of collagen Q: roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function
    • Feng G., Krejci E., Molgo J., Cunningham J.M., Massoulié J., and Sanes J.R. Genetic analysis of collagen Q: roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function. J. Cell Biol. 144 (1999) 1349-1360
    • (1999) J. Cell Biol. , vol.144 , pp. 1349-1360
    • Feng, G.1    Krejci, E.2    Molgo, J.3    Cunningham, J.M.4    Massoulié, J.5    Sanes, J.R.6
  • 28
    • 28744450131 scopus 로고    scopus 로고
    • Acetylcholinesterase (AChE) gene modification in transgenic animals: functional consequences of selected exon and regulatory region deletion
    • Camp S., Zhang L., Marquez M., de la Torre B., Long J.M., Bucht G., and Taylor P. Acetylcholinesterase (AChE) gene modification in transgenic animals: functional consequences of selected exon and regulatory region deletion. Chem. Biol. Interact. 157/158 (2005) 79-86
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 79-86
    • Camp, S.1    Zhang, L.2    Marquez, M.3    de la Torre, B.4    Long, J.M.5    Bucht, G.6    Taylor, P.7
  • 29
    • 33845932262 scopus 로고    scopus 로고
    • Remodeling of the neuromuscular junction in mice with deleted exons 5 and 6 of acetylcholinesterase
    • Girard E., Bernard V., Camp S., Taylor P., Krejci E., and Molgo J. Remodeling of the neuromuscular junction in mice with deleted exons 5 and 6 of acetylcholinesterase. J. Mol. Neurosci. 30 (2006) 99-100
    • (2006) J. Mol. Neurosci. , vol.30 , pp. 99-100
    • Girard, E.1    Bernard, V.2    Camp, S.3    Taylor, P.4    Krejci, E.5    Molgo, J.6
  • 30
    • 28744451208 scopus 로고    scopus 로고
    • V.N. Talesa, C. Antognelli (Eds.), Proceedings of the VIIIth International Meeting on Cholinesterases, Chem. Biol. Interact. 157/158 (2005) 1-434.
    • V.N. Talesa, C. Antognelli (Eds.), Proceedings of the VIIIth International Meeting on Cholinesterases, Chem. Biol. Interact. 157/158 (2005) 1-434.
  • 32
    • 0027401977 scopus 로고
    • Tissue-specific expression and alternative mRNA processing of the mammalian acetylcholinesterase gene
    • Li Y., Camp S., and Taylor P. Tissue-specific expression and alternative mRNA processing of the mammalian acetylcholinesterase gene. J. Biol. Chem. 268 (1993) 5790-5797
    • (1993) J. Biol. Chem. , vol.268 , pp. 5790-5797
    • Li, Y.1    Camp, S.2    Taylor, P.3
  • 33
    • 0033597864 scopus 로고    scopus 로고
    • Novel messenger RNA and alternative promoter for murine acetylcholinesterase
    • Atanasova E., Chiappa S., Wieben E., and Brimijoin S. Novel messenger RNA and alternative promoter for murine acetylcholinesterase. J. Biol. Chem. 274 (1999) 21078-21084
    • (1999) J. Biol. Chem. , vol.274 , pp. 21078-21084
    • Atanasova, E.1    Chiappa, S.2    Wieben, E.3    Brimijoin, S.4
  • 35
    • 0025019290 scopus 로고
    • Structure of the gene for human butyrylcholinesterase. Evidence for a single copy
    • Arpagaus M., Kott M., Vatsis K.P., Bartels C.F., La Du B.N., and Lockridge O. Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry 29 1 (1990) 124-131
    • (1990) Biochemistry , vol.29 , Issue.1 , pp. 124-131
    • Arpagaus, M.1    Kott, M.2    Vatsis, K.P.3    Bartels, C.F.4    La Du, B.N.5    Lockridge, O.6
  • 36
    • 40349085910 scopus 로고    scopus 로고
    • Acetylcholinesterase from the invertebrate Ciona intestinalis is capable of assembling into asymmetric forms when co-expressed with vertebrate collagenic tail peptide
    • Frederick A., Tsigelny I., Cohenour F., Spiker C., Krejci E., Chatonnet A., Bourgoin S., Richards G., Allen T., Whitlock M.H., and Pezzementi L. Acetylcholinesterase from the invertebrate Ciona intestinalis is capable of assembling into asymmetric forms when co-expressed with vertebrate collagenic tail peptide. FEBS J. 275 (2008) 1309-1322
    • (2008) FEBS J. , vol.275 , pp. 1309-1322
    • Frederick, A.1    Tsigelny, I.2    Cohenour, F.3    Spiker, C.4    Krejci, E.5    Chatonnet, A.6    Bourgoin, S.7    Richards, G.8    Allen, T.9    Whitlock, M.H.10    Pezzementi, L.11
  • 37
    • 0034697999 scopus 로고    scopus 로고
    • Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, mutations and in vivo expression
    • Combes D., Fedon Y., Grauso M., Toutant J.-P., and Arpagaus M. Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, mutations and in vivo expression. J. Mol. Biol. 300 (2000) 727-742
    • (2000) J. Mol. Biol. , vol.300 , pp. 727-742
    • Combes, D.1    Fedon, Y.2    Grauso, M.3    Toutant, J.-P.4    Arpagaus, M.5
  • 38
    • 0034813088 scopus 로고    scopus 로고
    • Acetylcholinesterase genes in the nematode Caenorhabditis elegans
    • Combes D., Fedon Y., Toutant J.-P., and Arpagaus M. Acetylcholinesterase genes in the nematode Caenorhabditis elegans. Int. Rev. Cytol. 209 (2001) 207-239
    • (2001) Int. Rev. Cytol. , vol.209 , pp. 207-239
    • Combes, D.1    Fedon, Y.2    Toutant, J.-P.3    Arpagaus, M.4
  • 39
    • 0041879942 scopus 로고    scopus 로고
    • Multiple ace genes encoding acetylcholinesterases of Caenorhabditis elegans have distinct tissue expression
    • Combes D., Fedon Y., Toutant J.P., and Arpagaus M. Multiple ace genes encoding acetylcholinesterases of Caenorhabditis elegans have distinct tissue expression. Eur. J. Neurosci. 18 (2003) 497-512
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 497-512
    • Combes, D.1    Fedon, Y.2    Toutant, J.P.3    Arpagaus, M.4
  • 40
    • 0032972039 scopus 로고    scopus 로고
    • Molecular cloning and expression of a full-length cDNA encoding acetylcholinesterase in optic lobes of the squid Loligo opalescens: a new member of the cholinesterase family resistant to diisopropylfluorophosphate
    • Talesa V., Grauso M., Arpagaus M., Giovannini E., Romani R., and Rosi G. Molecular cloning and expression of a full-length cDNA encoding acetylcholinesterase in optic lobes of the squid Loligo opalescens: a new member of the cholinesterase family resistant to diisopropylfluorophosphate. J. Neurochem. 72 (1999) 1250-1258
    • (1999) J. Neurochem. , vol.72 , pp. 1250-1258
    • Talesa, V.1    Grauso, M.2    Arpagaus, M.3    Giovannini, E.4    Romani, R.5    Rosi, G.6
  • 41
    • 0035897109 scopus 로고    scopus 로고
    • Soluble and membrane-bound acetylcholinesterases in Mytilus galloprovincialis (Pelecypoda: Filibranchia) from the northern Adriatic sea
    • Talesa V., Romani R., Antognelli C., Giovannini E., and Rosi G. Soluble and membrane-bound acetylcholinesterases in Mytilus galloprovincialis (Pelecypoda: Filibranchia) from the northern Adriatic sea. Chem.-Biol. Int. 134 (2001) 151-166
    • (2001) Chem.-Biol. Int. , vol.134 , pp. 151-166
    • Talesa, V.1    Romani, R.2    Antognelli, C.3    Giovannini, E.4    Rosi, G.5
  • 42
    • 0024489712 scopus 로고
    • Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms
    • Toutant J.-P. Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms. Prog. Neurobiol. 32 (1988) 423-446
    • (1988) Prog. Neurobiol. , vol.32 , pp. 423-446
    • Toutant, J.-P.1
  • 43
    • 53149144293 scopus 로고    scopus 로고
    • A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila
    • Weill M., Fort P., Berthomieu A., Dubois M.P., Pasteur N., and Raymond M. A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila. Proc. Biol. Sci. 269 (2002) 2007-2016
    • (2002) Proc. Biol. Sci. , vol.269 , pp. 2007-2016
    • Weill, M.1    Fort, P.2    Berthomieu, A.3    Dubois, M.P.4    Pasteur, N.5    Raymond, M.6
  • 44
    • 0035984514 scopus 로고    scopus 로고
    • Resistance-associated point mutations of organophosphate insensitive acetylcholinesterase, in the olive fruit fly Bactrocera oleae
    • Vontas J.G., Hejazi M.J., Hawkes N.J., Cosmidis N., Loukas M., Janes R.W., and Hemingway J. Resistance-associated point mutations of organophosphate insensitive acetylcholinesterase, in the olive fruit fly Bactrocera oleae. Insect Mol. Biol. 11 (2002) 329-336
    • (2002) Insect Mol. Biol. , vol.11 , pp. 329-336
    • Vontas, J.G.1    Hejazi, M.J.2    Hawkes, N.J.3    Cosmidis, N.4    Loukas, M.5    Janes, R.W.6    Hemingway, J.7
  • 45
    • 0026033050 scopus 로고
    • Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site
    • Moran P., Raab H., Kohr W.J., and Caras I.W. Glycophospholipid membrane anchor attachment. Molecular analysis of the cleavage/attachment site. J. Biol. Chem. 266 2 (1991) 1250-1257
    • (1991) J. Biol. Chem. , vol.266 , Issue.2 , pp. 1250-1257
    • Moran, P.1    Raab, H.2    Kohr, W.J.3    Caras, I.W.4
  • 46
    • 0028981209 scopus 로고
    • How glycosylphosphatidylinositol-anchored membrane proteins are made
    • Udenfriend S., and Kodukula K. How glycosylphosphatidylinositol-anchored membrane proteins are made. Annu. Rev. Biochem. 64 (1995) 563-591
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 563-591
    • Udenfriend, S.1    Kodukula, K.2
  • 47
    • 0035958951 scopus 로고    scopus 로고
    • Addition of a glycophosphatidylinositol to acetylcholinesterase; processing, degradation, and secretion
    • Coussen F., Ayon A., Le Goff A., Leroy J., Massoulié J., and Bon S. Addition of a glycophosphatidylinositol to acetylcholinesterase; processing, degradation, and secretion. J. Biol. Chem. 276 (2001) 27881-27892
    • (2001) J. Biol. Chem. , vol.276 , pp. 27881-27892
    • Coussen, F.1    Ayon, A.2    Le Goff, A.3    Leroy, J.4    Massoulié, J.5    Bon, S.6
  • 48
    • 0032540305 scopus 로고    scopus 로고
    • Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle
    • Cousin X., Bon S., Massoulié J., and Bon C. Identification of a novel type of alternatively spliced exon from the acetylcholinesterase gene of Bungarus fasciatus. Molecular forms of acetylcholinesterase in the snake liver and muscle. J. Biol. Chem. 273 (1998) 9812-9820
    • (1998) J. Biol. Chem. , vol.273 , pp. 9812-9820
    • Cousin, X.1    Bon, S.2    Massoulié, J.3    Bon, C.4
  • 50
    • 0024095840 scopus 로고
    • Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form
    • Sikorav J.L., Duval N., Anselmet A., Bon S., Krejci E., Legay C., Osterlund M., Reimund B., and Massoulié J. Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form. EMBO J. 7 (1988) 2983-2993
    • (1988) EMBO J. , vol.7 , pp. 2983-2993
    • Sikorav, J.L.1    Duval, N.2    Anselmet, A.3    Bon, S.4    Krejci, E.5    Legay, C.6    Osterlund, M.7    Reimund, B.8    Massoulié, J.9
  • 51
    • 0027506675 scopus 로고
    • Expression of a cDNA encoding the glycolipid-anchored form of rat acetylcholinesterase
    • Legay C., Bon S., and Massoulié J. Expression of a cDNA encoding the glycolipid-anchored form of rat acetylcholinesterase. FEBS Lett. 315 (1993) 163-166
    • (1993) FEBS Lett. , vol.315 , pp. 163-166
    • Legay, C.1    Bon, S.2    Massoulié, J.3
  • 53
    • 0034629337 scopus 로고    scopus 로고
    • Comparative expression of homologous proteins. A novel mode of transcriptional regulation by the coding sequence folding compatibility of chimeras
    • Morel N., and Massoulié J. Comparative expression of homologous proteins. A novel mode of transcriptional regulation by the coding sequence folding compatibility of chimeras. J. Biol. Chem. 275 (2000) 7304-7312
    • (2000) J. Biol. Chem. , vol.275 , pp. 7304-7312
    • Morel, N.1    Massoulié, J.2
  • 54
    • 0037027812 scopus 로고    scopus 로고
    • Transcriptional regulation of gene expression by the coding sequence: an attempt to enhance expression of human AChE
    • Weill C.O., Vorlova S., Berna N., Ayon A., and Massoulié J. Transcriptional regulation of gene expression by the coding sequence: an attempt to enhance expression of human AChE. Biotechnol. Bioeng. 80 (2002) 490-497
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 490-497
    • Weill, C.O.1    Vorlova, S.2    Berna, N.3    Ayon, A.4    Massoulié, J.5
  • 55
    • 0031439890 scopus 로고    scopus 로고
    • Cloning and expression of acetylcholinesterase from Electrophorus: splicing pattern of the 3′ exons in vivo and in transfected mammalian cells
    • Simon S., and Massoulié J. Cloning and expression of acetylcholinesterase from Electrophorus: splicing pattern of the 3′ exons in vivo and in transfected mammalian cells. J. Biol. Chem. 273 (1997) 33045-33055
    • (1997) J. Biol. Chem. , vol.273 , pp. 33045-33055
    • Simon, S.1    Massoulié, J.2
  • 56
    • 0347510256 scopus 로고    scopus 로고
    • Intronic elements appear essential for the differentiation-specific expression of acetylcholinesterase in C2C12 myotubes
    • Doctor B.P., Taylor P., Quinn D., Rotundo R., and Gentry M. (Eds), Plenum Press, New York
    • Camp S., and Taylor P. Intronic elements appear essential for the differentiation-specific expression of acetylcholinesterase in C2C12 myotubes. In: Doctor B.P., Taylor P., Quinn D., Rotundo R., and Gentry M. (Eds). Structure and Function of Cholinesterases and Related Proteins (1998), Plenum Press, New York 630
    • (1998) Structure and Function of Cholinesterases and Related Proteins , pp. 630
    • Camp, S.1    Taylor, P.2
  • 57
    • 0033551249 scopus 로고    scopus 로고
    • An intronic enhancer containing an N-box motif is required for synapse- and tissue-specific expression of the acetylcholinesterase gene in skeletal muscle fibers
    • Chan R.Y., Boudreau-Larivière C., Angus L.M., Mankal F.A., and Jasmin B.J. An intronic enhancer containing an N-box motif is required for synapse- and tissue-specific expression of the acetylcholinesterase gene in skeletal muscle fibers. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 4627-4632
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4627-4632
    • Chan, R.Y.1    Boudreau-Larivière, C.2    Angus, L.M.3    Mankal, F.A.4    Jasmin, B.J.5
  • 58
    • 0038795202 scopus 로고    scopus 로고
    • ATP acts via P2Y1 receptors to stimulate acetylcholinesterase and acetylcholine receptor expression: transduction and transcription control
    • Choi R.C., Siow N.L., Cheng A.W., Ling K.K., Tung E.K., Simon J., Barnard E.A., and Tsim K.W. ATP acts via P2Y1 receptors to stimulate acetylcholinesterase and acetylcholine receptor expression: transduction and transcription control. J. Neurosci. 23 (2003) 4445-4456
    • (2003) J. Neurosci. , vol.23 , pp. 4445-4456
    • Choi, R.C.1    Siow, N.L.2    Cheng, A.W.3    Ling, K.K.4    Tung, E.K.5    Simon, J.6    Barnard, E.A.7    Tsim, K.W.8
  • 59
    • 0024230928 scopus 로고
    • Biogenesis of acetylcholinesterase molecular forms in muscle. Evidence for a rapidly turning over, catalytically inactive precursor pool
    • Rotundo R.L. Biogenesis of acetylcholinesterase molecular forms in muscle. Evidence for a rapidly turning over, catalytically inactive precursor pool. J. Biol. Chem. 263 (1988) 19398-19406
    • (1988) J. Biol. Chem. , vol.263 , pp. 19398-19406
    • Rotundo, R.L.1
  • 61
    • 0027535819 scopus 로고
    • A conformation-dependent monoclonal antibody against active chicken acetylcholinesterase
    • Chatel J.M., Vallette F.M., Massoulié J., and Grassi J. A conformation-dependent monoclonal antibody against active chicken acetylcholinesterase. FEBS Lett. 319 1/2 (1993) 12-15
    • (1993) FEBS Lett. , vol.319 , Issue.1-2 , pp. 12-15
    • Chatel, J.M.1    Vallette, F.M.2    Massoulié, J.3    Grassi, J.4
  • 62
    • 0027932932 scopus 로고
    • Two-site immunoradiometric assay of chicken acetylcholinesterase: active and inactive molecular forms in brain and muscle
    • Chatel J.M., Eichler J., Vallette F.M., Bon S., Massoulié J., and Grassi J. Two-site immunoradiometric assay of chicken acetylcholinesterase: active and inactive molecular forms in brain and muscle. J. Neurochem. 63 3 (1994) 1111-1118
    • (1994) J. Neurochem. , vol.63 , Issue.3 , pp. 1111-1118
    • Chatel, J.M.1    Eichler, J.2    Vallette, F.M.3    Bon, S.4    Massoulié, J.5    Grassi, J.6
  • 63
    • 0030592512 scopus 로고    scopus 로고
    • Calcitonin gene-related peptide increases the expression of acetylcholinesterase in cultured chick myotubes
    • Choi R.C., Leung P.W., Dong T.T., Wan D.C., and Tsim K.W. Calcitonin gene-related peptide increases the expression of acetylcholinesterase in cultured chick myotubes. Neurosci. Lett. 217 (1996) 165-168
    • (1996) Neurosci. Lett. , vol.217 , pp. 165-168
    • Choi, R.C.1    Leung, P.W.2    Dong, T.T.3    Wan, D.C.4    Tsim, K.W.5
  • 64
    • 0028960892 scopus 로고
    • The activity of an endoplasmic reticulum-localized pool of acetylcholinesterase is modulated by heat shock
    • Eichler J., and Silman I. The activity of an endoplasmic reticulum-localized pool of acetylcholinesterase is modulated by heat shock. J. Biol. Chem. 270 9 (1995) 4466-4472
    • (1995) J. Biol. Chem. , vol.270 , Issue.9 , pp. 4466-4472
    • Eichler, J.1    Silman, I.2
  • 65
    • 50649112846 scopus 로고    scopus 로고
    • Protein disulfide isomerase regulates assembly and expression of synaptic acetylcholinesterase in skeletal muscle cells: role of muscle activity
    • Suzhou, China (Abstract)
    • Ruiz C.A., and Rotundo R.L. Protein disulfide isomerase regulates assembly and expression of synaptic acetylcholinesterase in skeletal muscle cells: role of muscle activity. Proceedings of the IXth International Meeting on Cholinesterases. Suzhou, China (2007) 91 (Abstract)
    • (2007) Proceedings of the IXth International Meeting on Cholinesterases , pp. 91
    • Ruiz, C.A.1    Rotundo, R.L.2
  • 66
    • 0003207871 scopus 로고
    • Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene
    • Rotundo R.L., Gomez A.M., Fernandez-Valle C., and Randall W.R. Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene. Proc. Natl. Acad. Sci. U.S.A. 85 20 (1988) 7805-7809
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , Issue.20 , pp. 7805-7809
    • Rotundo, R.L.1    Gomez, A.M.2    Fernandez-Valle, C.3    Randall, W.R.4
  • 67
    • 0019394904 scopus 로고
    • The quaternary structure of chicken acetylcholinesterase and butyrylcholinesterase; effect of collagenase and trypsin
    • Allemand P., Bon S., Massoulié J., and Vigny M. The quaternary structure of chicken acetylcholinesterase and butyrylcholinesterase; effect of collagenase and trypsin. J. Neurochem. 36 3 (1981) 860-867
    • (1981) J. Neurochem. , vol.36 , Issue.3 , pp. 860-867
    • Allemand, P.1    Bon, S.2    Massoulié, J.3    Vigny, M.4
  • 69
    • 12544256389 scopus 로고    scopus 로고
    • Determinants of the t peptide involved in folding, degradation and secretion of acetylcholinesterase
    • Falasca C., Perrier N.A., Massoulié J., and Bon S. Determinants of the t peptide involved in folding, degradation and secretion of acetylcholinesterase. J. Biol. Chem. 280 (2005) 878-886
    • (2005) J. Biol. Chem. , vol.280 , pp. 878-886
    • Falasca, C.1    Perrier, N.A.2    Massoulié, J.3    Bon, S.4
  • 70
    • 33646913370 scopus 로고    scopus 로고
    • A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein family
    • De Jaco A., Comoletti D., Kovarik Z., Gaietta G., Radic Z., Lockridge O., Ellisman M.H., and Taylor P. A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein family. J. Biol. Chem. 281 (2006) 9667-9676
    • (2006) J. Biol. Chem. , vol.281 , pp. 9667-9676
    • De Jaco, A.1    Comoletti, D.2    Kovarik, Z.3    Gaietta, G.4    Radic, Z.5    Lockridge, O.6    Ellisman, M.H.7    Taylor, P.8
  • 71
    • 12344334864 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation: exceptions to the rule
    • Schmitz A., and Herzog V. Endoplasmic reticulum-associated degradation: exceptions to the rule. Eur. J. Cell Biol. 83 (2004) 501-509
    • (2004) Eur. J. Cell Biol. , vol.83 , pp. 501-509
    • Schmitz, A.1    Herzog, V.2
  • 72
    • 0024636530 scopus 로고
    • Glycosyl-phosphatidylinositol: a versatile anchor for cell surface proteins
    • Low M.G. Glycosyl-phosphatidylinositol: a versatile anchor for cell surface proteins. FASEB J. 3 (1989) 1600-1608
    • (1989) FASEB J. , vol.3 , pp. 1600-1608
    • Low, M.G.1
  • 73
    • 0005946413 scopus 로고    scopus 로고
    • Intracellular transport of GPI-anchored proteins
    • Muñiz M., and Riezman H. Intracellular transport of GPI-anchored proteins. EMBO J. 19 (2000) 10-15
    • (2000) EMBO J. , vol.19 , pp. 10-15
    • Muñiz, M.1    Riezman, H.2
  • 74
    • 0035421238 scopus 로고    scopus 로고
    • PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8
    • Ohishi K., Inoue N., and Kinoshita T. PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 20 (2001) 4088-4098
    • (2001) EMBO J. , vol.20 , pp. 4088-4098
    • Ohishi, K.1    Inoue, N.2    Kinoshita, T.3
  • 75
    • 2142652150 scopus 로고    scopus 로고
    • Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation
    • Belbeoc'h S., Falasca C., Leroy J., Ayon A., Massoulié J., and Bon S. Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation. Eur. J. Biochem. 271 (2004) 1476-1487
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1476-1487
    • Belbeoc'h, S.1    Falasca, C.2    Leroy, J.3    Ayon, A.4    Massoulié, J.5    Bon, S.6
  • 77
    • 0027440769 scopus 로고
    • Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation
    • Fra A.M., Fagioli C., Finazzi D., Sitia R., and Alberini C.M. Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation. EMBO J. 12 (1993) 4755-4761
    • (1993) EMBO J. , vol.12 , pp. 4755-4761
    • Fra, A.M.1    Fagioli, C.2    Finazzi, D.3    Sitia, R.4    Alberini, C.M.5
  • 78
    • 0042313982 scopus 로고    scopus 로고
    • The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway
    • Belbeoc'h S., Massoulié J., and Bon S. The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway. EMBO J. 22 (2003) 3536-3545
    • (2003) EMBO J. , vol.22 , pp. 3536-3545
    • Belbeoc'h, S.1    Massoulié, J.2    Bon, S.3
  • 79
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B., Ye Y., and Rapoport T.A. Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3 (2002) 246-255
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 80
    • 33845282579 scopus 로고
    • Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states
    • Quinn D.M. Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states. Chem. Rev. 87 (1987) 955-979
    • (1987) Chem. Rev. , vol.87 , pp. 955-979
    • Quinn, D.M.1
  • 81
    • 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., Ariel N., Osman R., and Velan B. Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase. EMBO J. 13 15 (1994) 3448-3455
    • (1994) EMBO J. , vol.13 , Issue.15 , pp. 3448-3455
    • Shafferman, A.1    Ordentlich, A.2    Barak, D.3    Kronman, C.4    Ber, R.5    Bino, T.6    Ariel, N.7    Osman, R.8    Velan, B.9
  • 85
    • 0041691306 scopus 로고    scopus 로고
    • How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations
    • Xu Y., Shen J., Luo X., Silman I., Sussman J.L., Chen K., and Jiang H. How does huperzine A enter and leave the binding gorge of acetylcholinesterase? Steered molecular dynamics simulations. J. Am. Chem. Soc. 125 (2003) 11340-11349
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11340-11349
    • Xu, Y.1    Shen, J.2    Luo, X.3    Silman, I.4    Sussman, J.L.5    Chen, K.6    Jiang, H.7
  • 86
    • 0014750669 scopus 로고
    • On the question: is acetylcholinesterase an allosteric protein?
    • Kitz R.J., Braswell L.M., and Ginsburg S. On the question: is acetylcholinesterase an allosteric protein?. Mol. Pharmacol. 6 (1970) 108-121
    • (1970) Mol. Pharmacol. , vol.6 , pp. 108-121
    • Kitz, R.J.1    Braswell, L.M.2    Ginsburg, S.3
  • 87
    • 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 W.D., Szegletes T., and Rosenberry T.L. Acetylthiocholine binds to asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway. Biochemistry 39 (2000) 7753-7763
    • (2000) Biochemistry , vol.39 , pp. 7753-7763
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 88
    • 0023268737 scopus 로고
    • Interaction of noncompetitive inhibitors with the acetylcholine receptor. The site specificity and spectroscopic properties of ethidium binding
    • Herz J.M., Johnson D.A., and Taylor P. Interaction of noncompetitive inhibitors with the acetylcholine receptor. The site specificity and spectroscopic properties of ethidium binding. J. Biol. Chem. 262 (1987) 7238-7247
    • (1987) J. Biol. Chem. , vol.262 , pp. 7238-7247
    • Herz, J.M.1    Johnson, D.A.2    Taylor, P.3
  • 89
    • 0028845803 scopus 로고
    • Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite
    • Barak D., Ordentlich A., Bromberg A., Kronman C., Marcus D., Lazar A., Ariel N., Velan B., and Shafferman A. Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite. Biochemistry 34 (1995) 15444-15452
    • (1995) Biochemistry , vol.34 , pp. 15444-15452
    • Barak, D.1    Ordentlich, A.2    Bromberg, A.3    Kronman, C.4    Marcus, D.5    Lazar, A.6    Ariel, N.7    Velan, B.8    Shafferman, A.9
  • 90
    • 0025265527 scopus 로고
    • Novel allosteric sites on human erythrocyte acetylcholinesterase identified by two monoclonal antibodies
    • Olson C.E., Chhajlani V., August J.T., and Schmell E.D. Novel allosteric sites on human erythrocyte acetylcholinesterase identified by two monoclonal antibodies. Arch. Biochem. Biophys. 227 (1990) 361-367
    • (1990) Arch. Biochem. Biophys. , vol.227 , pp. 361-367
    • Olson, C.E.1    Chhajlani, V.2    August, J.T.3    Schmell, E.D.4
  • 91
    • 0032488637 scopus 로고    scopus 로고
    • Allosteric control of acetylcholinesterase activity by monoclonal antibodies
    • Saxena A., Hur R., and Doctor B.P. Allosteric control of acetylcholinesterase activity by monoclonal antibodies. Biochemistry 37 (1998) 145-154
    • (1998) Biochemistry , vol.37 , pp. 145-154
    • Saxena, A.1    Hur, R.2    Doctor, B.P.3
  • 92
    • 0029133139 scopus 로고
    • Allosteric control of acetylcholinesterase catalysis by fasciculin
    • Radić Z., Quinn D.M., Vellom D.C., Camp S., and Taylor P. Allosteric control of acetylcholinesterase catalysis by fasciculin. J. Biol. Chem. 270 35 (1995) 20391-20399
    • (1995) J. Biol. Chem. , vol.270 , Issue.35 , pp. 20391-20399
    • Radić, Z.1    Quinn, D.M.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 93
    • 0032573399 scopus 로고    scopus 로고
    • A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase
    • Stojan J., Marcel V., Estrada-Mondaca S., Klaebe A., Masson P., and Fournier D. A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase. FEBS Lett. 440 (1998) 85-88
    • (1998) FEBS Lett. , vol.440 , pp. 85-88
    • Stojan, J.1    Marcel, V.2    Estrada-Mondaca, S.3    Klaebe, A.4    Masson, P.5    Fournier, D.6
  • 94
    • 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 W.D., Thomas P.J., and Rosenberry T.L. Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 38 (1999) 122-133
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 95
    • 0037013985 scopus 로고    scopus 로고
    • Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior
    • Masson P., Froment M.T., Fort S., Ribes F., Bec N., Balny C., and Schopfer L.M. Butyrylcholinesterase-catalyzed hydrolysis of N-methylindoxyl acetate: analysis of volume changes upon reaction and hysteretic behavior. Biochim. Biophys. Acta 1597 (2002) 229-243
    • (2002) Biochim. Biophys. Acta , vol.1597 , pp. 229-243
    • Masson, P.1    Froment, M.T.2    Fort, S.3    Ribes, F.4    Bec, N.5    Balny, C.6    Schopfer, L.M.7
  • 98
    • 33644781969 scopus 로고    scopus 로고
    • Rat butyrylcholinesterase-catalysed hydrolysis of N-alkyl homologues of benzoylcholine
    • Hrabovska A., Debouzy J.C., Froment M.T., Devinsky F., Paulikova I., and Masson P. Rat butyrylcholinesterase-catalysed hydrolysis of N-alkyl homologues of benzoylcholine. FEBS J. 273 (2006) 1185-1197
    • (2006) FEBS J. , vol.273 , pp. 1185-1197
    • Hrabovska, A.1    Debouzy, J.C.2    Froment, M.T.3    Devinsky, F.4    Paulikova, I.5    Masson, P.6
  • 99
    • 0017884240 scopus 로고
    • Active-site catalytic efficiency of acetylcholinesterase molecular forms in Electrophorus, Torpedo, rat and chicken
    • Vigny M., Bon S., Massoulié J., and Leterrier F. Active-site catalytic efficiency of acetylcholinesterase molecular forms in Electrophorus, Torpedo, rat and chicken. Eur. J. Biochem. 85 (1978) 317-323
    • (1978) Eur. J. Biochem. , vol.85 , pp. 317-323
    • Vigny, M.1    Bon, S.2    Massoulié, J.3    Leterrier, F.4
  • 100
    • 0021355165 scopus 로고
    • Interactions with lectins indicate differences in the carbohydrate composition of the membrane-bound enzymes acetylcholinesterase and 5′-nucleotidase in different cell types
    • Méflah K., Bernard S., and Massoulié J. Interactions with lectins indicate differences in the carbohydrate composition of the membrane-bound enzymes acetylcholinesterase and 5′-nucleotidase in different cell types. Biochimie 66 (1984) 59-69
    • (1984) Biochimie , vol.66 , pp. 59-69
    • Méflah, K.1    Bernard, S.2    Massoulié, J.3
  • 101
    • 0028778469 scopus 로고
    • G4 forms of acetylcholinesterase and butyrylcholinesterase in normal and dystrophic mouse muscle differ in their interaction with Ricinus communis agglutinin
    • Cabezas-Herrera J., Moral-Naranjo M.T., Campoy F.J., and Vidal C.J. G4 forms of acetylcholinesterase and butyrylcholinesterase in normal and dystrophic mouse muscle differ in their interaction with Ricinus communis agglutinin. Biochim. Biophys. Acta 1225 (1994) 283-288
    • (1994) Biochim. Biophys. Acta , vol.1225 , pp. 283-288
    • Cabezas-Herrera, J.1    Moral-Naranjo, M.T.2    Campoy, F.J.3    Vidal, C.J.4
  • 102
    • 0026674465 scopus 로고
    • Differential inhibition of acetylcholinesterase molecular forms in normal and Alzheimer disease brain
    • Ogane N., Giacobini E., and Struble R. Differential inhibition of acetylcholinesterase molecular forms in normal and Alzheimer disease brain. Brain Res. 589 (1992) 307-312
    • (1992) Brain Res. , vol.589 , pp. 307-312
    • Ogane, N.1    Giacobini, E.2    Struble, R.3
  • 103
    • 0042286681 scopus 로고    scopus 로고
    • Potencies and selectivities of inhibitors of acetylcholinesterase and its molecular forms in normal and Alzheimer's disease brain
    • Rakonczay Z. Potencies and selectivities of inhibitors of acetylcholinesterase and its molecular forms in normal and Alzheimer's disease brain. Acta Biol. Hung. 54 (2003) 183-189
    • (2003) Acta Biol. Hung. , vol.54 , pp. 183-189
    • Rakonczay, Z.1
  • 104
    • 0019218509 scopus 로고
    • The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from human erythrocytes, sheep basal ganglia and electric eel
    • George S.T., and Balasubramanian A.S. The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from human erythrocytes, sheep basal ganglia and electric eel. Eur. J. Biochem. 111 (1980) 511-524
    • (1980) Eur. J. Biochem. , vol.111 , pp. 511-524
    • George, S.T.1    Balasubramanian, A.S.2
  • 105
    • 0028079652 scopus 로고
    • Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities
    • Checler F., Grassi J., and Vincent J.P. Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities. J. Neurochem. 62 (1994) 756-763
    • (1994) J. Neurochem. , vol.62 , pp. 756-763
    • Checler, F.1    Grassi, J.2    Vincent, J.P.3
  • 106
    • 16544387273 scopus 로고    scopus 로고
    • Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development
    • Boopathy R., and Layer P.G. Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development. Protein J. 23 (2004) 325-333
    • (2004) Protein J. , vol.23 , pp. 325-333
    • Boopathy, R.1    Layer, P.G.2
  • 107
    • 0030778075 scopus 로고    scopus 로고
    • In vitro phosphorylation of acetylcholinesterase at non-consensus protein kinase A sites enhances the rate of acetylcholine hydrolysis
    • Grifman M., Arbel A., Ginzberg D., Glick D., Elgavish S., Shaanan B., and Soreq H. In vitro phosphorylation of acetylcholinesterase at non-consensus protein kinase A sites enhances the rate of acetylcholine hydrolysis. Brain Res. Mol. Brain Res. 51 (1997) 179-187
    • (1997) Brain Res. Mol. Brain Res. , vol.51 , pp. 179-187
    • Grifman, M.1    Arbel, A.2    Ginzberg, D.3    Glick, D.4    Elgavish, S.5    Shaanan, B.6    Soreq, H.7
  • 108
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., and Ron D. Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2 (2000) 326-332
    • (2000) Nat. Cell Biol. , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 109
    • 0023721654 scopus 로고
    • Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases. II. Electrophoretic variants and phosphatidylinositol phospholipase C-sensitive and -insensitive forms
    • Bon S., Toutant J.P., Méflah K., and Massoulié J. Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases. II. Electrophoretic variants and phosphatidylinositol phospholipase C-sensitive and -insensitive forms. J. Neurochem. 51 (1988) 786-794
    • (1988) J. Neurochem. , vol.51 , pp. 786-794
    • Bon, S.1    Toutant, J.P.2    Méflah, K.3    Massoulié, J.4
  • 110
    • 33947518165 scopus 로고    scopus 로고
    • Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes
    • Noureddine H., Schmitt C., Liu W.Q., Garbay C., Massoulié J., and Bon S. Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes. J. Biol. Chem. 282 (2007) 3487-3497
    • (2007) J. Biol. Chem. , vol.282 , pp. 3487-3497
    • Noureddine, H.1    Schmitt, C.2    Liu, W.Q.3    Garbay, C.4    Massoulié, J.5    Bon, S.6
  • 111
    • 0024241620 scopus 로고
    • Exercise selectively increases G4 AChE activity in fast-twitch muscle
    • Fernandez H.L., and Donoso J.A. Exercise selectively increases G4 AChE activity in fast-twitch muscle. J. Appl. Physiol. 65 (1988) 2245-2252
    • (1988) J. Appl. Physiol. , vol.65 , pp. 2245-2252
    • Fernandez, H.L.1    Donoso, J.A.2
  • 112
    • 0025427579 scopus 로고
    • Regulation by exercise of the pool of G4 acetylcholinesterase characterizing fast muscles: opposite effect of running training in antagonist muscles
    • Jasmin B.J., and Gisiger V. Regulation by exercise of the pool of G4 acetylcholinesterase characterizing fast muscles: opposite effect of running training in antagonist muscles. J. Neurosci. 10 (1990) 1444-1454
    • (1990) J. Neurosci. , vol.10 , pp. 1444-1454
    • Jasmin, B.J.1    Gisiger, V.2
  • 113
    • 0026097189 scopus 로고
    • Swimming training increases the G4 acetylcholinesterase content of both fast ankle extensors and flexors
    • Gisiger V., Sherker S., and Gardiner P.F. Swimming training increases the G4 acetylcholinesterase content of both fast ankle extensors and flexors. FEBS Lett. 278 (1991) 271-273
    • (1991) FEBS Lett. , vol.278 , pp. 271-273
    • Gisiger, V.1    Sherker, S.2    Gardiner, P.F.3
  • 114
    • 0026541643 scopus 로고
    • Trophic regulation of acetylcholinesterase isoenzymes in adult mammalian skeletal muscles
    • Fernandez H.L., and Hodges-Savola C.A. Trophic regulation of acetylcholinesterase isoenzymes in adult mammalian skeletal muscles. Neurochem. Res. 17 (1992) 115-124
    • (1992) Neurochem. Res. , vol.17 , pp. 115-124
    • Fernandez, H.L.1    Hodges-Savola, C.A.2
  • 115
    • 0028346147 scopus 로고
    • Acetylcholinesterase adaptation to voluntary wheel running is proportional to the volume of activity in fast, but not slow, rat hindlimb muscles
    • Gisiger V., Bélisle M., and Gardiner P.F. Acetylcholinesterase adaptation to voluntary wheel running is proportional to the volume of activity in fast, but not slow, rat hindlimb muscles. Eur. J. Neurosci. 6 (1994) 673-680
    • (1994) Eur. J. Neurosci. , vol.6 , pp. 673-680
    • Gisiger, V.1    Bélisle, M.2    Gardiner, P.F.3
  • 116
    • 34249694687 scopus 로고    scopus 로고
    • Regulation of a transcript encoding the proline-rich membrane anchor of globular muscle acetylcholinesterase. The suppressive roles of myogenesis and innervating nerves
    • Xie H.Q., Choi R.C., Leung K.W., Siow N.L., Kong L.W., Lau F.T., Peng H.B., and Tsim K.W. Regulation of a transcript encoding the proline-rich membrane anchor of globular muscle acetylcholinesterase. The suppressive roles of myogenesis and innervating nerves. J. Biol. Chem. 282 (2007) 11765-11775
    • (2007) J. Biol. Chem. , vol.282 , pp. 11765-11775
    • Xie, H.Q.1    Choi, R.C.2    Leung, K.W.3    Siow, N.L.4    Kong, L.W.5    Lau, F.T.6    Peng, H.B.7    Tsim, K.W.8
  • 117
    • 0030668464 scopus 로고    scopus 로고
    • Tetramerization domain of human butyrylcholinesterase is at the C-terminus
    • Blong R.M., Bedows E., and Lockridge O. Tetramerization domain of human butyrylcholinesterase is at the C-terminus. Biochem. J. 327 (1997) 747-757
    • (1997) Biochem. J. , vol.327 , pp. 747-757
    • Blong, R.M.1    Bedows, E.2    Lockridge, O.3
  • 119
    • 42449151347 scopus 로고    scopus 로고
    • Lamellipodin proline rich peptides associated with native plasma butyrylcholinesterase tetramers
    • Li H., Schopfer L.M., Masson P., and Lockridge O. Lamellipodin proline rich peptides associated with native plasma butyrylcholinesterase tetramers. Biochem. J. 411 (2008) 425-432
    • (2008) Biochem. J. , vol.411 , pp. 425-432
    • Li, H.1    Schopfer, L.M.2    Masson, P.3    Lockridge, O.4
  • 120
    • 28744458055 scopus 로고    scopus 로고
    • Mouse AChE binds in vivo to domain IV of laminin-1beta
    • Paraoanu L.E., and Layer P.G. Mouse AChE binds in vivo to domain IV of laminin-1beta. Chem. Biol. Interact. 157/158 (2005) 411-413
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 411-413
    • Paraoanu, L.E.1    Layer, P.G.2
  • 121
    • 0033577899 scopus 로고    scopus 로고
    • Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan
    • Peng H.B., Xie H., Rossi S.G., and Rotundo R.L. Acetylcholinesterase clustering at the neuromuscular junction involves perlecan and dystroglycan. J. Cell Biol. 145 (1999) 911-921
    • (1999) J. Cell Biol. , vol.145 , pp. 911-921
    • Peng, H.B.1    Xie, H.2    Rossi, S.G.3    Rotundo, R.L.4
  • 122
    • 0036159070 scopus 로고    scopus 로고
    • Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice
    • Arikawa-Hirasawa E., Rossi S.G., Rotundo R.L., and Yamada Y. Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice. Nat. Neurosci. 5 (2002) 119-123
    • (2002) Nat. Neurosci. , vol.5 , pp. 119-123
    • Arikawa-Hirasawa, E.1    Rossi, S.G.2    Rotundo, R.L.3    Yamada, Y.4
  • 124
    • 28744433847 scopus 로고    scopus 로고
    • Acetylcholinesterase and molecular interactions at the neuromuscular junction
    • Guerra M., Cartaud A., Cartaud J., and Legay C. Acetylcholinesterase and molecular interactions at the neuromuscular junction. Chem. Biol. Interact. 157/158 (2005) 57-61
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 57-61
    • Guerra, M.1    Cartaud, A.2    Cartaud, J.3    Legay, C.4
  • 126
    • 0023847896 scopus 로고
    • Sequential activation of butyrylcholinesterase in rostral half somites and acetylcholinesterase in motoneurones and myotomes preceding growth of motor axons
    • Layer P.G., Alber R., and Rathjen F.G. Sequential activation of butyrylcholinesterase in rostral half somites and acetylcholinesterase in motoneurones and myotomes preceding growth of motor axons. Development 102 (1988) 387-396
    • (1988) Development , vol.102 , pp. 387-396
    • Layer, P.G.1    Alber, R.2    Rathjen, F.G.3
  • 127
    • 0029977348 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • Greenfield S. Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem. Int. 28 (1996) 485-490
    • (1996) Neurochem. Int. , vol.28 , pp. 485-490
    • Greenfield, S.1
  • 130
    • 0031820915 scopus 로고    scopus 로고
    • Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs
    • Botti S.A., Felder C.E., Sussman J.L., and Silman I. Electrotactins: a class of adhesion proteins with conserved electrostatic and structural motifs. Protein Eng. 11 (1998) 415-420
    • (1998) Protein Eng. , vol.11 , pp. 415-420
    • Botti, S.A.1    Felder, C.E.2    Sussman, J.L.3    Silman, I.4
  • 131
    • 34249902781 scopus 로고    scopus 로고
    • Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering
    • Comoletti D., Grishaev A., Whitten A.E., Tsigelny I., Taylor P., and Trewhella J. Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure 15 (2007) 693-705
    • (2007) Structure , vol.15 , pp. 693-705
    • Comoletti, D.1    Grishaev, A.2    Whitten, A.E.3    Tsigelny, I.4    Taylor, P.5    Trewhella, J.6
  • 132
    • 0034625250 scopus 로고    scopus 로고
    • Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons
    • Scheiffele P., Fan J., Choih J., Fetter R., and Serafini T. Neuroligin expressed in nonneuronal cells triggers presynaptic development in contacting axons. Cell 101 (2000) 657-669
    • (2000) Cell , vol.101 , pp. 657-669
    • Scheiffele, P.1    Fan, J.2    Choih, J.3    Fetter, R.4    Serafini, T.5
  • 133
    • 0242317361 scopus 로고    scopus 로고
    • Making connections: cholinesterase-domain proteins in the CNS
    • Scholl F.G., and Scheiffele P. Making connections: cholinesterase-domain proteins in the CNS. TINS 26 (2003) 618-624
    • (2003) TINS , vol.26 , pp. 618-624
    • Scholl, F.G.1    Scheiffele, P.2
  • 135
    • 0032506149 scopus 로고    scopus 로고
    • Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis
    • Grifman M., Galyam N., Seidman S., and Soreq H. Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 13935-13940
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13935-13940
    • Grifman, M.1    Galyam, N.2    Seidman, S.3    Soreq, H.4
  • 136
    • 0030985407 scopus 로고    scopus 로고
    • Neurite differentiation is modulated in neuroblastoma cells engineered for altered acetylcholinesterase expression
    • Koenigsberger C., Chiappa S., and Brimijoin S. Neurite differentiation is modulated in neuroblastoma cells engineered for altered acetylcholinesterase expression. J. Neurochem. 69 (1997) 1389-1397
    • (1997) J. Neurochem. , vol.69 , pp. 1389-1397
    • Koenigsberger, C.1    Chiappa, S.2    Brimijoin, S.3
  • 137
    • 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., and Soreq H. Acetylcholinesterase enhances neurite growth and synapse development through alternative contributions of its hydrolytic capacity, core protein, and variable C termini. J. Neurosci. 18 (1998) 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    Soreq, H.7
  • 138
    • 0031903979 scopus 로고    scopus 로고
    • Acetylcholinesterase antibody treatment results in neurite detachment and reduced outgrowth from cultured neurons: further evidence for a cell adhesive role for neuronal acetylcholinesterase
    • Sharma K.V., and Bigbee J.W. Acetylcholinesterase antibody treatment results in neurite detachment and reduced outgrowth from cultured neurons: further evidence for a cell adhesive role for neuronal acetylcholinesterase. J. Neurosci. Res. 53 (1998) 454-464
    • (1998) J. Neurosci. Res. , vol.53 , pp. 454-464
    • Sharma, K.V.1    Bigbee, J.W.2
  • 139
    • 0035863556 scopus 로고    scopus 로고
    • Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth
    • Sharma K.V., Koenigsberger C., Brimijoin S., and Bigbee J.W. Direct evidence for an adhesive function in the noncholinergic role of acetylcholinesterase in neurite outgrowth. J. Neurosci. Res. 63 (2001) 165-175
    • (2001) J. Neurosci. Res. , vol.63 , pp. 165-175
    • Sharma, K.V.1    Koenigsberger, C.2    Brimijoin, S.3    Bigbee, J.W.4
  • 140
    • 0037498151 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes neurite elongation, synapse formation, and surface expression of AMPA receptors in hippocampal neurones
    • Olivera S., Rodriguez-Ithurralde D., and Henley J.M. Acetylcholinesterase promotes neurite elongation, synapse formation, and surface expression of AMPA receptors in hippocampal neurones. Mol. Cell. Neurosci. 23 (2003) 96-106
    • (2003) Mol. Cell. Neurosci. , vol.23 , pp. 96-106
    • Olivera, S.1    Rodriguez-Ithurralde, D.2    Henley, J.M.3
  • 141
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism
    • Layer P.G., Weikert T., and Alber R. Cholinesterases regulate neurite growth of chick nerve cells in vitro by means of a non-enzymatic mechanism. Cell Tissue Res. 273 (1993) 219-226
    • (1993) Cell Tissue Res. , vol.273 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 142
    • 0037114681 scopus 로고    scopus 로고
    • Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth
    • De Jaco A., Augusti-Tocco G., and Biagioni S. Alternative acetylcholinesterase molecular forms exhibit similar ability to induce neurite outgrowth. J. Neurosci. Res. 70 (2002) 756-765
    • (2002) J. Neurosci. Res. , vol.70 , pp. 756-765
    • De Jaco, A.1    Augusti-Tocco, G.2    Biagioni, S.3
  • 143
    • 0037199344 scopus 로고    scopus 로고
    • Rescue of the acetylcholinesterase knockout mouse by feeding a liquid diet; phenotype of the adult acetylcholinesterase deficient mouse
    • Duysen E.G., Stribley J.A., Fry D.L., Hinrichs S.H., and Lockridge O. Rescue of the acetylcholinesterase knockout mouse by feeding a liquid diet; phenotype of the adult acetylcholinesterase deficient mouse. Brain Res. Dev. Brain Res. 137 (2002) 43-54
    • (2002) Brain Res. Dev. Brain Res. , vol.137 , pp. 43-54
    • Duysen, E.G.1    Stribley, J.A.2    Fry, D.L.3    Hinrichs, S.H.4    Lockridge, O.5
  • 144
    • 33846552537 scopus 로고    scopus 로고
    • Reduced nicotinic receptor function in sympathetic ganglia is responsible for the hypothermia in the acetylcholinesterase knockout mouse
    • Sun M., Lee C.J., and Shin H.-S. Reduced nicotinic receptor function in sympathetic ganglia is responsible for the hypothermia in the acetylcholinesterase knockout mouse. J. Physiol. 578 (2007) 751-764
    • (2007) J. Physiol. , vol.578 , pp. 751-764
    • Sun, M.1    Lee, C.J.2    Shin, H.-S.3
  • 145
    • 34447649707 scopus 로고    scopus 로고
    • Neuropathological and immunochemical studies of brain parenchyma in acetylcholinesterase knockout mice: implications in Alzheimer's disease
    • Rice S.G., Nowak L., Duysen E.G., Lockridge O., Lahiri D.K., and Reyes P.F. Neuropathological and immunochemical studies of brain parenchyma in acetylcholinesterase knockout mice: implications in Alzheimer's disease. J. Alzheimers Dis. 11 (2007) 481-489
    • (2007) J. Alzheimers Dis. , vol.11 , pp. 481-489
    • Rice, S.G.1    Nowak, L.2    Duysen, E.G.3    Lockridge, O.4    Lahiri, D.K.5    Reyes, P.F.6
  • 146
    • 0023845757 scopus 로고
    • Modified properties of serum cholinesterases in primary carcinomas
    • Zakut H., Even L., Birkenfeld S., Malinger G., Zisling R., and Soreq H. Modified properties of serum cholinesterases in primary carcinomas. Cancer 61 (1988) 727-737
    • (1988) Cancer , vol.61 , pp. 727-737
    • Zakut, H.1    Even, L.2    Birkenfeld, S.3    Malinger, G.4    Zisling, R.5    Soreq, H.6
  • 147
    • 0025249281 scopus 로고
    • Expression of alternatively terminated unusual human butyrylcholinesterase messenger RNA transcripts, mapping to chromosome 3q26-ter, in nervous system tumors
    • Gnatt A., Prody C.A., Zamir R., Lieman-Hurwitz J., Zakut H., and Soreq H. Expression of alternatively terminated unusual human butyrylcholinesterase messenger RNA transcripts, mapping to chromosome 3q26-ter, in nervous system tumors. Cancer Res. 50 7 (1990) 1983-1987
    • (1990) Cancer Res. , vol.50 , Issue.7 , pp. 1983-1987
    • Gnatt, A.1    Prody, C.A.2    Zamir, R.3    Lieman-Hurwitz, J.4    Zakut, H.5    Soreq, H.6
  • 149
    • 28744440838 scopus 로고    scopus 로고
    • Expression of cholinesterases in brain and non-brain tumours
    • Vidal C.J. Expression of cholinesterases in brain and non-brain tumours. Chem. Biol. Interact. 157/158 (2005) 227-232
    • (2005) Chem. Biol. Interact. , vol.157-158 , pp. 227-232
    • Vidal, C.J.1
  • 151
    • 0026316185 scopus 로고
    • A role for cholinesterases in tumorigenesis?
    • Soreq H., Lapidot-Lifson Y., and Zakut H. A role for cholinesterases in tumorigenesis?. Cancer Cells 3 (1991) 511-516
    • (1991) Cancer Cells , vol.3 , pp. 511-516
    • Soreq, H.1    Lapidot-Lifson, Y.2    Zakut, H.3
  • 152
    • 0025175718 scopus 로고
    • Manipulations of cholinesterase gene expression modulate murine megakaryocytopoiesis in vitro
    • Patinkin D., Seidman S., Eckstein F., Benseler F., Zakut H., and Soreq H. Manipulations of cholinesterase gene expression modulate murine megakaryocytopoiesis in vitro. Mol. Cell. Biol. 10 (1990) 6046-6050
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6046-6050
    • Patinkin, D.1    Seidman, S.2    Eckstein, F.3    Benseler, F.4    Zakut, H.5    Soreq, H.6
  • 153
  • 154
    • 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., Ginzberg D., Eckstein F., and Zakut H. Antisense oligonucleotide inhibition of acetylcholinesterase gene expression induces progenitor cell expansion and suppresses hematopoietic apoptosis ex vivo. Proc. Natl. Acad. Sci. U.S.A. 91 17 (1994) 7907-7911
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , Issue.17 , pp. 7907-7911
    • Soreq, H.1    Patinkin, D.2    Lev-Lehman, E.3    Grifman, M.4    Ginzberg, D.5    Eckstein, F.6    Zakut, H.7
  • 155
    • 0037308205 scopus 로고    scopus 로고
    • The role of readthrough acetylcholinesterase in the pathophysiology of myasthenia gravis
    • Brenner T., Hama-Amitay Y., Evron T., Boneva N., Seidman S., and Soreq H. The role of readthrough acetylcholinesterase in the pathophysiology of myasthenia gravis. FASEB J. 17 (2003) 222-241
    • (2003) FASEB J. , vol.17 , pp. 222-241
    • Brenner, T.1    Hama-Amitay, Y.2    Evron, T.3    Boneva, N.4    Seidman, S.5    Soreq, H.6
  • 158
    • 10844253547 scopus 로고    scopus 로고
    • Acetylcholinesterase plays a pivotal role in apoptosome formation
    • Park S.E., Kim N.D., and Yoo Y.H. Acetylcholinesterase plays a pivotal role in apoptosome formation. Cancer Res. 64 (2004) 2652-2655
    • (2004) Cancer Res. , vol.64 , pp. 2652-2655
    • Park, S.E.1    Kim, N.D.2    Yoo, Y.H.3
  • 160
    • 0032574973 scopus 로고    scopus 로고
    • Acute stress facilitates long-lasting changes in cholinergic gene expression
    • Kaufer D., Friedman A., Seidman S., and Soreq H. Acute stress facilitates long-lasting changes in cholinergic gene expression. Nature 393 (1998) 373-377
    • (1998) Nature , vol.393 , pp. 373-377
    • Kaufer, D.1    Friedman, A.2    Seidman, S.3    Soreq, H.4
  • 162
    • 23244463063 scopus 로고    scopus 로고
    • The readthrough variant of acetylcholinesterase remains very minor after heat shock, organophosphate inhibition and stress, in cell culture and in vivo
    • Perrier N.A., Salani M., Falasca C., Bon S., Augusti-Tocco G., and Massoulié J. The readthrough variant of acetylcholinesterase remains very minor after heat shock, organophosphate inhibition and stress, in cell culture and in vivo. J. Neurochem. 94 (2005) 629-638
    • (2005) J. Neurochem. , vol.94 , pp. 629-638
    • Perrier, N.A.1    Salani, M.2    Falasca, C.3    Bon, S.4    Augusti-Tocco, G.5    Massoulié, J.6
  • 163
    • 0037422539 scopus 로고    scopus 로고
    • Interaction of "readthrough" acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior
    • Birikh K.R., Sklan E.H., Shoham S., and Soreq H. Interaction of "readthrough" acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior. Proc. Natl. Acad. Sci. U.S.A. 100 (2003) 283-288
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 283-288
    • Birikh, K.R.1    Sklan, E.H.2    Shoham, S.3    Soreq, H.4
  • 165
    • 0036789955 scopus 로고    scopus 로고
    • The stress-associated acetylcholinesterase variant AChE-R is expressed in human CD34(+) hematopoietic progenitors and its C-terminal peptide ARP promotes their proliferation
    • Deutsch V.R., Pick M., Perry C., Grisaru D., Hemo Y., Golan-Hadari D., Grant A., Eldor A., and Soreq H. The stress-associated acetylcholinesterase variant AChE-R is expressed in human CD34(+) hematopoietic progenitors and its C-terminal peptide ARP promotes their proliferation. Exp. Hematol. 30 (2002) 1153-1161
    • (2002) Exp. Hematol. , vol.30 , pp. 1153-1161
    • Deutsch, V.R.1    Pick, M.2    Perry, C.3    Grisaru, D.4    Hemo, Y.5    Golan-Hadari, D.6    Grant, A.7    Eldor, A.8    Soreq, H.9
  • 166
    • 0037137221 scopus 로고    scopus 로고
    • Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-beta peptide
    • Cottingham M.G., Hollinshead M.S., and Vaux D.J. Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-beta peptide. Biochemistry 41 (2002) 13539-13547
    • (2002) Biochemistry , vol.41 , pp. 13539-13547
    • Cottingham, M.G.1    Hollinshead, M.S.2    Vaux, D.J.3
  • 167
    • 0041817863 scopus 로고    scopus 로고
    • The intact human acetylcholinesterase C-terminal oligomerization domain is alpha-helical in situ and in isolation, but a shorter fragment forms beta-sheet-rich amyloid fibrils and protofibrillar oligomers
    • Cottingham M.G., Voskuil J.L.A., and Vaux D.J.T. The intact human acetylcholinesterase C-terminal oligomerization domain is alpha-helical in situ and in isolation, but a shorter fragment forms beta-sheet-rich amyloid fibrils and protofibrillar oligomers. Biochemistry 42 (2003) 10863-10873
    • (2003) Biochemistry , vol.42 , pp. 10863-10873
    • Cottingham, M.G.1    Voskuil, J.L.A.2    Vaux, D.J.T.3
  • 168
    • 0037716469 scopus 로고    scopus 로고
    • Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus
    • Bon C.L.M., and Greenfield S.A. Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. Eur. J. Neurosci. 17 (2003) 1991-1995
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 1991-1995
    • Bon, C.L.M.1    Greenfield, S.A.2
  • 169
    • 2442696373 scopus 로고    scopus 로고
    • Bioactivity of a peptide derived from acetylcholinesterase in hippocampal organotypic cultures
    • Day T., and Greenfield S.A. Bioactivity of a peptide derived from acetylcholinesterase in hippocampal organotypic cultures. Exp. Brain Res. 155 (2004) 500-508
    • (2004) Exp. Brain Res. , vol.155 , pp. 500-508
    • Day, T.1    Greenfield, S.A.2
  • 171
    • 33644912312 scopus 로고    scopus 로고
    • An acetylcholinesterase-derived peptide inhibits endocytic membrane activity in a human metastatic breast cancer cell line
    • Onganer P.U., Djamgoz M.B., Whyte K., and Greenfield S.A. An acetylcholinesterase-derived peptide inhibits endocytic membrane activity in a human metastatic breast cancer cell line. Biochim. Biophys. Acta 1760 (2006) 415-420
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 415-420
    • Onganer, P.U.1    Djamgoz, M.B.2    Whyte, K.3    Greenfield, S.A.4
  • 172
    • 0026335386 scopus 로고
    • Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression
    • Li Y., Camp S., Rachinsky T.L., Getman D., and Taylor P. Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression. J. Biol. Chem. 266 (1991) 23083-23090
    • (1991) J. Biol. Chem. , vol.266 , pp. 23083-23090
    • Li, Y.1    Camp, S.2    Rachinsky, T.L.3    Getman, D.4    Taylor, P.5
  • 173
    • 0027412198 scopus 로고
    • Promoter elements and transcriptional control of the mouse acetylcholinesterase gene
    • Li Y., Camp S., Rachinsky T.L., Bongiorno C., and Taylor P. Promoter elements and transcriptional control of the mouse acetylcholinesterase gene. J. Biol. Chem. 268 5 (1993) 3563-3572
    • (1993) J. Biol. Chem. , vol.268 , Issue.5 , pp. 3563-3572
    • Li, Y.1    Camp, S.2    Rachinsky, T.L.3    Bongiorno, C.4    Taylor, P.5
  • 174
    • 0037189942 scopus 로고    scopus 로고
    • A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis
    • Hussein A.S., Harel M., and Selkirk M.E. A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis. Mol. Biochem. Parasitol. 123 (2002) 125-134
    • (2002) Mol. Biochem. Parasitol. , vol.123 , pp. 125-134
    • Hussein, A.S.1    Harel, M.2    Selkirk, M.E.3
  • 175
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard L., and Helenius A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 3 (2003) 181-191
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2


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