메뉴 건너뛰기




Volumn 212, Issue , 2011, Pages 29-59

The use of cholinesterases in ecotoxicology

Author keywords

[No Author keywords available]

Indexed keywords

CHOLINESTERASE; CHOLINESTERASE INHIBITOR;

EID: 79953653234     PISSN: 01795953     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8453-1_2     Document Type: Article
Times cited : (130)

References (116)
  • 2
    • 0018180747 scopus 로고
    • Characteristics of cholinesterase of the earthworm Eisenia foetida
    • Andersen RA, Aune T, Barstad JAB (1978) Characteristics of cholinesterase of the earthworm Eisenia foetida. Compar Biochem Physiol Part C: Compar Pharmacol 61(1): 81-87. (Pubitemid 9037223)
    • (1978) Comparative Biochemistry and Physiology , vol.C61 , Issue.1 , pp. 81-87
    • Anderson, R.A.1    Aune, T.2    Barstad, J.A.B.3
  • 3
    • 34547876457 scopus 로고    scopus 로고
    • Cholinesterase activity in gilthead seabream (Sparus aurata) larvae: Characterization and sensitivity to the organophosphate azinphosmethyl
    • DOI 10.1016/j.aquatox.2007.06.009, PII S0166445X07002482
    • Arufe MI, Arellano JM, García L, Albendín G, Sarasquete C (2007) Cholinesterase activity in gilthead seabream (Sparus aurata) larvae: characterization and sensitivity to the organophosphate azinphosmethyl. Aquat Toxicol 84: 328-336. (Pubitemid 47260732)
    • (2007) Aquatic Toxicology , vol.84 , Issue.3 , pp. 328-336
    • Arufe, M.I.1    Arellano, J.M.2    Garcia, L.3    Albendin, G.4    Sarasquete, C.5
  • 4
    • 0346098284 scopus 로고    scopus 로고
    • Effects of sublethal fenitrothion ingestion on cholinesterase inhibition, standard metabolism, thermal preference, and prey-capture ability in the Australian central bearded dragon (Pogona vitticeps, Agamidae)
    • DOI 10.1897/02-555
    • Bain D, Buttemer WA, Astheimer L, Fildes K, Hooper MJ (2004) Effects of sublethal fenitrothion ingestion on cholinesterase inhibition, standard metabolism, thermal preference, and prey-capture ability in the Australian central bearded dragon (Pogona vitticeps, Agamidae) Environ Toxicol Chem 23(1): 109-16. (Pubitemid 38049659)
    • (2004) Environmental Toxicology and Chemistry , vol.23 , Issue.1 , pp. 109-116
    • Bain, D.1    Buttemer, W.A.2    Astheimer, L.3    Fildes, K.4    Hooper, M.J.5
  • 5
    • 1242318578 scopus 로고    scopus 로고
    • Role of B-esterases in assessing toxicity of organophosphorus (chlorpyrifos, malathion) and carbamate (carbofuran) pesticides to Daphnia magna
    • DOI 10.1016/j.aquatox.2003.07.004
    • Barata C, Solayan A, Porte C (2004) Role of B-esterases in assessing toxicity of organophosphorus (chlorpyrifos, malathion) and carbamate (carbofuran) pesticides to Daphnia magna. Aquat Toxicol 66: 125-139. (Pubitemid 38229248)
    • (2004) Aquatic Toxicology , vol.66 , Issue.2 , pp. 125-139
    • Barata, C.1    Solayan, A.2    Porte, C.3
  • 6
    • 67349257504 scopus 로고    scopus 로고
    • Cholinesterases in the Antarctic scallop Adamussium colbecki: Characterization and sensitivity to pollutants
    • Bonacci S, Corsi I, Focardi S (2009) Cholinesterases in the Antarctic scallop Adamussium colbecki: Characterization and sensitivity to pollutants. Ecotoxicol Environ Saf 72: 1481-1488.
    • (2009) Ecotoxicol Environ Saf , vol.72 , pp. 1481-1488
    • Bonacci, S.1    Corsi, I.2    Focardi, S.3
  • 7
    • 0030046771 scopus 로고    scopus 로고
    • The membrane anchor of mammalian brain acetylcholinesterase consists of a single glycosylated protein of 22 kDa
    • DOI 10.1016/0014-5793(96)00041-5
    • Boschetti N, Brodbeck U (1996) The membrane anchor of mammalian brain acetylcholinesterase consists of a single glycosylated protein of 22 kDa. FEBS Letters 380: 133-136. (Pubitemid 26058745)
    • (1996) FEBS Letters , vol.380 , Issue.1-2 , pp. 133-136
    • Boschetti, N.1    Brodbeck, U.2
  • 8
    • 0142199918 scopus 로고    scopus 로고
    • Characterisation of choline esterases and their tissue and subcellular distribution in mussel (Mytilus edulis)
    • DOI 10.1016/S0141-1136(03)00067-9
    • Brown M, Davies IM, Moffat CF, Redshaw J, Craft JA (2004) Characterisation of choline esterases and their tissue and subcellular distribution in mussel (Mytilus edulis) Mar Environ Res 57: 155-169. (Pubitemid 37315828)
    • (2004) Marine Environmental Research , vol.57 , Issue.3 , pp. 155-169
    • Brown, M.1    Davies, I.M.2    Moffat, C.F.3    Redshaw, J.4    Craft, J.A.5
  • 10
    • 79953657671 scopus 로고    scopus 로고
    • Neurobehavioral responses of the freshwater teleost, Cyprinus carpio (Linnaeus.) under quinalphos intoxication
    • Chebbi SG, David M (2009) Neurobehavioral responses of the freshwater teleost, Cyprinus carpio (Linnaeus.) under quinalphos intoxication. Biotechnol Animal Husband 25(3-4): 241-249.
    • (2009) Biotechnol Animal Husband , vol.25 , Issue.3-4 , pp. 241-249
    • Chebbi, S.G.1    David, M.2
  • 11
    • 0032557420 scopus 로고    scopus 로고
    • Over-expression of acetylcholinesterase stimulates the expression of agrin in NG108-15 cells
    • DOI 10.1016/S0304-3940(98)00320-6, PII S0304394098003206
    • Choi RCY, Yama SCY, Hui B, Wan DCC, Tsim KWK (1998) Over-expression of acetylcholinesterase stimulates the expression of agrin in NG108-15 cells. Neurosci Lett 248: 17-20. (Pubitemid 28267092)
    • (1998) Neuroscience Letters , vol.248 , Issue.1 , pp. 17-20
    • Choi, R.C.Y.1    Yam, S.C.Y.2    Hui, B.3    Wan, D.C.C.4    Tsim, K.W.K.5
  • 12
    • 33947309206 scopus 로고    scopus 로고
    • Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: Specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide
    • Chuiko GM (2000) Comparative study of acetylcholinesterase and butyrylcholinesterase in brain and serum of several freshwater fish: specific activities and in vitro inhibition by DDVP, an organophosphorus pesticide. Compar Biochem Physiol, part C Toxicol Pharmacol 127(3): 233-42.
    • (2000) Compar Biochem Physiol, Part C Toxicol Pharmacol , vol.127 , Issue.3 , pp. 233-42
    • Chuiko, G.M.1
  • 14
    • 34247573481 scopus 로고    scopus 로고
    • Effects of copper and cadmium on cholinesterase and glutathione S-transferase activities of two marine gastropods (Monodonta lineata and Nucella lapillus)
    • DOI 10.1016/j.cbpc.2007.02.014, PII S1532045607000889
    • Cunha I, Mangas-Ramirez E, Guilhermino L (2007) Effects of copper and cadmium on cholinesterase and glutathione S-transferase activities of two marine gastropods (Monodonta lineata and Nucella lapillus). Compar Biochem Physiol, Part C 145: 648-657. (Pubitemid 46671531)
    • (2007) Comparative Biochemistry and Physiology - C Toxicology and Pharmacology , vol.145 , Issue.4 , pp. 648-657
    • Cunha, I.1    Mangas-Ramirez, E.2    Guilhermino, L.3
  • 16
    • 0030907519 scopus 로고    scopus 로고
    • Esterases in the zebra mussel Dreissena polymorpha: Activities, inhibition, and binding to organophosphates
    • DOI 10.1016/S0166-445X(96)00831-4, PII S0166445X96008314
    • Dauberschmidt C, Dietrich DR, Christian Schlatter C (1997) Esterases in the zebra mussel Dreissena polymorpha: activities, inhibition, and binding to organophosphates. Aquat Toxicol 37(4): 295-305. (Pubitemid 27223358)
    • (1997) Aquatic Toxicology , vol.37 , Issue.4 , pp. 295-305
    • Dauberschmidt, C.1    Dietrich, D.R.2    Schlatter, C.3
  • 17
    • 37149003168 scopus 로고    scopus 로고
    • Cholinesterase activity as a biomarker of pesticide exposure in Allolobophora chlorotica earthworms living in apple orchards under different management strategies
    • DOI 10.1897/06-355.1
    • Denoyelle R, Rault M, Mazzia C, Mascle O, Capowiez Y (2007) Cholinesterase activity as a biomarker of pesticide exposure in Allolobophora chlorotica earthworms living in apple orchards under different management strategies. Environ Toxicol Chem 26(12): 2644-9. (Pubitemid 350252940)
    • (2007) Environmental Toxicology and Chemistry , vol.26 , Issue.12 , pp. 2644-2649
    • Denoyelle, R.1    Rault, M.2    Mazzia, C.3    Mascle, O.4    Capowiez, Y.5
  • 18
    • 0037458635 scopus 로고    scopus 로고
    • Post-transcriptional regulation of acetylcholinesterase mRNAs in nerve growth factor-treated PC12 cells by the RNA-binding protein HuD
    • DOI 10.1074/jbc.M209383200
    • Deschênes-Furry J, Bélanger G, Perrone-Bizzozero N, Jasmin BJ (2003) Post-transcriptional Regulation of Acetylcholinesterase mRNAs in Nerve Growth Factor-treated PC12 Cells by the RNA-binding Protein HuD. J Biolog Chem 278(8): 5710-5717. (Pubitemid 36800815)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.8 , pp. 5710-5717
    • Deschenes-Furry, J.1    Belanger, G.2    Perrone-Bizzozero, N.3    Jasmin, B.J.4
  • 19
    • 33746914317 scopus 로고    scopus 로고
    • Effects of an organophosphate on Daphnia magna at suborganismal and organismal levels: Implications for population dynamics
    • DOI 10.1016/j.ecoenv.2006.01.008, PII S0147651306000248
    • Duquesne S (2006) Effects of an organophosphate on Daphnia magna at suborganismal and organismal levels: Implications for population dynamics. Ecotoxicol Environ Saf 65: 145-150. (Pubitemid 44190108)
    • (2006) Ecotoxicology and Environmental Safety , vol.65 , Issue.2 , pp. 145-150
    • Duquesne, S.1
  • 21
    • 0030176761 scopus 로고    scopus 로고
    • Acetylcholinesterase Inhibition in the Crayfish Procambarus clarkii Exposed to Fenitrothion
    • Escartín E, Porte C (1996) Acetylcholinesterase Inhibition in the Crayfish Procambarus clarkii Exposed to Fenitrothion. Ecotoxicolo Environ Saf 34: 160-164.
    • (1996) Ecotoxicolo Environ Saf , vol.34 , pp. 160-164
    • Escartín, E.1    Porte, C.2
  • 23
    • 0035992170 scopus 로고    scopus 로고
    • Cholinesterase activity and effects of its inhibition by neurotoxic drugs in Dictyostelium discoideum
    • DOI 10.1016/S0045-6535(02)00143-1, PII S0045653502001431
    • Falugi C, Amaroli A, Evangelisti V, Viarengo A, Delmonte Corrado MU (2002) Cholinesterase activity and effects of its inhibition by neurotoxic drugs in Dictyostelium discoideum. Chemosphere 48: 407-414. (Pubitemid 34650943)
    • (2002) Chemosphere , vol.48 , Issue.4 , pp. 407-414
    • Falugi, C.1    Amaroli, A.2    Evangelisti, V.3    Viarengo, A.4    Delmonte Corrado, M.U.5
  • 24
    • 34547153170 scopus 로고    scopus 로고
    • Muscular and brain cholinesterase sensitivities to azinphos methyl and carbaryl in the juvenile rainbow trout Oncorhynchus mykiss
    • DOI 10.1016/j.cbpc.2007.04.002, PII S1532045607001068
    • Ferrari A, Venturino A, Pechén de D'Angelo AM (2007) Muscular and brain cholinesterase sensitivities to azinphos methyl and carbaryl in the juvenile rainbow trout Oncorhynchus mykiss. Compar Biochem Physiol, Part C 146: 308-313. (Pubitemid 47127005)
    • (2007) Comparative Biochemistry and Physiology - C Toxicology and Pharmacology , vol.146 , Issue.3 , pp. 308-313
    • Ferrari, A.1    Venturino, A.2    Pechen De D'Angelo, A.M.3
  • 25
    • 0036258955 scopus 로고    scopus 로고
    • Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe)
    • DOI 10.1016/S1532-0456(02)00050-9, PII S1532045602000509
    • Forget J, Livet S, Leboulenger F (2002) Partial purification and characterization of acetylcholinesterase (AChE) from the estuarine copepod Eurytemora affinis (Poppe). Compar Biochem Physiol Part C 132: 85-92. (Pubitemid 34556931)
    • (2002) Comparative Biochemistry and Physiology - C Toxicology and Pharmacology , vol.132 , Issue.1 , pp. 85-92
    • Forget, J.1    Livet, S.2    Leboulenger, F.3
  • 26
    • 0032828083 scopus 로고    scopus 로고
    • Partial purification and enzymatic characterization of acetylcholinesterase from the intertidal marine copepod Tigriopus brevicornis
    • DOI 10.1016/S0305-0491(99)00073-5, PII S0305049199000735
    • Forget J, Bocquené G (1999) Partial purification and enzymatic characterization of acetylcholinesterase from the intertidal marine copepod Tigriopus brevicornis. Compar Biochem Physiol Part B 123: 345-350. (Pubitemid 29414772)
    • (1999) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.123 , Issue.4 , pp. 345-350
    • Forget, J.1    Bocquene, G.2
  • 27
    • 0024283578 scopus 로고
    • Acetylcholinesterase from Drosophila melanogaster-Identification of two subunits encoded by the same gene
    • Fournier D, Bride JM, Karch F, Bergé JB (1988) Acetylcholinesterase from Drosophila melanogaster-Identification of two subunits encoded by the same gene. FEBS Letters 238(2): 333-337.
    • (1988) FEBS Letters , vol.238 , Issue.2 , pp. 333-337
    • Fournier, D.1    Bride, J.M.2    Karch, F.3    Bergé, J.B.4
  • 28
    • 33646470860 scopus 로고    scopus 로고
    • Cholinesterase from the common prawn (Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds
    • Frasco MF, Fournier D, Carvalho F, Guilhermino L (2006) Cholinesterase from the common prawn (Palaemon serratus) eyes: Catalytic properties and sensitivity to organophosphate and carbamate compounds. Aquat Toxicol 77: 412-421.
    • (2006) Aquat Toxicol , vol.77 , pp. 412-421
    • Frasco, M.F.1    Fournier, D.2    Carvalho, F.3    Guilhermino, L.4
  • 29
    • 28244482330 scopus 로고    scopus 로고
    • Do metals inhibit acetylcholinesterase (AchE)? Implementation of assay conditions for the use of AchE activity as a biomarker of metal toxicity
    • DOI 10.1080/13547500500264660
    • Frasco MF, Fournier D, Carvalho F, Guilhermino L (2005) Do metals inhibit acetylcholinesterase (AChE)? Implementation of assay conditions for the use of AChE activity as a biomarker of metal toxicity. Biomarkers 10(5): 360-375. (Pubitemid 41701226)
    • (2005) Biomarkers , vol.10 , Issue.5 , pp. 360-375
    • Frasco, M.F.1    Fournier, D.2    Carvalho, F.3    Guilhermino, L.4
  • 30
    • 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: 37-45. (Pubitemid 32061543)
    • (2001) Environmental Toxicology and Chemistry , vol.20 , Issue.1 , pp. 37-45
    • Fulton, M.H.1    Key, P.B.2
  • 31
    • 34247499110 scopus 로고    scopus 로고
    • Acetylcholinesterase activity in the earthworm Eisenia andrei at different conditions of carbaryl exposure
    • DOI 10.1016/j.cbpc.2007.03.002, PII S1532045607000932
    • Gambi N, Pasteris A, Fabbri E (2007) Acetylcholinesterase activity in the earthworm Eisenia andrei at different conditions of carbaryl exposure. Compar Biochem Physiol, Part C 145: 678-685. (Pubitemid 46660758)
    • (2007) Comparative Biochemistry and Physiology - C Toxicology and Pharmacology , vol.145 , Issue.4 , pp. 678-685
    • Gambi, N.1    Pasteris, A.2    Fabbri, E.3
  • 32
    • 0036433158 scopus 로고    scopus 로고
    • Increased expression of an acetylcholinesterase gene may confer organophosphate resistance in the greenbug, Schizaphis graminum (Homoptera: Aphididae)
    • DOI 10.1016/S0048-3575(02)00105-0, PII S0048357502001050
    • Gao JR, Zhu KY (2002) Increased expression of an acetylcholinesterase gene may confer organophosphate resistance in the greenbug, Schizaphis graminum (Homoptera: Aphididae). Pesticide Biochem Physiol 73: 164-173. (Pubitemid 35352992)
    • (2002) Pesticide Biochemistry and Physiology , vol.73 , Issue.3 , pp. 164-173
    • Gao, J.-R.1    Zhu, K.Y.2
  • 33
    • 0033869281 scopus 로고    scopus 로고
    • Characterization of cholinesterase from guppy (Poecilia reticulata) muscle and its in vitro inhibition by environmental contaminants
    • Garcia LM, Castro B, Ribeiro R, Guilhermino L (2000) Characterization of cholinesterase from guppy (Poecilia reticulata) muscle and its in vitro inhibition by environmental contaminants. Biomarkers 5(4): 274-284. (Pubitemid 30641271)
    • (2000) Biomarkers , vol.5 , Issue.4 , pp. 274-284
    • Garcia, L.M.1    Castro, B.2    Ribeiro, R.3    Guilhermino, L.4
  • 34
    • 4043074138 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: New roles and therapeutic alternatives
    • DOI 10.1016/j.phrs.2003.11.017, PII S1043661804000854
    • Giacobini E (2004) Cholinesterase inhibitors: new roles and therapeutic alternatives. Pharmacological Res 50: 433-440. (Pubitemid 39078534)
    • (2004) Pharmacological Research , vol.50 , Issue.4 , pp. 433-440
    • Giacobini, E.1
  • 35
    • 77952135903 scopus 로고    scopus 로고
    • In vivo acute effects of several pharmaceutical drugs (diazepam, clofibrate, clofibric acid) and detergents (sodium dodecyl-sulphate and benzalkonium chloride) on cholinesterases from Gambusia holbrooki
    • Gonçalves A, Padrão J, Gonçalves F, Nunes B (2010) In vivo acute effects of several pharmaceutical drugs (diazepam, clofibrate, clofibric acid) and detergents (sodium dodecyl-sulphate and benzalkonium chloride) on cholinesterases from Gambusia holbrooki. Fresenius Environ Bull 19(4): 628-634.
    • (2010) Fresenius Environ Bull , vol.19 , Issue.4 , pp. 628-634
    • Gonçalves, A.1    Padrão, J.2    Gonçalves, F.3    Nunes, B.4
  • 36
    • 0019506626 scopus 로고
    • Regulation of Acetylcholinesterase Activity by Nerve Growth Factor
    • Greene LA, Rukenstein A (1981) Regulation of Acetylcholinesterase Activity by Nerve Growth Factor. J Biolog Chem 256(12): 6363-6367.
    • (1981) J Biolog Chem , vol.256 , Issue.12 , pp. 6363-6367
    • Greene, L.A.1    Rukenstein, A.2
  • 37
    • 0034689161 scopus 로고    scopus 로고
    • In vitro and in vivo inhibition of Daphnia magna acetylcholinesterase by surfactant agents: Possible implications for contamination biomonitoring
    • DOI 10.1016/S0048-9697(99)00485-4, PII S0048969799004854
    • Guilhermino L, Lacerda MN, Nogueira AJA, Soares AMVM (2000) In vitro and in vivo inhibition of Daphnia magna acetylcholinesterase by surfactant agents: possible implications for contamination biomonitoring. Sci Tot Env 247: 137-141. (Pubitemid 30145666)
    • (2000) Science of the Total Environment , vol.247 , Issue.2-3 , pp. 137-141
    • Guilhermino, L.1    Lacerda, M.N.2    Nogueira, A.J.A.3    Soares, A.M.V.M.4
  • 39
    • 2242420933 scopus 로고    scopus 로고
    • Plasma cholinesterase levels of mountain plovers (Charadrius montanus) wintering in Central California, USA
    • Iko WM, Archuleta AS, Knopf FL (2003) Plasma cholinesterase levels of mountain plovers (Charadrius montanus) wintering in central California, USA. Environ Toxicol Chem 22(1): 119-25. (Pubitemid 35471328)
    • (2003) Environmental Toxicology and Chemistry , vol.22 , Issue.1 , pp. 119-125
    • Iko, W.M.1    Archuleta, A.S.2    Knopf, F.L.3
  • 41
    • 0035949809 scopus 로고    scopus 로고
    • Biotransformation of organophosphorus compounds
    • Jokanovic M (2001) Biotransformation of organophosphorus compounds. Toxicology 166: 139-160.
    • (2001) Toxicology , vol.166 , pp. 139-160
    • Jokanovic, M.1
  • 42
    • 33947610970 scopus 로고    scopus 로고
    • Characterization of cholinesterases in marbled sole, Limanda yokohamae, and their inhibition in vitro by the fungicide iprobenfos
    • DOI 10.1016/j.marenvres.2006.12.007, PII S0141113606002200
    • Jung JH, Addison RF, Shim WJ (2007) Characterization of cholinesterases in marbled sole, Limanda yokohamae, and their inhibition in vitro by the fungicide iprobenfos. Mar Environl Res 63: 471-478 (Pubitemid 46483668)
    • (2007) Marine Environmental Research , vol.63 , Issue.5 , pp. 471-478
    • Jung, J.-H.1    Addison, R.F.2    Shim, W.J.3
  • 43
    • 0036290021 scopus 로고    scopus 로고
    • Characterization of cholinesterase activity in tissues of the grass shrimp (Palaemonetes pugio)
    • DOI 10.1016/S0048-3575(02)00006-8, PII S0048357502000068
    • Key PB, Fulton MH (2002) Characterization of cholinesterase activity in tissues of the grass shrimp (Palaemonetes pugio). Pesticide Biochem Physiol 72: 186-192. (Pubitemid 34706633)
    • (2002) Pesticide Biochemistry and Physiology , vol.72 , Issue.3 , pp. 186-192
    • Key, P.B.1    Fulton, M.H.2
  • 44
    • 0014750669 scopus 로고
    • On the question: Is acetylcholinesterase an allosteric protein?
    • Kitz RJ, Braswell LM, Ginsburg S (1970) On the question: is acetylcholinesterase an allosteric protein? Molecular Pharmacol 6: 108-121.
    • (1970) Molecular Pharmacol , vol.6 , pp. 108-121
    • Kitz, R.J.1    Braswell, L.M.2    Ginsburg, S.3
  • 45
    • 79953658104 scopus 로고    scopus 로고
    • Biomarker responses in coral trout (Plectropomus leopardus) as an indicator of exposure to contaminants in a coral reef environment
    • Klumpp D, Humphrey C, King SC (2007) Biomarker responses in coral trout (Plectropomus leopardus) as an indicator of exposure to contaminants in a coral reef environment. Austral J Ecotoxicol 13: 9-17.
    • (2007) Austral J Ecotoxicol , vol.13 , pp. 9-17
    • Klumpp, D.1    Humphrey, C.2    King, S.C.3
  • 46
    • 33749037761 scopus 로고    scopus 로고
    • AChE levels in mussels and fish collected off Lithuania and Poland (southern Baltic)
    • Kopecka J, Rybakowas A, Barsiené J, Pempkowiak J (2004) AChE levels in mussels and fish collected off Lithuania and Poland (southern Baltic). Oceanologia 46(3): 405-418.
    • (2004) Oceanologia , vol.46 , Issue.3 , pp. 405-418
    • Kopecka, J.1    Rybakowas, A.2    Barsiené, J.3    Pempkowiak, J.4
  • 48
    • 74849112998 scopus 로고    scopus 로고
    • Inhibition of cholinesterases and carboxylesterases of two invertebrate species, Biomphalaria glabrata and Lumbriculus variegatus, by the carbamate pesticide carbaryl
    • Kristoff G, Guerrero NR, Cochón AC (2010) Inhibition of cholinesterases and carboxylesterases of two invertebrate species, Biomphalaria glabrata and Lumbriculus variegatus, by the carbamate pesticide carbaryl. Aquat Toxicol 96(2): 115-23.
    • (2010) Aquat Toxicol , vol.96 , Issue.2 , pp. 115-23
    • Kristoff, G.1    Guerrero, N.R.2    Cochón, A.C.3
  • 49
    • 56449097158 scopus 로고    scopus 로고
    • B-type esterases in the snail Xeropicta derbentina: An enzymological analysis to evaluate their use as biomarkers of pesticide exposure
    • Laguerre C, Sanchez-Hernandez JC, Köhler HR, Triebskorn R, Capowiez Y, Rault M, Mazzia C (2009) B-type esterases in the snail Xeropicta derbentina: An enzymological analysis to evaluate their use as biomarkers of pesticide exposure. Environ Pollut 157: 199-207.
    • (2009) Environ Pollut , vol.157 , pp. 199-207
    • Laguerre, C.1    Sanchez-Hernandez, J.C.2    Köhler, H.R.3    Triebskorn, R.4    Capowiez, Y.5    Rault, M.6    Mazzia, C.7
  • 50
    • 53049109848 scopus 로고    scopus 로고
    • Determination of esterase activity and characterization of cholinesterases in the reef fish Haemulon plumieri
    • Leticia AG, Gerardo GB (2008) Determination of esterase activity and characterization of cholinesterases in the reef fish Haemulon plumieri. Ecotoxicol Environm Saf 71: 787-797.
    • (2008) Ecotoxicol Environm Saf , vol.71 , pp. 787-797
    • Leticia, A.G.1    Gerardo, G.B.2
  • 51
    • 38649110135 scopus 로고    scopus 로고
    • Effects of nonionic and ionic surfactants on survival, oxidative stress, and cholinesterase activity of planarian
    • DOI 10.1016/j.chemosphere.2007.08.032, PII S0045653507010569
    • Li M-H (2008) Effects of nonionic and ionic surfactants on survival, oxidative stress, and cholinesterase activity of planarian. Chemosphere 70: 1796-1803 (Pubitemid 351173247)
    • (2008) Chemosphere , vol.70 , Issue.10 , pp. 1796-1803
    • Li, M.-H.1
  • 52
    • 26444490621 scopus 로고    scopus 로고
    • Humans appear no more sensitive than laboratory animals to the inhibition of red blood cell cholinesterase by dichlorvos
    • DOI 10.1016/j.yrtph.2005.06.013, PII S027323000500111X
    • MacGregor JA, Plunkett LM, Youngren SH, Manley A, Plunkett JB, Starr TB (2005) Humans appear no more sensitive than laboratory animals to the inhibition of red blood cell cholinesterase by dichlorvos. Regulatory Toxicol Pharmacol 43: 150-167. (Pubitemid 41427808)
    • (2005) Regulatory Toxicology and Pharmacology , vol.43 , Issue.2 , pp. 150-167
    • MacGregor, J.A.1    Plunkett, L.M.2    Youngren, S.H.3    Manley, A.4    Plunkett, J.B.5    Starr, T.B.6
  • 54
    • 0033956134 scopus 로고    scopus 로고
    • The key role of butyrylcholinesterase during neurogenesis and neural disorders: An antisense-5'butyrylcholinesterase-DNA study
    • DOI 10.1016/S0301-0082(99)00047-7, PII S0301008299000477
    • Mack A, Robitzki A (2000) The key role of butyrylcholinesterase during neurogenesis and neural disorders: an antisense-5'butyrylcholinesterase-DNA study. Progress in Neurobiol 60: 607-628. (Pubitemid 30100400)
    • (2000) Progress in Neurobiology , vol.60 , Issue.6 , pp. 607-628
    • Mack, A.1    Robitzki, A.2
  • 55
    • 17644435468 scopus 로고    scopus 로고
    • Theoretical and experimental investigations of electrostatic effects on acetylcholinesterase catalysis and inhibition
    • DOI 10.1016/S0009-2797(99)00018-6, PII S0009279799000186
    • Malany S, Baker N, Verweyst N, Medhekar R, Quinn DM, Velan B, Kronman C, Shafferman A (1999) Theoretical and experimental investigations of electrostatic effects on acetylcholinesterase catalysis and inhibition. Chemico-Biolog Interact 119-120: 99-110. (Pubitemid 29278543)
    • (1999) Chemico-Biological Interactions , vol.119-120 , pp. 99-110
    • Malany, S.1    Baker, N.2    Verweyst, M.3    Medhekar, R.4    Quinn, D.M.5    Velan, B.6    Kronman, C.7    Shafferman, A.8
  • 57
    • 0020021171 scopus 로고
    • The molecular forms of cholinesterase and acetylcholinesterase in vertebrates
    • Massoulié J, Bon S (1982) The molecular forms of cholinesterase and acetylcholinesterase in vertebrates. Ann Rev Neurosci 5: 57-106.
    • (1982) Ann Rev Neurosci , vol.5 , pp. 57-106
    • Massoulié, J.1    Bon, S.2
  • 58
    • 21444437128 scopus 로고    scopus 로고
    • Monitoring exposure of northern cardinals, Cardinalis cardinalis, to cholinesterase-inhibiting pesticides: Enzyme activity, reactivations, and indicators of environmental stress
    • DOI 10.1897/04-385R.1
    • Maul JD, Farris JL (2005) Monitoring exposure of northern cardinals, Cardinalis cardinalis, to cholinesterase-inhibiting pesticides: enzyme activity, reactivations, and indicators of environmental stress. Environ Toxicol Chem 24(7): 1721-30. (Pubitemid 40917194)
    • (2005) Environmental Toxicology and Chemistry , vol.24 , Issue.7 , pp. 1721-1730
    • Maul, J.D.1    Farris, J.L.2
  • 59
    • 0029987754 scopus 로고    scopus 로고
    • Monitoring exposure of nestling songbirds to agricultural application of an organophosphorus insecticide using cholinesterase activity
    • DOI 10.1897/1551-5028(1996)015<0544:MEONST>2.3.CO;2
    • McInnes PF, Andersen DE, Hoff DJ, Hooper MJ, Kinkell LL (1996) Monitoring exposure of nestling songbirds to agricultural application of an organophosphorus insecticide using cholinesterase activity. Environ Toxicol Chem 15(4): 544-552. (Pubitemid 26110328)
    • (1996) Environmental Toxicology and Chemistry , vol.15 , Issue.4 , pp. 544-552
    • Mcinnes, P.F.1    Andersen, D.E.2    Hoff, D.J.3    Hooper, M.J.4    Kinkel, L.L.5
  • 60
    • 0037219182 scopus 로고    scopus 로고
    • Involvement of oxidative stress in the enhancement of acetylcholinesterase activity induced by amyloid beta-peptide
    • DOI 10.1016/S0168-0102(02)00201-8, PII S0168010202002018
    • Melo JB, Agostinho P, Oliveira CR (2003) Involvement of oxidative stress in the enhancement of acetylcholinesterase activity induced by amyloid beta-peptide. Neurosci Res 45: 117-127. (Pubitemid 36044475)
    • (2003) Neuroscience Research , vol.45 , Issue.1 , pp. 117-127
    • Melo, J.B.1    Agostinho, P.2    Oliveira, C.R.3
  • 62
    • 26444498011 scopus 로고    scopus 로고
    • Characterization of the cholinesterases present in head tissues of the estuarine fish Pomatoschistus microps: Application to biomonitoring
    • DOI 10.1016/j.ecoenv.2004.12.007, PII S0147651304002520
    • Monteiro M, Quintaneiro C, Morgado F, Soares AMVM, Guilhermino L (2005) Characterization of the cholinesterases present in head tissues of the estuarine fish Pomatoschistus microps: Application to biomonitoring. Ecotoxicol Environ Saf 62: 341-347 (Pubitemid 41430382)
    • (2005) Ecotoxicology and Environmental Safety , vol.62 , Issue.3 , pp. 341-347
    • Monteiro, M.1    Quintaneiro, C.2    Morgado, F.3    Soares, A.M.V.M.4    Guilhermino, L.5
  • 63
    • 0032986278 scopus 로고    scopus 로고
    • Cholinesterases from the marine mussels Mytilus galloprovincialis Lmk. and M. edulis L. and from the freshwater bivalve Corbicula fluminea Muller
    • DOI 10.1016/S0742-8413(98)10130-5, PII S0742841398101305
    • Mora P, Fournier D, Narbonne JF (1999) Cholinesterases from the marine mussels Mytilus galloprovincialis Lmk. and M. edulis L. and from the freshwater bivalve Corbicula fluminea Müller. Compar Biochem Physiol Part C 122: 353-361. (Pubitemid 29127135)
    • (1999) Comparative Biochemistry and Physiology - C Pharmacology Toxicology and Endocrinology , vol.122 , Issue.3 , pp. 353-361
    • Mora, P.1    Fournier, D.2    Narbonne, J.-F.3
  • 64
    • 24644441756 scopus 로고    scopus 로고
    • Characterization and use of the total head soluble cholinesterases from mosquitofish (Gambusia holbrooki) for screening of anticholinesterase activity
    • DOI 10.1080/14756360500094094
    • Nunes B, Carvalho F, Guilhermino L (2005) Characterization and use of the total head soluble cholinesterases from mosquitofish (Gambusia holbrooki) for screening of anticholinesterase activity. J Enzym Inhibit Medic Chem 20(4): 369-376. (Pubitemid 41269284)
    • (2005) Journal of Enzyme Inhibition and Medicinal Chemistry , vol.20 , Issue.4 , pp. 369-376
    • Nunes, B.1    Carvalho, F.2    Guilhermino, L.3
  • 65
    • 0029134578 scopus 로고
    • Regulatory and research issues related to cholinesterase inhibition
    • Padilla S (1995) Regulatory and research issues related to cholinesterase inhibition. Toxicology 102: 215-220.
    • (1995) Toxicology , vol.102 , pp. 215-220
    • Padilla, S.1
  • 66
    • 0842308021 scopus 로고    scopus 로고
    • Recovery of acetylcholine esterase activity of Drawida willsi (Oligochaeta) following application of three pesticides to soil
    • DOI 10.1016/j.chemosphere.2003.10.052
    • Panda S, Sahu SK (2004) Recovery of acetylcholine esterase activity of Drawida willsi (Oligochaeta) following application of three pesticides to soil. Chemosphere 55: 283-290. (Pubitemid 38175281)
    • (2004) Chemosphere , vol.55 , Issue.2 , pp. 283-290
    • Panda, S.1    Sahu, S.K.2
  • 67
    • 0034013945 scopus 로고    scopus 로고
    • Monitoring wading bird exposure to agricultural chemicals using serum cholinesterase activity
    • Parsons KC, Matz AC, Hooper MJ, Pokras MA (1999) Monitoring wading bird exposure to agricultural chemicals using serum cholinesterase activity. Environ Toxicol Chem 19(5): 1317-1323. (Pubitemid 30230880)
    • (2000) Environmental Toxicology and Chemistry , vol.19 , Issue.5 , pp. 1317-1323
    • Parsons, K.C.1    Matz, A.C.2    Hooper, M.J.3    Pokras, M.A.4
  • 68
    • 75849149895 scopus 로고    scopus 로고
    • Environmental fate and toxicity of ionic liquids: A review
    • Pham TPT, Cho CW, Yun YS (2010) Environmental fate and toxicity of ionic liquids: A review. Water Res 44: 352-372.
    • (2010) Water Res , vol.44 , pp. 352-372
    • Pham, T.P.T.1    Cho, C.W.2    Yun, Y.S.3
  • 70
    • 0018084384 scopus 로고
    • Multiple forms of acetylcholinesterase in Allolobophora caliginosa: purification and partial characterization
    • Principato GB, Ambrosini MV, Menghini A, Giovannini E, Dell'Agata M (1978) Multiple forms of acetylcholinesterase in Allolobophora caliginosa: Purification and partial characterization. Compar Biochem Physiol Part C: Compar Pharmacol 61(1): 147-151. (Pubitemid 9037232)
    • (1978) Comparative Biochemistry and Physiology , vol.C61 , Issue.1 , pp. 147-151
    • Principato, G.B.1    Ambrosini, M.V.2    Menghini, A.3
  • 71
    • 0033784607 scopus 로고    scopus 로고
    • Inhibition of Acetylcholinesterase and Different ATPases by a Novel Phosphorothionate (RPR-II) in Rat Brain
    • Rahman MF, Siddiqui MKJ, Jamil K (2000) Inhibition of Acetylcholinesterase and Different ATPases by a Novel Phosphorothionate (RPR-II) in Rat Brain. Ecotoxicol Environ Saf 47: 125-129.
    • (2000) Ecotoxicol Environ Saf , vol.47 , pp. 125-129
    • Rahman, M.F.1    Mkj, S.2    Jamil, K.3
  • 74
    • 36749021121 scopus 로고    scopus 로고
    • Earthworm biomarkers of pesticide contamination: Current status and perspectives
    • DOI 10.1584/jpestics.R07-14
    • Rodríguez-Castellano L, Sanchez-Hernandez JC (2007a) Earthworm biomarkers of pesticide contamination: Current status and perspectives. J Pesticide Sci 32: 360-371. (Pubitemid 350206957)
    • (2007) Journal of Pesticide Science , vol.32 , Issue.4 , pp. 360-371
    • Rodriguez-Castellanos, L.1    Sanchez-Hernandez, J.C.2
  • 75
    • 34548476284 scopus 로고    scopus 로고
    • Chemical reactivation and aging kinetics of organophosphorus-inhibited cholinesterases from two earthworm species
    • DOI 10.1897/06-625R1.1
    • Rodríguez-Castellanos L, Sanchez-Hernandez JC (2007b) Chemical Reactivation and Aging Kinetics of Organophosphorus-Inhibited Cholinesterases from Two Earthworms Species. Environ Toxicol Chem 26(9): 1992-2000. (Pubitemid 47373216)
    • (2007) Environmental Toxicology and Chemistry , vol.26 , Issue.9 , pp. 1992-2000
    • Rodriguez-Castellanos, L.1    Sanchez-Hernandez, J.C.2
  • 76
    • 39749192088 scopus 로고    scopus 로고
    • Characterization of muscle cholinesterases from two demersal flatfish collected near a municipal wastewater outfall in Southern California
    • DOI 10.1016/j.ecoenv.2007.06.008, PII S0147651307001339
    • Rodríguez-Fuentes G, Armstrong J, Schlenk D (2008) Characterization of muscle cholinesterases from two demersal flatfish collected near a municipal wastewater outfall in Southern California. Ecotoxicol Environ Saf 69: 466-471. (Pubitemid 351305028)
    • (2008) Ecotoxicology and Environmental Safety , vol.69 , Issue.3 , pp. 466-471
    • Rodriguez-Fuentes, G.1    Armstrong, J.2    Schlenk, D.3
  • 77
    • 2942552566 scopus 로고    scopus 로고
    • Characterization of cholinesterase activity from different tissues of Nile tilapia (Oreochromis niloticus)
    • DOI 10.1016/j.marenvres.2004.03.037, PII S0141113604000881
    • Rodríguez-Fuentes G, Gold-Bouchot G (2004) Characterization of cholinesterase activity from different tissues of Nile tilapia (Oreochromus niloticus). Mar Environ Res 58: 505-509. (Pubitemid 38738922)
    • (2004) Marine Environmental Research , vol.58 , Issue.2-5 , pp. 505-509
    • Rodriguez-Fuentes, G.1    Gold-Bouchot, G.2
  • 78
    • 0038666518 scopus 로고    scopus 로고
    • Increased acetylcholinesterase activities in specimens of Sparus auratus exposed to sublethal copper concentrations
    • DOI 10.1016/S0009-2797(03)00058-9
    • Romani R, Antognelli C, Baldracchini F, De Santis A, Isani G, Giovannini E, Rosi G (2003) Increased acetylcholinesterase activities in specimens of Sparus auratus exposed to sublethal copper concentrations. Chemico-Biological Interact 145: 321-329. (Pubitemid 36549115)
    • (2003) Chemico-Biological Interactions , vol.145 , Issue.3 , pp. 321-329
    • Romani, R.1    Antognelli, C.2    Baldracchini, F.3    De Santis, A.4    Isani, G.5    Giovannini, E.6    Rosi, G.7
  • 79
    • 0030724170 scopus 로고    scopus 로고
    • Serum 'B' esterases as a nondestructive biomarker for monitoring the exposure of reptiles to organophosphorus insecticides
    • DOI 10.1006/eesa.1997.1560
    • Sanchez JC, Fossi MC, Focardi S (1997) Serum "B" Esterases as a Nondestructive Biomarker for Monitoring the Exposure of Reptiles to Organophosphorus Insecticides. Ecotoxicol Environ Saf 37: 45-52. (Pubitemid 27456439)
    • (1997) Ecotoxicology and Environmental Safety , vol.38 , Issue.1 , pp. 45-52
    • Sanchez, J.C.1    Fossi, M.C.2    Focardi, S.3
  • 80
    • 0034892739 scopus 로고    scopus 로고
    • The use of carbamates, atropine, and 2-pyridine aldoxime methoiodide in the protection of Artemia salina against poisoning by carbophenothion
    • Sánchez-Fortún S, Barahona V (2001) The use of carbamates, atropine, and 2-pyridine aldoxime methoiodide in the protection of Artemia salina against poisoning by carbophenothion. Environ Toxicol Chem 20(9): 2008-2013. (Pubitemid 32772133)
    • (2001) Environmental Toxicology and Chemistry , vol.20 , Issue.9 , pp. 2008-2013
    • Sanchez-Fortun, S.1    Barahona, V.2
  • 81
    • 55549143075 scopus 로고    scopus 로고
    • Ecotoxicological perspectives of B-esterases in the assessment of pesticide contamination
    • Plattenberg RH (ed.) Nova Science Publishers, New York, USA
    • Sánchez-Hernandez JC (2007) Ecotoxicological perspectives of B-esterases in the assessment of pesticide contamination. In: Plattenberg RH (ed.) Environmental Pollution: New Research. Nova Science Publishers, New York, USA, pp. 1-45.
    • (2007) Environmental Pollution: New Research. , pp. 1-45
    • Sánchez-Hernandez, J.C.1
  • 82
    • 4344652673 scopus 로고    scopus 로고
    • Inhibition of plasma butyrylcholinesterase activity in the lizard Gallotia galloti palmae by pesticides: A field study
    • DOI 10.1016/j.envpol.2004.05.008, PII S0269749104001940
    • Sánchez-Hernández JC, Carbonell R, Henríquez Pérez A, Montealegre M, Gómez L (2004) Inhibition of plasma butyrylcholinesterase activity in the lizard Gallotia galloti palmae by pesticides: a field study. Environ Pollut 132: 479-488. (Pubitemid 39119517)
    • (2004) Environmental Pollution , vol.132 , Issue.3 , pp. 479-488
    • Sanchez-Hernandez, J.C.1    Carbonell, R.2    Henriquez Perez, A.3    Montealegre, M.4    Gomez, L.5
  • 83
    • 0037301453 scopus 로고    scopus 로고
    • Evaluating reptile exposure to cholinesterase-inhibiting agrochemicals by serum butyrylcholinesterase activity
    • DOI 10.1897/1551-5028(2003)022<0296:ERETCI>2.0.CO;2
    • Sanchez-Hernandez JC (2003) Evaluating reptile exposure to cholinesterase-inhibiting agrochemicals by serum butyrylcholinesterase activity. Environ Toxicol Chem 22(2): 296-301. (Pubitemid 36105868)
    • (2003) Environmental Toxicology and Chemistry , vol.22 , Issue.2 , pp. 296-301
    • Sanchez-Hernandez, J.C.1
  • 84
    • 0036838112 scopus 로고    scopus 로고
    • Lizard cholinesterases as biomarkers of pesticide exposure: Enzymological characterization
    • Sanchez-Hernandez JC, Sanchez BM (2002) Lizard cholinesterases as biomarkers of pesticide exposure: enzymological characterization. Environ Toxicol Chem 21(11): 2319-25. (Pubitemid 35155125)
    • (2002) Environmental Toxicology and Chemistry , vol.21 , Issue.11 , pp. 2319-2325
    • Sanchez-Hernandez, J.C.1    Sanchez, B.M.2
  • 85
    • 0002799645 scopus 로고    scopus 로고
    • Wildlife exposure to organophosphorus insecticides
    • Sánchez-Hernandez JC (2001) Wildlife exposure to organophosphorus insecticides. Rev Environ Contam Toxicol 172: 21-63.
    • (2001) Rev Environ Contam Toxicol , vol.172 , pp. 21-63
    • Sánchez-Hernandez, J.C.1
  • 86
    • 0034084828 scopus 로고    scopus 로고
    • In vitro and in vivo cholinesterase inhibition in lacertides by phosphonate- and phosphorothioate-type organophosphates
    • DOI 10.1006/pest.1999.2471
    • Sánchez-Hernandez JC, Walker CH (2000) In vitro and in vivo cholinesterase inhibition in Lacertides by phosphonate-and phosphorothioate-type organophosphates. Pesticide Biochem Physiol 67: 1-12. (Pubitemid 30416588)
    • (2000) Pesticide Biochemistry and Physiology , vol.67 , Issue.1 , pp. 1-12
    • Sanchez-Hernandez, J.C.1    Walker, C.H.2
  • 89
    • 10644231932 scopus 로고    scopus 로고
    • Comparative thresholds for acetylcholinesterase inhibition and behavioral impairment in coho salmon exposed to chlorpyrifos
    • DOI 10.1897/04-195R.1
    • Sandahl JF, Baldwin DH, Jenkins JJ, Scholz NL (2005) Comparative thresholds for acetylcholinesterase inhibition and behavioral impairment in Coho salmon exposed to chlorpyrifos. Environ Toxicol Chem 24(1): 136-145. (Pubitemid 39658152)
    • (2005) Environmental Toxicology and Chemistry , vol.24 , Issue.1 , pp. 136-145
    • Sandahl, J.F.1    Baldwin, D.H.2    Jenkins, J.J.3    Scholz, N.L.4
  • 90
    • 79953645838 scopus 로고    scopus 로고
    • Reptile Cholinesterase Characterization and Use in Monitoring Anticholinesterases
    • Texas Tech University
    • Schmidt SR (2003) Reptile Cholinesterase Characterization and Use in Monitoring Anticholinesterases. Thesis in Environmental Toxicology. Texas Tech University.
    • (2003) Thesis in Environmental Toxicology
    • Schmidt, S.R.1
  • 91
    • 0027985365 scopus 로고
    • Heavy metal content (Hg2+, Cd2+, Pb2+) in various body parts: Its impact on cholinesterase activity and binding glycoproteins in the grasshopper Aiolopus thalassinus adults
    • Schmidt GH, Ibrahim NMM (1994) Heavy metal content (Hg2+, Cd2+, Pb2+) in various body parts: Its impact on cholinesterase activity and binding glycoproteins in the grasshopper Aiolopus thalassinus adults. Ecotoxicol Environ Saf 29(2): 148-164.
    • (1994) Ecotoxicol Environ Saf , vol.29 , Issue.2 , pp. 148-164
    • Schmidt, G.H.1    Ibrahim, N.M.M.2
  • 93
    • 0027491242 scopus 로고
    • Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells
    • Schweitzer ES (1993) Regulated and constitutive secretion of distinct molecular forms of acetylcholinesterase from PC12 cells. J Cell Sci 106: 731-740. (Pubitemid 23346786)
    • (1993) Journal of Cell Science , vol.106 , Issue.3 , pp. 731-740
    • Schweitzer, E.S.1
  • 94
    • 0029897490 scopus 로고    scopus 로고
    • Non-classical actions of cholinesterases: Role in cellular differentiation, tumorigenesis and Alzheimer's disease
    • DOI 10.1016/0197-0186(95)00099-2
    • Small DH, Michaelson S, Sberna G (1996) Non-classical actions of cholinesterases: role in cellular differentiation, tumorigenesis and Alzheimer's disease. Neurochem Internat 5/6: 453-483. (Pubitemid 26161318)
    • (1996) Neurochemistry International , vol.28 , Issue.5-6 , pp. 453-483
    • Small, D.H.1    Michaelson, S.2    Sberna, G.3
  • 95
    • 43049175166 scopus 로고    scopus 로고
    • Esterases activities and lipid peroxidation levels in muscle tissue of the shanny Lipophrys pholis along several sites from the Portuguese Coast
    • Solé M, Lobera G, Lima D, Reis-Henriques MA, Santos MM (2008) Esterases activities and lipid peroxidation levels in muscle tissue of the shanny Lipophrys pholis along several sites from the Portuguese Coast. Mar Pollut Bull 56: 999-1007.
    • (2008) Mar Pollut Bull , vol.56 , pp. 999-1007
    • Solé, M.1    Lobera, G.2    Lima, D.3    Ma, R.4    Santos, M.M.5
  • 96
    • 34948882256 scopus 로고    scopus 로고
    • Variability in Acetylcholinesterase upon Exposure to Chlorpyrifos and Carbaryl in Hybrid Catfish
    • Somnuek C, Cheevaporn V, Saengkul C and Beamish FWH (2007) Variability in Acetylcholinesterase upon Exposure to Chlorpyrifos and Carbaryl in Hybrid Catfish. ScienceAsia 33: 301-305.
    • (2007) ScienceAsia , vol.33 , pp. 301-305
    • Somnuek, C.1    Cheevaporn, V.2    Saengkul, C.3    Beamish, F.W.H.4
  • 97
    • 38549175562 scopus 로고    scopus 로고
    • Cholinesterase activities in the scallop Pecten jacobaeus: Characterization and effects of exposure to aquatic contaminants
    • Stefano B, Ilaria C, Silvano F (2008) Cholinesterase activities in the scallop Pecten jacobaeus: Characterization and effects of exposure to aquatic contaminants. Sci Tot Env 392: 99-109.
    • (2008) Sci Tot Env , vol.392 , pp. 99-109
    • Stefano, B.1    Ilaria, C.2    Silvano, F.3
  • 98
    • 0027010746 scopus 로고
    • Earthworms for toxicity testing; species differences in response towards cholinesterase inhibiting insecticides
    • Stenersen J, Brekke E, Engelstad F (1992) Earthworms for toxicity testing; species differences in response towards cholinesterase inhibiting insecticides. Soil Biol Biochem 24(12): 1761-1764. (Pubitemid 24407054)
    • (1992) Soil Biology & Biochemistry , vol.24 , Issue.12 , pp. 1761-1764
    • Stenersen, J.1    Brekke, E.2    Engelstad, F.3
  • 99
    • 0001903334 scopus 로고
    • Esterases of earthworms. Part I: Characterisation of the cholinesterases in Eisenia foetida (Savigny) by substrates and inhibitors
    • Stenersen J (1980) Esterases of earthworms. Part I: Characterisation of the cholinesterases in Eisenia foetida (Savigny) by substrates and inhibitors. Compar Biochem Physiol Part C: Compar Pharmacol 66(1): 37-44.
    • (1980) Compar Biochem Physiol Part C: Compar Pharmacol , vol.66 , Issue.1 , pp. 37-44
    • Stenersen, J.1
  • 100
    • 0032996160 scopus 로고    scopus 로고
    • Cholinesterases of marine teleost fish: Enzymological characterization and potential use in the monitoring of neurotoxic contamination
    • DOI 10.1016/S0141-1136(98)00127-5, PII S0141113698001275
    • Sturm A, Silva de Assis HC, Hansen PD (1999a) Cholinesterases of marine teleost fish: enzymological characterization and potential use in the monitoring of neurotoxic contamination. Mar Environ Res 47: 389-398. (Pubitemid 29090218)
    • (1999) Marine Environmental Research , vol.47 , Issue.4 , pp. 389-398
    • Sturm, A.1    Da Silva De Assis, H.C.2    Hansen, P.-D.3
  • 101
    • 0032956075 scopus 로고    scopus 로고
    • Potential use of cholinesterase in monitoring low levels of organophosphates in small streams: Natural variability in three-spined stickleback (Gasterosteus aculeatus) and relation to pollution
    • DOI 10.1897/1551-5028(1999)018<0194:PUOCIM>2.3.CO;2
    • Sturm A, Wogram J, Hansen PD, Liess M (1999b) Potential use of cholinesterase in monitoring low levels of organophosphates in small streams: natural variability in three-spined stickleback (Gasterosteus aculeatus) and relation to pollution. Environ Toxicol Chem 18(2): 194-200. (Pubitemid 29058959)
    • (1999) Environmental Toxicology and Chemistry , vol.18 , Issue.2 , pp. 194-200
    • Sturm, A.1    Wogram, J.2    Hansen, P.-D.3    Liess, M.4
  • 102
    • 0035897109 scopus 로고    scopus 로고
    • Soluble and membrane-bound acetylcholinesterases in Mytilus galloprovincialis (Pelecypoda: Filibranchia) from the northern Adriatic sea
    • DOI 10.1016/S0009-2797(01)00152-1, PII S0009279701001521
    • Talesa V, Romani R, Antognelli C, Giovannini E, Rosi G (2001) Soluble and membrane-bound acetylcholinesterases in Mytilus galloprovincialis (Pelecypoda: Filibranchia) from the northern Adriatic sea. Chemico-Biological Interact 134: 151-166. (Pubitemid 32304508)
    • (2001) Chemico-Biological Interactions , vol.134 , Issue.2 , pp. 151-166
    • Talesa, V.1    Romani, R.2    Antognelli, C.3    Giovannini, E.4    Rosi, G.5
  • 103
    • 0030732474 scopus 로고    scopus 로고
    • Acetylcholinesterase in Spirographis spallanzanii (Polychaeta: Sedentaria): Presence of two dimeric membrane-bound forms
    • DOI 10.1016/S0300-9084(97)86149-4
    • Talesa V, Romani R, Rosi G, Giovannini E (1997) Acetylcholinesterase in Spirographis spallanzanii (Polychaeta: Sedentaria): Presence of two dimeric membrane-bound forms. Biochimie 79: 397-405. (Pubitemid 27462522)
    • (1997) Biochimie , vol.79 , Issue.7 , pp. 397-405
    • Talesa, V.1    Romani, R.2    Rosi, G.3    Giovannini, E.4
  • 104
    • 0028980217 scopus 로고
    • Acetylcholinesterase in tentacles in Octopus vulgaris (cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms
    • Talesa V, Grauso M, Giovannini E, Rosi G, Toutant JP (1995a) Acetylcholinesterase in tentacles in Octopus vulgaris (cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms. Neurochem Internat 27(2): 201-211.
    • (1995) Neurochem Internat , vol.27 , Issue.2 , pp. 201-211
    • Talesa, V.1    Grauso, M.2    Giovannini, E.3    Rosi, G.4    Toutant, J.P.5
  • 105
    • 0028959657 scopus 로고
    • Solubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis)
    • Talesa V, Grauso M, Giovannini E, Rosi G, Toutant JP (1995b) Solubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis). Biochem J 306: 687-692.
    • (1995) Biochem J , vol.306 , pp. 687-692
    • Talesa, V.1    Grauso, M.2    Giovannini, E.3    Rosi, G.4    Toutant, J.P.5
  • 106
    • 79953651900 scopus 로고    scopus 로고
    • The signaling pathway of calcitonin gene-related peptide-induced acetylcholinesterase expression in muscle is mediated by cyclic AMP
    • Arcachon, France September 1-5, 1998
    • Tsim KWK (1998) The signaling pathway of calcitonin gene-related peptide-induced acetylcholinesterase expression in muscle is mediated by cyclic AMP. Abstract book of the Xth International Symposium on Cholinergic Mechanisms, Arcachon, France September 1-5, 1998: 109.
    • (1998) Abstract Book of the Xth International Symposium on Cholinergic Mechanisms , vol.109
    • Kwk, T.1
  • 107
    • 0037626992 scopus 로고    scopus 로고
    • Characterization of cholinesterase activity in three bivalves inhabiting the North Adriatic sea and their possible use as sentinel organisms for biosurveillance programmes
    • DOI 10.1016/S0048-9697(03)00227-4
    • Valbonesi P, Sartor G, Fabbri E (2003) Characterization of cholinesterase activity in three bivalves inhabiting the North Adriatic sea and their possible use as sentinel organisms for biosurveillance programmes. Sci To Environ 312: 79-88. (Pubitemid 36836205)
    • (2003) Science of the Total Environment , vol.312 , Issue.1-3 , pp. 79-88
    • Valbonesi, P.1    Sartor, G.2    Fabbri, E.3
  • 108
    • 0037367981 scopus 로고    scopus 로고
    • Effect of dichlorvos on cholinesterase activity of the European sea bass (Dicentrarchus labrax)
    • DOI 10.1016/S0048-3575(03)00019-1
    • Varó I, Navarro JC, Amat F, Guilhermino L (2003) Effect of dichlorvos on cholinesterase activity of the European sea bass (Dicentrarchus labrax). Pesticide Biochem Physiol 75: 61-72. (Pubitemid 36521978)
    • (2003) Pesticide Biochemistry and Physiology , vol.75 , Issue.3 , pp. 61-72
    • Varo, I.1    Navarro, J.C.2    Amat, F.3    Guilhermino, L.4
  • 109
    • 0035987529 scopus 로고    scopus 로고
    • Characterisation of cholinesterases and evaluation of the inhibitory potential of chlorpyrifos and dichlorvos to Artemia salina and Artemia parthenogenetica
    • DOI 10.1016/S0045-6535(02)00075-9, PII S0045653502000759
    • Varó I, Navarro JC, Amat F, Guilhermino L(2002) Characterisation of cholinesterases and evaluation of the inhibitory potential of chlorpyrifos and dichlorvos to Artemia salina and Artemia parthenogenetica. Chemosphere 48: 563-569. (Pubitemid 34654385)
    • (2002) Chemosphere , vol.48 , Issue.6 , pp. 563-569
    • Varo, I.1    Navarro, J.C.2    Amat, F.3    Guilhermino, L.4
  • 111
    • 0034617441 scopus 로고    scopus 로고
    • The promoter of human acetylcholinesterase is activated by a cyclic adenosine 3',5'-monophosphate-dependent pathway in cultured NG108-15 neuroblastoma cells
    • DOI 10.1016/S0304-3940(00)01200-3, PII S0304394000012003
    • Wan DCC, Choi RCY, Siow NL, Tsim KWK (2000) The promoter of human acetylcholinesterase is activated by a cyclic adenosine 3', 5'-monophosphate- dependent pathway in cultured NG108-15 neuroblastoma cells. Neurosc Lett 288: 81-85. (Pubitemid 30408443)
    • (2000) Neuroscience Letters , vol.288 , Issue.1 , pp. 81-85
    • Wan, D.C.C.1    Choi, R.C.Y.2    Siow, N.L.3    Tsim, K.W.K.4
  • 112
    • 0035204959 scopus 로고    scopus 로고
    • Effects of salinity on aldicarb toxicity in juvenile rainbow trout (Oncorhynchus mykiss) and striped bass (Morone saxatilis x chrysops)
    • DOI 10.1093/toxsci/64.2.200
    • Wang J, Grisle S, Schlenk D (2001) Effects of Salinity on Aldicarb Toxicity in Juvenile Rainbow Trout (Oncorhynchus mykiss) and Striped Bass (Morone saxatilis × chrysops) Toxicolog Sci 64: 200-207. (Pubitemid 33130311)
    • (2001) Toxicological Sciences , vol.64 , Issue.2 , pp. 200-207
    • Wang, J.1    Grisle, S.2    Schlenk, D.3
  • 113
    • 0034967875 scopus 로고    scopus 로고
    • Effects of parathion on acetylcholinesterase, butyrylcholinesterase, and carboxylesterase in three-spined stickleback (Gasterosteus aculeatus) following short-term exposure
    • Wogram J, Sturm A, Segner H, Liesse M (2001) Effects of parathion on acetylcholinesterase, butyrilcholinesterase, and carboxylesterase in three-spined stickleback (Gasterosteus aculeatues) following short-term exposure. Environ Toxicol Chem 20(7): 1528-1531. (Pubitemid 32550013)
    • (2001) Environmental Toxicology and Chemistry , vol.20 , Issue.7 , pp. 1528-1531
    • Wogram, J.1    Sturm, A.2    Segner, H.3    Liess, M.4
  • 114
    • 34347206337 scopus 로고    scopus 로고
    • Cholinesterase activity in Gammarus pulex (Crustacea Amphipoda): Characterization and effects of chlorpyrifos
    • DOI 10.1016/j.tox.2007.04.010, PII S0300483X07002314
    • Xuereb B, Noury P, Felten V, Garric J, Geffard O (2007) Cholinesterase activity in Gammarus pulex (Crustacea Amphipoda): characterization and effects of chlorpyrifos. Toxicology 236: 178-189. (Pubitemid 46992696)
    • (2007) Toxicology , vol.236 , Issue.3 , pp. 178-189
    • Xuereb, B.1    Noury, P.2    Felten, V.3    Garric, J.4    Geffard, O.5
  • 115
    • 0036237097 scopus 로고    scopus 로고
    • Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells
    • DOI 10.1016/S0168-0102(02)00005-6, PII S0168010202000056
    • Yang L, He HY, Zhang XJ (2002) Increased expression of intranuclear AChE involved in apoptosis of SK-N-SH cells. Neurosci Res 42: 261-268. (Pubitemid 34414986)
    • (2002) Neuroscience Research , vol.42 , Issue.4 , pp. 261-268
    • Yang, L.1    He, H.-Y.2    Zhang, X.-J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.