메뉴 건너뛰기




Volumn 29, Issue 1, 1999, Pages 21-57

The role of phosphotriesterases in the detoxication of organophosphorus compounds

Author keywords

Detoxication; Organophosphorus compounds; Phosphotriesterase

Indexed keywords

ARYLDIALKYLPHOSPHATASE; CALCIUM ION; DIISOPROPYL FLUOROPHOSPHATASE; DIVALENT CATION; EDETIC ACID; ESTERASE; INSECTICIDE; MAGNESIUM ION; MANGANESE; NICKEL; ORGANOPHOSPHORUS COMPOUND; PHOSPHATASE; PHOSPHOTRIESTERASE; SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 0032963556     PISSN: 10408444     EISSN: None     Source Type: Journal    
DOI: 10.1080/10408449991349177     Document Type: Article
Times cited : (81)

References (238)
  • 1
    • 0013552003 scopus 로고
    • Properties and analytical methods
    • World Health Organisation, Ed., Geneva
    • World Health Organisation, Properties and analytical methods. In: World Health Organisation, Ed., Organophosphorus Insecticides: A General Introduction. Geneva: 1986, 23-29.
    • (1986) Organophosphorus Insecticides: A General Introduction , pp. 23-29
  • 2
    • 0000780279 scopus 로고
    • Organophosphorus compounds
    • Spencer, P.S. and Schaumburg, H.H., Eds., Baltimore
    • Davis, C.S. and Richardson, R.J., Organophosphorus Compounds. In: Spencer, P.S. and Schaumburg, H.H., Eds., Experimental and Clinical Neurotoxicology, Baltimore, 1980, 527-544.
    • (1980) Experimental and Clinical Neurotoxicology , pp. 527-544
    • Davis, C.S.1    Richardson, R.J.2
  • 3
    • 0028149404 scopus 로고
    • Mammalian toxicology of organophosphorus pesticides
    • Sultatos, L.G., Mammalian toxicology of organophosphorus pesticides. J. Toxicol. Environ. Health., 43, 271-289, 1994.
    • (1994) J. Toxicol. Environ. Health. , vol.43 , pp. 271-289
    • Sultatos, L.G.1
  • 4
    • 85038195592 scopus 로고
    • Aspectos toxicológicos de las armas químicas
    • Repetto, M., Aspectos toxicológicos de las armas químicas. Rev. Toxicol., 8, 526, 1991.
    • (1991) Rev. Toxicol. , vol.8 , pp. 526
    • Repetto, M.1
  • 5
    • 0002600053 scopus 로고
    • Acylated amino acids in inhibited B-esterases
    • Neuberger, A. and Tatum, E.L., Eds., Amsterdam: North-Holland Publishing
    • Aldridge, W.N. and Reiner, E., Acylated amino acids in inhibited B-esterases. In: Neuberger, A. and Tatum, E.L., Eds., Enzyme Inhibitors as Substrates. Amsterdam: North-Holland Publishing, 1972, 170-175.
    • (1972) Enzyme Inhibitors as Substrates , pp. 170-175
    • Aldridge, W.N.1    Reiner, E.2
  • 6
    • 0013523989 scopus 로고
    • Metabolism and mode of action
    • World Health Organisation, Ed., Geneva
    • World Health Organisation, Metabolism and mode of action. In: World Health Organisation, Ed., Organophosphorus Insecticides: A General Introduction. Geneva, 1986, 39-48.
    • (1986) Organophosphorus Insecticides: A General Introduction , pp. 39-48
  • 7
    • 0013552004 scopus 로고
    • Effects of organophosphorus insecticides on the nervous system
    • World Health Organisation, Ed., Geneva
    • World Health Organisation, Effects of organophosphorus insecticides on the nervous system, In: World Health Organisation, Ed., Organophosphorus Insecticides: A General Introduction. Geneva, 1986, 39-48.
    • (1986) Organophosphorus Insecticides: A General Introduction , pp. 39-48
  • 8
    • 0026512759 scopus 로고
    • The pathogenesis of organophosphate poly-neuropathy
    • Lotti, M., The pathogenesis of organophosphate poly-neuropathy. Crit. Rev. Toxicol., 21, 465-487, 1992.
    • (1992) Crit. Rev. Toxicol. , vol.21 , pp. 465-487
    • Lotti, M.1
  • 9
    • 0024979442 scopus 로고
    • Polineuropatía retardad inducida por organofosforados: Una gran desconocida
    • Barril, J. and Carrera M.V., Polineuropatía retardad inducida por organofosforados: una gran desconocida. Med. Clin., 92, 787-793, 1989.
    • (1989) Med. Clin. , vol.92 , pp. 787-793
    • Barril, J.1    Carrera, M.V.2
  • 10
    • 0026512759 scopus 로고
    • The pathogenesis of organophosphate polyneuropathy
    • Lotti, M., The pathogenesis of organophosphate polyneuropathy. Crit. Rev. Toxicol., 21, 465-487., 1992.
    • (1992) Crit. Rev. Toxicol. , vol.21 , pp. 465-487
    • Lotti, M.1
  • 11
    • 0000598077 scopus 로고
    • The target for initiation of delayed neurotoxicity by organophosphorus esters: Biochemical and toxicological applications
    • Johnson, M.K., The target for initiation of delayed neurotoxicity by organophosphorus esters: biochemical and toxicological applications. Rev. Biochem. Toxicol., 4, 141-212., 1982.
    • (1982) Rev. Biochem. Toxicol. , vol.4 , pp. 141-212
    • Johnson, M.K.1
  • 12
    • 0027244371 scopus 로고
    • The cytoskeleton as a target for organophosphorus ester-induced delayed neurotoxicity (OPIDN)
    • AbouDonia, M.B., The cytoskeleton as a target for organophosphorus ester-induced delayed neurotoxicity (OPIDN). Chem. Biol. Interact., 87, 383-393, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 383-393
    • Aboudonia, M.B.1
  • 13
    • 0029029401 scopus 로고
    • Involvement of cytoskeletal proteins in the mechanisms of organophosphorus ester-induced delayed neurotoxicity
    • AbouDonia, M.B., Involvement of cytoskeletal proteins in the mechanisms of organophosphorus ester-induced delayed neurotoxicity. Clin. Exp. Pharmacol. Physiol., 22, 358-359, 1995.
    • (1995) Clin. Exp. Pharmacol. Physiol. , vol.22 , pp. 358-359
    • Aboudonia, M.B.1
  • 14
    • 0028971195 scopus 로고
    • 2+/ calmodulin-dependent protein kinase in the brain subcellular fractions of diisopropyl phosphorofluoridate (DFP)-treated hen
    • 2+/ calmodulin-dependent protein kinase in the brain subcellular fractions of diisopropyl phosphorofluoridate (DFP)-treated hen. Neurochem. Res., 20, 1095-1105, 1995.
    • (1995) Neurochem. Res. , vol.20 , pp. 1095-1105
    • Gupta, R.P.1    Aboudonia, M.B.2
  • 15
    • 0023123105 scopus 로고
    • Neurotoxic effects of organophosphorus insecticides. An intermediate syndrome
    • Senanayake, N. and Karalliedde, L., Neurotoxic effects of organophosphorus insecticides. An intermediate syndrome. N. Engl. J. Med., 316, 761-763, 1987.
    • (1987) N. Engl. J. Med. , vol.316 , pp. 761-763
    • Senanayake, N.1    Karalliedde, L.2
  • 16
    • 0029559458 scopus 로고
    • The intermediate syndrome in organophosphate poisoning: An overview of experimental and clinical observations
    • DeBleecker, J.L., The intermediate syndrome in organophosphate poisoning: an overview of experimental and clinical observations. J. Toxicol., Clin. Toxicol., 33, 683-686, 1995.
    • (1995) J. Toxicol., Clin. Toxicol. , vol.33 , pp. 683-686
    • DeBleecker, J.L.1
  • 18
    • 0021223127 scopus 로고
    • Lung injury and delayed toxicity produced by O,S,S-trimethyl phosphorodithioate, an impurity of malathion
    • Konno, N., Fukuto, T.R., and Imamura, T., Lung injury and delayed toxicity produced by O,S,S-trimethyl phosphorodithioate, an impurity of malathion. Toxicol. Appl. Pharmacol., 75, 219-228, 1984.
    • (1984) Toxicol. Appl. Pharmacol. , vol.75 , pp. 219-228
    • Konno, N.1    Fukuto, T.R.2    Imamura, T.3
  • 19
    • 0023779933 scopus 로고
    • Studies on the metabolism of the pneumotoxin O,S,S-trimethyl phosphorodithioate. II. Lung and liver slices
    • Nemery, B. and Aldridge, W.N., Studies on the metabolism of the pneumotoxin O,S,S-trimethyl phosphorodithioate. II. Lung and liver slices. Biochem. Pharmacol., 37, 3717-3722, 1988.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3717-3722
    • Nemery, B.1    Aldridge, W.N.2
  • 20
    • 0023693195 scopus 로고
    • Studies on the metabolism of the pneumotoxin O,S,S-trimethyl phosphorodithioate. I. Lung and liver microsomes
    • Nemery, B. and Aldridge, W.N., Studies on the metabolism of the pneumotoxin O,S,S-trimethyl phosphorodithioate. I. Lung and liver microsomes. Biochem. Pharmacol., 37, 3709-3715, 1988.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3709-3715
    • Nemery, B.1    Aldridge, W.N.2
  • 21
    • 0024532357 scopus 로고
    • Acceleration of anterograde axonal transport in cat sciatic nerve by diisopropyl phosphorofluoridate
    • Carrington, C.D., Lapadula, D.M., and AbouDonia, M.B., Acceleration of anterograde axonal transport in cat sciatic nerve by diisopropyl phosphorofluoridate. Brain. Res., 476, 179-182, 1989.
    • (1989) Brain. Res. , vol.476 , pp. 179-182
    • Carrington, C.D.1    Lapadula, D.M.2    AbouDonia, M.B.3
  • 22
    • 0030841699 scopus 로고    scopus 로고
    • Alteration in neurofilament axonal transport in the sciatic nerve of the diisopropyl phosphorofluoridate (DFP)-treated hen
    • Gupta, R.P., AbdelRahman, A., Wilmarth, K.W., and AbouDonia, M.B., Alteration in neurofilament axonal transport in the sciatic nerve of the diisopropyl phosphorofluoridate (DFP)-treated hen. Biochem. Pharmacol., 53, 12, 1799-1806, 1997
    • (1997) Biochem. Pharmacol. , vol.53 , Issue.12 , pp. 1799-1806
    • Gupta, R.P.1    AbdelRahman, A.2    Wilmarth, K.W.3    AbouDonia, M.B.4
  • 23
    • 0023617040 scopus 로고
    • Progressive deficit of retrograde axonal transport is associated with the pathogenesis of di-n-butyl dichlorvos axonopathy
    • Moretto, A., Lotti, M., Sabri, M.I., and Spencer, P.S., Progressive deficit of retrograde axonal transport is associated with the pathogenesis of di-n-butyl dichlorvos axonopathy. J. Neurochem., 49, 1515-1522, 1987.
    • (1987) J. Neurochem. , vol.49 , pp. 1515-1522
    • Moretto, A.1    Lotti, M.2    Sabri, M.I.3    Spencer, P.S.4
  • 24
    • 0028927947 scopus 로고
    • Changes in membrane fluidity evoked by organophosphorus insecticide bromfenvinfos and its methylated analogue
    • Blasiak, J., Changes in membrane fluidity evoked by organophosphorus insecticide bromfenvinfos and its methylated analogue. Comp. Biochem. Physiol., 110C, 1521, 1995.
    • (1995) Comp. Biochem. Physiol. , vol.110 C , pp. 1521
    • Blasiak, J.1
  • 25
    • 85060748189 scopus 로고
    • Changes in the fluidity of model lipid membranes evoked by the organophosphorus insecticide methylbromfenvinfos
    • Blasiak, J., Changes in the fluidity of model lipid membranes evoked by the organophosphorus insecticide methylbromfenvinfos. Acta. Biochim. Pol., 40, 3941, 1993.
    • (1993) Acta. Biochim. Pol. , vol.40 , pp. 3941
    • Blasiak, J.1
  • 26
    • 0013558538 scopus 로고
    • Parathion and methylparathion-altered fluidity of native and model membranes
    • Blasiak, J., Parathion and methylparathion-altered fluidity of native and model membranes. Pestic. Biochem. Physiol., 45, 7280, 1993.
    • (1993) Pestic. Biochem. Physiol. , vol.45 , pp. 7280
    • Blasiak, J.1
  • 27
    • 0027430621 scopus 로고
    • Protective action of cholesterol against changes in membrane fluidity induced by methylparathion
    • Blasiak, J., Protective action of cholesterol against changes in membrane fluidity induced by methylparathion. Acta Biochim. Pol., 40, 35-38, 1993.
    • (1993) Acta Biochim. Pol. , vol.40 , pp. 35-38
    • Blasiak, J.1
  • 28
    • 0028082250 scopus 로고
    • Effects of parathion on membrane organization and its implications for the mechanisms of toxicity
    • AntunesMadeira, M.C., Videira, R.A., and Madeira, V.M., Effects of parathion on membrane organization and its implications for the mechanisms of toxicity. Biochim. Biophys. Acta, 1190, 149-154, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 149-154
    • AntunesMadeira, M.C.1    Videira, R.A.2    Madeira, V.M.3
  • 29
    • 0030586009 scopus 로고    scopus 로고
    • The role of nicotinic receptors and calcium channela in mipafox induced inhibition of catecholamine release in bovine chromaffin cells
    • Gutiérrez, L.M., Sogorb, M.A., Vilanova, E., and Viniegra, S., The role of nicotinic receptors and calcium channela in mipafox induced inhibition of catecholamine release in bovine chromaffin cells. Environ. Toxicol. Pharmacol., 1, 241-247, 1996.
    • (1996) Environ. Toxicol. Pharmacol. , vol.1 , pp. 241-247
    • Gutiérrez, L.M.1    Sogorb, M.A.2    Vilanova, E.3    Viniegra, S.4
  • 30
    • 0028093118 scopus 로고
    • Interaction of organophosphorus compounds with muscarinic receptors in SH-SY5Y human neuroblastoma cells
    • Ehrich, M., Intropido, L., and Costa, L.G., Interaction of organophosphorus compounds with muscarinic receptors in SH-SY5Y human neuroblastoma cells. J. Toxicol. Environ. Health., 43, 51-63, 1994.
    • (1994) J. Toxicol. Environ. Health. , vol.43 , pp. 51-63
    • Ehrich, M.1    Intropido, L.2    Costa, L.G.3
  • 31
    • 0028986964 scopus 로고
    • The effects of diisopropylphosphorofluoridate (DFP) on the ganglioside profile in the chicken (Gallus domesticus) hindbrain
    • Bush, D.M., Lehning, E.J., and Bursian, S.J., The effects of diisopropylphosphorofluoridate (DFP) on the ganglioside profile in the chicken (Gallus domesticus) hindbrain. Neurotoxicology, 16, 55-62, 1995.
    • (1995) Neurotoxicology , vol.16 , pp. 55-62
    • Bush, D.M.1    Lehning, E.J.2    Bursian, S.J.3
  • 32
    • 0029838286 scopus 로고    scopus 로고
    • +)- ATPase by parathion and methylparathion
    • +)- ATPase by parathion and methylparathion. Pestic. Biochem. Physiol., 54, 40-47, 1996.
    • (1996) Pestic. Biochem. Physiol. , vol.54 , pp. 40-47
    • Blasiak, J.1
  • 33
    • 0029074581 scopus 로고
    • 2+)-ATPase by the organophosphorus insecticides parathion and methylparathion
    • 2+)-ATPase by the organophosphorus insecticides parathion and methylparathion. Comp. Biochem. Physiol., 110C, 119-125, 1995.
    • (1995) Comp. Biochem. Physiol. , vol.110 C , pp. 119-125
    • Blasiak, J.1
  • 36
    • 0029123631 scopus 로고
    • Developmental neurotoxicity of chlorpyrifos, cellular mechanisms
    • Whitney, K.D., Seidler, F.J., and Slotkin, T.A., Developmental neurotoxicity of chlorpyrifos, cellular mechanisms. Toxicol. Appl. Pharmacol., 134, 53-62, 1995.
    • (1995) Toxicol. Appl. Pharmacol. , vol.134 , pp. 53-62
    • Whitney, K.D.1    Seidler, F.J.2    Slotkin, T.A.3
  • 37
    • 0029268082 scopus 로고
    • Lactate dehydrogenase isoenzymes in mammalian cells exposed to isophenphos
    • Rodrigues, M.A., Fernandes, M.J., and Angelo, M.D., Lactate dehydrogenase isoenzymes in mammalian cells exposed to isophenphos. Biomed. Environ. Sci., 8, 18-22, 1995.
    • (1995) Biomed. Environ. Sci. , vol.8 , pp. 18-22
    • Rodrigues, M.A.1    Fernandes, M.J.2    Angelo, M.D.3
  • 38
    • 0026015301 scopus 로고
    • In vitro effects of organophosphorus compounds on calmodulin activity
    • Pala, I., Vig, P.J., Desaiah, D., and Srinivasan, A., In vitro effects of organophosphorus compounds on calmodulin activity. J. Appl. Toxicol., 11, 391-395, 1991.
    • (1991) J. Appl. Toxicol. , vol.11 , pp. 391-395
    • Pala, I.1    Vig, P.J.2    Desaiah, D.3    Srinivasan, A.4
  • 39
    • 0001220247 scopus 로고
    • Effects of pesticides on domestic animals
    • Hayes, W.J., Jr. and Laws, E.R., Jr., Eds., Academic Press, England, 1991
    • Oehme, F.W., Effects of pesticides on domestic animals, vol. 1. In: Hayes, W.J., Jr. and Laws, E.R., Jr., Eds., Handbook of Pesticide Toxicology. Academic Press, England, 1991, 453-461.
    • (1991) Handbook of Pesticide Toxicology , vol.1 , pp. 453-461
    • Oehme, F.W.1
  • 41
    • 70350567023 scopus 로고
    • An enzyme hydrolysing diethyl p-nitrophenyl phosphate (E600) and identity with the A-esterase of mammalian sera
    • Aldridge, W.N., An enzyme hydrolysing diethyl p-nitrophenyl phosphate (E600) and identity with the A-esterase of mammalian sera. Biochem. J., 53, 117-124, 1953.
    • (1953) Biochem. J. , vol.53 , pp. 117-124
    • Aldridge, W.N.1
  • 42
    • 85038205116 scopus 로고    scopus 로고
    • New type of esterases in hogkidney extract
    • Bergman., F., Segal, R., and Rimon, S., New type of esterases in hogkidney extract. Biochem. J., 67, 481-486.
    • Biochem. J. , vol.67 , pp. 481-486
    • Bergman, F.1    Segal, R.2    Rimon, S.3
  • 43
  • 44
    • 0013552770 scopus 로고
    • Enzyme nomenclature
    • International Union of Biochemistry, Enzyme nomenclature. Eur. J. Biochem., 179, 511-515, 1989.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 511-515
  • 45
    • 0013523492 scopus 로고
    • The develpment of an improved system of nomenclature and classification of esterases
    • Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Ellis Horwwod Limited, England
    • Walker, C.H., The develpment of an improved system of nomenclature and classification of esterases. In: Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Enzymes Hydrolysing Organophosphorus Compounds. Ellis Horwwod Limited, England, 1989, 236-245.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 236-245
    • Walker, C.H.1
  • 46
    • 0023375904 scopus 로고
    • Distinction between A-esterases and arylesterases implication for esterase classification
    • Mackness, M.I., Thompson, H.M., Hardy, A.R., and Walker, C.H., Distinction between A-esterases and arylesterases implication for esterase classification. Biochem. J., 245, 293-296, 1987.
    • (1987) Biochem. J. , vol.245 , pp. 293-296
    • Mackness, M.I.1    Thompson, H.M.2    Hardy, A.R.3    Walker, C.H.4
  • 47
    • 0002597846 scopus 로고
    • Suggestions for a nomenclature and classification of enzymes hydrolysing organophosphorus compounds
    • Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Ellis Horwwod Limited, England
    • Aldridge, W.N., Hoskin, F.C.G., Reiner, E., and Walker, C.H. Suggestions for a nomenclature and classification of enzymes hydrolysing organophosphorus compounds. In: Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Enzymes Hydrolysing Organophosphorus Compounds. Ellis Horwwod Limited, England, 1989, 246-253.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 246-253
    • Aldridge, W.N.1    Hoskin, F.C.G.2    Reiner, E.3    Walker, C.H.4
  • 49
    • 0027164737 scopus 로고
    • Recommendations of the IUBMB nomenclature committee comments concerning classification and nomenclature of esterases hydrolysing organophosphorus compounds
    • Reiner, E., Recommendations of the IUBMB Nomenclature Committee Comments Concerning Classification and Nomenclature of Esterases Hydrolysing Organophosphorus Compounds. Chem. Biol. Interact., 87, 15-16, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 15-16
    • Reiner, E.1
  • 50
    • 0000568827 scopus 로고
    • Distribution and nature of the aquatic organophosphorus acid anhydrases: Enzymes for organophosphate detoxification
    • Landis, W.G., Distribution and nature of the aquatic organophosphorus acid anhydrases: enzymes for organophosphate detoxification. Rev. Aquat. Sci., 5, 267-285, 1991.
    • (1991) Rev. Aquat. Sci. , vol.5 , pp. 267-285
    • Landis, W.G.1
  • 51
    • 0027325860 scopus 로고
    • The classification of esterases which hydrolyse organophosphates-recent developments
    • Walker, C.H., The classification of esterases which hydrolyse organophosphates-recent developments. Chem. Biol. Interact., 87, 17-24, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 17-24
    • Walker, C.H.1
  • 52
    • 84872639802 scopus 로고
    • An enzyme in animal tissues capable of hydrolysing the organophosphorus-fluoride bond of alkyl fluorophosphateses
    • Mazur, A., An enzyme in animal tissues capable of hydrolysing the organophosphorus-fluoride bond of alkyl fluorophosphateses. J. Biol. Chem., 164, 271-289, 1946.
    • (1946) J. Biol. Chem. , vol.164 , pp. 271-289
    • Mazur, A.1
  • 53
    • 0025788322 scopus 로고
    • Purification of rabbit and human serum paraoxonase
    • Furlong, C.E., Richter, R.J., Chapline, C., and Crabb, J.W., Purification of rabbit and human serum paraoxonase. Biochemistry 30, 10133-10140, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10133-10140
    • Furlong, C.E.1    Richter, R.J.2    Chapline, C.3    Crabb, J.W.4
  • 54
    • 0026096803 scopus 로고
    • Purification of human serum paraoxonase arylesterase-evidence for one esterase catalyzing both activities
    • Gan, K.N., Smolen, A., Eckerson, H.W., and La Du, B.N., Purification of human serum paraoxonase arylesterase-evidence for one esterase catalyzing both activities. Drug Metab. Dispos., 19, 100-106, 1991.
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 100-106
    • Gan, K.N.1    Smolen, A.2    Eckerson, H.W.3    La Du, B.N.4
  • 55
    • 0025719481 scopus 로고
    • Characterization of cDNA clones encoding rabbit and human serum paraoxonase-the mature protein retains its signal sequence
    • Hassett, C., Richter, R.J., Humbert, R., Chapline, C., Crabb, J.W., Omiecinski, C.J., and Furlong, C.E., Characterization of cDNA clones encoding rabbit and human serum paraoxonase-the mature protein retains its signal sequence. Biochemistry, 30, 10141-10149, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10141-10149
    • Hassett, C.1    Richter, R.J.2    Humbert, R.3    Chapline, C.4    Crabb, J.W.5    Omiecinski, C.J.6    Furlong, C.E.7
  • 57
    • 0024993942 scopus 로고
    • Distribution and some biochemical properties of rat paraoxonase activity
    • Pellín, M.C., Moretto, A., Lotti, M., and Vilanova, E., Distribution and some biochemical properties of rat paraoxonase activity. Neurotoxicol. Teratol., 12, 611-614, 1990.
    • (1990) Neurotoxicol. Teratol. , vol.12 , pp. 611-614
    • Pellín, M.C.1    Moretto, A.2    Lotti, M.3    Vilanova, E.4
  • 60
    • 0021837405 scopus 로고
    • In vitro degradation of four isomers of soman in human serum
    • De Bisschop, H.C., Mainil, J.G., and Willems, J.L., In vitro degradation of four isomers of soman in human serum. Biochem. Pharmacol., 34, 1895-1900, 1985.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 1895-1900
    • De Bisschop, H.C.1    Mainil, J.G.2    Willems, J.L.3
  • 61
    • 0001242303 scopus 로고
    • The enzymatic hydrolysis of p-nitrophenyl ethyl phosphonates by mammalian plasmas
    • Becker, E.L. and Barbaro, J.F., The enzymatic hydrolysis of p-nitrophenyl ethyl phosphonates by mammalian plasmas. Biochem. Pharmacol., 13, 1219-1227, 1964.
    • (1964) Biochem. Pharmacol. , vol.13 , pp. 1219-1227
    • Becker, E.L.1    Barbaro, J.F.2
  • 62
    • 0013559376 scopus 로고
    • A stereospecific esterase hydrolysing an organophosphorus compound
    • DíazAlejo N., Sogorb, M.A., Vicedo, J.L., and Vilanova, E., A stereospecific esterase hydrolysing an organophosphorus compound. Toxicol. Lett., Supplement 1/74, 19, 1994.
    • (1994) Toxicol. Lett. , vol.19 , Issue.SUPPL. 1-74
    • Díazalejo, N.1    Sogorb, M.A.2    Vicedo, J.L.3    Vilanova, E.4
  • 63
    • 0019281829 scopus 로고
    • Hydrolysis of O,O-dimethyl-2,2-dichlorovinyl phosphate (DDVP) by esterases in parasitic helminths and in vertebrate plasma and erythrocytes
    • Reiner E., Simeon, V., and ShrinjericSpoljar, M., Hydrolysis of O,O-dimethyl-2,2-dichlorovinyl phosphate (DDVP) by esterases in parasitic helminths and in vertebrate plasma and erythrocytes. Comp. Biochem. Physiol., 66C, 149-152, 1980.
    • (1980) Comp. Biochem. Physiol. , vol.66 C , pp. 149-152
    • Reiner, E.1    Simeon, V.2    ShrinjericSpoljar, M.3
  • 64
    • 0019296451 scopus 로고
    • A-esterase activities in relation to the differential toxicity of pirimiphos-methyl to birds and mammals
    • Brealey, C., Walker, C., and Baldwin, B., A-esterase activities in relation to the differential toxicity of pirimiphos-methyl to birds and mammals. Pestic. Sci., 11, 546-554, 1980.
    • (1980) Pestic. Sci. , vol.11 , pp. 546-554
    • Brealey, C.1    Walker, C.2    Baldwin, B.3
  • 65
    • 0024496198 scopus 로고
    • Humn serum A-esterases, hydrolysis of O,O-dimethyl-2,2-dichlorovinyl phosphate
    • Traverso, R., Moretto, A., and Lotti, M., Humn serum A-esterases, hydrolysis of O,O-dimethyl-2,2-dichlorovinyl phosphate. Biochem. Pharmacol., 1989; 38, 671-676.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 671-676
    • Traverso, R.1    Moretto, A.2    Lotti, M.3
  • 67
    • 0024517571 scopus 로고
    • Degradation by rat tissues in vitro of organophosphorus esters which inhibit cholinesterase
    • Pla, A. and Johnson, M.K., Degradation by rat tissues in vitro of organophosphorus esters which inhibit cholinesterase. Biochem. Pharmacol., 38, 1527-1533, 1988.
    • (1988) Biochem. Pharmacol. , vol.38 , pp. 1527-1533
    • Pla, A.1    Johnson, M.K.2
  • 68
    • 0029048815 scopus 로고
    • Organophosphate detoxication potential of various rat tissues via A-esterase and aliesterase activities
    • Pond, A.L., Chambers, H.W., and Chambers, J.E., Organophosphate detoxication potential of various rat tissues via A-esterase and aliesterase activities. Toxicol. Lett., 78, 245-252, 1995.
    • (1995) Toxicol. Lett. , vol.78 , pp. 245-252
    • Pond, A.L.1    Chambers, H.W.2    Chambers, J.E.3
  • 69
    • 0028036743 scopus 로고
    • Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver
    • Gil, F., Gonzalvo, M.C., Hernández, A.F., Villanueva, E., and Pla, A., Differences in the kinetic properties, effect of calcium and sensitivity to inhibitors of paraoxon hydrolase activity in rat plasma and microsomal fraction from rat liver. Biochem. Pharmacol., 48, 1559-1568, 1994.
    • (1994) Biochem. Pharmacol. , vol.48 , pp. 1559-1568
    • Gil, F.1    Gonzalvo, M.C.2    Hernández, A.F.3    Villanueva, E.4    Pla, A.5
  • 70
    • 0025081573 scopus 로고
    • Hen liver and plasma can metabolize hexylDCP phosphoramidate at a rate comparable to that of rat
    • DiazAlejo, N., Pellín, M.C., Vicedo, J.L., and Vilanova, E., Hen liver and plasma can metabolize hexylDCP phosphoramidate at a rate comparable to that of rat. Neurotoxol. Teratol., 12, 615-617, 1990.
    • (1990) Neurotoxol. Teratol. , vol.12 , pp. 615-617
    • DiazAlejo, N.1    Pellín, M.C.2    Vicedo, J.L.3    Vilanova, E.4
  • 71
    • 0030602884 scopus 로고    scopus 로고
    • Identification and isolation of two rat serum proteins with A-esterase activity toward paraoxon and chlorpyrifos-oxn
    • Pond, A.L., Coyne, C.P., Chambers, H.W., and Chambers, J.E., Identification and isolation of two rat serum proteins with A-esterase activity toward paraoxon and chlorpyrifos-oxn. Biochem. Pharmacol., 52, 363-369, 1996.
    • (1996) Biochem. Pharmacol. , vol.52 , pp. 363-369
    • Pond, A.L.1    Coyne, C.P.2    Chambers, H.W.3    Chambers, J.E.4
  • 72
    • 0021056004 scopus 로고
    • Organophosphate detoxicating hydrolases in different vertebrate species
    • Chemnitius, J.M., Losh, H., Losh, K., and Zech, R., Organophosphate detoxicating hydrolases in different vertebrate species. Comp. Biochem. Physiol., 76C, 85-93, 1983.
    • (1983) Comp. Biochem. Physiol. , vol.76 C , pp. 85-93
    • Chemnitius, J.M.1    Losh, H.2    Losh, K.3    Zech, R.4
  • 75
    • 0031044916 scopus 로고    scopus 로고
    • Purification and characterization of paraoxon hydrolase from rat liver
    • Rodrigo, L., Gil, F., Hernández, A.F., Marina, A., Vázquez, J., and Pla, A., Purification and characterization of paraoxon hydrolase from rat liver. Biochem. J., 821, 595-601, 1997.
    • (1997) Biochem. J. , vol.821 , pp. 595-601
    • Rodrigo, L.1    Gil, F.2    Hernández, A.F.3    Marina, A.4    Vázquez, J.5    Pla, A.6
  • 76
    • 0024501160 scopus 로고
    • Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP)
    • Little, J., Broomfield, C., FoxTalbot, M., Boucher, L., MacIver, B., and Lenz, D., Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP). Biochem. Pharmacol., 38, 23-29, 1989.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 23-29
    • Little, J.1    Broomfield, C.2    Foxtalbot, M.3    Boucher, L.4    Maciver, B.5    Lenz, D.6
  • 77
    • 0020959573 scopus 로고
    • Characterization of a DFPhydrolysing enzyme in squid posterior salivary gland by use of soman, DFP and manganous ion
    • Hoskin, F.C.G. and Prusch, R.D., Characterization of a DFPhydrolysing enzyme in squid posterior salivary gland by use of soman, DFP and manganous ion. Comp. Biochem. Physiol., 75, 17-20, 1983.
    • (1983) Comp. Biochem. Physiol. , vol.75 , pp. 17-20
    • Hoskin, F.C.G.1    Prusch, R.D.2
  • 78
    • 0013493305 scopus 로고
    • The intracelular localization of liver and kidney sarinase
    • Adie, P.A. and Tuba, J., The intracelular localization of liver and kidney sarinase. Can. J. Biochem. Physiol., 36, 21-24, 1958.
    • (1958) Can. J. Biochem. Physiol. , vol.36 , pp. 21-24
    • Adie, P.A.1    Tuba, J.2
  • 79
    • 0013491212 scopus 로고
    • The detoxication of organophosphorus compounds: A tale of two enzymes-or are
    • Hoskin, F.C. and Steinmann, K.E., The detoxication of organophosphorus compounds: A tale of two enzymes-or are. Proc. Int. Conf. Env. Haz. Agrochem., 1, 434-447, 1983.
    • (1983) Proc. Int. Conf. Env. Haz. Agrochem. , vol.1 , pp. 434-447
    • Hoskin, F.C.1    Steinmann, K.E.2
  • 80
    • 0024591188 scopus 로고
    • Activation and degradation of the phosphorothionate insecticides parathion and EPN by rat brain
    • Forsyth, C. and Chambers, J., Activation and degradation of the phosphorothionate insecticides parathion and EPN by rat brain. Biochem. Pharmacol., 38, 1597-1603, 1986.
    • (1986) Biochem. Pharmacol. , vol.38 , pp. 1597-1603
    • Forsyth, C.1    Chambers, J.2
  • 81
    • 0026659317 scopus 로고
    • Initial characterization of the organophosphate acid anhydrase activity of the chicken, Gallus domesticus
    • Westra, B.D. and Landis, W.G., Initial characterization of the organophosphate acid anhydrase activity of the chicken, Gallus domesticus. Comp. Biochem. Physiol., 102C, 253-265, 1992.
    • (1992) Comp. Biochem. Physiol. , vol.102 C , pp. 253-265
    • Westra, B.D.1    Landis, W.G.2
  • 82
    • 0026657242 scopus 로고
    • Discovery, initial characterization and comparison of the organophosphate acid hydrolyzing activities of the bobwhite quai, stilt and mallard
    • Landis, W.G. and Shough, N.J., Discovery, initial characterization and comparison of the organophosphate acid hydrolyzing activities of the bobwhite quai, stilt and mallard. Comp. Biochem. Physiol., 102C, 527-535, 1992.
    • (1992) Comp. Biochem. Physiol. , vol.102 C , pp. 527-535
    • Landis, W.G.1    Shough, N.J.2
  • 83
    • 0030681407 scopus 로고    scopus 로고
    • Biochemical factors contributing to toxicity differences among chlorpyrifos, parathion, and methyl parathion in mosquitofish (Gambusia affinis)
    • Boone, J.S. and Chambers, J.E., Biochemical factors contributing to toxicity differences among chlorpyrifos, parathion, and methyl parathion in mosquitofish (Gambusia affinis). Aquatic. Toxicol., 39, 333-343, 1997.
    • (1997) Aquatic. Toxicol. , vol.39 , pp. 333-343
    • Boone, J.S.1    Chambers, J.E.2
  • 84
    • 0027178919 scopus 로고
    • A partial primary structure of squid hepatopancreas organophosphorus acid anhydrolase
    • KopecSmyth, K., Deschamps, J.R., Loomis, L.D., and Ward, K.B., A partial primary structure of squid hepatopancreas organophosphorus acid anhydrolase. Chem. Biol. Interact., 87, 49-54, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 49-54
    • KopecSmyth, K.1    Deschamps, J.R.2    Loomis, L.D.3    Ward, K.B.4
  • 85
    • 0027653478 scopus 로고
    • Purification and properties of a diisopropyl-fluorophosphatase from squid Todarodes-pacificus-Steenstrup
    • Wang, F., Xiao, M.Z., and Mu, S.F., Purification and properties of a diisopropyl-fluorophosphatase from squid Todarodes-pacificus-Steenstrup. J. Biochem. Toxicol., 8, 161-166, 1993.
    • (1993) J. Biochem. Toxicol. , vol.8 , pp. 161-166
    • Wang, F.1    Xiao, M.Z.2    Mu, S.F.3
  • 86
    • 0023701385 scopus 로고
    • Organofluorophosphate-hydrolysing activity in an estuarine clam, Rangia cuneata
    • Anderson, R.S., Durst, H.D., and Landis, W.G., Organofluorophosphate-hydrolysing activity in an estuarine clam, Rangia cuneata. Comp. Biochem. Physiol., 91C, 575-578, 1988.
    • (1988) Comp. Biochem. Physiol. , vol.91 C , pp. 575-578
    • Anderson, R.S.1    Durst, H.D.2    Landis, W.G.3
  • 87
    • 0026588174 scopus 로고
    • Identification and characterization of the organophosphate acid anhydrase activity of the Blue Mussel
    • Noellgen, R.M. and Landis, W.G., Identification and characterization of the organophosphate acid anhydrase activity of the Blue Mussel, Mytilus edulis. Comp. Biochem. Physiol., 102C, 615-623, 1992.
    • (1992) Mytilus Edulis. Comp. Biochem. Physiol. , vol.102 C , pp. 615-623
    • Noellgen, R.M.1    Landis, W.G.2
  • 88
    • 0025734823 scopus 로고
    • High paraoxon-hydrolyzing activity in organophosphorous insecticide-resistant mosquitoes
    • Watanabe, M., Takebe, S., and Kobashi, K., High paraoxon-hydrolyzing activity in organophosphorous insecticide-resistant mosquitoes. Chem. Pharmac. Bull., 39, 980-985, 1991.
    • (1991) Chem. Pharmac. Bull. , vol.39 , pp. 980-985
    • Watanabe, M.1    Takebe, S.2    Kobashi, K.3
  • 89
    • 0025826133 scopus 로고
    • Role of esterases in resistance of insects to insecticides
    • Devonshire, A.L., Role of esterases in resistance of insects to insecticides. Biochem. Soc. Trans., 19, 755-759, 1991.
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 755-759
    • Devonshire, A.L.1
  • 90
    • 0025968498 scopus 로고
    • Purification and characterization of a secreted recombinant phosphotriesterase (Parathion Hydrolase) from Streptomyces lividans
    • Rowland, S.S., Speedie, M.K., and Pogell, B.M., Purification and characterization of a secreted recombinant phosphotriesterase (Parathion Hydrolase) from Streptomyces lividans. Appl. Environ. Microbiol., 57, 440-444, 1991.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 440-444
    • Rowland, S.S.1    Speedie, M.K.2    Pogell, B.M.3
  • 91
    • 0024332036 scopus 로고
    • Parathion hydrolase specified by the Flavobacterium opd gene: Relationship between the gene and protein
    • Mulbry, W.W. and Karns, F.S., Parathion hydrolase specified by the Flavobacterium opd gene: relationship between the gene and protein. J. Bacteriol., 171, 6740-6746, 1989.
    • (1989) J. Bacteriol. , vol.171 , pp. 6740-6746
    • Mulbry, W.W.1    Karns, F.S.2
  • 92
    • 0021865664 scopus 로고
    • Inhibition of a soman and diisopropylphosphorofluoridate (DFP)-detoxifying enzyme by mipafox
    • Hoskin, F.C.G., Inhibition of a soman and diisopropylphosphorofluoridate (DFP)-detoxifying enzyme by mipafox. Biochem. Pharmacol., 34, 2069-2072, 1985.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 2069-2072
    • Hoskin, F.C.G.1
  • 93
    • 0027320253 scopus 로고
    • Stereoselectivity of soman detoxication by organophosphorus acid anhydrases from Escherichia coli
    • Hoskin, F.C.G., Gallo, B.J., Steeves, D.M., and Walker, J.E., Stereoselectivity of soman detoxication by organophosphorus acid anhydrases from Escherichia coli. Chem. Biol. Interact., 87, 269-278, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 269-278
    • Hoskin, F.C.G.1    Gallo, B.J.2    Steeves, D.M.3    Walker, J.E.4
  • 94
    • 0026073674 scopus 로고
    • Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate
    • De Frank, J.J. and Cheng, T.C., Purification and properties of an organophosphorus acid anhydrase from a halophilic bacterial isolate. J. Bacteriol., 173, 1938-1943, 1991.
    • (1991) J. Bacteriol. , vol.173 , pp. 1938-1943
    • De Frank, J.J.1    Cheng, T.C.2
  • 95
    • 0028104672 scopus 로고
    • Phosphodiesterase and phosphotriestease in Rhizobium and Bradyrhizobium strains and their roles in the degradation of organophosphorus pesticides
    • Add Alla, M.H., Phosphodiesterase and phosphotriestease in Rhizobium and Bradyrhizobium strains and their roles in the degradation of organophosphorus pesticides. Lett. Appl. Microbiol., 19, 240-243, 1994.
    • (1994) Lett. Appl. Microbiol. , vol.19 , pp. 240-243
    • Add Alla, M.H.1
  • 96
    • 0021844179 scopus 로고
    • An organofluorophosphate-hydrolyzing activity in Tetrahymena thermophila
    • Landis, W.G., Savage, R.S., and Hoskin, F.C.G., An organofluorophosphate-hydrolyzing activity in Tetrahymena thermophila. J. Protozool., 32, 517-519, 1985.
    • (1985) J. Protozool. , vol.32 , pp. 517-519
    • Landis, W.G.1    Savage, R.S.2    Hoskin, F.C.G.3
  • 97
    • 0022711089 scopus 로고
    • Kinetics of the DFPase activity in Tetrahimena thermophila
    • Landis, W.G., Haley, M.V., and Johnson, D.W., Kinetics of the DFPase activity in Tetrahimena thermophila. J. Protozool., 33, 216-218, 1986.
    • (1986) J. Protozool. , vol.33 , pp. 216-218
    • Landis, W.G.1    Haley, M.V.2    Johnson, D.W.3
  • 98
    • 0024566262 scopus 로고
    • Alternative substrates and an inhibitor of the organophosphate acid anhydrase activities of the protozoan, Tetrahymena thermophila
    • Landis, W.G., Chester, N.A., Haley, M.V., Johnson, D.W., Tauber, R.M., and Durst, H.D., Alternative substrates and an inhibitor of the organophosphate acid anhydrase activities of the protozoan, Tetrahymena thermophila. Comp. Biochem. Physiol., 92C, 211-216, 1989.
    • (1989) Comp. Biochem. Physiol. , vol.92 C , pp. 211-216
    • Landis, W.G.1    Chester, N.A.2    Haley, M.V.3    Johnson, D.W.4    Tauber, R.M.5    Durst, H.D.6
  • 99
    • 0023277824 scopus 로고
    • Discovery of multiple organofluorophosphate hydrolyzing activities in the protozoan Tetrahymena thermophila
    • Landis, W.G., Haley, D.M., Haley, M.V., Johnson, D.W., Durst, H.D., and Savage, R.E., Jr., Discovery of multiple organofluorophosphate hydrolyzing activities in the protozoan Tetrahymena thermophila. J. Appl. Toxicol., 7(1), 35-41, 1987.
    • (1987) J. Appl. Toxicol. , vol.7 , Issue.1 , pp. 35-41
    • Landis, W.G.1    Haley, D.M.2    Haley, M.V.3    Johnson, D.W.4    Durst, H.D.5    Savage R.E., Jr.6
  • 100
  • 101
    • 0024573466 scopus 로고
    • Diisopropylfluorophosphate hydrolysis by a phosphotriesterase from Pseudomonas diminuta
    • Dumas, D.P., Wild, J.R., and Raushel, F.M., Diisopropylfluorophosphate hydrolysis by a phosphotriesterase from Pseudomonas diminuta. Biotechnol. Appl. Biochem., 11, 235-243, 1989.
    • (1989) Biotechnol. Appl. Biochem. , vol.11 , pp. 235-243
    • Dumas, D.P.1    Wild, J.R.2    Raushel, F.M.3
  • 102
    • 0025117439 scopus 로고
    • Inactivation organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D.P., Durst, H.D., Landis, W.G., Raushel, F.M., and Wild, J.R., Inactivation organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta. Arch. Biochem. Biphys., 277, 155-159, 1990.
    • (1990) Arch. Biochem. Biphys. , vol.277 , pp. 155-159
    • Dumas, D.P.1    Durst, H.D.2    Landis, W.G.3    Raushel, F.M.4    Wild, J.R.5
  • 103
    • 0024316913 scopus 로고
    • Purification and properties of the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D.P., Caldwell, S.R., Wild, J.R., and Raushel, F.M., Purification and properties of the phosphotriesterase from Pseudomonas diminuta. J. Biol. Chem., 264, 19659-19665, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19659-19665
    • Dumas, D.P.1    Caldwell, S.R.2    Wild, J.R.3    Raushel, F.M.4
  • 104
    • 0028933772 scopus 로고
    • Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase
    • Lai, K., Stolowich, N.J., and Wild, J.R., Characterization of P-S bond hydrolysis in organophosphorothioate pesticides by organophosphorus hydrolase. Arch. Biochem. Biophys., 318, 5904, 1995.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 5904
    • Lai, K.1    Stolowich, N.J.2    Wild, J.R.3
  • 105
    • 0028243622 scopus 로고
    • Stereospecific enzymatic hydrolysis of phosphorus-sulfur bonds in chiral organophosphate triesters
    • Chae, M.Y., Postula, J.J., and Raushel, F.M., Stereospecific enzymatic hydrolysis of phosphorus-sulfur bonds in chiral organophosphate triesters. Bioorg. Medicinal Chem. Lett., 4, 1473-1478, 1994.
    • (1994) Bioorg. Medicinal Chem. Lett. , vol.4 , pp. 1473-1478
    • Chae, M.Y.1    Postula, J.J.2    Raushel, F.M.3
  • 106
    • 0028946531 scopus 로고
    • Hydrolysis of tetriso by an enzyme derived from Pseudomonas diminuta as a model for the detoxication of O-ethyl S-(2-diisopropyl-aminoethyl) methylphosphonothiolate (VX)
    • Hoskin, F.C.G., Walker, J.E., Dettbarn W.D., and Wild, J.R., Hydrolysis of tetriso by an enzyme derived from Pseudomonas diminuta as a model for the detoxication of O-ethyl S-(2-diisopropyl-aminoethyl) methylphosphonothiolate (VX). Biochem. Pharmacol., 49, 711715, 1995.
    • (1995) Biochem. Pharmacol. , vol.49 , pp. 711-715
    • Hoskin, F.C.G.1    Walker, J.E.2    Dettbarn, W.D.3    Wild, J.R.4
  • 107
    • 0024281297 scopus 로고
    • Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase
    • Lewis, V.E., Donarski, W.J., Wild, J.R., and Raushel, F.M., Mechanism and stereochemical course at phosphorus of the reaction catalyzed by a bacterial phosphotriesterase. Biochemistry, 27, 1591-1597, 1988.
    • (1988) Biochemistry , vol.27 , pp. 1591-1597
    • Lewis, V.E.1    Donarski, W.J.2    Wild, J.R.3    Raushel, F.M.4
  • 108
    • 0025290724 scopus 로고
    • Expression of Pseudomonas diminuta phosphotriesterase activity in the fall armyworm confers resistance to insecticides
    • Dumas., D.P., Wild, J.R., and Raushel, F.M., Expression of Pseudomonas diminuta phosphotriesterase activity in the fall armyworm confers resistance to insecticides. Experientia, 46, 729-731, 1990.
    • (1990) Experientia , vol.46 , pp. 729-731
    • Dumas, D.P.1    Wild, J.R.2    Raushel, F.M.3
  • 109
    • 0027137293 scopus 로고
    • Antiferromagnetic coupling in the binucleal metal cluster of manganese-substituted phosphotriesterase
    • Chae, M.Y., Omburo, G.A., Lindahl, P.A., and Raushel, F.M., Antiferromagnetic coupling in the binucleal metal cluster of manganese-substituted phosphotriesterase. J. Am. Chem. Soc., 115, 12173-12174, 1993.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12173-12174
    • Chae, M.Y.1    Omburo, G.A.2    Lindahl, P.A.3    Raushel, F.M.4
  • 110
    • 0028286461 scopus 로고
    • Bimetallic binding motifs in organophosphorus hydrolase are important for catalysis and structural organization
    • Lai, K.H., Dave, K.I., and Wild, J.R., Bimetallic binding motifs in organophosphorus hydrolase are important for catalysis and structural organization. J. Biol. Chem., 269, 1657916584, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16579-16584
    • Lai, K.H.1    Dave, K.I.2    Wild, J.R.3
  • 111
    • 0028939465 scopus 로고
    • Utilization of cooper as a paramagnetic probe for the binuclear metal center of phosphotriesterase
    • Chae, M.Y., Omburo, G.A., Lindahl, P.A., and Raushel F.M., Utilization of cooper as a paramagnetic probe for the binuclear metal center of phosphotriesterase. Arch. Biochem. Biophys., 316, 765-772, 1995.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 765-772
    • Chae, M.Y.1    Omburo, G.A.2    Lindahl, P.A.3    Raushel, F.M.4
  • 112
    • 0023195693 scopus 로고
    • Interaction of some unsustituted phosphoramidate analogs of methamidophos (O,S-dimethyl phosphorothioamidate) with acetylcholinesterase and neuropathy target esterase of hen brain
    • Vilanova, E., Johnson, M.K., and Vicedo, J.L., Interaction of some unsustituted phosphoramidate analogs of methamidophos (O,S-dimethyl phosphorothioamidate) with acetylcholinesterase and neuropathy target esterase of hen brain. Pest. Biochem. Physiol., 28, 224-238, 1987.
    • (1987) Pest. Biochem. Physiol. , vol.28 , pp. 224-238
    • Vilanova, E.1    Johnson, M.K.2    Vicedo, J.L.3
  • 113
    • 0024576965 scopus 로고
    • Biochemical and clinical test of the delayed neuropathic potencial of some O-alkyl O-dichlorophenyl phosphoramidate analogues of methamidophos (O,S-dimethyl phosphorothioamidate)
    • Johnson, M.K., Vilanova, E. and Read D.J., Biochemical and clinical test of the delayed neuropathic potencial of some O-alkyl O-dichlorophenyl phosphoramidate analogues of methamidophos (O,S-dimethyl phosphorothioamidate). Toxicology, 54, 89-100, 1989.
    • (1989) Toxicology , vol.54 , pp. 89-100
    • Johnson, M.K.1    Vilanova, E.2    Read, D.J.3
  • 114
    • 0027265635 scopus 로고
    • Hydrolysis of some organophosphorus dichlorophenyl esters by hen brain homogenates and rabbit serum compared with hydrolysis of paraoxon
    • Reiner, E., Johnson, M.K., and Jokanovic, M., Hydrolysis of some organophosphorus dichlorophenyl esters by hen brain homogenates and rabbit serum compared with hydrolysis of paraoxon. Chem. Biol. Interact., 87, 127-131, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 127-131
    • Reiner, E.1    Johnson, M.K.2    Jokanovic, M.3
  • 115
    • 85038197759 scopus 로고
    • Characterization des cholinesterases et d'autres esterases apres electrophorese et immuno-electroforese en gelose. I. Applications a I'etude des esterases du serum humain normal
    • Uriel, A., Characterization des cholinesterases et d'autres esterases apres electrophorese et immuno-electroforese en gelose. I. Applications a I'etude des esterases du serum humain normal. Ann. Inst. Pasteur., 191, 101-104, 1961.
    • (1961) Ann. Inst. Pasteur. , vol.191 , pp. 101-104
    • Uriel, A.1
  • 116
    • 0015851138 scopus 로고
    • Effects of lipid removal on the molecular size and kinetics properties of bovine plasma arylesterase
    • Kitchen, B.J., Masters, C.J., and Winzor, D.J., Effects of lipid removal on the molecular size and kinetics properties of bovine plasma arylesterase. Biochem. J., 135, 93-99, 1973.
    • (1973) Biochem. J. , vol.135 , pp. 93-99
    • Kitchen, B.J.1    Masters, C.J.2    Winzor, D.J.3
  • 117
    • 0016715828 scopus 로고
    • Further evidence for the concept of bovine plasma arylesterase as a lipoprotein
    • Don, M.M., Masters, C.J., and Winzor, D.J., Further evidence for the concept of bovine plasma arylesterase as a lipoprotein. Biochem. J. 151, 625-630, 1975.
    • (1975) Biochem. J. , vol.151 , pp. 625-630
    • Don, M.M.1    Masters, C.J.2    Winzor, D.J.3
  • 118
    • 0020503835 scopus 로고
    • Partial purification and properties of sheep serum "A" esterases
    • Mackness, M.I., and Walker, C.H., Partial purification and properties of sheep serum "A" esterases. Biochem. Pharmacol., 32, 2291-2296, 1983.
    • (1983) Biochem. Pharmacol. , vol.32 , pp. 2291-2296
    • Mackness, M.I.1    Walker, C.H.2
  • 119
    • 0022295054 scopus 로고
    • The separation of sheep and human serum A-esterase activity into the lipoprotein fraction by ultracentrifugation
    • Mackness, M.I., Hallam, S.D., Peard, T., Warner, S., and Walker, C.H., The separation of sheep and human serum A-esterase activity into the lipoprotein fraction by ultracentrifugation. Comp. Biochem. Physiol., 83B, 675-677, 1985.
    • (1985) Comp. Biochem. Physiol. , vol.83 B , pp. 675-677
    • Mackness, M.I.1    Hallam, S.D.2    Peard, T.3    Warner, S.4    Walker, C.H.5
  • 120
    • 0002486729 scopus 로고
    • Human serum organophosphatase: Biochemical characteristicis and polymorphic inheritance
    • Reiner, E., Aldridge, W.N., and Hoskin, F.C.G. Eds.. Ellis Horwwod Limited, England
    • La Du, B.N., and Novais, J., Human serum organophosphatase: biochemical characteristicis and polymorphic inheritance. In: Reiner, E., Aldridge, W.N., and Hoskin, F.C.G. Eds., Enzymes Hydrolysing Organophosphorus Compounds. Ellis Horwwod Limited, England, 1989, 41-52.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 41-52
    • La Du, B.N.1    Novais, J.2
  • 121
    • 0027412483 scopus 로고
    • Identification of a distinct human high-density lipoprotein subspecies defined by a lipoproteinassociated protein, K-45. Identity of K-45 with paraoxonase
    • Blatter, M.C., James, R.W, Messmer, S., Barja, F., and Pometta, D., Identification of a distinct human high-density lipoprotein subspecies defined by a lipoproteinassociated protein, K-45. Identity of K-45 with paraoxonase. Eur. J. Biochem., 211, 871-879, 1993.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 871-879
    • Blatter, M.C.1    James, R.W.2    Messmer, S.3    Barja, F.4    Pometta, D.5
  • 124
    • 0002071967 scopus 로고
    • Stereoselective hydrolysis of soman and other chiral organophosphates by mammaliam phosphoryl-phosphateses
    • Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds.. Ellis Horwwod Limited, England
    • De Jong, L.P.A., Van Dijk, C., and Benschop, P., Stereoselective hydrolysis of soman and other chiral organophosphates by mammaliam phosphoryl-phosphateses. In: Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Enzymes Hydrolysing Organophosphorus Compounds. Ellis Horwwod Limited, England, 1989, 65-78.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 65-78
    • De Jong, L.P.A.1    Van Dijk, C.2    Benschop, P.3
  • 126
    • 0027787717 scopus 로고
    • Chiral high-performance liquid chromatography and gas chromatography of the stereoisomers of O-hexyl, O-2,5-dichlorophenyl phosphoramidate
    • DíazAlejo, N. and Vilanova E., Chiral high-performance liquid chromatography and gas chromatography of the stereoisomers of O-hexyl, O-2,5-dichlorophenyl phosphoramidate. J. Chromatogr., 622, 179-186, 1993.
    • (1993) J. Chromatogr. , vol.622 , pp. 179-186
    • Díazalejo, N.1    Vilanova, E.2
  • 127
    • 85038199169 scopus 로고    scopus 로고
    • Cuantificación y análisis de los estereoisómeros de hexil 2,5 diclorofenil fosforamidato tras ser hidrolizados por plasma de gallina
    • DíazAlejo, N., Sogorb, M.A., Vicedo, J.L., Carrera, V., Escudero, M.A., and Vilanova, E., Cuantificación y análisis de los estereoisómeros de hexil 2,5 diclorofenil fosforamidato tras ser hidrolizados por plasma de gallina. Rev. Toxicol., 10, 80.
    • Rev. Toxicol. , vol.10 , pp. 80
    • Díazalejo, N.1    Sogorb, M.A.2    Vicedo, J.L.3    Carrera, V.4    Escudero, M.A.5    Vilanova, E.6
  • 130
    • 0345563215 scopus 로고    scopus 로고
    • Inhibition and aging of neuropathy target esterase by the stereoisomers of a phosphoramidate related to methamidophos
    • Sogorb, M.A., DíazAlejo, N., Pellín, M.C., and Vilanova, E., Inhibition and aging of neuropathy target esterase by the stereoisomers of a phosphoramidate related to methamidophos. Toxicol. Lett., 93, 95-102, 1997.
    • (1997) Toxicol. Lett. , vol.93 , pp. 95-102
    • Sogorb, M.A.1    DíazAlejo, N.2    Pellín, M.C.3    Vilanova, E.4
  • 131
    • 85038195233 scopus 로고    scopus 로고
    • Differences in the interaction between O-hexyl O-2,5-dichlorophenyl phosphoramidate stereoisomers and neuropathy target esterase
    • Sogorb, M.A., DíazAlejo, N., Ñíguez, N., and Vilanova, E., Differences in the interaction between O-hexyl O-2,5-dichlorophenyl phosphoramidate stereoisomers and neuropathy target esterase. Toxicol. Lett., Suppl. 1/88, 24, 1996.
    • (1996) Toxicol. Lett. , Issue.SUPPL. 1-88 , pp. 24
    • Sogorb, M.A.1    DíazAlejo, N.2    Ñíguez, N.3    Vilanova, E.4
  • 133
    • 0026062669 scopus 로고
    • Anomalous biochemical responses in tests of the delayed neuropathic potential of methamidophos (O,S-Dimethyl phosphorothioamidate), its resolved isomers and of some higher O-alkyl homologues
    • Johnson, M.K., Vilanova, E., and Read, D.J., Anomalous biochemical responses in tests of the delayed neuropathic potential of methamidophos (O,S-Dimethyl phosphorothioamidate), its resolved isomers and of some higher O-alkyl homologues. Arch. Toxicol., 65, 618-624, 1991.
    • (1991) Arch. Toxicol. , vol.65 , pp. 618-624
    • Johnson, M.K.1    Vilanova, E.2    Read, D.J.3
  • 134
    • 0027282226 scopus 로고
    • Effect of some metallic cations and organic compounds on the O-hexyl O-2,5-dichlorophenyl phosphoramidate hydrolyzing activity in hen plasma
    • Sogorb, M.A., DíazAlejo, N., Vilanova, E., Vicedo, J.L., and Carrera, V., Effect of some metallic cations and organic compounds on the O-hexyl O-2,5-dichlorophenyl phosphoramidate hydrolyzing activity in hen plasma, Arch. Toxicol., 67, 416-421, 1993.
    • (1993) Arch. Toxicol. , vol.67 , pp. 416-421
    • Sogorb, M.A.1    DíazAlejo, N.2    Vilanova, E.3    Vicedo, J.L.4    Carrera, V.5
  • 135
    • 85038201486 scopus 로고
    • Activadores e inhibidores de una actividad hidrolasa que destoxifica compuestos organofosforados en plasma de gallina
    • Sogorb, M.A., DíazAlejo, N., Vilanova, E., Vicedo, J.L., and Carrera, V., Activadores e inhibidores de una actividad hidrolasa que destoxifica compuestos organofosforados en plasma de gallina. Rev. Toxicol., 10, 79, 1993.
    • (1993) Rev. Toxicol. , vol.10 , pp. 79
    • Sogorb, M.A.1    DíazAlejo, N.2    Vilanova, E.3    Vicedo, J.L.4    Carrera, V.5
  • 136
    • 0028944183 scopus 로고
    • Mechanism-based inactivation of phosphotriesterase by reaction of a critical histidine with a ketene intermediate
    • Banzon, J.A., Kuo, J.M., Miles, B.W., Fischer, D.R., Stang, P.J., and Raushel, F.M., Mechanism-based inactivation of phosphotriesterase by reaction of a critical histidine with a ketene intermediate. Biochemistry, 34, 743-749, 1995.
    • (1995) Biochemistry , vol.34 , pp. 743-749
    • Banzon, J.A.1    Kuo, J.M.2    Miles, B.W.3    Fischer, D.R.4    Stang, P.J.5    Raushel, F.M.6
  • 138
    • 0030832116 scopus 로고    scopus 로고
    • Inhibitors directed toward the binuclear center of the phosphotriesterase
    • Hong, S.B. and Raushel, F.M., Inhibitors directed toward the binuclear center of the phosphotriesterase. J. Enzy. Inhibit., 12, 191-203, 1997.
    • (1997) J. Enzy. Inhibit. , vol.12 , pp. 191-203
    • Hong, S.B.1    Raushel, F.M.2
  • 139
    • 0028925802 scopus 로고
    • Histidine-254 is essential for the inactivation of phosphotriesterase with the alkynyl phosphate esters and diethyl pyrocarbonate
    • Banzon, J.A., Kuo, J.M., Fischer, D.R., Stang, P.J., and Raushel, F.M., Histidine-254 is essential for the inactivation of phosphotriesterase with the alkynyl phosphate esters and diethyl pyrocarbonate. Biochemistry, 34, 750-754, 1995.
    • (1995) Biochemistry , vol.34 , pp. 750-754
    • Banzon, J.A.1    Kuo, J.M.2    Fischer, D.R.3    Stang, P.J.4    Raushel, F.M.5
  • 140
    • 0025606322 scopus 로고
    • Chemical and kinetic evidence for an essential histidine in the phosphotriesterase from Pseudomonas diminuta
    • Dumas, D.P. and Raushel, F.M., Chemical and kinetic evidence for an essential histidine in the phosphotriesterase from Pseudomonas diminuta, J. Biol. Chem., 265, 21498-21503, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21498-21503
    • Dumas, D.P.1    Raushel, F.M.2
  • 141
    • 0002475328 scopus 로고
    • Insight into putative mechanism of esterase acting simultaneously on carboxyl and phosphoryl compounds
    • Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds.. Ellis Horwwod Limited, England
    • Järv, J., Insight into putative mechanism of esterase acting simultaneously on carboxyl and phosphoryl compounds. In: Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Enzymes Hydrolysing Organophosphorus Compounds. Ellis Horwwod Limited, England, 1989, 221-225.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 221-225
    • Järv, J.1
  • 142
    • 0028924030 scopus 로고
    • The role of calcium in the hydrolysis of the organophosphate paraoxon by human serum A-esterase
    • Vitarius, J.A. and Sultatos, L.G., The role of calcium in the hydrolysis of the organophosphate paraoxon by human serum A-esterase. Life Sci., 56, 125-134, 1994.
    • (1994) Life Sci. , vol.56 , pp. 125-134
    • Vitarius, J.A.1    Sultatos, L.G.2
  • 143
    • 0028258144 scopus 로고
    • Non-calcium-dependent activity hydrolysing organophosphorus compounds in hen plasma
    • DíazAlejo, N., Sogorb, M.A., Vicedo, J.L., Barril, J., and Vilanova, E., Non-calcium-dependent activity hydrolysing organophosphorus compounds in hen plasma. Comp. Biochem. Physiol., 107(C), 213-219, 1994.
    • (1994) Comp. Biochem. Physiol. , vol.107 , Issue.C , pp. 213-219
    • DíazAlejo, N.1    Sogorb, M.A.2    Vicedo, J.L.3    Barril, J.4    Vilanova, E.5
  • 144
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • Omburo, G.A., Kuo, J.M., Mullins, L.S., and Raushel, F.M., Characterization of the zinc binding site of bacterial phosphotriesterase. J. Biol. Chem., 267, 13278-13283, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13278-13283
    • Omburo, G.A.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 145
    • 0026026523 scopus 로고
    • Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase
    • Smolen, A., Eckerson, H.W., Gan, K.N., Hailat, N., and La Du, B.N., Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase. Drug. Metabolism. Dispos., 19, 107-112, 1991.
    • (1991) Drug. Metabolism. Dispos. , vol.19 , pp. 107-112
    • Smolen, A.1    Eckerson, H.W.2    Gan, K.N.3    Hailat, N.4    La Du, B.N.5
  • 146
    • 0003080565 scopus 로고
    • A-esterases and B-esterases in Perspective
    • Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Ellis Horwwod Limited, England
    • Aldridge, N.W., A-esterases and B-esterases in Perspective. In: Enzymes hydrolysing organophosphorus compounds. In: Reiner, E., Aldridge, W.N., and Hoskin, F.C.G., Eds., Ellis Horwwod Limited, England, 1989, 114.
    • (1989) Enzymes Hydrolysing Organophosphorus Compounds , pp. 114
    • Aldridge, N.W.1
  • 147
    • 0001086412 scopus 로고
    • Hydrolysis of paraoxon in mammalian bood
    • Erdös, E.G. and Boggs, L.E., Hydrolysis of paraoxon in mammalian bood, Nature, 190, 716-717, 1961.
    • (1961) Nature , vol.190 , pp. 716-717
    • Erdös, E.G.1    Boggs, L.E.2
  • 148
    • 0031967954 scopus 로고    scopus 로고
    • Phosphotdesterase activity identified in purified serum albumins
    • Sogorb, M.A., DíazAlejo, N., Escudero, M.A., and Vilanova, E., Phosphotdesterase activity identified in purified serum albumins. Arch. Toxicol., 72, 219-226, 1998.
    • (1998) Arch. Toxicol. , vol.72 , pp. 219-226
    • Sogorb, M.A.1    DíazAlejo, N.2    Escudero, M.A.3    Vilanova, E.4
  • 149
    • 85038206126 scopus 로고    scopus 로고
    • Hen serum albumin hydrolyzes an organophosphorus compound
    • Sogorb, M.A., DíazAlejo, N., Vicedo, J.L., and Vilanova, E., Hen serum albumin hydrolyzes an organophosphorus compound. Toxicol. Lett., Suppl. 1/ 88, 88, 1996.
    • (1996) Toxicol. Lett. , Issue.SUPPL. 1-88 , pp. 88
    • Sogorb, M.A.1    DíazAlejo, N.2    Vicedo, J.L.3    Vilanova, E.4
  • 152
    • 0027325864 scopus 로고
    • The kinetics of O-hexyl O-2,5-dichlorophenyl phosphoramidate hydrolyzing activity in hen plasma
    • Sogorb, M.A., Vilanova, E., and DíazAlejo, N., The kinetics of O-hexyl O-2,5-dichlorophenyl phosphoramidate hydrolyzing activity in hen plasma. Chem. Biol. Interact., 87, 117-125, 1993.
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 117-125
    • Sogorb, M.A.1    Vilanova, E.2    DíazAlejo, N.3
  • 153
    • 0016804683 scopus 로고
    • Acetylation of human serum albumin by pnitrophenyl acetate
    • Means, G.E. and Bender, M., Acetylation of human serum albumin by pnitrophenyl acetate. Biochemistry, 14, 4989-4994, 1975.
    • (1975) Biochemistry , vol.14 , pp. 4989-4994
    • Means, G.E.1    Bender, M.2
  • 154
    • 0028240005 scopus 로고
    • Kinetic mechanism of the detoxification of the organophosphate paraoxon by human serum A-esterase
    • Vitarius, J.A. and Sultatos, L.G., Kinetic mechanism of the detoxification of the organophosphate paraoxon by human serum A-esterase. Drug. Metab. Dispos., 22, 472-478, 1994.
    • (1994) Drug. Metab. Dispos. , vol.22 , pp. 472-478
    • Vitarius, J.A.1    Sultatos, L.G.2
  • 155
    • 0031054145 scopus 로고    scopus 로고
    • A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase
    • Lockridge, O., Blong, R.M., Masson, P., Froment, M.T., Millard, C.B., and Broomfield, C.A., A single amino acid substitution, Gly 117His, confers phosphotriesterase (organophosphorus acid anhydride hydrolase) activity on human butyrylcholinesterase. Biochemistry, 36,786-795. 1997.
    • (1997) Biochemistry , vol.36 , pp. 786-795
    • Lockridge, O.1    Blong, R.M.2    Masson, P.3    Froment, M.T.4    Millard, C.B.5    Broomfield, C.A.6
  • 157
    • 0029165744 scopus 로고
    • Comparison of purified human and rabbit serum paraoxonases
    • Kuo, C.L. and La Du, B.N., Comparison of purified human and rabbit serum paraoxonases. Drug Metab. Dispos., 23, 935-944, 1995.
    • (1995) Drug Metab. Dispos. , vol.23 , pp. 935-944
    • Kuo, C.L.1    La Du, B.N.2
  • 158
    • 0023806064 scopus 로고
    • Role of genetic polymorphism of human plasma paraoxonase/arylesterase in hydrolysis of the insecticide metabolites chlorpyrifos oxon and paraoxon
    • Furlong, C.E., Richter, R.J., Seidel, S.L., and Motulsky, A.G., Role of genetic polymorphism of human plasma paraoxonase/arylesterase in hydrolysis of the insecticide metabolites chlorpyrifos oxon and paraoxon. Am. J. Hum. Genet., 43, 230-238, 1988.
    • (1988) Am. J. Hum. Genet. , vol.43 , pp. 230-238
    • Furlong, C.E.1    Richter, R.J.2    Seidel, S.L.3    Motulsky, A.G.4
  • 159
    • 0013493306 scopus 로고
    • Pharmacogenetic studies on human serum paraoxonase: Relative paraoxonase arylesterase activities
    • Eckerson, H.W., Wyte, C.M., and La-Du, B.N., Pharmacogenetic studies on human serum paraoxonase: relative paraoxonase arylesterase activities. Fed. Proc. Fed. Am. Soc. Exp. Biol., 40, 724, 1981.
    • (1981) Fed. Proc. Fed. Am. Soc. Exp. Biol. , vol.40 , pp. 724
    • Eckerson, H.W.1    Wyte, C.M.2    La-Du, B.N.3
  • 160
    • 0023806064 scopus 로고
    • Role of genetic polymorphism of human plasma paraoxonase/arylesterase in hydrolysis of the insecticide metabolites chlorpyrifos oxon and paraoxon
    • Furlong, C.E., Richter, R.J., Seidel, S.L., and Motulsky, A.G., Role of genetic polymorphism of human plasma paraoxonase/arylesterase in hydrolysis of the insecticide metabolites chlorpyrifos oxon and paraoxon. Am. J. Hum. Genet., 43, 230-238, 1988.
    • (1988) Am. J. Hum. Genet. , vol.43 , pp. 230-238
    • Furlong, C.E.1    Richter, R.J.2    Seidel, S.L.3    Motulsky, A.G.4
  • 161
    • 0030293198 scopus 로고    scopus 로고
    • The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin
    • Davies, H.G., Richter, R.J., Keifer, M., Broomfield, C.A., Sowalla, J., and Furlong, C.E., The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat. Genet., 14, 334-336, 1996.
    • (1996) Nat. Genet. , vol.14 , pp. 334-336
    • Davies, H.G.1    Richter, R.J.2    Keifer, M.3    Broomfield, C.A.4    Sowalla, J.5    Furlong, C.E.6
  • 163
    • 0027486997 scopus 로고
    • Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: Glutamine or arginine at position 191, for the respective A or B allozymes
    • Adkins, S., Gan, K.N., Mody, M., and La Du, B.N., Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes. Am. J. Hum. Genet., 52, 598-608. 1993.
    • (1993) Am. J. Hum. Genet. , vol.52 , pp. 598-608
    • Adkins, S.1    Gan, K.N.2    Mody, M.3    La Du, B.N.4
  • 164
    • 0002198623 scopus 로고    scopus 로고
    • Paraoxonase polymorphism Met-Leu54 is associated with modified serum concentrations of the enzyme. A possible link between the paraoxonase gene and increased risk of cardiovascular disease in diabetes
    • Garin, M.C., James, R.W., Dussoix, P., Blanche, H., Passa, P., Froguel, P., and Ruiz, J., Paraoxonase polymorphism Met-Leu54 is associated with modified serum concentrations of the enzyme. A possible link between the paraoxonase gene and increased risk of cardiovascular disease in diabetes. J. Clin. Invest., 99, 62-66, 1997.
    • (1997) J. Clin. Invest. , vol.99 , pp. 62-66
    • Garin, M.C.1    James, R.W.2    Dussoix, P.3    Blanche, H.4    Passa, P.5    Froguel, P.6    Ruiz, J.7
  • 165
    • 0022405037 scopus 로고
    • Linkage relationships of paraoxonase (PON) with others markers: Indication of PON-cystic fibrosis synteny
    • Eiberg, H., Mohr, J., Schmiegelon, K., Nielsen, L.S., and Williamson, R., Linkage relationships of paraoxonase (PON) with others markers: indication of PON-cystic fibrosis synteny. Clin. Genet.. 25, 265-271, 1985.
    • (1985) Clin. Genet. , vol.25 , pp. 265-271
    • Eiberg, H.1    Mohr, J.2    Schmiegelon, K.3    Nielsen, L.S.4    Williamson, R.5
  • 166
    • 0022350960 scopus 로고
    • Cystic fibrosis locus defines by a genetically linked polymorphism DNA marker
    • Tsui, L.C., Cystic fibrosis locus defines by a genetically linked polymorphism DNA marker. Science, 230, 1054-1057. 1985.
    • (1985) Science , vol.230 , pp. 1054-1057
    • Tsui, L.C.1
  • 167
    • 0030956394 scopus 로고    scopus 로고
    • Paraoxonase (PON1) gene in mice: Sequencing, chromosomal localization and developmental expression
    • Li, W.F., Matthews, C., Disteche, C.M., Costa, L.G., and Furlong, C.E., Paraoxonase (PON1) gene in mice: sequencing, chromosomal localization and developmental expression. Pharmacogenetics., 7, 137-144, 1997.
    • (1997) Pharmacogenetics , vol.7 , pp. 137-144
    • Li, W.F.1    Matthews, C.2    Disteche, C.M.3    Costa, L.G.4    Furlong, C.E.5
  • 168
    • 0029937118 scopus 로고    scopus 로고
    • The human serum paraoxonase/ arylesterase gene (PON1) is one member of a multigene family
    • Primo-Parmo, S.L., Sorenson, R.C., Teiber, J., and La-Du, B.N., The human serum paraoxonase/ arylesterase gene (PON1) is one member of a multigene family. Genomics, 33, 498-507, 1996.
    • (1996) Genomics , vol.33 , pp. 498-507
    • Primo-Parmo, S.L.1    Sorenson, R.C.2    Teiber, J.3    La-Du, B.N.4
  • 169
    • 0024008341 scopus 로고
    • Cloning and sequencing of a plasmidborne gene (opd) encoding a phosphotriesterase
    • McDaniel, C.S., Harper, L.L., and Wild, J.R., Cloning and sequencing of a plasmidborne gene (opd) encoding a phosphotriesterase. J. Bacteriol., 170, 2306-2311, 1988.
    • (1988) J. Bacteriol. , vol.170 , pp. 2306-2311
    • McDaniel, C.S.1    Harper, L.L.2    Wild, J.R.3
  • 170
    • 0022479569 scopus 로고
    • Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by Southern hybridization with opd from Pseudomonas diminuta
    • Mulbry, W.W., Karns, J.S., Kearney, P.C., Nelson, J.O., McDaniel, C.S., and Wild, J.R., Identification of a plasmid-borne parathion hydrolase gene from Flavobacterium sp. by Southern hybridization with opd from Pseudomonas diminuta. Appl. Environ. Microbiol., 51 (5), 926-930, 1986.
    • (1986) Appl. Environ. Microbiol. , vol.51 , Issue.5 , pp. 926-930
    • Mulbry, W.W.1    Karns, J.S.2    Kearney, P.C.3    Nelson, J.O.4    McDaniel, C.S.5    Wild, J.R.6
  • 171
    • 0024097524 scopus 로고
    • Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes
    • Harper, L.L., McDaniel, C.S., Miller, C.E., and Wild, J.R., Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes. Appl. Environ. Microbiol., 54, 2586-2589, 1988.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 2586-2589
    • Harper, L.L.1    McDaniel, C.S.2    Miller, C.E.3    Wild, J.R.4
  • 172
    • 0028609492 scopus 로고
    • Three-dimensional structure of phosphotriesterase: An enzyme capable of detoxifying organophosphate nerve agents
    • Benning, M.M., Kuo, J.M., Raushel, F.M., and Holden, H.M., Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents. Biochemistry, 33, 15001-15007, 1994.
    • (1994) Biochemistry , vol.33 , pp. 15001-15007
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 173
    • 0027893349 scopus 로고
    • Structural characterization of the divalent cation sites of bacterial phosphotriesterase by Cd-113 NMR spectroscopy
    • Omburo, G.A., Mullins, L.S., and Raushel, F.M., Structural characterization of the divalent cation sites of bacterial phosphotriesterase by Cd-113 NMR spectroscopy. Biochemistry, 32, 9148-9155, 1993.
    • (1993) Biochemistry , vol.32 , pp. 9148-9155
    • Omburo, G.A.1    Mullins, L.S.2    Raushel, F.M.3
  • 174
    • 0028288223 scopus 로고
    • Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis
    • Kuo, J.M. and Raushel, F.M., Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis. Biochemistry, 33, 4265-4272, 1994.
    • (1994) Biochemistry , vol.33 , pp. 4265-4272
    • Kuo, J.M.1    Raushel, F.M.2
  • 175
    • 0029993512 scopus 로고    scopus 로고
    • Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate
    • Van Hooke, J.L., Benning, M.M., Raushel, F.M., and Holden, H.M., Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate. Biochemistry, 35, 6020-6025, 1996.
    • (1996) Biochemistry , vol.35 , pp. 6020-6025
    • Van Hooke, J.L.1    Benning, M.M.2    Raushel, F.M.3    Holden, H.M.4
  • 176
    • 0028847160 scopus 로고
    • Phosphorus-31 NMR relaxation studies of diethyl p-metoxyphenyl phosphate bound to phosphotriesterase
    • Mullins, I.S., Chae, M.Y., and Raushel, F.M., Phosphorus-31 NMR relaxation studies of diethyl p-metoxyphenyl phosphate bound to phosphotriesterase. Bioorg. Medicinal Chem. Letter, 5, 3067-3072, 1995.
    • (1995) Bioorg. Medicinal Chem. Letter , vol.5 , pp. 3067-3072
    • Mullins, I.S.1    Chae, M.Y.2    Raushel, F.M.3
  • 177
    • 0029032588 scopus 로고
    • Three-dimensional structure of the binuclear metal center of phosphotriesterase
    • Benning, M.M., Kuo, J.M., Raushel, F.M., and Holden, H.M., Three-dimensional structure of the binuclear metal center of phosphotriesterase. Biochemistry, 34(25), 7973-7978, 1995.
    • (1995) Biochemistry , vol.34 , Issue.25 , pp. 7973-7978
    • Benning, M.M.1    Kuo, J.M.2    Raushel, F.M.3    Holden, H.M.4
  • 178
    • 0028855016 scopus 로고
    • 2 is required for the assembly of the binuclear metal center of phosphotriesterase
    • 2 is required for the assembly of the binuclear metal center of phosphotriesterase. J. Am. Chem. Soc., 117, 7580-7581, 1995.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7580-7581
    • Hong, S.B.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 179
    • 0343580454 scopus 로고    scopus 로고
    • Perturbations to the active site of phosphotriesterase
    • Kuo, J.M., Chae, M.Y., and Raushel, F.M., Perturbations to the active site of phosphotriesterase. Biochemistry, 36, 1982-1988, 1997.
    • (1997) Biochemistry , vol.36 , pp. 1982-1988
    • Kuo, J.M.1    Chae, M.Y.2    Raushel, F.M.3
  • 180
    • 0024340489 scopus 로고
    • Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta
    • Donarski, W.J., Dumas, D.P., Heitmeyer D.P., Lewis V.E., and Raushel, F.M., Structure-activity relationships in the hydrolysis of substrates by the phosphotriesterase from Pseudomonas diminuta. Bio-chemistry, 28, 4650-4655. 1989.
    • (1989) Bio-Chemistry , vol.28 , pp. 4650-4655
    • Donarski, W.J.1    Dumas, D.P.2    Heitmeyer, D.P.3    Lewis, V.E.4    Raushel, F.M.5
  • 181
    • 0029759529 scopus 로고    scopus 로고
    • Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase
    • Hong, S.B. and Raushel, F.M., Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase. Biochemistry, 35, 10904-10912, 1996.
    • (1996) Biochemistry , vol.35 , pp. 10904-10912
    • Hong, S.B.1    Raushel, F.M.2
  • 182
    • 0025836538 scopus 로고
    • Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudo-monas diminuta
    • Caldwell, S.R., Newcomb, J.R., Schlecht, K.A., and Raushel, F.M., Limits of diffusion in the hydrolysis of substrates by the phosphotriesterase from Pseudo-monas diminuta. Biochemistry, 30, 7438-7444, 1991.
    • (1991) Biochemistry , vol.30 , pp. 7438-7444
    • Caldwell, S.R.1    Newcomb, J.R.2    Schlecht, K.A.3    Raushel, F.M.4
  • 183
    • 0024561567 scopus 로고
    • "A-esterases". Enzymes looking for a role?
    • Mackness, M.I., "A-esterases". enzymes looking for a role? Biochem. Pharmacol., 38, 385-390, 1989.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 385-390
    • Mackness, M.I.1
  • 184
    • 0029960552 scopus 로고    scopus 로고
    • Las esterasas que hidrolizan compuestos organofosforados: Un mecanismo eficaz de destoxificación
    • Sogorb, M.A., Pla, A., and Vilanova, E., Las esterasas que hidrolizan compuestos organofosforados: un mecanismo eficaz de destoxificación. Rev. Toxicol., 13, 43-48, 1996.
    • (1996) Rev. Toxicol. , vol.13 , pp. 43-48
    • Sogorb, M.A.1    Pla, A.2    Vilanova, E.3
  • 185
    • 0029928952 scopus 로고    scopus 로고
    • Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme
    • Cheng, T.C., Harvey, S.P., and Chen, G.L., Cloning and expression of a gene encoding a bacterial enzyme for decontamination of organophosphorus nerve agents and nucleotide sequence of the enzyme. Appl. Environ. Microbiol., 62, 1636-1641, 1996.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1636-1641
    • Cheng, T.C.1    Harvey, S.P.2    Chen, G.L.3
  • 186
    • 0030786411 scopus 로고    scopus 로고
    • Molecular cloning and expression pattern of rpr-1, a resiniferatoxin-binding, phosphotriesterase-related protein, expressed in rat kidney tubules
    • Davies, J.A., Buchman, V.L., Krylova, O., and Ninkina, N.N., Molecular cloning and expression pattern of rpr-1, a resiniferatoxin-binding, phosphotriesterase-related protein, expressed in rat kidney tubules. FEBS Lett., 410, 378-382. 1997.
    • (1997) FEBS Lett. , vol.410 , pp. 378-382
    • Davies, J.A.1    Buchman, V.L.2    Krylova, O.3    Ninkina, N.N.4
  • 187
    • 0019400999 scopus 로고
    • Genetics of paraoxonase
    • Eiberg, H. and Mohr, J., Genetics of paraoxonase. Ann. Hum. Genet., 45, 323-330, 1981.
    • (1981) Ann. Hum. Genet. , vol.45 , pp. 323-330
    • Eiberg, H.1    Mohr, J.2
  • 188
    • 0028883658 scopus 로고
    • Serum paraoxonase activity, concentration, and phenotype distribution in diabetes mellitus and its relationship to serum lipids and lipoproteins
    • Abbott, C.A., Mackness, M.I., Kumar, S., Boulton, A.J., and Durrington, P.N., Serum paraoxonase activity, concentration, and phenotype distribution in diabetes mellitus and its relationship to serum lipids and lipoproteins. Arterioscler. Thromb. Vasc. Biol., 15, 1812-1818, 1995.
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1812-1818
    • Abbott, C.A.1    Mackness, M.I.2    Kumar, S.3    Boulton, A.J.4    Durrington, P.N.5
  • 190
    • 0029611091 scopus 로고
    • Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera
    • Reiner, E., Simeon-Rudolf, V., and SkrinjaricSpoljar, M., Catalytic properties and distribution profiles of paraoxonase and cholinesterase phenotypes in human sera. Toxicol. Lett., 82/83, 447-52, 1995.
    • (1995) Toxicol. Lett. , vol.82-83 , pp. 447-452
    • Reiner, E.1    Simeon-Rudolf, V.2    SkrinjaricSpoljar, M.3
  • 191
    • 0023638028 scopus 로고
    • Low A-esterase activity in serum of patients with fish-eye disease
    • Mackness, M.I., Walker, C.H., and Carlson, L.A., Low A-esterase activity in serum of patients with fish-eye disease. Clin. Chem., 33(4), 587-588, 1987.
    • (1987) Clin. Chem. , vol.33 , Issue.4 , pp. 587-588
    • Mackness, M.I.1    Walker, C.H.2    Carlson, L.A.3
  • 192
    • 0030065867 scopus 로고    scopus 로고
    • A mouse kidney- and liver-expressed eDNA having homology with a prokaryotic parathion hydrolase (phosphotriesterase)-encoding gene: Abnormal expression in injured and polycystic kidneys
    • Hou, X., Maser, R.L., Magenheimer, B.S., and Calvet, J.P., A mouse kidney- and liver-expressed eDNA having homology with a prokaryotic parathion hydrolase (phosphotriesterase)-encoding gene: abnormal expression in injured and polycystic kidneys. Gene, 168, 157-163, 1996.
    • (1996) Gene , vol.168 , pp. 157-163
    • Hou, X.1    Maser, R.L.2    Magenheimer, B.S.3    Calvet, J.P.4
  • 193
    • 0023852347 scopus 로고
    • Multiple forms of sheep serum A-esterase activity associated with the high-density lipoproteins
    • Mackness, M.I. and Walker, C., Multiple forms of sheep serum A-esterase activity associated with the high-density lipoproteins. Biochem. J., 250, 539-545, 1988.
    • (1988) Biochem. J. , vol.250 , pp. 539-545
    • Mackness, M.I.1    Walker, C.2
  • 195
    • 0025864611 scopus 로고
    • Paraoxonase prevents accumulation of lipoperoxides in low-density Lipoprotein
    • Mackness, M.I., Arrol, S., and Durrington, P.N., Paraoxonase prevents accumulation of lipoperoxides in low-density Lipoprotein. FEBS Letters, 286, 152-154, 1991.
    • (1991) FEBS Letters , vol.286 , pp. 152-154
    • Mackness, M.I.1    Arrol, S.2    Durrington, P.N.3
  • 197
    • 0028809494 scopus 로고
    • A variant of human paraoxonase/arylesterase (HUMPONA) gene is a risk factor for coronary artery disease
    • Serrato, M. and Marian, A.J., A variant of human paraoxonase/arylesterase (HUMPONA) gene is a risk factor for coronary artery disease. J. Clin. Invest., 96, 3005-3008, 1995.
    • (1995) J. Clin. Invest. , vol.96 , pp. 3005-3008
    • Serrato, M.1    Marian, A.J.2
  • 198
    • 0029918732 scopus 로고    scopus 로고
    • Genetic-dietary regulation of serum paraoxonase expression and its role in atherogenesis in a mouse
    • Shih, D.M., Gu, L., Hama, S., Xia, Y.R., Navab, M., Fogelman, A.M., and Lusis, A.J., Genetic-dietary regulation of serum paraoxonase expression and its role in atherogenesis in a mouse. J. Clin. Invest., 97, 1630-1639, 1996.
    • (1996) J. Clin. Invest. , vol.97 , pp. 1630-1639
    • Shih, D.M.1    Gu, L.2    Hama, S.3    Xia, Y.R.4    Navab, M.5    Fogelman, A.M.6    Lusis, A.J.7
  • 200
    • 0013534443 scopus 로고    scopus 로고
    • No correlation between paraoxonase activity and HDL levels in human serum in a local population
    • Díaz., J., Céspedes, V., Molina, R., Sastre, J.F., Vilanova, E., and Carrera, V., No correlation between paraoxonase activity and HDL levels in human serum in a local population. Toxicol. Lett., Suppl./88, 28-29, 1996.
    • (1996) Toxicol. Lett. , Issue.SUPPL.-88 , pp. 28-29
    • Díaz, J.1    Céspedes, V.2    Molina, R.3    Sastre, J.F.4    Vilanova, E.5    Carrera, V.6
  • 201
    • 0029788728 scopus 로고    scopus 로고
    • The Gln-Arg191 polymorphism of the human paraoxonase gene (HUMPONA) is not associated with the risk of coronary artery disease in Finns
    • Antikainen, M., Murtomaki, S., Syvanne, K.M., Pahlman, R., Tahvanainen, E., Jauhiainen, M., Frick, M.H., and Ehnholm, C., The Gln-Arg191 polymorphism of the human paraoxonase gene (HUMPONA) is not associated with the risk of coronary artery disease in Finns. J. Clin. Invest., 98, 883-885, 1996.
    • (1996) J. Clin. Invest. , vol.98 , pp. 883-885
    • Antikainen, M.1    Murtomaki, S.2    Syvanne, K.M.3    Pahlman, R.4    Tahvanainen, E.5    Jauhiainen, M.6    Frick, M.H.7    Ehnholm, C.8
  • 203
    • 0027435542 scopus 로고
    • The role of high-density lipoprotein and lipid-soluble antioxidant vitamins in inhibiting low-density lipoprotein oxidation
    • Mackness, M.I., Abbott, C., Arrol, S., and Durrington, P.N., The role of high-density lipoprotein and lipid-soluble antioxidant vitamins in inhibiting low-density lipoprotein oxidation. Biochem. J., 294, 829-834, 1993.
    • (1993) Biochem. J. , vol.294 , pp. 829-834
    • Mackness, M.I.1    Abbott, C.2    Arrol, S.3    Durrington, P.N.4
  • 204
    • 0027763632 scopus 로고
    • Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase
    • Mackness, M.I., Arrol, S., Abbott, C., and Durrington, P.N., Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase. Atherosclerosis, 104(12), 129-135, 1993.
    • (1993) Atherosclerosis , vol.104 , Issue.12 , pp. 129-135
    • Mackness, M.I.1    Arrol, S.2    Abbott, C.3    Durrington, P.N.4
  • 205
    • 0029020612 scopus 로고
    • HDL, its enzymes and its potential to influence lipid peroxidation
    • Mackness, M.I. and Durrington, P.N., HDL, its enzymes and its potential to influence lipid peroxidation. Atherosclerosis, 115(2), 243-253, 1995.
    • (1995) Atherosclerosis , vol.115 , Issue.2 , pp. 243-253
    • Mackness, M.I.1    Durrington, P.N.2
  • 207
    • 77957187829 scopus 로고
    • Kinetics analyses of the microsomal biotransformation of the phosphorothioate insecticides chlorpyrifos and parathion
    • Sultatos, L.G. and Murphy, S.D., Kinetics analyses of the microsomal biotransformation of the phosphorothioate insecticides chlorpyrifos and parathion. Fundam. App. Toxicol., 3, 16-21, 1983.
    • (1983) Fundam. App. Toxicol. , vol.3 , pp. 16-21
    • Sultatos, L.G.1    Murphy, S.D.2
  • 208
    • 0022968805 scopus 로고
    • The effects of phenobarbital pretreatment on the metabolism and acute toxicity on the pesticide parathion in the mouse
    • Sultatos, L.G., The effects of phenobarbital pretreatment on the metabolism and acute toxicity on the pesticide parathion in the mouse. Toxicol. Appl. Pharmacol., 86, 105-111, 1986.
    • (1986) Toxicol. Appl. Pharmacol. , vol.86 , pp. 105-111
    • Sultatos, L.G.1
  • 209
    • 0026542178 scopus 로고
    • Biotransformation of the insecticide parathion by mouse brain
    • Soranno, T.M. and Sultatos, L.G., Biotransformation of the insecticide parathion by mouse brain. Toxicol. Lett., 60, 27-37, 1992.
    • (1992) Toxicol. Lett. , vol.60 , pp. 27-37
    • Soranno, T.M.1    Sultatos, L.G.2
  • 210
    • 0023518615 scopus 로고
    • Intrinsic metabolic clearance of parathion and paraoxon by livers from fish and rodents
    • Wallace, K.B. and Dargan, J.E., Intrinsic metabolic clearance of parathion and paraoxon by livers from fish and rodents. Toxicol. Appl. Pharmacol., 90, 235-242, 1987.
    • (1987) Toxicol. Appl. Pharmacol. , vol.90 , pp. 235-242
    • Wallace, K.B.1    Dargan, J.E.2
  • 211
    • 0021234237 scopus 로고
    • The role of hepatic biotransformation in mechating the acute toxicity of the phosphorothionate insecticide chlorpyrifos
    • Sultatos, L.G., Shao, M., and Murphy, S.D., The role of hepatic biotransformation in mechating the acute toxicity of the phosphorothionate insecticide chlorpyrifos. Toxicol. Appl. Pharmacol., 73, 60-68, 1984.
    • (1984) Toxicol. Appl. Pharmacol. , vol.73 , pp. 60-68
    • Sultatos, L.G.1    Shao, M.2    Murphy, S.D.3
  • 212
    • 0023813781 scopus 로고
    • Factors affecting the hepatic biotransformation of the phosphorothioate pesticide chlorpyrifos
    • Sultatos, L.G., Factors affecting the hepatic biotransformation of the phosphorothioate pesticide chlorpyrifos. Toxicology, 51, 191-200, 1988.
    • (1988) Toxicology , vol.51 , pp. 191-200
    • Sultatos, L.G.1
  • 213
    • 0025856512 scopus 로고
    • Metabolic activation of the organophosphorus insecticides chlorpyrifos and fenitrothion by perfused rat liver
    • Sultatos, L.G., Metabolic activation of the organophosphorus insecticides chlorpyrifos and fenitrothion by perfused rat liver. Toxicology, 68, 19, 1991.
    • (1991) Toxicology , vol.68 , pp. 19
    • Sultatos, L.G.1
  • 214
    • 0023499756 scopus 로고
    • Metabolic activation of the pesticide azinphos-methyl by perfused mouse livers
    • Sultatos, L.G. and Minor, L.D., Metabolic activation of the pesticide azinphos-methyl by perfused mouse livers. Toxicol. App. Pharmacol., 90, 227-234, 1987.
    • (1987) Toxicol. App. Pharmacol. , vol.90 , pp. 227-234
    • Sultatos, L.G.1    Minor, L.D.2
  • 215
    • 0028273152 scopus 로고
    • Role of detoxication pathways in acute toxicity levels of phosphorothionate insecticides in the rat
    • Chambers, J.E., Ma, T., Boone, J.S., and Chambers, H.W., Role of detoxication pathways in acute toxicity levels of phosphorothionate insecticides in the rat. Life Sci., 54, 1357-1364, 1994.
    • (1994) Life Sci. , vol.54 , pp. 1357-1364
    • Chambers, J.E.1    Ma, T.2    Boone, J.S.3    Chambers, H.W.4
  • 216
    • 0029586060 scopus 로고
    • Biochemical mechanisms contributing to species differences in insecticidal toxicity
    • Chambers, J.E. and Carr, R.L., Biochemical mechanisms contributing to species differences in insecticidal toxicity. Toxicology, 105, 291-304, 1995.
    • (1995) Toxicology , vol.105 , pp. 291-304
    • Chambers, J.E.1    Carr, R.L.2
  • 217
    • 0022339788 scopus 로고
    • Paraoxon hydrolysis vs. covalent binding in the elimination of paraoxon in the rabbit
    • Butler, E.G., Eckerson, H.W., and La-Du, B.N., Paraoxon hydrolysis vs. covalent binding in the elimination of paraoxon in the rabbit. Drug. Metab. Dispos., 13, 640-645, 1985.
    • (1985) Drug. Metab. Dispos. , vol.13 , pp. 640-645
    • Butler, E.G.1    Eckerson, H.W.2    La-Du, B.N.3
  • 218
    • 0029905656 scopus 로고    scopus 로고
    • Structural and functional diversity of paraoxonases
    • La Du, B.N., Structural and functional diversity of paraoxonases [news]. Nat. Med., 2(11), 1186-1187, 1996.
    • (1996) Nat. Med. , vol.2 , Issue.11 , pp. 1186-1187
    • La Du, B.N.1
  • 219
    • 0023219503 scopus 로고
    • 'A' esterases and their role in regulating the toxicity of organophosphates
    • Walker, C.H. and Mackness, M.I., 'A' esterases and their role in regulating the toxicity of organophosphates. Arch. Toxicol., 60, 30-33, 1987.
    • (1987) Arch. Toxicol. , vol.60 , pp. 30-33
    • Walker, C.H.1    Mackness, M.I.2
  • 220
    • 0021017871 scopus 로고
    • Haloxoninduced delayed neurotoxicity: Effect of plasma A (aryl) esterase activity on severity of lesions in sheep
    • Jortner, B.S., Pope, A.M., and Heavner, J.E., Haloxoninduced delayed neurotoxicity: effect of plasma A (aryl) esterase activity on severity of lesions in sheep. Neurotoxicology, 4, 241-246, 1983.
    • (1983) Neurotoxicology , vol.4 , pp. 241-246
    • Jortner, B.S.1    Pope, A.M.2    Heavner, J.E.3
  • 221
    • 0030324043 scopus 로고    scopus 로고
    • Maturational differences in chlorpyrifos-oxonase activity may contribute to age-related sensitivity to chiorpyrifos
    • Mortensen, S.R., Chanda, S.M., Hooper, M.J., and Padilla, S., Maturational differences in chlorpyrifos-oxonase activity may contribute to age-related sensitivity to chiorpyrifos. J. Biochem. Toxicol., 11, 279-287, 1996.
    • (1996) J. Biochem. Toxicol. , vol.11 , pp. 279-287
    • Mortensen, S.R.1    Chanda, S.M.2    Hooper, M.J.3    Padilla, S.4
  • 222
    • 0028958850 scopus 로고
    • Paraoxonase protects against chlorpyrifos toxicity in mice
    • Li, W.F., Furlong, C.E., and Costa, L.G., Paraoxonase protects against chlorpyrifos toxicity in mice. Toxicol. Lett., 76, 219-226, 1995.
    • (1995) Toxicol. Lett. , vol.76 , pp. 219-226
    • Li, W.F.1    Furlong, C.E.2    Costa, L.G.3
  • 223
    • 0027367163 scopus 로고
    • Serum paraoxonase status: A major factor in determining resistance to organophosphates
    • Li, W.F., Costa, L.G., and Furlong, C.E., Serum paraoxonase status: a major factor in determining resistance to organophosphates. J. Toxicol. Environ, Health, 40, 337-346, 1993.
    • (1993) J. Toxicol. Environ, Health , vol.40 , pp. 337-346
    • Li, W.F.1    Costa, L.G.2    Furlong, C.E.3
  • 224
    • 0026564530 scopus 로고
    • A purified recombinant organophosphorus acid anhydrase protects mice against soman
    • Broomfield, C.A., A purified recombinant organophosphorus acid anhydrase protects mice against soman. Pharmacol. Toxicol., 70, 65-66, 1992.
    • (1992) Pharmacol. Toxicol. , vol.70 , pp. 65-66
    • Broomfield, C.A.1
  • 225
    • 77957180029 scopus 로고
    • Phosphotriesterase - A promising candidate for use in detoxification of organophosphates
    • Tuovinen, K., KalisteKorhonen, E., Raushel, F.M., and Hanninen, O., Phosphotriesterase - a promising candidate for use in detoxification of organophosphates. Fundam. Appl. Toxicol., 23, 578-584, 1994.
    • (1994) Fundam. Appl. Toxicol. , vol.23 , pp. 578-584
    • Tuovinen, K.1    Kalistekorhonen, E.2    Raushel, F.M.3    Hanninen, O.4
  • 227
    • 26844554200 scopus 로고    scopus 로고
    • Protection of organophosphate-inactivated esterases with phosphotriesterase
    • Tuovinen, K., KalisteKorhonen, E., Raushel, F.M., and Hanninen, O., Protection of organophosphate-inactivated esterases with phosphotriesterase. Fundam. Appl. Toxicol., 31(2), 210-217, 1996.
    • (1996) Fundam. Appl. Toxicol. , vol.31 , Issue.2 , pp. 210-217
    • Tuovinen, K.1    Kalistekorhonen, E.2    Raushel, F.M.3    Hanninen, O.4
  • 230
    • 0030446786 scopus 로고    scopus 로고
    • Phosphotriesterase, pralid-oxime-2-chloride (2PAM) and eptastigmine treatments and their combinations in DFP intoxication
    • Tuovinen, K., KalisteKorhonen, E., Raushel, F.M., and Hänninen, O., Phosphotriesterase, pralid-oxime-2-chloride (2PAM) and eptastigmine treatments and their combinations in DFP intoxication. Toxicol. App. Pharmacol., 141, 555-560.
    • Toxicol. App. Pharmacol. , vol.141 , pp. 555-560
    • Tuovinen, K.1    Kalistekorhonen, E.2    Raushel, F.M.3    Hänninen, O.4
  • 231
    • 0028535251 scopus 로고
    • High-level expression of the bacterial opd gene in Drosophila melanogaster: Improved inducible insecticide resistance
    • Benedict, M.Q., Scott, J.A., and Cockburn, A.F., High-level expression of the bacterial opd gene in Drosophila melanogaster: improved inducible insecticide resistance. Insect. Mol. Biol., 3, 247-252, 1994.
    • (1994) Insect. Mol. Biol. , vol.3 , pp. 247-252
    • Benedict, M.Q.1    Scott, J.A.2    Cockburn, A.F.3
  • 232
    • 0020037124 scopus 로고
    • Hydrolysis of nerve gas by squidtype diisopropyl phosphorofluoridate hydrolyzing enzyme on agarose resin
    • Hoskin, F.C. and Roush, A.H., Hydrolysis of nerve gas by squidtype diisopropyl phosphorofluoridate hydrolyzing enzyme on agarose resin. Science, 215, 1255-1257, 1982.
    • (1982) Science , vol.215 , pp. 1255-1257
    • Hoskin, F.C.1    Roush, A.H.2
  • 233
    • 0026235932 scopus 로고
    • Detoxification of organophosphate pesticides using a nylon-based immobilized phosphotriesterase from pseudomonas diminuta
    • Caldwell, S.R. and Raushel, F.M., Detoxification of organophosphate pesticides using a nylon-based immobilized phosphotriesterase from pseudomonas diminuta. App. Biochem. Biotechnol., 31, 59-73, 1991.
    • (1991) App. Biochem. Biotechnol. , vol.31 , pp. 59-73
    • Caldwell, S.R.1    Raushel, F.M.2
  • 234
    • 0026071672 scopus 로고
    • Detoxification of organophosphate pesticides using an immobilized phosphotriesterase from Pseudomonas diminuta
    • Caldwell, S.R. and Raushel, F.M., Detoxification of Organophosphate Pesticides Using an Immobilized Phosphotriesterase from Pseudomonas diminuta. Biotech. Bioeng., 37, 103-109, 1991.
    • (1991) Biotech. Bioeng. , vol.37 , pp. 103-109
    • Caldwell, S.R.1    Raushel, F.M.2
  • 235
    • 0030754819 scopus 로고    scopus 로고
    • Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase
    • Watkins, L.M., Mahoney, H.J., McCulloch, J.K., and Raushel, F.M., Augmented hydrolysis of diisopropyl fluorophosphate in engineered mutants of phosphotriesterase. J. Biol. Chem, 272, 25596-256601, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 25596-256601
    • Watkins, L.M.1    Mahoney, H.J.2    McCulloch, J.K.3    Raushel, F.M.4
  • 236
    • 0030670779 scopus 로고    scopus 로고
    • A combinatorial library for the binuclear metal center of bacterial phosphotriesterase
    • Watkins, L.M., Kuo, J.M., Chen-Goodspeed, M., and Raushel, F.M., A combinatorial library for the binuclear metal center of bacterial phosphotriesterase. Prot. Struct. Funct. Genet., 29, 553-561, 1997.
    • (1997) Prot. Struct. Funct. Genet. , vol.29 , pp. 553-561
    • Watkins, L.M.1    Kuo, J.M.2    Chen-Goodspeed, M.3    Raushel, F.M.4
  • 237
    • 0003242424 scopus 로고    scopus 로고
    • The development of a new biosensor based on recombinant E. coli for the direct detection of organophosphorus neurotoxins. Biosens
    • Rainina, E.I., Efremenco, E.N., Varfolomeyev, S.D., Simonian, A.L., and Wild, J.R., The development of a new biosensor based on recombinant E. coli for the direct detection of organophosphorus neurotoxins. Biosens. Bioelectron, 11. 991-1000, 1996.
    • (1996) Bioelectron , vol.11 , pp. 991-1000
    • Rainina, E.I.1    Efremenco, E.N.2    Varfolomeyev, S.D.3    Simonian, A.L.4    Wild, J.R.5
  • 238
    • 0021806095 scopus 로고
    • A fruit fly bioassay with phosphotriesterase for detection of certain organophosphorus insecticide residues
    • Chiang, T., Dean, M.C., and McDaniel, C.S., A fruit fly bioassay with phosphotriesterase for detection of certain organophosphorus insecticide residues. Bull. Environ. Contain. Toxicol., 34, 809-814, 1985.
    • (1985) Bull. Environ. Contain. Toxicol. , vol.34 , pp. 809-814
    • Chiang, T.1    Dean, M.C.2    McDaniel, C.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.