메뉴 건너뛰기




Volumn 131, Issue SUPPL. 1, 2005, Pages

Functional genomics of nematode acetylcholinesterases

Author keywords

Acetylcholinesterase; Cholinergic; Nematode; Neurotransmitter

Indexed keywords

1,5 BIS(4 ALLYLDIMETHYLAMMONIUMPHENYL)PENTAN 3 ONE DIBROMIDE; ACETYLCHOLINE; ACETYLCHOLINESTERASE; ALDICARB; ALKALOID; ALPHA CHACONINE; CARBAMIC ACID; CHOLINESTERASE; CHOLINESTERASE INHIBITOR; DECAMETHONIUM; DICHLORVOS; DONEPEZIL; EDROPHONIUM; EVODIA FRUIT; FASCICULIN; FENTHION; GALANTAMINE; GREEN FLUORESCENT PROTEIN; HALOXON; ISO OMPA; LEVAMISOLE; METRIFONATE; NEUROTOXIN; NEUROTRANSMITTER; ORGANOPHOSPHATE; PHYSOSTIGMINE; RIVASTIGMINE; SOLANINE; TRITERPENE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33645559579     PISSN: 00311820     EISSN: 14698161     Source Type: Journal    
DOI: 10.1017/S0031182005008206     Document Type: Review
Times cited : (44)

References (111)
  • 2
    • 5044229021 scopus 로고    scopus 로고
    • Identification of mutations conferring insecticide-insensitive AChE in the cotton-melon aphid, Aphis gossypii Glover
    • ANDREWS, M. C., CALLAGHAN, A., FIELD, L. M., WILLIAMSON, M. S. & MOORES, G. D. (2004). Identification of mutations conferring insecticide-insensitive AChE in the cotton-melon aphid, Aphis gossypii Glover. Insect Molecular Biology 13, 555-561.
    • (2004) Insect Molecular Biology , vol.13 , pp. 555-561
    • Andrews, M.C.1    Callaghan, A.2    Field, L.M.3    Williamson, M.S.4    Moores, G.D.5
  • 3
    • 0028308367 scopus 로고
    • cDNA sequence, gene structure, and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class a in the nematode Caenorhabditis elegans
    • ARPAGAUS, M., FEDON, Y., COUSIN, X., CHATONNET, A., BERGÉ, J.-B., FOURNIER, D. & TOUTANT, J.-P. (1994). cDNA sequence, gene structure, and in vitro expression of ace-1, the gene encoding acetylcholinesterase of class A in the nematode Caenorhabditis elegans. Journal of Biological Chemistry 269, 9957-9965.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 9957-9965
    • Arpagaus, M.1    Fedon, Y.2    Cousin, X.3    Chatonnet, A.4    Bergé, J.-B.5    Fournier, D.6    Toutant, J.-P.7
  • 4
    • 0001537321 scopus 로고
    • Two selective inhibitors of cholinesterase
    • AUSTIN, L. & BERRY, W. K. (1953). Two selective inhibitors of cholinesterase. Biochemical Journal 54, 695-700.
    • (1953) Biochemical Journal , vol.54 , pp. 695-700
    • Austin, L.1    Berry, W.K.2
  • 5
    • 0036015626 scopus 로고    scopus 로고
    • Analysis of the sequence and expression of a second putative acetylcholinesterase cDNA from organophosphate-susceptible and organophosphate-resistant cattle ticks
    • BAXTER, G. D. & BARKER, S. C. (2002). Analysis of the sequence and expression of a second putative acetylcholinesterase cDNA from organophosphate-susceptible and organophosphate-resistant cattle ticks. Insect Biochemistry and Molecular Biology 32, 815-820.
    • (2002) Insect Biochemistry and Molecular Biology , vol.32 , pp. 815-820
    • Baxter, G.D.1    Barker, S.C.2
  • 6
    • 0022493194 scopus 로고
    • Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase
    • BAZELYANSKY, M., ROBEY, E. & KIRSCH, J. F. (1986). Fractional diffusion-limited component of reactions catalyzed by acetylcholinesterase. Biochemistry 25, 125-130.
    • (1986) Biochemistry , vol.25 , pp. 125-130
    • Bazelyansky, M.1    Robey, E.2    Kirsch, J.F.3
  • 7
    • 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. & BON, S. (2004). Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation. Euopean Journal of Biochemistry 271, 1476-1487.
    • (2004) Euopean Journal of Biochemistry , vol.271 , pp. 1476-1487
    • Belbeoc'h, S.1    Falasca, C.2    Leroy, J.3    Ayon, A.4    Massoulié, J.5    Bon, S.6
  • 9
    • 0028965514 scopus 로고
    • Trans-splicing and polycistronic transcription in Caenorhabditis elegans
    • BLUMENTHAL, T. (1995). Trans-splicing and polycistronic transcription in Caenorhabditis elegans. Trends in Genetics 11, 132-136.
    • (1995) Trends in Genetics , vol.11 , pp. 132-136
    • Blumenthal, T.1
  • 10
    • 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. & MASSOULIÉ, J. (2004). The C-terminal t peptide of acetylcholinesterase forms an alpha helix that supports homomeric and heteromeric interactions. European Journal of Biochemistry 271, 33-47.
    • (2004) European Journal of Biochemistry , vol.271 , pp. 33-47
    • Bon, S.1    Dufourcq, J.2    Leroy, J.3    Cornut, I.4    Massoulié, J.5
  • 11
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • BOURNE, Y., TAYLOR, P. & MARCHOT, P. (1995). Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell 83, 503-512.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 12
    • 0025948504 scopus 로고
    • Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne
    • CHANG, S. & OPPERMAN, C. H. (1991). Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne. Molecular and Biochemical Parasitology 49, 205-214.
    • (1991) Molecular and Biochemical Parasitology , vol.49 , pp. 205-214
    • Chang, S.1    Opperman, C.H.2
  • 13
    • 0001244640 scopus 로고
    • Separation and characterization of Heterodera glycines acetylcholinesterase molecular forms
    • CHANG, S. & OPPERMAN, C. H. (1992). Separation and characterization of Heterodera glycines acetylcholinesterase molecular forms. Journal of Nematology 24, 148-155.
    • (1992) Journal of Nematology , vol.24 , pp. 148-155
    • Chang, S.1    Opperman, C.H.2
  • 14
    • 0034697999 scopus 로고    scopus 로고
    • Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression
    • COMBES, D., FEDON, Y., GRAUSO, M., TOUTANT, J. P. & ARPAGAUS, M. (2000). Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression. Journal of Molecular Biology 300, 727-742.
    • (2000) Journal of Molecular Biology , vol.300 , pp. 727-742
    • Combes, D.1    Fedon, Y.2    Grauso, M.3    Toutant, J.P.4    Arpagaus, M.5
  • 15
    • 0041879942 scopus 로고    scopus 로고
    • Multiple ace genes encoding acetylcholinesterases of Caenorhabditis elegans have distinct tissue expression
    • COMBES, D., FEDON, Y., TOUTANT, J. P. & ARPAGAUS, M. (2003). Multiple ace genes encoding acetylcholinesterases of Caenorhabditis elegans have distinct tissue expression. European Journal of Neuroscience 18, 497-512.
    • (2003) European Journal of Neuroscience , vol.18 , pp. 497-512
    • Combes, D.1    Fedon, Y.2    Toutant, J.P.3    Arpagaus, M.4
  • 16
    • 0034519915 scopus 로고    scopus 로고
    • Neurotransmitters in neuronal reflexes regulating intestinal secretion
    • COOKE, H. J. (2000). Neurotransmitters in neuronal reflexes regulating intestinal secretion. Annals of the New York Academy of Sciences 915, 77-80.
    • (2000) Annals of the New York Academy of Sciences , vol.915 , pp. 77-80
    • Cooke, H.J.1
  • 17
    • 15844399958 scopus 로고    scopus 로고
    • Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom
    • COUSIN, X., BON, S., DUVAL, N., MASSOULIÉ, J. & BON, C. (1996a). Cloning and expression of acetylcholinesterase from Bungarus fasciatus venom. Journal of Biological Chemistry 271, 15099-15108.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 15099-15108
    • Cousin, X.1    Bon, S.2    Duval, N.3    Massoulié, J.4    Bon, C.5
  • 18
    • 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. & BON, C. (1998). 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. Journal of Biological Chemistry 273, 9812-9820.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 9812-9820
    • Cousin, X.1    Bon, S.2    Massoulié, J.3    Bon, C.4
  • 21
    • 0033618267 scopus 로고    scopus 로고
    • Structure and promoter activity of the 5′ flanking region of ace-1, the gene encoding acetylcholinesterase of class A in Caenorhabditis elegans
    • CULETTO, E., COMBES, D., FEDON, Y., ROIG, A., TOUTANT, J. P. & ARPAGAUS, M. (1999). Structure and promoter activity of the 5′ flanking region of ace-1, the gene encoding acetylcholinesterase of class A in Caenorhabditis elegans. Journal of Molecular Biology 290, 951-966.
    • (1999) Journal of Molecular Biology , vol.290 , pp. 951-966
    • Culetto, E.1    Combes, D.2    Fedon, Y.3    Roig, A.4    Toutant, J.P.5    Arpagaus, M.6
  • 23
    • 0019525053 scopus 로고
    • A second class of acetylcholinesterase-deficient mutants of the nematode Caenorhabditis elegans
    • CULOTTI, J. G., VON EHRENSTEIN, G., CULOTTI, M. R. & RUSSELL, R. L. (1981). A second class of acetylcholinesterase-deficient mutants of the nematode Caenorhabditis elegans. Genetics 97, 281-305.
    • (1981) Genetics , vol.97 , pp. 281-305
    • Culotti, J.G.1    Von Ehrenstein, G.2    Culotti, M.R.3    Russell, R.L.4
  • 24
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
    • CYGLER, M., SCHRAG, J. D., SUSSMAN, J. L., HAREL, M., SILMAN, I., GENTRY, M. K. & DOCTOR, B. P. (1993). Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Science 2, 366-382.
    • (1993) Protein Science , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 25
    • 0032105405 scopus 로고    scopus 로고
    • The hypothesis of an ambient level of acetylcholine in the central nervous system
    • DESCARRIES, L. (1998). The hypothesis of an ambient level of acetylcholine in the central nervous system. Journal of Physiology Paris 92, 215-220.
    • (1998) Journal of Physiology Paris , vol.92 , pp. 215-220
    • Descarries, L.1
  • 26
    • 0026786726 scopus 로고
    • Characterization of cholinesterases from the parasitic nematode Trichinella spiralis
    • DE VOS, T. & DICK, T. A. (1992). Characterization of cholinesterases from the parasitic nematode Trichinella spiralis. Comparative Biochemistry and Physiology C 103, 129-134.
    • (1992) Comparative Biochemistry and Physiology C , vol.103 , pp. 129-134
    • De Vos, T.1    Dick, T.A.2
  • 27
    • 0041921105 scopus 로고    scopus 로고
    • Current treatments for Alzheimer's disease: Cholinesterase inhibitors
    • DOODY, R. S. (2003). Current treatments for Alzheimer's disease: cholinesterase inhibitors. Journal of Clinical Psychiatry 64 (Suppl. 9), 11-17.
    • (2003) Journal of Clinical Psychiatry , vol.64 , Issue.9 SUPPL. , pp. 11-17
    • Doody, R.S.1
  • 29
    • 0015041059 scopus 로고
    • The effect of host immunity upon some enzymes of the parasitic nematode, Nippostrongylus brasiliensis
    • EDWARDS, A. J., BURT, J. S. & OGILVIE, B. M. (1971). The effect of host immunity upon some enzymes of the parasitic nematode, Nippostrongylus brasiliensis. Parasitology 62, 339-347.
    • (1971) Parasitology , vol.62 , pp. 339-347
    • Edwards, A.J.1    Burt, J.S.2    Ogilvie, B.M.3
  • 30
    • 0028177161 scopus 로고
    • Differential effects of "peripheral" site ligands on Torpedo and chicken acetylcholinesterase
    • EICHLER, J., ANSELMENT, A., SUSSMAN, J. L., MASSOULIÉ, J. & SILMAN, I. (1994). Differential effects of "peripheral" site ligands on Torpedo and chicken acetylcholinesterase. Molecular Pharmacology 45, 335-340.
    • (1994) Molecular Pharmacology , vol.45 , pp. 335-340
    • Eichler, J.1    Anselment, A.2    Sussman, J.L.3    Massoulié, J.4    Silman, I.5
  • 31
    • 0005023450 scopus 로고
    • Etude expérimentale de l'activité anthelminthique de quelques cucurbitacines
    • FORGACS, P., PROVOST, J. & TIBERGHION, R. (1970). Etude expérimentale de l'activité anthelminthique de quelques cucurbitacines. Actualites de Chimie Thérapeutique 5, 205-210.
    • (1970) Actualites de Chimie Thérapeutique , vol.5 , pp. 205-210
    • Forgacs, P.1    Provost, J.2    Tiberghion, R.3
  • 34
    • 4444229179 scopus 로고    scopus 로고
    • The changing landscape of antiparasitic drug discovery for veterinary medicine
    • GEARY, T. G., CONDER, G. A. & BISHOP, B. (2004). The changing landscape of antiparasitic drug discovery for veterinary medicine. Trends in Parasitology 20, 449-455.
    • (2004) Trends in Parasitology , vol.20 , pp. 449-455
    • Geary, T.G.1    Conder, G.A.2    Bishop, B.3
  • 38
    • 0032513228 scopus 로고    scopus 로고
    • Existence of four acetylcholinesterase genes in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae
    • GRAUSO, M., CULETTO, E., COMBES, D., FEDON, Y., TOUTANT, J.-P. & ARPAGAUS, M. (1998). Existence of four acetylcholinesterase genes in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. FEBS Letters 424, 279-284.
    • (1998) FEBS Letters , vol.424 , pp. 279-284
    • Grauso, M.1    Culetto, E.2    Combes, D.3    Fedon, Y.4    Toutant, J.-P.5    Arpagaus, M.6
  • 39
    • 0019525451 scopus 로고
    • The isolation of a field isolate of Haemonchus contortus in Queensland showing multiple anthelmintic resistance
    • GREEN, P. E., FORSYTH, B. A., ROWAN, K. J. & PAYNE, G. (1981). The isolation of a field isolate of Haemonchus contortus in Queensland showing multiple anthelmintic resistance. Australian Veterinary Journal 57, 79-84.
    • (1981) Australian Veterinary Journal , vol.57 , pp. 79-84
    • Green, P.E.1    Forsyth, B.A.2    Rowan, K.J.3    Payne, G.4
  • 40
    • 0642309501 scopus 로고    scopus 로고
    • Acetylcholinesterase: A multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease
    • GREENBLATT, H. M., DVIR, H., SILMAN, I. & SUSSMAN, J. L. (2003). Acetylcholinesterase: a multifaceted target for structure-based drug design of anticholinesterase agents for the treatment of Alzheimer's disease. Journal of Molecular Neuroscience 20, 369-383.
    • (2003) Journal of Molecular Neuroscience , vol.20 , pp. 369-383
    • Greenblatt, H.M.1    Dvir, H.2    Silman, I.3    Sussman, J.L.4
  • 41
    • 0028352166 scopus 로고
    • Purification and biochemical characterisation of acetylcholinesterase (AChE) from the excretory/secretory products of Trichostrongylus colubriformis
    • GRIFFITHS, G. & PRITCHARD, D. I. (1994). Purification and biochemical characterisation of acetylcholinesterase (AChE) from the excretory/secretory products of Trichostrongylus colubriformis. Parasitology 108, 579-586.
    • (1994) Parasitology , vol.108 , pp. 579-586
    • Griffiths, G.1    Pritchard, D.I.2
  • 42
    • 0031574297 scopus 로고    scopus 로고
    • Purification and properties of monomeric (G1) forms of acetylcholinesterase secreted by Nippostrongylus brasiliensis
    • GRIGG, M. E., TANG, L., HUSSEIN, A. S. & SELKIRK, M. E. (1997). Purification and properties of monomeric (G1) forms of acetylcholinesterase secreted by Nippostrongylus brasiliensis. Molecular and Biochemical Parasitology 90, 513-524.
    • (1997) Molecular and Biochemical Parasitology , vol.90 , pp. 513-524
    • Grigg, M.E.1    Tang, L.2    Hussein, A.S.3    Selkirk, M.E.4
  • 43
    • 0010989660 scopus 로고
    • The Ace locus of Drosophila melanogaster: Structural gene for acetylcholinesterase with an unusual 5′ leader
    • HALL, L. M. C. & SPIERER, P. (1986). The Ace locus of Drosophila melanogaster: structural gene for acetylcholinesterase with an unusual 5′ leader. EMBO Journal 5, 2949-2954.
    • (1986) EMBO Journal , vol.5 , pp. 2949-2954
    • Hall, L.M.C.1    Spierer, P.2
  • 46
    • 0033515474 scopus 로고    scopus 로고
    • Cloning, expression, and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis
    • HUSSEIN, A. S., CHACÓN, M. R., SMITH, A. M., TOSADO-ACEVEDO, R. & SELKIRK, M. E. (1999). Cloning, expression, and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. Journal of Biological Chemistry 274, 9312-9319.
    • (1999) Journal of Biological Chemistry , vol.274 , pp. 9312-9319
    • Hussein, A.S.1    Chacón, M.R.2    Smith, A.M.3    Tosado-Acevedo, R.4    Selkirk, M.E.5
  • 47
    • 0032806017 scopus 로고    scopus 로고
    • Nippostrongylus brasiliensis: Characterisation of a somatic amphiphilic acetylcholinesterase with properties distinct from the secreted enzymes
    • HUSSEIN, A. S., GRIGG, M. E. & SELKIRK, M. E. (1999). Nippostrongylus brasiliensis: characterisation of a somatic amphiphilic acetylcholinesterase with properties distinct from the secreted enzymes. Experimental Parasitology 91, 144-150.
    • (1999) Experimental Parasitology , vol.91 , pp. 144-150
    • Hussein, A.S.1    Grigg, M.E.2    Selkirk, M.E.3
  • 48
    • 0037189942 scopus 로고    scopus 로고
    • A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis
    • HUSSEIN, A. S., HAREL, M. & SELKIRK, M. E. (2002). A distinct family of acetylcholinesterases is secreted by Nippostrongylus brasiliensis. Molecular and Biochemical Parasitology 123, 125-134.
    • (2002) Molecular and Biochemical Parasitology , vol.123 , pp. 125-134
    • Hussein, A.S.1    Harel, M.2    Selkirk, M.E.3
  • 49
    • 0036079595 scopus 로고    scopus 로고
    • Suppression of secreted acetylcholinesterase expression in Nippostrongylus brasiliensis by RNA interference
    • HUSSEIN, A. S., KICHENIN, K. & SELKIRK, M. E. (2002). Suppression of secreted acetylcholinesterase expression in Nippostrongylus brasiliensis by RNA interference. Molecular and Biochemical Parasitology 122, 91-94.
    • (2002) Molecular and Biochemical Parasitology , vol.122 , pp. 91-94
    • Hussein, A.S.1    Kichenin, K.2    Selkirk, M.E.3
  • 50
    • 0034008857 scopus 로고    scopus 로고
    • Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis
    • HUSSEIN, A. S., SMITH, A. M., CHACON, M. R. & SELKIRK, M. E. (2000). Determinants of substrate specificity of a second non-neuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. European Journal of Biochemistry 267, 2276-2282.
    • (2000) European Journal of Biochemistry , vol.267 , pp. 2276-2282
    • Hussein, A.S.1    Smith, A.M.2    Chacon, M.R.3    Selkirk, M.E.4
  • 53
    • 0023985973 scopus 로고
    • The acetylcholinesterase genes of C. elegans: Identification of a third gene (ace-3) and mosaic mapping of a synthetic lethal phenotype
    • JOHNSON, C. D., RAND, J. R., HERMAN, R. K., STERN, B. D. & RUSSELL, R. L. (1988). The acetylcholinesterase genes of C. elegans: identification of a third gene (ace-3) and mosaic mapping of a synthetic lethal phenotype. Neuron 1, 165-173.
    • (1988) Neuron , vol.1 , pp. 165-173
    • Johnson, C.D.1    Rand, J.R.2    Herman, R.K.3    Stern, B.D.4    Russell, R.L.5
  • 54
    • 0015262882 scopus 로고
    • Protective immunity to Nippostrongylus brasiliensis in the rat III. Modulation of worm acetylcholinesterase by antibodies
    • JONES, V. E. & OGILVIE, B. M. (1972). Protective immunity to Nippostrongylus brasiliensis in the rat III. Modulation of worm acetylcholinesterase by antibodies. Immunology 22, 119-129.
    • (1972) Immunology , vol.22 , pp. 119-129
    • Jones, V.E.1    Ogilvie, B.M.2
  • 55
    • 0032574973 scopus 로고    scopus 로고
    • Acute stress facilitates long-lasting changes in cholinergic gene expression
    • KAUFER, D., FRIEDMAN, A., SEIDMAN, S. & SOREQ, H. (1998). Acute stress facilitates long-lasting changes in cholinergic gene expression. Nature 393, 373-377.
    • (1998) Nature , vol.393 , pp. 373-377
    • Kaufer, D.1    Friedman, A.2    Seidman, S.3    Soreq, H.4
  • 57
    • 0021985875 scopus 로고
    • A novel class of acetylcholinesterase, revealed by mutations, in the nematode Caenorhabditis elegans
    • KOLSON, D. L. & RUSSELL, R. L. (1985). A novel class of acetylcholinesterase, revealed by mutations, in the nematode Caenorhabditis elegans. Journal of Neurogenetics 2, 93-110.
    • (1985) Journal of Neurogenetics , vol.2 , pp. 93-110
    • Kolson, D.L.1    Russell, R.L.2
  • 61
    • 0000642174 scopus 로고
    • The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the "excretory glands"
    • LEE, D. L. (1970). The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the "excretory glands". Tissue and Cell 2, 225-231.
    • (1970) Tissue and Cell , vol.2 , pp. 225-231
    • Lee, D.L.1
  • 62
    • 0030152902 scopus 로고    scopus 로고
    • Why do some nematode parasites of the alimentary tract secrete acetylcholinesterase?
    • LEE, D. L. (1996). Why do some nematode parasites of the alimentary tract secrete acetylcholinesterase? International Journal for Parasitology 26, 499-508.
    • (1996) International Journal for Parasitology , vol.26 , pp. 499-508
    • Lee, D.L.1
  • 63
    • 0018879884 scopus 로고
    • Levamisole-resistant mutants of the nematode Caenorhabditis elegans appear to lack pharmacological acetylcholine receptors
    • LEWIS, J. A., WU, C. H., LEVINE, J. H. & BERG, H. (1980). Levamisole-resistant mutants of the nematode Caenorhabditis elegans appear to lack pharmacological acetylcholine receptors. Neuroscience 5, 967-989.
    • (1980) Neuroscience , vol.5 , pp. 967-989
    • Lewis, J.A.1    Wu, C.H.2    Levine, J.H.3    Berg, H.4
  • 64
    • 1842539316 scopus 로고    scopus 로고
    • Mutations in acetylcholinesterase associated with insecticide resistance in the cotton aphid, Aphis gossypii Glover
    • LI, F. & HAN, Z. (2004). Mutations in acetylcholinesterase associated with insecticide resistance in the cotton aphid, Aphis gossypii Glover. Insect Biochemistry and Molecular Biology 34, 397-405.
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , pp. 397-405
    • Li, F.1    Han, Z.2
  • 66
    • 0034009408 scopus 로고    scopus 로고
    • Pesticides and susceptible populations: People with butyrylcholinesterase genetic variants may be at risk
    • LOCKRIDGE, O. & MASSON, P. (2000). Pesticides and susceptible populations: people with butyrylcholinesterase genetic variants may be at risk. Neurotoxicology 21, 113-126.
    • (2000) Neurotoxicology , vol.21 , pp. 113-126
    • Lockridge, O.1    Masson, P.2
  • 67
    • 0030767507 scopus 로고    scopus 로고
    • Modes of action of anthelmintic drugs
    • MARTIN, R. J. (1997). Modes of action of anthelmintic drugs. Veterinary Journal 154, 11-34.
    • (1997) Veterinary Journal , vol.154 , pp. 11-34
    • Martin, R.J.1
  • 69
    • 0036560908 scopus 로고    scopus 로고
    • The origin of the molecular diversity and functional anchoring of cholinesterases
    • MASSOULIÉ, J. (2002). The origin of the molecular diversity and functional anchoring of cholinesterases. Neurosignals 11, 130-143.
    • (2002) Neurosignals , vol.11 , pp. 130-143
    • Massoulié, J.1
  • 70
    • 0027981671 scopus 로고
    • The immunogenicity of the acetylcholinesterases of the cattle lungworm, Dictyocaulus viviparus
    • McKEAND, J. B., KNOX, D. P., DUNCAN, J. L. & KENNEDY, M. W. (1994). The immunogenicity of the acetylcholinesterases of the cattle lungworm, Dictyocaulus viviparus. International Journal for Parasitology 24, 501-510.
    • (1994) International Journal for Parasitology , vol.24 , pp. 501-510
    • McKeand, J.B.1    Knox, D.P.2    Duncan, J.L.3    Kennedy, M.W.4
  • 71
    • 4444290353 scopus 로고    scopus 로고
    • Veterinary anthelmintics: Old and new
    • McKELLAR, Q. A. & JACKSON, F. (2004). Veterinary anthelmintics: old and new. Trends in Parasitology 20, 456-461.
    • (2004) Trends in Parasitology , vol.20 , pp. 456-461
    • McKellar, Q.A.1    Jackson, F.2
  • 72
    • 0000372029 scopus 로고    scopus 로고
    • Muscle: Structure, function and development
    • Eds. Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R. Cold Spring Harbor Press, Cold Spring Harbor, New York
    • MOERMAN, D. G. & FIRE, A. (1997). Muscle: structure, function and development. In C. elegans II (Eds. Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R.), pp. 417-470. Cold Spring Harbor Press, Cold Spring Harbor, New York.
    • (1997) C. Elegans II , pp. 417-470
    • Moerman, D.G.1    Fire, A.2
  • 73
    • 0029053849 scopus 로고
    • Caenorhabditis elegans mutants resistant to inhibitors of acetylcholinesterase
    • NGUYEN, M., ALFONSO, A., JOHNSON, C. D. & RAND, J. B. (1995). Caenorhabditis elegans mutants resistant to inhibitors of acetylcholinesterase. Genetics 140, 527-535.
    • (1995) Genetics , vol.140 , pp. 527-535
    • Nguyen, M.1    Alfonso, A.2    Johnson, C.D.3    Rand, J.B.4
  • 76
    • 0029819784 scopus 로고    scopus 로고
    • Paneth cell defensins: Endogenous peptide components of intestinal host defense
    • OUELLETTE, A. J. & SELSTED, M. E. (1996). Paneth cell defensins: endogenous peptide components of intestinal host defense. FASEB Journal 10, 1280-1289.
    • (1996) FASEB Journal , vol.10 , pp. 1280-1289
    • Ouellette, A.J.1    Selsted, M.E.2
  • 77
    • 0029044370 scopus 로고
    • Atanine (3-dimethylallyl-4-methoxy-2-quinolone), an alkaloid with anthelmintic activity from the Chinese medicinal plant, Evodia rutaecarpa
    • PERRETT, S. & WHITFIELD, P. J. (1995). Atanine (3-dimethylallyl-4- methoxy-2-quinolone), an alkaloid with anthelmintic activity from the Chinese medicinal plant, Evodia rutaecarpa. Planta Medica 61, 276-278.
    • (1995) Planta Medica , vol.61 , pp. 276-278
    • Perrett, S.1    Whitfield, P.J.2
  • 78
    • 0032908417 scopus 로고    scopus 로고
    • Molecular cloning of an acetylcholinesterase gene from the plant parasitic nematodes, Meloidogyne incognita and Meloidogyne javanica
    • PIOTTE, C., ARTHAUD, L., ABAD, P. & ROSSO, M. N. (1999). Molecular cloning of an acetylcholinesterase gene from the plant parasitic nematodes, Meloidogyne incognita and Meloidogyne javanica. Molecular and Biochemical Parasitology 99, 247-256.
    • (1999) Molecular and Biochemical Parasitology , vol.99 , pp. 247-256
    • Piotte, C.1    Arthaud, L.2    Abad, P.3    Rosso, M.N.4
  • 79
    • 0027952894 scopus 로고
    • The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine
    • PRITCHARD, D. I., BROWN, A. & TOUTANT, J.-P. (1994). The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine. European Journal of Biochemistry 219, 317-323.
    • (1994) European Journal of Biochemistry , vol.219 , pp. 317-323
    • Pritchard, D.I.1    Brown, A.2    Toutant, J.-P.3
  • 80
    • 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. (1992). Expression of recombinant acetylcholinesterase in a baculovirus system: kinetic properties of glutamate 199 mutants. Biochemistry 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
  • 81
    • 0027517144 scopus 로고
    • Three distinct domains in the cholinesterase molecule confer selectivity for acetyl-and butyrylcholinesterase inhibitors
    • RADIC, Z., PICKERING, N. A., VELLOM, D. C., CAMP, S. & TAYLOR, P. (1993). Three distinct domains in the cholinesterase molecule confer selectivity for acetyl-and butyrylcholinesterase inhibitors. Biochemistry 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
  • 82
    • 0001704141 scopus 로고    scopus 로고
    • Synaptic transmission
    • Eds. Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • RAND, J. B. & NONET, M. L. (1997a). Synaptic transmission. In C. elegans II (Eds. Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R.), pp. 611-643. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1997) C. Elegans II , pp. 611-643
    • Rand, J.B.1    Nonet, M.L.2
  • 83
    • 0003060331 scopus 로고    scopus 로고
    • Neurotransmitter assignments for specific neurons
    • Eds. Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • RAND, J. B. & NONET, M. L. (1997b). Neurotransmitter assignments for specific neurons. In C. elegans II (Eds. Riddle, D. L., Blumenthal, T., Meyer, B. J. & Priess, J. R.), pp. 1049-1052. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1997) C. Elegans II , pp. 1049-1052
    • Rand, J.B.1    Nonet, M.L.2
  • 84
    • 0019877268 scopus 로고
    • Cholinesterase in the parasitic nematode Stephanurus dentatus. Characterisation and sex dependence of a secretory cholinesterase
    • RHOADS, M. L. (1981). Cholinesterase in the parasitic nematode Stephanurus dentatus. Characterisation and sex dependence of a secretory cholinesterase. Journal of Biological Chemistry 256, 9316-9323.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 9316-9323
    • Rhoads, M.L.1
  • 85
    • 0002294584 scopus 로고
    • Secretory cholinesterases of nematodes: Possible functions in the host-parasite relationship
    • RHOADS, M. L. (1984). Secretory cholinesterases of nematodes: possible functions in the host-parasite relationship. Tropical Veterinarian 2, 3-10.
    • (1984) Tropical Veterinarian , vol.2 , pp. 3-10
    • Rhoads, M.L.1
  • 88
    • 0015452489 scopus 로고
    • Release of cholinesterase by adult Nippostrongylus brasiliensis in vitro
    • SANDERSON, B. E. (1972). Release of cholinesterase by adult Nippostrongylus brasiliensis in vitro. Zeitschrift für Parasitenkunde 40, 1-7.
    • (1972) Zeitschrift für Parasitenkunde , vol.40 , pp. 1-7
    • Sanderson, B.E.1
  • 89
    • 0015351146 scopus 로고
    • Nippostrongylus brasiliensis: Relation between immune damage and acetylcholinesterase levels
    • SANDERSON, B. E., JENKINS, D. C. & OGILVIE, B. M. (1972). Nippostrongylus brasiliensis: relation between immune damage and acetylcholinesterase levels. International Journal for Parasitology 2, 227-232.
    • (1972) International Journal for Parasitology , vol.2 , pp. 227-232
    • Sanderson, B.E.1    Jenkins, D.C.2    Ogilvie, B.M.3
  • 90
    • 0017236328 scopus 로고
    • Nippostrongylus brasiliensis: Further studies of the relation between host immunity and worm acetylcholinesterase levels
    • SANDERSON, B. E., JENKINS, D. C. & PHILLIPSON, R. F. (1976). Nippostrongylus brasiliensis: further studies of the relation between host immunity and worm acetylcholinesterase levels. International Journal for Parasitology 6, 99-102.
    • (1976) International Journal for Parasitology , vol.6 , pp. 99-102
    • Sanderson, B.E.1    Jenkins, D.C.2    Phillipson, R.F.3
  • 91
    • 0032893559 scopus 로고    scopus 로고
    • Anthelmintic resistance: Past, present and future
    • SANGSTER, N. C. (1999). Anthelmintic resistance: past, present and future. International Journal for Parasitology 29, 115-124.
    • (1999) International Journal for Parasitology , vol.29 , pp. 115-124
    • Sangster, N.C.1
  • 92
    • 0025953486 scopus 로고
    • Effects of cholinergic drugs on longitudinal contraction in levamisole-susceptible and -resistant Haemonchus contortus
    • SANGSTER, N. C., DAVIS, C. W. & COLLINS, G. H. (1991). Effects of cholinergic drugs on longitudinal contraction in levamisole-susceptible and -resistant Haemonchus contortus. International Journal for Parasitology 21, 689-695.
    • (1991) International Journal for Parasitology , vol.21 , pp. 689-695
    • Sangster, N.C.1    Davis, C.W.2    Collins, G.H.3
  • 93
    • 0026638027 scopus 로고
    • Bethanechol and a G-protein activator, NaF/AlCl3, induce secretory response in Paneth cells of mouse intestine
    • SATOH, Y., ISHIKAWA, K., OOMORI, Y., TAKEDA, S. & ONO, K. (1992). Bethanechol and a G-protein activator, NaF/AlCl3, induce secretory response in Paneth cells of mouse intestine. Cell and Tissue Research 269, 213-220.
    • (1992) Cell and Tissue Research , vol.269 , pp. 213-220
    • Satoh, Y.1    Ishikawa, K.2    Oomori, Y.3    Takeda, S.4    Ono, K.5
  • 94
    • 0002638639 scopus 로고
    • Steroid alkaloids. Solanum groups
    • Ed. Manske, R. H., Academic Press, New York
    • SCHREIBER, K. (1968). Steroid alkaloids. Solanum groups. In The Alkaloids (Ed. Manske, R. H.), pp. 1-192. Academic Press, New York.
    • (1968) The Alkaloids , pp. 1-192
    • Schreiber, K.1
  • 95
    • 0027538616 scopus 로고
    • Actions of cholinergic drugs in the nematode Ascaris suum. Complex pharmacology of muscle and motorneurons
    • SEGERBERG, M. A. & STRETTON, A. O. (1993). Actions of cholinergic drugs in the nematode Ascaris suum. Complex pharmacology of muscle and motorneurons. Journal of General Physiology 101, 271-296.
    • (1993) Journal of General Physiology , vol.101 , pp. 271-296
    • Segerberg, M.A.1    Stretton, A.O.2
  • 96
    • 0008223663 scopus 로고    scopus 로고
    • Acetylcholinesterase secretion by nematodes
    • Eds. Kennedy, M. W. & Harnett, W., Wallingford, Oxon, CAB International, Wallingford, Oxon
    • SELKIRK, M. E., HENSON, S., RUSSELL, W. S. & HUSSEIN, A. S. (2001). Acetylcholinesterase secretion by nematodes. In Parasitic Nematodes (Eds. Kennedy, M. W. & Harnett, W.), pp. 211-228. Wallingford, Oxon, CAB International, Wallingford, Oxon.
    • (2001) Parasitic Nematodes , pp. 211-228
    • Selkirk, M.E.1    Henson, S.2    Russell, W.S.3    Hussein, A.S.4
  • 97
    • 0007912520 scopus 로고
    • In vitro anthelmintic screening of indigenous medicinal plants against Haemonchus contortus of sheep and goats
    • SHARMA, L. D., BAHGA, H. S. & SRIVASTAVA, P. S. (1971). In vitro anthelmintic screening of indigenous medicinal plants against Haemonchus contortus of sheep and goats. Indian Journal of Animal Research 1, 33-38.
    • (1971) Indian Journal of Animal Research , vol.1 , pp. 33-38
    • Sharma, L.D.1    Bahga, H.S.2    Srivastava, P.S.3
  • 98
    • 0032476586 scopus 로고    scopus 로고
    • A four-to-one association between peptide motifs: Four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway
    • SIMON, S., KREJCI, E. & MASSOULIÉ, J. (1998). A four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway. EMBO Journal 17, 6178-6187.
    • (1998) EMBO Journal , vol.17 , pp. 6178-6187
    • Simon, S.1    Krejci, E.2    Massoulié, J.3
  • 101
  • 102
    • 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. & SILMAN, I. (1991). Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 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    Silman, I.7
  • 103
    • 0031416457 scopus 로고    scopus 로고
    • Expression of a single dimeric membrane-bound acetylcholinesterase in Parascaris equorum
    • TALESA, V., ROMANI, R., GRAUSO, M., ROSI, G. & GIOVANNINI, E. (1997). Expression of a single dimeric membrane-bound acetylcholinesterase in Parascaris equorum. Parasitology 115, 653-660.
    • (1997) Parasitology , vol.115 , pp. 653-660
    • Talesa, V.1    Romani, R.2    Grauso, M.3    Rosi, G.4    Giovannini, E.5
  • 105
    • 0024489712 scopus 로고
    • Insect acetylcholinesterase: Catalytic properties, tissue distribution and molecular forms
    • TOUTANT, J.-P. (1989). Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms. Progress in Neurobiology 32, 423-446.
    • (1989) Progress in Neurobiology , vol.32 , pp. 423-446
    • Toutant, J.-P.1
  • 107
    • 0037180778 scopus 로고    scopus 로고
    • The inflammatory reflex
    • TRACEY, K. J. (2002). The inflammatory reflex. Nature 420, 853-859.
    • (2002) Nature , vol.420 , pp. 853-859
    • Tracey, K.J.1
  • 108
    • 34250090541 scopus 로고
    • Steroidal glycoalkaloids in tubers and leaves of Solanum species used in potato breeding
    • VAN GELDER, W. M. J., VINKE, J. H. & SCHEFFER, J. J. C. (1988). Steroidal glycoalkaloids in tubers and leaves of Solanum species used in potato breeding. Euphytica 37S, 147-158.
    • (1988) Euphytica , vol.37 S , pp. 147-158
    • Van Gelder, W.M.J.1    Vinke, J.H.2    Scheffer, J.J.C.3
  • 109
    • 0027459560 scopus 로고
    • Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity
    • VELLOM, D. C., RADIC, Z., LI, Y., PICKERING, N. A., CAMP, S. & TAYLOR, P. (1993). Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity. Biochemistry 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
  • 111
    • 0002880367 scopus 로고
    • Acetylcholinesterase X. Mechanism of the catalysis of acylation reactions
    • WILSON, I. B., BERGMANN, F. & NACHMANSOHN, D. (1950). Acetylcholinesterase X. Mechanism of the catalysis of acylation reactions. Journal of Biological Chemistry 186, 781-790.
    • (1950) Journal of Biological Chemistry , vol.186 , pp. 781-790
    • Wilson, I.B.1    Bergmann, F.2    Nachmansohn, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.