메뉴 건너뛰기




Volumn 113, Issue 6, 2014, Pages 2231-2238

Acetylcholinesterase secreted by Anisakis simplex larvae (Nematoda: Anisakidae) parasitizing herring, Clupea harengus: An inverse relationship of enzyme activity in the host-parasite system

Author keywords

Acetylcholinesterase; Anisakis simplex; Herring; Host parasite system

Indexed keywords

ACETYLCHOLINESTERASE; MICROBIAL ENZYME;

EID: 84903817754     PISSN: 09320113     EISSN: 14321955     Source Type: Journal    
DOI: 10.1007/s00436-014-3878-9     Document Type: Article
Times cited : (14)

References (54)
  • 1
    • 0026697345 scopus 로고
    • Acetylcholinesterases of the nematode Steinernema carpocapsae. Characterization of two types of amphiphilic forms differing in their mode of membrane association
    • Arpagaus M, Richier P, Berge JB, Toutant JP (1992) Acetylcholinesterases of the nematode Steinernema carpocapsae. Characterization of two types of amphiphilic forms differing in their mode of membrane association. Eur J Biochem 207:1101-1108
    • (1992) Eur J Biochem , vol.207 , pp. 1101-1108
    • Arpagaus, M.1    Richier, P.2    Berge, J.B.3    Toutant, J.P.4
  • 3
    • 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
    • DOI 10.1016/S0965-1748(01)00168-0, PII S0965174801001680
    • Baxter GD, Barker SC (2002) Analysis of the sequence and expression of a second putative acetylcholinesterase cDNA from organophosphatesusceptible and organophosphate-resistant cattle ticks. Insect Biochem Mol Biol 32:815-820 (Pubitemid 34601763)
    • (2002) Insect Biochemistry and Molecular Biology , vol.32 , Issue.7 , pp. 815-820
    • Baxter, G.D.1    Barker, S.C.2
  • 4
  • 5
    • 0002470944 scopus 로고    scopus 로고
    • Biological effects of contaminants: Cholinesterase inhibition by organophosphate and carbamate compounds
    • Bocquene G, Galgani F (1998) Biological effects of contaminants: cholinesterase inhibition by organophosphate and carbamate compounds. ICES Techniques in Marine Environmental Sciences No.22, pp 1-12
    • (1998) ICES Techniques in Marine Environmental Sciences , Issue.22 , pp. 1-12
    • Bocquene, G.1    Galgani, F.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding
    • Bradford M (1976) A rapid and sensitive method for the quantitation of microgramquantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.1
  • 8
    • 0025948504 scopus 로고
    • Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne
    • Chang S, Opperman CH (1991) Characterization of acetylcholinesterase molecular forms of the root-knot nematode, Meloidogyne. Mol Biochem Parasitol 49:205-214
    • (1991) Mol Biochem Parasitol , vol.49 , pp. 205-214
    • Chang, S.1    Opperman, C.H.2
  • 9
    • 0001244640 scopus 로고
    • Separation and characterization of Heterodera glycines acetylcholinesterase molecular forms
    • Chang S, Opperman CH (1992) Separation and characterization of Heterodera glycines acetylcholinesterase molecular forms. J Nematol 24:148-155
    • (1992) J Nematol , vol.24 , pp. 148-155
    • Chang, S.1    Opperman, C.H.2
  • 10
    • 0034807653 scopus 로고    scopus 로고
    • Levels of total acetylcholinesterase in Drosophila melanogaster in relation to insecticide resistance
    • DOI 10.1006/pest.2001.2549
    • Charpentier A, Fournier D (2001) Levels of total acetylcholinesterase in Drosophila melanogaster in relation to insecticide resistance. Pesticide Biochem Physiol 70(2):100-107 (Pubitemid 32901091)
    • (2001) Pesticide Biochemistry and Physiology , vol.70 , Issue.2 , pp. 100-107
    • Charpentier, A.1    Fournier, D.2
  • 11
    • 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 JP, Arpagaus M (2000) Four genes encode acetylcholinesterases in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression. JMol Biol 300:727-742
    • (2000) JMol Biol , vol.300 , pp. 727-742
    • Combes, D.1    Fedon, Y.2    Grauso, M.3    Toutant, J.P.4    Arpagaus, M.5
  • 12
    • 0033041880 scopus 로고    scopus 로고
    • Recovery of acetylcholinesterase activity in the common carp (Cyprinus carpio L.) after inhibition by organophosphate and carbamate compounds
    • Dembele K, Haubruge E, Gaspar C (1999) Recovery of acetylcholinesterase activity in the common carp (Cyprinus carpio L.) after inhibition by organophosphate and carbamate compounds. Bull Environ Contam Toxicol 62:731-742
    • (1999) Bull Environ Contam Toxicol , vol.62 , pp. 731-742
    • Dembele, K.1    Haubruge, E.2    Gaspar, C.3
  • 13
    • 0026786726 scopus 로고
    • Characterization of cholinesterases from the parasitic nematode Trichinella spiralis
    • DeVos T, Dick TA (1992) Characterization of cholinesterases from the parasitic nematode Trichinella spiralis. Comp Biochem Physiol C Comp Pharmacol 103(1):129-134
    • (1992) Comp Biochem Physiol C Comp Pharmacol , vol.103 , Issue.1 , pp. 129-134
    • DeVos, T.1    Dick, T.A.2
  • 14
    • 1042297190 scopus 로고    scopus 로고
    • Cholinesterase activity as a bioindi-cator for monitoring marine pollution in the Baltic sea and the Mediterranean sea
    • Garrigues P, Barth H, Walker CH, Narbonne JF (eds) Elsevier, Amsterdam
    • Dizer H, da Silva de Assis HC, Hansen P-D (2001) Cholinesterase activity as a bioindi-cator for monitoring marine pollution in the Baltic sea and the Mediterranean sea. In: Garrigues P, Barth H, Walker CH, Narbonne JF (eds) Biomarkers in marine organisms: a practical approach. Elsevier, Amsterdam, p 491
    • (2001) Biomarkers in Marine Organisms: A Practical Approach , pp. 491
    • Dizer, H.1    Da Silva De Assis, H.C.2    Hansen, P.-D.3
  • 16
    • 28744431613 scopus 로고    scopus 로고
    • Mutations of acetylcholinesterase which confer insecticide resistance in insect populations
    • Fournier D (2005) Mutations of acetylcholinesterase which confer insecticide resistance in insect populations. Chem Biol Interact 157(158):257-261
    • (2005) Chem Biol Interact , vol.157 , Issue.158 , pp. 257-261
    • Fournier, D.1
  • 17
    • 0026681643 scopus 로고
    • Acetylcholinesterase two types of modifications confer resistance to insecticide
    • Fournier D, Bride JM, Hoffmann F, Karch F (1992) Acetylcholinesterase two types of modifications confer resistance to insecticide. J Biol Chem 267:14270-14274
    • (1992) J Biol Chem , vol.267 , pp. 14270-14274
    • Fournier, D.1    Bride, J.M.2    Hoffmann, F.3    Karch, F.4
  • 18
    • 0035166230 scopus 로고    scopus 로고
    • Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects
    • Fulton MH, Key PB (2001) Acetylcholinesterase inhibition in estuarine fish and invertebrates as an indicator of organophosphorus insecticide exposure and effects. Environ Toxicol Chem 20(1):37-45 (Pubitemid 32061543)
    • (2001) Environmental Toxicology and Chemistry , vol.20 , Issue.1 , pp. 37-45
    • Fulton, M.H.1    Key, P.B.2
  • 19
    • 0028352166 scopus 로고
    • Purification and biochemical characterization of acetylcholinesterase (AChE) from the excretory/secretory products of Trichostrongylus colubriformis
    • Griffiths G, Pritchard DI (1994) Purification and biochemical characterisation of acetylcholinesterase (AChE) from the excretory/secretory products of Trichostrongylus colubriformis. Parasitology 108:579-586 (Pubitemid 24201464)
    • (1994) Parasitology , vol.108 , Issue.5 , pp. 579-586
    • Griffiths, G.1    Pritchard, D.I.2
  • 20
    • 0031574297 scopus 로고    scopus 로고
    • 1) forms of acetylcholinesterase secreted by Nippostrongylus brasiliensis
    • DOI 10.1016/S0166-6851(97)00202-8, PII S0166685197002028
    • Grigg ME, Tang L, Hussein AS, Selkirk ME (1997) Purification and properties of monomeric (G1) forms of acetylcholinesterase secreted by Nippostrongylus brasiliensis. Mol Biochem Parasitol 90:513-524 (Pubitemid 28039806)
    • (1997) Molecular and Biochemical Parasitology , vol.90 , Issue.2 , pp. 513-524
    • Grigg, M.E.1    Tang, L.2    Hussein, A.S.3    Selkirk, M.E.4
  • 21
    • 0022844790 scopus 로고
    • Comparative toxicity, cholinergic effects, and tissue levels of S,S,S,-tri-n-butyl phosphorotrithioate (DEF) to channel catfish (Ictalurus punctatus) and blue crabs (Callinectes sapidus)
    • Habig C, Di Guilio RT, Nomeir AA, Abou Donia AMB (1986) Comparative toxicity, cholinergic effects and tissue levels of S, S, S-tri-n-butyl phosphorotrithioate (DEF) to channel catfish (Ictalurus punctatus) and blue crab (Callinectes sapidus). Aquat Toxicol 9(4-5):193-206 (Pubitemid 17229844)
    • (1986) Aquatic Toxicology , vol.9 , Issue.4-5 , pp. 193-206
    • Habig, C.1    Digiulio, R.T.2    Nomeir, A.A.3
  • 22
    • 0032806017 scopus 로고    scopus 로고
    • Nippostrongylus brasiliensis: Characterisation of a somatic amphiphilic acetylcholinesterase with properties distinct from the secreted enzymes
    • DOI 10.1006/expr.1998.4360
    • Hussein AS, Grigg ME, Selkirk ME (1999a) Nippostrongylus brasiliensis: characterisation of a somatic amphiphilic acetylcholinesterase with properties distinct from the secreted enzymes. Exp Parasitol 91:144-150 (Pubitemid 29370091)
    • (1999) Experimental Parasitology , vol.91 , Issue.2 , pp. 144-150
    • Hussein, A.S.1    Grigg, M.E.2    Selkirk, M.E.3
  • 23
    • 0033515474 scopus 로고    scopus 로고
    • Cloning, expression, and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis
    • Hussein AS, Chaco NMR, Smith AM, Tosado-Acevedo R, Selkirk ME (1999b) Cloning, expression, and properties of a nonneuronal secreted acetylcholinesterase from the parasitic nematode Nippostrongylus brasiliensis. J Biol Chem 274:9312-9319
    • (1999) J Biol Chem , vol.274 , pp. 9312-9319
    • Hussein, A.S.1    Chaco, N.M.R.2    Smith, A.M.3    Tosado-Acevedo, R.4    Selkirk, M.E.5
  • 24
    • 0037340274 scopus 로고    scopus 로고
    • Invertebrate biomarkers: Links to toxicosis that predict population decline
    • DOI 10.1016/S0147-6513(02)00119-7
    • Hyne RV, Maher WA (2003) Invertebrate biomarkers: links to toxicosis that predict population decline. Ecotoxicol Environ Saf 54(3):366-374 (Pubitemid 36315874)
    • (2003) Ecotoxicology and Environmental Safety , vol.54 , Issue.3 , pp. 366-374
    • Hyne, R.V.1    Maher, W.A.2
  • 25
    • 78650310655 scopus 로고    scopus 로고
    • Three acetylcholinesterases of the pinewood nematode, Bursaphelenchus xylophilus: Insights into distinct physiological functions
    • Kang JS, Lee DW, Choia JY, Je YH, Koh YH, Lee SH (2011a) Three acetylcholinesterases of the pinewood nematode, Bursaphelenchus xylophilus : insights into distinct physiological functions. Mol Biochem Parasitol 175:154-161
    • (2011) Mol Biochem Parasitol , vol.175 , pp. 154-161
    • Kang, J.S.1    Lee, D.W.2    Choia, J.Y.3    Je, Y.H.4    Koh, Y.H.5    Lee, S.H.6
  • 26
    • 79955687141 scopus 로고    scopus 로고
    • A soluble acetylcholinesterase provides chemical defense against xenobiotics in the pinewood nematode
    • doi:10.1371/journal.pone.0019063
    • Kang JS, Lee DW, Koh YH, Lee SH (2011b) A soluble acetylcholinesterase provides chemical defense against xenobiotics in the pinewood nematode. PLoS ONE 6(4):e19063. doi:10.1371/journal.pone.0019063
    • (2011) PLoS ONE , vol.6 , Issue.4
    • Kang, J.S.1    Lee, D.W.2    Koh, Y.H.3    Lee, S.H.4
  • 27
    • 0019125395 scopus 로고
    • Brain acetylcholinesterase inhibition and hepatic activation of acephate and fenitrothion in rainbow trout (Salmo gairdneri)
    • Klaverkamp JF, Hobden BR (1980) Brain acetylcholinesterase inhibition and hepatic activation of acephate and fenitrothion in rainbow trout (Salmo gairdneri). Can J Fish Aquat Sci 37(9):1450-1453. doi:10.1139/f80-186 (Pubitemid 11199670)
    • (1980) Canadian Journal of Fisheries and Aquatic Sciences , vol.37 , Issue.9 , pp. 1450-1453
    • Klaverkamp, J.F.1    Hobden, B.R.2
  • 28
    • 0034876003 scopus 로고    scopus 로고
    • Fenitroxon insensitive acetylcholinesterases of the housefly Musca domestica associated with point mutations
    • Kozaki T, Shono T, Tomita T, Kono Y (2001) Fenitroxon insensitive acetylcholinesterases of the housefly Musca domestica associated with point mutations. Insect Biochem Mol Biol 31:991- 997
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 991-997
    • Kozaki, T.1    Shono, T.2    Tomita, T.3    Kono, Y.4
  • 30
    • 2942568148 scopus 로고    scopus 로고
    • A putative neuromuscular acetylcholinesterase gene from Dictyocaulus viviparus
    • DOI 10.1016/j.molbiopara.2004.04.003, PII S0166685104001136
    • Lazari O, Selkirk ME, Ploeger HW, Matthews JB (2004) A putative neuromuscular acetylcholinesterase gene from Dictyocaulus viviparus. Mol Biochem Parasitol 136:313-317 (Pubitemid 38758001)
    • (2004) Molecular and Biochemical Parasitology , vol.136 , Issue.2 , pp. 313-317
    • Lazari, O.1    Selkirk, M.E.2    Ploeger, H.W.3    Matthews, J.B.4
  • 31
    • 0000642174 scopus 로고
    • The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the "excretory glands"
    • Lee DL (1970) The fine structure of the excretory system in adult Nippostrongylus brasiliensis (Nematoda) and a suggested function for the "excretory glands". Tissue Cell 2:225-231
    • (1970) Tissue Cell , vol.2 , pp. 225-231
    • Lee, D.L.1
  • 32
    • 33644623912 scopus 로고    scopus 로고
    • Molecular characterization of two acetylcholinesterase genes from the oriental tobacco budworm, Helicoverpa assulta (Guenée)
    • DOI 10.1016/j.bbagen.2005.10.009, PII S0304416505003363
    • Lee D-W, Kim S-S, Shin SW, Kim WT, Boo KS (2006) Molecular characterization of two acetylcholinesterase genes from the oriental tobacco budworm, Helicoverpa assulta (Guenee). Biochim Biophys Acta 1760:125-133 (Pubitemid 43320499)
    • (2006) Biochimica et Biophysica Acta - General Subjects , vol.1760 , Issue.2 , pp. 125-133
    • Lee, D.-W.1    Kim, S.-S.2    Shin, S.W.3    Kim, W.T.4    Boo, K.S.5
  • 33
    • 0036560908 scopus 로고    scopus 로고
    • The origin of the molecular diversity and functional anchoring of cholinesterases
    • Massoulie J (2002) The origin of the molecular diversity and functional anchoring of cholinesterases. Neurosignals 11:130-143
    • (2002) Neurosignals , vol.11 , pp. 130-143
    • Massoulie, J.1
  • 35
    • 84857445481 scopus 로고    scopus 로고
    • Degradation of carbofuran derivatives in restricted water environments: Basic hydrolysis in AOT-based microemulsions
    • Morales J, Manso JA, Cid A, Lodeiro C, Mejuto JC (2012) Degradation of carbofuran derivatives in restricted water environments: basic hydrolysis in AOT-based microemulsions. J Colloid Interface Sci 372:113-120
    • (2012) J Colloid Interface Sci , vol.372 , pp. 113-120
    • Morales, J.1    Manso, J.A.2    Cid, A.3    Lodeiro, C.4    Mejuto, J.C.5
  • 36
    • 21244475158 scopus 로고    scopus 로고
    • Biomarkers of contaminant exposure: Results of a field study with flounder (Platichthys flesus) from the southern Baltic Sea
    • DOI 10.1016/j.marpolbul.2005.02.007, PII S0025326X05000585
    • Napierska D, Podolska M (2005) Biomarkers of contaminant exposure: results of a field study with flounder (Platichthys flesus) from the southern Baltic Sea. Mar Pollut Bull 50:758-767 (Pubitemid 40898332)
    • (2005) Marine Pollution Bulletin , vol.50 , Issue.7 , pp. 758-767
    • Napierska, D.1    Podolska, M.2
  • 37
    • 84893875823 scopus 로고    scopus 로고
    • Muscular AChE and hepatic EROD as biomarkers of exposure in male Baltic cod (Gadus morhua)
    • Marine Environmental Research. Applied Science Publishers, Essex, ISSN 0141-1136
    • Niemi H, Jonsson H, Schneider R, Schiedek D (2002) Muscular AChE and hepatic EROD as biomarkers of exposure in male Baltic cod (Gadus morhua). Mar Environ Res 54(3-5):841-842. In: Marine Environmental Research. Applied Science Publishers, Essex, ISSN 0141-1136
    • (2002) Mar Environ Res , vol.54 , Issue.3-5 , pp. 841-842
    • Niemi, H.1    Jonsson, H.2    Schneider, R.3    Schiedek, D.4
  • 38
    • 52249103110 scopus 로고    scopus 로고
    • Multiple insecticide resistance mechanisms involving metabolic changes and insensitive target sites selected in anopheline vectors of malaria in Sri Lanka
    • Perera MDB, Hemingway J, Karunaratne SP (2008) Multiple insecticide resistance mechanisms involving metabolic changes and insensitive target sites selected in anopheline vectors of malaria in Sri Lanka. Malar J 7:168
    • (2008) Malar J , vol.7 , pp. 168
    • Perera, M.D.B.1    Hemingway, J.2    Karunaratne, S.P.3
  • 39
    • 81055155797 scopus 로고    scopus 로고
    • A tetrameric acetylcholinesterase from the parasitic nematode Dictyocaulus viviparus associates with the vertebrate tail proteins PRiMA and ColQ
    • Pezzementi L, Krejci E, Chatonnet A, Selkirk ME, Matthews JB (2012) A tetrameric acetylcholinesterase from the parasitic nematode Dictyocaulus viviparus associates with the vertebrate tail proteins PRiMA and ColQ. Mol Biochem Parasitol 181:40-48
    • (2012) Mol Biochem Parasitol , vol.181 , pp. 40-48
    • Pezzementi, L.1    Krejci, E.2    Chatonnet, A.3    Selkirk, M.E.4    Matthews, J.B.5
  • 40
    • 30044439817 scopus 로고    scopus 로고
    • Acetylcholinesterase activity in hosts (herring Clupea harengus) and parasites (Anisakis simplex larvae) from the southern Baltic
    • DOI 10.1016/j.icesjms.2005.08.001, PII S1054313905001414
    • Podolska M, Napierska D (2006) Acetylcholinesterase activity in hosts (herring Clupea harengus) and parasites (Anisakis simplex larvae) from the southern Baltic. ICES J Mar Sci 63(1):161-168. doi:10.1016/j.icesjms.2005.08.001 (Pubitemid 43048823)
    • (2006) ICES Journal of Marine Science , vol.63 , Issue.1 , pp. 161-168
    • Podolska, M.1    Napierska, D.2
  • 41
    • 43049092601 scopus 로고    scopus 로고
    • The impact of carbofuran on acetylcholinesterase activity in Anisakis simplex larvae from Baltic herring
    • doi: 10.1016/j.pestbp.2008.01.008 doi:10.1016/j.pestbp.2008.01. 008#doilink
    • Podolska M, Mulkiewicz E, Napierska D (2008) The impact of carbofuran on acetylcholinesterase activity in Anisakis simplex larvae from Baltic herring. Pestic Biochem Physiol 91(2):104-109. doi: 10.1016/j.pestbp.2008.01.008 doi:10.1016/j.pestbp.2008.01.008#doilink
    • (2008) Pestic Biochem Physiol , vol.91 , Issue.2 , pp. 104-109
    • Podolska, M.1    Mulkiewicz, E.2    Napierska, D.3
  • 42
    • 84871913182 scopus 로고    scopus 로고
    • Acetylcholinesterase secretion by third-stage larvae of Anisakis simplex (Nematoda: Anisakidae) from Baltic herring
    • Podolska M, Nadolna K, Wa̧s A, Gosz E, Szostakowska B (2012) Acetylcholinesterase secretion by third-stage larvae of Anisakis simplex (Nematoda: Anisakidae) from Baltic herring. Bull Eur Assoc Fish Pathol 32(6):225-232
    • (2012) Bull Eur Assoc Fish Pathol , vol.32 , Issue.6 , pp. 225-232
    • Podolska, M.1    Nadolna, K.2    Wa̧s, A.3    Gosz, E.4    Szostakowska, B.5
  • 43
    • 0029040105 scopus 로고
    • The survival strategies of hookworms
    • doi: 10.1016/0169-4758(95)80206-1 DOI:10.1016/0169-4758%2895%2980206- 1#doilink
    • Pritchard D(1995) The survival strategies of hookworms. Parasitol Today 11(7):255-259. doi: 10.1016/0169-4758(95)80206-1 DOI:10.1016/0169- 4758%2895%2980206-1#doilink
    • (1995) Parasitol Today , vol.11 , Issue.7 , pp. 255-259
    • Pritchard, D.1
  • 44
    • 0027952894 scopus 로고
    • The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine
    • Pritchard DI, Brown A, Toutant J-P (1994) The molecular forms of acetylcholinesterase from Necator americanus (Nematoda), a hookworm parasite of the human intestine. Eur J Biochem 219:317-323 (Pubitemid 24053646)
    • (1994) European Journal of Biochemistry , vol.219 , Issue.1-2 , pp. 317-323
    • Pritchard, D.I.1    Brown, A.2    Toutant, J.-P.3
  • 45
    • 0015452489 scopus 로고
    • Release of cholinesterase by adult Nippostrongylus brasiliensis in vitro
    • Sanderson BE (1972) Release of cholinesterase by adult Nippostrongylus brasiliensis in vitro. Z Parasitenkunde 40(1):1-7
    • (1972) Z Parasitenkunde , vol.40 , Issue.1 , pp. 1-7
    • Sanderson, B.E.1
  • 46
    • 28744443582 scopus 로고    scopus 로고
    • Nematode acetylcholinesterases are encoded by multiple genes and perform non-overlapping functions
    • DOI 10.1016/j.cbi.2005.10.039, PII S0009279705002826
    • Selkirk ME, Lazari O, Hussein AS, Matthews JB (2005a) Nematode acetylcholinesterases are encoded by multiple genes and perform non-overlapping functions. Chem Biol Interact 157-158:263-268 (Pubitemid 41757661)
    • (2005) Chemico-Biological Interactions , vol.157-158 , pp. 263-268
    • Selkirk, M.E.1    Lazari, O.2    Hussein, A.S.3    Matthews, J.B.4
  • 47
    • 33645559579 scopus 로고    scopus 로고
    • Functional genomics of nematode acetylcholinesterases
    • Selkirk ME, Lazari O, Matthews JB (2005b) Functional genomics of nematode acetylcholinesterases. Parasitology 131:S3-S18
    • (2005) Parasitology , vol.131
    • Selkirk, M.E.1    Lazari, O.2    Matthews, J.B.3
  • 48
    • 0031890110 scopus 로고    scopus 로고
    • Secretory acetylcholinesterase of Setaria cervi microfilariae and its antigenic cross-reactivity with Wuchereria bancrofti
    • DOI 10.1046/j.1365-3156.1998.00171.x
    • Sharma S, Misra S, Rathaur S (1998) Secretory acetylcholinesterase of Setaria cervi microfilariae and its antigenic cross reactivity with Wuchereria bancrofti. Trop Med Int Health 3:46-51 (Pubitemid 28081019)
    • (1998) Tropical Medicine and International Health , vol.3 , Issue.1 , pp. 46-51
    • Sharma, S.1    Misra, S.2    Rathaur, S.3
  • 49
    • 0031416457 scopus 로고    scopus 로고
    • Expression of a single dimeric membrane-bound acetylcholinesterase in Parascaris equorum
    • DOI 10.1017/S0031182097001662
    • 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 (Pubitemid 28078662)
    • (1997) Parasitology , vol.115 , Issue.6 , pp. 653-660
    • Talesa, V.1    Romani, R.2    Grauso, M.3    Rosi, G.4    Giovannini, E.5
  • 50
    • 0024489712 scopus 로고
    • Insect acetylcholinesterase: Catalytic properties, tissue distribution and molecular forms
    • Toutant JP (1989) Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms. Prog Neurobiol 32:423-446
    • (1989) Prog Neurobiol , vol.32 , pp. 423-446
    • Toutant, J.P.1
  • 51
    • 0035477633 scopus 로고    scopus 로고
    • Identification and characterization of mutations in housefly (Musca domestica) acetylcholinesterase involved in insecticide resistance
    • DOI 10.1042/0264-6021:3590175
    • Walsh SB, Dolden TA, Moores GD, Kristensen M, Lewis T, Devonshire AL, Williamson MS (2001) Identification and characterization of mutations in housefly (Musca domestica) acetylcholinesterase involved in insecticide resistance. Biochem J 359:175-181 (Pubitemid 32939219)
    • (2001) Biochemical Journal , vol.359 , Issue.1 , pp. 175-181
    • Walsh, S.B.1    Dolden, T.A.2    Moores, G.D.3    Kristensen, M.4    Lewis, T.5    Devonshire, A.L.6    Williamson, M.S.7
  • 52
    • 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
    • DOI 10.1098/rspb.2002.2122
    • Weill M, Fort P, Berthomieu A, Dubois MP, Pasteur N, Raymond M (2002) A novel acetylcholinesterase gene in mosquitoes codes for the insecticide target and is non-homologous to the ace gene in Drosophila. Proc R Soc Lond B 269:2007-2016 (Pubitemid 35177010)
    • (2002) Education Economics , vol.269 , Issue.1504 , pp. 2007-2016
    • Weill, M.1    Fort, P.2    Berthomieu, A.3    Dubois, M.P.4    Pasteur, N.5    Raymond, M.6
  • 54
    • 0000333685 scopus 로고
    • Technical and biological considerations for the analysis of brain cholinesterase of rainbow trout
    • doi:10.1577/1548-8659(1987)116<570:TABCFT>2
    • Zinkl JG, Shea PJ, Nakamoto RJ, Callman J (1987) Technical and biological considerations for the analysis of brain cholinesterase of rainbow trout. Trans Am Fish Soc 116(4):570-573. doi:10.1577/1548-8659(1987)116<570:TABCFT>2
    • (1987) Trans Am Fish Soc , vol.116 , Issue.4 , pp. 570-573
    • Zinkl, J.G.1    Shea, P.J.2    Nakamoto, R.J.3    Callman, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.