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Volumn 64, Issue 6, 2008, Pages 594-609

Gerry Brooks and epoxide hydrolases: Four decades to a pharmaceutical

Author keywords

Asymmetric organic synthesis; Cardiovascular diseases; Juvenile hormone; Xenobiotic metabolism

Indexed keywords

EPOXIDE HYDROLASE; INSECTICIDE; JUVENILE HORMONE;

EID: 44949226818     PISSN: 1526498X     EISSN: 15264998     Source Type: Journal    
DOI: 10.1002/ps.1583     Document Type: Conference Paper
Times cited : (44)

References (136)
  • 1
    • 0003501713 scopus 로고
    • Chlorinated Insecticides
    • CRC Press, Cleveland, OH
    • Brooks GT, Chlorinated Insecticides. Vol. 1. Technology and Application. CRC Press, Cleveland, OH (1974).
    • (1974) Technology and Application , vol.1
    • Brooks, G.T.1
  • 3
    • 0014710431 scopus 로고
    • Cyclodiene epoxide ring hydration by microsomes from mammalian liver and houseflies
    • Brooks GT, Harrison A and Lewis SE, Cyclodiene epoxide ring hydration by microsomes from mammalian liver and houseflies. Biochem Pharmacol 19:255-273 (1970).
    • (1970) Biochem Pharmacol , vol.19 , pp. 255-273
    • Brooks, G.T.1    Harrison, A.2    Lewis, S.E.3
  • 4
    • 44949153277 scopus 로고
    • Metabolism of polycyclic compounds. 5. Formation of 1:2-dihydroxy-1:2-dihydronaphthalenes
    • Booth J and Boyland E, Metabolism of polycyclic compounds. 5. Formation of 1:2-dihydroxy-1:2-dihydronaphthalenes. Biochem J 44:361-365 (1949).
    • (1949) Biochem J , vol.44 , pp. 361-365
    • Booth, J.1    Boyland, E.2
  • 5
    • 0343711095 scopus 로고
    • Studies in detoxication; the metabolism of chlorobenzene in the rabbit; isolation of dihydrodihydroxychlorobenzene, p-chlorophenylglucuronide, 4-chlorocatechol glucuronide and p-chlorophenylmercapturic acid
    • Smith JN, Spencer B and Williams RT, Studies in detoxication; the metabolism of chlorobenzene in the rabbit; isolation of dihydrodihydroxychlorobenzene, p-chlorophenylglucuronide, 4-chlorocatechol glucuronide and p-chlorophenylmercapturic acid. Biochem J 47:284-293 (1950).
    • (1950) Biochem J , vol.47 , pp. 284-293
    • Smith, J.N.1    Spencer, B.2    Williams, R.T.3
  • 6
    • 0014286663 scopus 로고
    • Oxidation of indene in liver microsomes
    • Leibman KC and Ortiz E, Oxidation of indene in liver microsomes. Mol Pharmacol 4:201-207 (1968).
    • (1968) Mol Pharmacol , vol.4 , pp. 201-207
    • Leibman, K.C.1    Ortiz, E.2
  • 7
    • 0000772808 scopus 로고
    • Role of arene oxide-oxepin system in the metabolism of aromatic substrates. I. In vitro conversion of benzene oxide to a premercapturic acid and a dihydrodiol
    • Jerina D, Daly J, Wiltkop B, Zaltzman-Nirenberg P and Udenfriend S, Role of arene oxide-oxepin system in the metabolism of aromatic substrates. I. In vitro conversion of benzene oxide to a premercapturic acid and a dihydrodiol. Arch Biochem Biophys 128:176-183 (1968).
    • (1968) Arch Biochem Biophys , vol.128 , pp. 176-183
    • Jerina, D.1    Daly, J.2    Wiltkop, B.3    Zaltzman-Nirenberg, P.4    Udenfriend, S.5
  • 8
    • 0014962887 scopus 로고
    • Epoxides as obligatory intermediates in the metabolism of olefins to glycols
    • Maynert EW, Foreman RL and Watabe T, Epoxides as obligatory intermediates in the metabolism of olefins to glycols. J Biol Chem 245:5234-5238 (1970).
    • (1970) J Biol Chem , vol.245 , pp. 5234-5238
    • Maynert, E.W.1    Foreman, R.L.2    Watabe, T.3
  • 9
    • 0014934298 scopus 로고
    • 1,2-Naphthalene oxide as an intermediate in the microsomal hydroxylation of naphthalene
    • Jerina D, Daly JW, Wiltkop B, Zaltzman-Nirenberg P and Udenfriend S, 1,2-Naphthalene oxide as an intermediate in the microsomal hydroxylation of naphthalene. Biochemistry 9:147-156 (1970).
    • (1970) Biochemistry , vol.9 , pp. 147-156
    • Jerina, D.1    Daly, J.W.2    Wiltkop, B.3    Zaltzman-Nirenberg, P.4    Udenfriend, S.5
  • 10
    • 0015835976 scopus 로고
    • Insect epoxide hydrase inhibition by juvenile hormone analogs and metabolic inhibitors
    • Brooks GT, Insect epoxide hydrase inhibition by juvenile hormone analogs and metabolic inhibitors. Nature (London) 245:382-384 (1973).
    • (1973) Nature (London) , vol.245 , pp. 382-384
    • Brooks, G.T.1
  • 11
    • 84983898079 scopus 로고
    • Inhibitors of cyclodiene epoxide ring hydrating enzymes of the blowfly, Calliphora erythrocephala
    • Brooks GT, Inhibitors of cyclodiene epoxide ring hydrating enzymes of the blowfly, Calliphora erythrocephala. Pestic Sci 5:177-183 (1974).
    • (1974) Pestic Sci , vol.5 , pp. 177-183
    • Brooks, G.T.1
  • 12
    • 0015753093 scopus 로고
    • Effects of metabolic inhibitors on insect epoxide hydratases
    • Brooks GT, Effects of metabolic inhibitors on insect epoxide hydratases. Biochem Soc Trans 1:1305-1305 (1974).
    • (1974) Biochem Soc Trans , vol.1 , pp. 1305-1305
    • Brooks, G.T.1
  • 13
    • 0016437250 scopus 로고    scopus 로고
    • Slade M, Brooks GT, Hetnarski HK and Wilkinson CF, Inhibition of the enzymatic hydration of the epoxide HEOM [1,2,3,4,9,9-hexachloro-6,7-epoxy-1,4, 4a,5,6,7,8,8a-octahydro-1,4-methanonaphthalene] in insects. Pestic Biochem Physiol 5:35-46 (1975).
    • Slade M, Brooks GT, Hetnarski HK and Wilkinson CF, Inhibition of the enzymatic hydration of the epoxide HEOM [1,2,3,4,9,9-hexachloro-6,7-epoxy-1,4, 4a,5,6,7,8,8a-octahydro-1,4-methanonaphthalene] in insects. Pestic Biochem Physiol 5:35-46 (1975).
  • 14
    • 0017129780 scopus 로고
    • The inhibition of HEOM epoxide hydrase in mammalian liver microsomes and insect pupal homogenates
    • Craven ACC, Brooks GT and Walker CH, The inhibition of HEOM epoxide hydrase in mammalian liver microsomes and insect pupal homogenates. Pestic Biochem Physiol 6:132-141 (1976).
    • (1976) Pestic Biochem Physiol , vol.6 , pp. 132-141
    • Craven, A.C.C.1    Brooks, G.T.2    Walker, C.H.3
  • 15
    • 0014800548 scopus 로고
    • Solubilization of epoxide hydrolase from liver microsomes
    • Watabe T and Kanehira S, Solubilization of epoxide hydrolase from liver microsomes. Chem Pharm Bull. 18:1295-1296 (1970).
    • (1970) Chem Pharm Bull , vol.18 , pp. 1295-1296
    • Watabe, T.1    Kanehira, S.2
  • 16
    • 0016590458 scopus 로고
    • Liver microsomal expoxide hydrase. Solubilization, purification, and characterization
    • Lu AY, Ryan D, Jerina DM, Daly JW and Levin W, Liver microsomal expoxide hydrase. Solubilization, purification, and characterization. J Biol Chem 250:8283-8288 (1975).
    • (1975) J Biol Chem , vol.250 , pp. 8283-8288
    • Lu, A.Y.1    Ryan, D.2    Jerina, D.M.3    Daly, J.W.4    Levin, W.5
  • 17
    • 0015208031 scopus 로고
    • Stereoselective hydrolysis of cis- and trans-stilbene oxides by hepatic microsomal epoxide hydrolase
    • Watabe T, Akamatsu K and Kiyonaga K, Stereoselective hydrolysis of cis- and trans-stilbene oxides by hepatic microsomal epoxide hydrolase. Biochem Biophys Res Commun 44:199-204 (1971).
    • (1971) Biochem Biophys Res Commun , vol.44 , pp. 199-204
    • Watabe, T.1    Akamatsu, K.2    Kiyonaga, K.3
  • 18
    • 0015231096 scopus 로고
    • Stereoselective hydrolysis of 2,3-epoxysteroids by hepatic microsomal epoxide hydrolase
    • Watabe T, Kiyonaga K, Akamatsu K and Hara S, Stereoselective hydrolysis of 2,3-epoxysteroids by hepatic microsomal epoxide hydrolase. Biochem Biophys Res Commun 43:1252-1258 (1971).
    • (1971) Biochem Biophys Res Commun , vol.43 , pp. 1252-1258
    • Watabe, T.1    Kiyonaga, K.2    Akamatsu, K.3    Hara, S.4
  • 19
    • 0020620574 scopus 로고
    • Radiometric assays for mammalian epoxide hydrolases and glutathione S-transferase
    • Gill SS, Ota K and Hammock BD, Radiometric assays for mammalian epoxide hydrolases and glutathione S-transferase. Anal Biochem 131:273-282 (1983).
    • (1983) Anal Biochem , vol.131 , pp. 273-282
    • Gill, S.S.1    Ota, K.2    Hammock, B.D.3
  • 20
    • 36949077003 scopus 로고
    • Mechanisms of resistance of the adult housefly (Musca domestica) to 'cyclodiene' insecticides
    • Brooks GT, Mechanisms of resistance of the adult housefly (Musca domestica) to 'cyclodiene' insecticides. Nature (London) 186:96-98 (1960).
    • (1960) Nature (London) , vol.186 , pp. 96-98
    • Brooks, G.T.1
  • 21
  • 22
    • 0013505154 scopus 로고
    • trans-Epoxide hydrolase: A key indicator enzyme for herbivory in arthropods
    • Mullin CA and Croft BA, trans-Epoxide hydrolase: a key indicator enzyme for herbivory in arthropods. Cell Molec Life Sci 40:176-178 (1984).
    • (1984) Cell Molec Life Sci , vol.40 , pp. 176-178
    • Mullin, C.A.1    Croft, B.A.2
  • 23
    • 0000719553 scopus 로고
    • Adaptive relationships of epoxide hydrolase in herbivorous arthropods
    • Mullin CA, Adaptive relationships of epoxide hydrolase in herbivorous arthropods. J Chem Ecol 14:1867-1888 (1988).
    • (1988) J Chem Ecol , vol.14 , pp. 1867-1888
    • Mullin, C.A.1
  • 24
    • 0022478673 scopus 로고
    • Microsomal and cytosolic epoxide hydrolase in Drosophila melanogaster
    • Jansen M, Baars AJ and Breimer DD, Microsomal and cytosolic epoxide hydrolase in Drosophila melanogaster. Biochem Pharmacol 35:2229-2232 (1986).
    • (1986) Biochem Pharmacol , vol.35 , pp. 2229-2232
    • Jansen, M.1    Baars, A.J.2    Breimer, D.D.3
  • 25
    • 0345688025 scopus 로고    scopus 로고
    • Characterization and cDNA cloning of a clofibrate-inducible microsomal epoxide hydrolase in Drosophila melanogaster
    • Taniai K, Inceoglu AB, Yukuhiro K and Hammock BD, Characterization and cDNA cloning of a clofibrate-inducible microsomal epoxide hydrolase in Drosophila melanogaster. Eur J Biochem 270:4696-4705 (2003).
    • (2003) Eur J Biochem , vol.270 , pp. 4696-4705
    • Taniai, K.1    Inceoglu, A.B.2    Yukuhiro, K.3    Hammock, B.D.4
  • 26
    • 0023543402 scopus 로고
    • Biochemical and genetic analysis of epoxide-metabolizing enzymes in susceptible and resistant house flies, Musca domestica L
    • Ottea JA, Plapp FW and Hammock BD, Biochemical and genetic analysis of epoxide-metabolizing enzymes in susceptible and resistant house flies, Musca domestica L. Pestic Biochem Physiol 29:138-145 (1987).
    • (1987) Pestic Biochem Physiol , vol.29 , pp. 138-145
    • Ottea, J.A.1    Plapp, F.W.2    Hammock, B.D.3
  • 27
    • 84990453220 scopus 로고
    • Novel assay for determining the metabolic fate of juvenile hormone III: A study with Drosophila melanogaster
    • Ottea JA, Harshman LG and Hammock BD, Novel assay for determining the metabolic fate of juvenile hormone III: a study with Drosophila melanogaster. Arch Insect Biochem Physiol 8:25-37 (1988).
    • (1988) Arch Insect Biochem Physiol , vol.8 , pp. 25-37
    • Ottea, J.A.1    Harshman, L.G.2    Hammock, B.D.3
  • 28
    • 0011628225 scopus 로고
    • Metabolism of cecropia juvenile hormone in lepidopterans
    • Slade M and Zibitt CH, Metabolism of cecropia juvenile hormone in lepidopterans. Pestic Chem 3:45-58 (1971).
    • (1971) Pestic Chem , vol.3 , pp. 45-58
    • Slade, M.1    Zibitt, C.H.2
  • 29
    • 0001877045 scopus 로고
    • Metabolism of cecropia juvenile hormone in insects and in mammals
    • ed. by Menn JJ and Beroza M. Academic Press, New York, NY, pp
    • Slade M and Zibitt CH, Metabolism of cecropia juvenile hormone in insects and in mammals, in Insect Juvenile Hormones: Chemistry and Action, ed. by Menn JJ and Beroza M. Academic Press, New York, NY, pp. 155-176 (1972).
    • (1972) Insect Juvenile Hormones: Chemistry and Action , pp. 155-176
    • Slade, M.1    Zibitt, C.H.2
  • 30
    • 44949249644 scopus 로고    scopus 로고
    • Gill SS, Hammock BD, Yamamoto I and Casida JE, Preliminary chromatographic studies on the metabolites and photodecomposition products of the juvenoid 1-(4′-ethylphenoxy-6,7-epoxy-3,7-dimethyl-2-octene, in Insect Juvenile Hormones: Chemistry and Action, ed. by Menn JJ and Beroza M. Academic Press, New York, NY, pp. 177-189 (1972).
    • Gill SS, Hammock BD, Yamamoto I and Casida JE, Preliminary chromatographic studies on the metabolites and photodecomposition products of the juvenoid 1-(4′-ethylphenoxy-6,7-epoxy-3,7-dimethyl-2-octene, in Insect Juvenile Hormones: Chemistry and Action, ed. by Menn JJ and Beroza M. Academic Press, New York, NY, pp. 177-189 (1972).
  • 31
    • 0342296033 scopus 로고
    • The degradative metabolism of juvenoids by insects
    • ed. by Gilbert LE. Plenum Press, New York, NY, pp
    • Hammock BD and Quistad GB, The degradative metabolism of juvenoids by insects, in The Juvenile Hormones, ed. by Gilbert LE. Plenum Press, New York, NY, pp. 374-393 (1976).
    • (1976) The Juvenile Hormones , pp. 374-393
    • Hammock, B.D.1    Quistad, G.B.2
  • 32
    • 0001621784 scopus 로고
    • Regulation of juvenile hormone titer: Degradation
    • ed. by Kerkut GA and Gilbert LI. Pergamon Press, New York, NY, pp
    • Hammock BD, Regulation of juvenile hormone titer: degradation, in Comprehensive Insect Physiology, Biochemistry, and Pharmacology, ed. by Kerkut GA and Gilbert LI. Pergamon Press, New York, NY, pp. 431-472 (1985).
    • (1985) Comprehensive Insect Physiology, Biochemistry, and Pharmacology , pp. 431-472
    • Hammock, B.D.1
  • 34
    • 0033869773 scopus 로고    scopus 로고
    • The juvenile hormones: Historical facts and speculations on future research directions
    • Gilbert LI, Granger NA and Roe RM, The juvenile hormones: historical facts and speculations on future research directions. Insect Biochem Mol Biol 30:617-644 (2000).
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 617-644
    • Gilbert, L.I.1    Granger, N.A.2    Roe, R.M.3
  • 35
    • 0015849224 scopus 로고
    • Mammalian epoxide hydrases: Inducible enzymes catalysing the inactivation of carcinogenic and cytotoxic metabolites derived from aromatic and olefinic compounds
    • Oesch F, Mammalian epoxide hydrases: inducible enzymes catalysing the inactivation of carcinogenic and cytotoxic metabolites derived from aromatic and olefinic compounds. Xenobiotica 3:305-340 (1973).
    • (1973) Xenobiotica , vol.3 , pp. 305-340
    • Oesch, F.1
  • 36
    • 0018095662 scopus 로고
    • Inhibition of epoxidation of methyl farnesoate to juvenile hormone III by cockroach corpus allatum homogenates
    • Hammock BD and Mumby SM, Inhibition of epoxidation of methyl farnesoate to juvenile hormone III by cockroach corpus allatum homogenates. Pestic Biochem Physiol 9:39-47 (1978).
    • (1978) Pestic Biochem Physiol , vol.9 , pp. 39-47
    • Hammock, B.D.1    Mumby, S.M.2
  • 37
    • 0015851844 scopus 로고
    • Juvenile hormone analogs: A possible case of mistaken identity?
    • Slade M and Wilkinson CF, Juvenile hormone analogs: a possible case of mistaken identity? Science (Washington) 181:672-674 (1973).
    • (1973) Science (Washington) , vol.181 , pp. 672-674
    • Slade, M.1    Wilkinson, C.F.2
  • 38
    • 0016383145 scopus 로고
    • Letter: Juvenile hormone synergists: a possible case of hasty conclusion?
    • Solomon KR and Walker WF, Letter: juvenile hormone synergists: a possible case of hasty conclusion? Science (Washington) 185:461-462 (1974).
    • (1974) Science (Washington) , vol.185 , pp. 461-462
    • Solomon, K.R.1    Walker, W.F.2
  • 39
    • 0010444789 scopus 로고
    • Purification of an epoxide hydrolase from the midgut of the southern armyworm (Spodoptera eridania)
    • Mullin CA and Wilkinson CF, Purification of an epoxide hydrolase from the midgut of the southern armyworm (Spodoptera eridania). Insect Biochem 10:681-691 (1980).
    • (1980) Insect Biochem , vol.10 , pp. 681-691
    • Mullin, C.A.1    Wilkinson, C.F.2
  • 40
    • 0019293791 scopus 로고
    • Insect epoxide hydrolase: Properties of a purified enzyme from the southern armyworm (Spodoptera eridania)
    • Mullin CA and Wilkinson CF, Insect epoxide hydrolase: properties of a purified enzyme from the southern armyworm (Spodoptera eridania). Pestic Biochem Physiol 14:192-207 (1980).
    • (1980) Pestic Biochem Physiol , vol.14 , pp. 192-207
    • Mullin, C.A.1    Wilkinson, C.F.2
  • 41
    • 0019295464 scopus 로고
    • Comparative inhibition of the juvenile hormone esterases from Trichoplusia ni, Tenebrio molitor and Musca domestica
    • Sparks TC and Hammock BD, Comparative inhibition of the juvenile hormone esterases from Trichoplusia ni, Tenebrio molitor and Musca domestica. Pestic Biochem Physiol 14:290-302 (1980).
    • (1980) Pestic Biochem Physiol , vol.14 , pp. 290-302
    • Sparks, T.C.1    Hammock, B.D.2
  • 42
    • 0022495652 scopus 로고
    • Transition state analogs as ligands for affinity purification of juvenile hormone esterase
    • Abdel-Aal YAI and Hammock BD, Transition state analogs as ligands for affinity purification of juvenile hormone esterase. Science (Washington) 233:1073-1076 (1986).
    • (1986) Science (Washington) , vol.233 , pp. 1073-1076
    • Abdel-Aal, Y.A.I.1    Hammock, B.D.2
  • 43
    • 0025307972 scopus 로고
    • Expression and effects of the juvenile hormone esterase in a baculovirus vector
    • Hammock BD, Bonning BC, Possee RD, Hanzlik TN and Maeda S, Expression and effects of the juvenile hormone esterase in a baculovirus vector. Nature (London) 344:458-461 (1990).
    • (1990) Nature (London) , vol.344 , pp. 458-461
    • Hammock, B.D.1    Bonning, B.C.2    Possee, R.D.3    Hanzlik, T.N.4    Maeda, S.5
  • 44
    • 23844470194 scopus 로고    scopus 로고
    • Precocious metamorphosis in transgenic silkworms overexpressing juvenile hormone esterase
    • Tan A, Tanaka H, Tamura T and Shiotsuki T, Precocious metamorphosis in transgenic silkworms overexpressing juvenile hormone esterase. Proc Natl Acad Sci USA 102:11751-11756 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11751-11756
    • Tan, A.1    Tanaka, H.2    Tamura, T.3    Shiotsuki, T.4
  • 45
    • 0027145512 scopus 로고
    • Juvenile hormone catabolism in Manduca sexta: Homologue selectivity of catabolism and identification of a diolphosphate conjugate as a major end product
    • Halarnkar PP, Jackson GP, Straub KM and Schooley DA, Juvenile hormone catabolism in Manduca sexta: homologue selectivity of catabolism and identification of a diolphosphate conjugate as a major end product. Cell Mol Life Sci 49:988-994 (1993).
    • (1993) Cell Mol Life Sci , vol.49 , pp. 988-994
    • Halarnkar, P.P.1    Jackson, G.P.2    Straub, K.M.3    Schooley, D.A.4
  • 46
    • 33745241666 scopus 로고    scopus 로고
    • Role of juvenile hormone esterase and epoxide hydrolase in reproduction of the cotton bollworm, Helicoverpa zea
    • Khalil SMS, Anspaugh DD and Roe RM, Role of juvenile hormone esterase and epoxide hydrolase in reproduction of the cotton bollworm, Helicoverpa zea. J Insect Physiol 52:669-678 (2006).
    • (2006) J Insect Physiol , vol.52 , pp. 669-678
    • Khalil, S.M.S.1    Anspaugh, D.D.2    Roe, R.M.3
  • 47
    • 0020406326 scopus 로고
    • Chalcone oxides - potent selective inhibitors of cytosolic epoxide hydrolase
    • Mullin CA and Hammock BD, Chalcone oxides - potent selective inhibitors of cytosolic epoxide hydrolase. Arch Biochem Biophys 216:423-439 (1982).
    • (1982) Arch Biochem Biophys , vol.216 , pp. 423-439
    • Mullin, C.A.1    Hammock, B.D.2
  • 48
    • 0025820693 scopus 로고
    • Inhibition of cytosolic epoxide hydrolase by trans-3-phenylglycidols
    • Dietze EC, Kuwano E, Casas J and Hammock BD, Inhibition of cytosolic epoxide hydrolase by trans-3-phenylglycidols. Biochem Pharmacol 42:1163-1175 (1991).
    • (1991) Biochem Pharmacol , vol.42 , pp. 1163-1175
    • Dietze, E.C.1    Kuwano, E.2    Casas, J.3    Hammock, B.D.4
  • 49
    • 0027479886 scopus 로고
    • Inhibition of epoxide hydrolase from human, monkey, bovine, rabbit, and murine liver by trans-3-phenylglycidols
    • Dietze EC, Casas J, Kuwano E and Hammock BD, Inhibition of epoxide hydrolase from human, monkey, bovine, rabbit, and murine liver by trans-3-phenylglycidols. Comp Biochem Physiol 104B:309-314 (1993).
    • (1993) Comp Biochem Physiol , vol.104 B , pp. 309-314
    • Dietze, E.C.1    Casas, J.2    Kuwano, E.3    Hammock, B.D.4
  • 50
    • 0033889626 scopus 로고    scopus 로고
    • Inhibition of insect juvenile hormone epoxide hydrolase: Asymmetric synthesis and assay of glycidol-ester and epoxyester inhibitors of Trichoplusia ni epoxide hydrolase
    • Linderman RJ, Roe RM, Harris SV and Thompson DM, Inhibition of insect juvenile hormone epoxide hydrolase: asymmetric synthesis and assay of glycidol-ester and epoxyester inhibitors of Trichoplusia ni epoxide hydrolase. Insect Biochem Mol Biol 30:767-774 (2000).
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 767-774
    • Linderman, R.J.1    Roe, R.M.2    Harris, S.V.3    Thompson, D.M.4
  • 51
    • 0027304431 scopus 로고
    • Juvenile hormone epoxide hydrolase. Photoaffinity labeling, purification, and characterization from tobacco hornworm eggs
    • Touhara K and Prestwich GD, Juvenile hormone epoxide hydrolase. Photoaffinity labeling, purification, and characterization from tobacco hornworm eggs. J Biol Chem 268:19604-19609 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 19604-19609
    • Touhara, K.1    Prestwich, G.D.2
  • 52
    • 0032078466 scopus 로고    scopus 로고
    • Expression and characterization of the recombinant juvenile hormone epoxide hydrolase (JHEH) from Manduca sexta
    • Debernard S, Morisseau C, Severson TF, Feng L, Wojtasek H, Prestwich GD et al, Expression and characterization of the recombinant juvenile hormone epoxide hydrolase (JHEH) from Manduca sexta. Insect Biochem Mol Biol 28:409-419 (1998).
    • (1998) Insect Biochem Mol Biol , vol.28 , pp. 409-419
    • Debernard, S.1    Morisseau, C.2    Severson, T.F.3    Feng, L.4    Wojtasek, H.5    Prestwich, G.D.6
  • 53
    • 12544254506 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of juvenile hormone epoxide hydrolase from the silkworm, Bombyx mori
    • Zhang QR, Xu WH, Chen FS and Li S, Molecular and biochemical characterization of juvenile hormone epoxide hydrolase from the silkworm, Bombyx mori. Insect Biochem Mol Biol 35:153-164 (2005).
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 153-164
    • Zhang, Q.R.1    Xu, W.H.2    Chen, F.S.3    Li, S.4
  • 55
    • 0039915284 scopus 로고    scopus 로고
    • Cloning and expression of a novel juvenile hormone-metabolizing epoxide hydrolase during larval-pupal metamorphosis of the cabbage looper, Trichoplusia ni
    • VanHook Harris S, Marin Thompson D, Linderman RJ, Tomalski MD and Roe RM, Cloning and expression of a novel juvenile hormone-metabolizing epoxide hydrolase during larval-pupal metamorphosis of the cabbage looper, Trichoplusia ni. Insect Mol Biol 8:85-96 (1999).
    • (1999) Insect Mol Biol , vol.8 , pp. 85-96
    • VanHook Harris, S.1    Marin Thompson, D.2    Linderman, R.J.3    Tomalski, M.D.4    Roe, R.M.5
  • 56
    • 0036673062 scopus 로고    scopus 로고
    • Cloning, partial purification and in vivo developmental profile of expression of the juvenile hormone epoxide hydrolase of Ctenocephalides felis
    • Keiser KC, Brandt KS, Silver GM and Wisnewski N, Cloning, partial purification and in vivo developmental profile of expression of the juvenile hormone epoxide hydrolase of Ctenocephalides felis. Arch Insect Biochem Physiol 50:191-206 (2002).
    • (2002) Arch Insect Biochem Physiol , vol.50 , pp. 191-206
    • Keiser, K.C.1    Brandt, K.S.2    Silver, G.M.3    Wisnewski, N.4
  • 57
    • 0036891429 scopus 로고    scopus 로고
    • Urea and amide-based inhibitors of the juvenile hormone epoxide hydrolase of the tobacco hornworm (Manduca sexta: Sphingidae)
    • Severson TF, Goodrow MH, Morisseau C, Dowdy DL and Hammock BD, Urea and amide-based inhibitors of the juvenile hormone epoxide hydrolase of the tobacco hornworm (Manduca sexta: Sphingidae). Insect Biochem Mol Biol 32:1741-1756 (2002).
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1741-1756
    • Severson, T.F.1    Goodrow, M.H.2    Morisseau, C.3    Dowdy, D.L.4    Hammock, B.D.5
  • 60
    • 0034036007 scopus 로고    scopus 로고
    • Insect parapheromones in olfaction: Research and semiochemical-based pest control strategies
    • Renou M and Guerrero A, Insect parapheromones in olfaction: research and semiochemical-based pest control strategies. Annu Rev Entomol 48:605-630 (2000).
    • (2000) Annu Rev Entomol , vol.48 , pp. 605-630
    • Renou, M.1    Guerrero, A.2
  • 61
    • 0036099923 scopus 로고    scopus 로고
    • Insect pheromone olfaction: New targets for the design of species selective pest control agents
    • Plettner E, Insect pheromone olfaction: new targets for the design of species selective pest control agents. Curr Med Chem 9:1075-1085 (2002).
    • (2002) Curr Med Chem , vol.9 , pp. 1075-1085
    • Plettner, E.1
  • 62
    • 0000878597 scopus 로고
    • Synthesis and inhibitory properties of pheromone analogues for the epoxide hydrolase of gypsy moth
    • Graham SM and Prestwich GD, Synthesis and inhibitory properties of pheromone analogues for the epoxide hydrolase of gypsy moth. J Org Chemistry 59:295-296 (1994).
    • (1994) J Org Chemistry , vol.59 , pp. 295-296
    • Graham, S.M.1    Prestwich, G.D.2
  • 63
    • 0031720849 scopus 로고    scopus 로고
    • Xenobiotic-metabolizing enzymes in pig nasal and hepatic tissues
    • Marini S, Xenobiotic-metabolizing enzymes in pig nasal and hepatic tissues. Xenobiotica 28:923-935 (1998).
    • (1998) Xenobiotica , vol.28 , pp. 923-935
    • Marini, S.1
  • 64
    • 14644429730 scopus 로고    scopus 로고
    • Epoxide hydrolases: Their roles and interactions with lipid metabolism
    • Newman JW, Morisseau C and Hammock BD, Epoxide hydrolases: their roles and interactions with lipid metabolism. Prog Lipid Res 44:1-51 (2005).
    • (2005) Prog Lipid Res , vol.44 , pp. 1-51
    • Newman, J.W.1    Morisseau, C.2    Hammock, B.D.3
  • 65
    • 0001564040 scopus 로고    scopus 로고
    • Epoxide hydrolases
    • ed. by Sipes I, McQueen C and Gandolfi A. Pergamon Press, Oxford, UK, pp
    • Hammock BD, Grant D and Storms D, Epoxide hydrolases, in Comprehensive Toxicology, ed. by Sipes I, McQueen C and Gandolfi A. Pergamon Press, Oxford, UK, pp. 283-305 (1997).
    • (1997) Comprehensive Toxicology , pp. 283-305
    • Hammock, B.D.1    Grant, D.2    Storms, D.3
  • 66
    • 0002802789 scopus 로고
    • Membrane-bound and soluble-fraction epoxide hydrolases: Methodological aspects
    • ed. by Zakim D and Vessey DA. John Wiley & Sons, Inc, New York, NY, pp
    • Wixtrom RN and Hammock BD, Membrane-bound and soluble-fraction epoxide hydrolases: methodological aspects, in Biochemical Pharmacology and Toxicology. Vol. 1, ed. by Zakim D and Vessey DA. John Wiley & Sons, Inc., New York, NY, pp 1-93 (1985).
    • (1985) Biochemical Pharmacology and Toxicology , vol.1 , pp. 1-93
    • Wixtrom, R.N.1    Hammock, B.D.2
  • 67
    • 0019642601 scopus 로고
    • Metabolism of epoxidized phosphatidylcholine by phospholipase A2 and epoxide hydrolase
    • Sevanian A, Stein RA and Mead JF, Metabolism of epoxidized phosphatidylcholine by phospholipase A2 and epoxide hydrolase. Lipids 16:781-789 (1981).
    • (1981) Lipids , vol.16 , pp. 781-789
    • Sevanian, A.1    Stein, R.A.2    Mead, J.F.3
  • 68
    • 13844316739 scopus 로고    scopus 로고
    • Epoxide hydrolases: Mechanisms, inhibitor designs, and biological roles
    • Morisseau C and Hammock BD, Epoxide hydrolases: mechanisms, inhibitor designs, and biological roles. Annu Rev Pharmacol Toxicol 45:311-333 (2005).
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 311-333
    • Morisseau, C.1    Hammock, B.D.2
  • 70
    • 0022508532 scopus 로고
    • Activation of benzo[a]pyrene and aflatoxin B1 to mutagenic chemical species by microsomal preparations from rat liver and small intestine in relation to microsomal epoxide hydrolase
    • Walters JM and Combes RD, Activation of benzo[a]pyrene and aflatoxin B1 to mutagenic chemical species by microsomal preparations from rat liver and small intestine in relation to microsomal epoxide hydrolase. Mutagenesis 1:45-48 (1986).
    • (1986) Mutagenesis , vol.1 , pp. 45-48
    • Walters, J.M.1    Combes, R.D.2
  • 71
    • 0015215847 scopus 로고
    • Mutagenicity of epoxides of polycyclic hydrocarbons correlates with carcinogenicity of parent hydrocarbons
    • Cookson MJ, Sims P and Grover PL, Mutagenicity of epoxides of polycyclic hydrocarbons correlates with carcinogenicity of parent hydrocarbons. Nat New Biol 234:186-187 (1971).
    • (1971) Nat New Biol , vol.234 , pp. 186-187
    • Cookson, M.J.1    Sims, P.2    Grover, P.L.3
  • 72
    • 0342840693 scopus 로고
    • An enzyme catalyzing the conjugation of epoxides with glutathione
    • Boyland E and Williams K, An enzyme catalyzing the conjugation of epoxides with glutathione. Biochem J 94:190-197 (1965).
    • (1965) Biochem J , vol.94 , pp. 190-197
    • Boyland, E.1    Williams, K.2
  • 73
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong RN, Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 10:2-18 (1997).
    • (1997) Chem Res Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 74
    • 0342327333 scopus 로고    scopus 로고
    • The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics
    • Siedegård J and Ekström G, The role of human glutathione transferases and epoxide hydrolases in the metabolism of xenobiotics. Environ Health Perspect 105:791-799 (1997).
    • (1997) Environ Health Perspect , vol.105 , pp. 791-799
    • Siedegård, J.1    Ekström, G.2
  • 75
    • 0030767139 scopus 로고    scopus 로고
    • Evidence for quinone metabolites of naphthalene covalently bound to sulfur nucleophiles of proteins of mouse Clara cell after exposure to naphthalene
    • Zheng J, Cho M, Brennan P, Chichester C, Buckpitt AR, Jones AD et al, Evidence for quinone metabolites of naphthalene covalently bound to sulfur nucleophiles of proteins of mouse Clara cell after exposure to naphthalene. Chem Res Toxicol 10:1008-1014 (1997).
    • (1997) Chem Res Toxicol , vol.10 , pp. 1008-1014
    • Zheng, J.1    Cho, M.2    Brennan, P.3    Chichester, C.4    Buckpitt, A.R.5    Jones, A.D.6
  • 76
    • 0033013364 scopus 로고    scopus 로고
    • Anticonvulsant hypersensitivity syndrome with an epoxide hydrolase defect
    • Yoo JH, Kang DS, Chun WH, Lee WJ and Lee AK, Anticonvulsant hypersensitivity syndrome with an epoxide hydrolase defect. Br J Dermatol 140:181-183 (1999).
    • (1999) Br J Dermatol , vol.140 , pp. 181-183
    • Yoo, J.H.1    Kang, D.S.2    Chun, W.H.3    Lee, W.J.4    Lee, A.K.5
  • 77
    • 0031910204 scopus 로고    scopus 로고
    • DNA adducts formation by polycyclic aromatic hydrocarbon dihydrodiol epoxides
    • Szeliga J and Dipple A, DNA adducts formation by polycyclic aromatic hydrocarbon dihydrodiol epoxides. Chem Res Toxicol 11:1-11 (1998).
    • (1998) Chem Res Toxicol , vol.11 , pp. 1-11
    • Szeliga, J.1    Dipple, A.2
  • 78
    • 0033588227 scopus 로고    scopus 로고
    • Targeted disruption of the microsomal epoxide hydrolase gene: Microsomal epoxide hydrolase is required for the carcinogenic activity of 7,12-dimethylbenz[α]anthracene
    • Miyata M, Kudo G, Lee YH, Yang TJ, Gelboin HV, Fernandez-Salguero P et al, Targeted disruption of the microsomal epoxide hydrolase gene: microsomal epoxide hydrolase is required for the carcinogenic activity of 7,12-dimethylbenz[α]anthracene. J Biol Chem 274:23963-23968 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 23963-23968
    • Miyata, M.1    Kudo, G.2    Lee, Y.H.3    Yang, T.J.4    Gelboin, H.V.5    Fernandez-Salguero, P.6
  • 79
    • 0141676333 scopus 로고    scopus 로고
    • Cell surface expression and bile acid transport function of one topological form of m-epoxide hydrolase
    • von Dippe P, Zhu QS and Levy D, Cell surface expression and bile acid transport function of one topological form of m-epoxide hydrolase. Biochem Biophys Res Commun 309:804-809 (2003).
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 804-809
    • von Dippe, P.1    Zhu, Q.S.2    Levy, D.3
  • 80
    • 0015235683 scopus 로고
    • Hepatic epoxide hydrase. Structure-activity relationships for substrates and inhibitors
    • Oesch F, Kaubisch N, Jerina DM and Daly JW, Hepatic epoxide hydrase. Structure-activity relationships for substrates and inhibitors. Biochemistry 10:4858-4866 (1971).
    • (1971) Biochemistry , vol.10 , pp. 4858-4866
    • Oesch, F.1    Kaubisch, N.2    Jerina, D.M.3    Daly, J.W.4
  • 81
    • 0015595054 scopus 로고
    • Induction, activation and inhibition of epoxide hydrase: An anomalous prevention of chlorobenzene-induced hepatotoxicity by an inhibitor of epoxide hydrase
    • Oesch F, Jerina DM, Daly JW and Rice JM, Induction, activation and inhibition of epoxide hydrase: an anomalous prevention of chlorobenzene-induced hepatotoxicity by an inhibitor of epoxide hydrase. Chem Biol Interact 6:189-202 (1973).
    • (1973) Chem Biol Interact , vol.6 , pp. 189-202
    • Oesch, F.1    Jerina, D.M.2    Daly, J.W.3    Rice, J.M.4
  • 82
    • 0024347786 scopus 로고
    • Inhibition of human liver microsomal epoxide hydrolase by valproate and valpromide: In vitro/in vivo correlation
    • Kerr BM, Rettie AE, Eddy AC, Loiseau P, Guyot M, Wilensky AJ et al, Inhibition of human liver microsomal epoxide hydrolase by valproate and valpromide: in vitro/in vivo correlation. Clin Pharmacol Ther 46:82-93 (1989).
    • (1989) Clin Pharmacol Ther , vol.46 , pp. 82-93
    • Kerr, B.M.1    Rettie, A.E.2    Eddy, A.C.3    Loiseau, P.4    Guyot, M.5    Wilensky, A.J.6
  • 83
    • 0027440418 scopus 로고
    • In vivo and in vitro correlation of microsomal epoxide hydrolase inhibition by progabide
    • Kroetz DL, Loiseau P, Guyot M and Levy RH, In vivo and in vitro correlation of microsomal epoxide hydrolase inhibition by progabide. Clin Pharmacol Ther 54:485-497 (1993).
    • (1993) Clin Pharmacol Ther , vol.54 , pp. 485-497
    • Kroetz, D.L.1    Loiseau, P.2    Guyot, M.3    Levy, R.H.4
  • 84
    • 0029815563 scopus 로고    scopus 로고
    • Clinically significant pharmacokinetic drug interactions with carbamazepine. An update
    • Spina E, Pisani F and Perucca E, Clinically significant pharmacokinetic drug interactions with carbamazepine. An update. Clin Pharmacokinet 31:198-214 (1996).
    • (1996) Clin Pharmacokinet , vol.31 , pp. 198-214
    • Spina, E.1    Pisani, F.2    Perucca, E.3
  • 85
    • 0025375550 scopus 로고
    • Unsubstituted amides: New class of potent inhibitors of human microsomal epoxide hydrolase
    • Kerr BM and Levy RH, Unsubstituted amides: new class of potent inhibitors of human microsomal epoxide hydrolase. Drug Metab Dispos 18:540-542 (1990).
    • (1990) Drug Metab Dispos , vol.18 , pp. 540-542
    • Kerr, B.M.1    Levy, R.H.2
  • 86
    • 18144370442 scopus 로고    scopus 로고
    • Variability in human sensitivity to 1,3-butadiene: Influence of polymorphisms in the 5′-flanking region of the microsomal epoxide hydrolase gene (EPHX1)
    • Abdel-Rahman SZ, Ammenheuser MM, Omiecinski CJ, Wickliffe JK, Rosenblatt JI and Ward JB, Variability in human sensitivity to 1,3-butadiene: influence of polymorphisms in the 5′-flanking region of the microsomal epoxide hydrolase gene (EPHX1). Toxicol Sci 85:624-631 (2005).
    • (2005) Toxicol Sci , vol.85 , pp. 624-631
    • Abdel-Rahman, S.Z.1    Ammenheuser, M.M.2    Omiecinski, C.J.3    Wickliffe, J.K.4    Rosenblatt, J.I.5    Ward, J.B.6
  • 87
    • 0023252403 scopus 로고
    • Comparative effects of butylated hydroxyanisole on hepatic in vivo DNA binding and in vitro biotransformation of aflatoxin B1 in the rat and mouse
    • Monroe DH and Eaton DL, Comparative effects of butylated hydroxyanisole on hepatic in vivo DNA binding and in vitro biotransformation of aflatoxin B1 in the rat and mouse. Toxicol Appl Pharmacol 90:401-409 (1987).
    • (1987) Toxicol Appl Pharmacol , vol.90 , pp. 401-409
    • Monroe, D.H.1    Eaton, D.L.2
  • 88
    • 34249792074 scopus 로고    scopus 로고
    • Characterization of resistance to bromobenzene-induced hepatotoxicity by microarray
    • Tanaka K, Kiyosawa N, Watanabe K and Manabe S, Characterization of resistance to bromobenzene-induced hepatotoxicity by microarray. J Toxicol Sci 32:129-134 (2007).
    • (2007) J Toxicol Sci , vol.32 , pp. 129-134
    • Tanaka, K.1    Kiyosawa, N.2    Watanabe, K.3    Manabe, S.4
  • 89
    • 0037389711 scopus 로고    scopus 로고
    • Male mice deficient in microsomal epoxide hydrolase are not susceptible to benzene-induced toxicity
    • Bauer AK, Faiola B, Abernethy DJ, Marchan R, Pluta LJ, Wong VA et al, Male mice deficient in microsomal epoxide hydrolase are not susceptible to benzene-induced toxicity. Toxicol Sci 72:201-209 (2003).
    • (2003) Toxicol Sci , vol.72 , pp. 201-209
    • Bauer, A.K.1    Faiola, B.2    Abernethy, D.J.3    Marchan, R.4    Pluta, L.J.5    Wong, V.A.6
  • 90
    • 0016243499 scopus 로고
    • Mammalian metabolism and environmental degradation of the juvenoid 1-(4′-ethylphenoxy)-3,7-dimethyl-6,7- epoxy-trans-2-octene and related compounds
    • Gill SS, Hammock BD and Casida JE, Mammalian metabolism and environmental degradation of the juvenoid 1-(4′-ethylphenoxy)-3,7-dimethyl-6,7- epoxy-trans-2-octene and related compounds. J Ag Food Chem 22:386-395 (1974).
    • (1974) J Ag Food Chem , vol.22 , pp. 386-395
    • Gill, S.S.1    Hammock, B.D.2    Casida, J.E.3
  • 91
    • 0017282880 scopus 로고
    • Soluble mammalian epoxide hydratase: Action on juvenile hormone and other terpenoid epoxides
    • Hammock BD, Gill SS, Stamoudis V and Gilbert LI, Soluble mammalian epoxide hydratase: action on juvenile hormone and other terpenoid epoxides. Comp Biochem Physiol 53B:263-265 (1976).
    • (1976) Comp Biochem Physiol , vol.53 B , pp. 263-265
    • Hammock, B.D.1    Gill, S.S.2    Stamoudis, V.3    Gilbert, L.I.4
  • 92
    • 39449131531 scopus 로고
    • Comparison of epoxide hydrases in the soluble and microsomal fractions of mammalian liver
    • ed. by Bhatnagar RS. Ann Arbor Science Publishers, Ann Arbor, MI, pp
    • Hammock BD, Gill SS, Mumby SM and Ota K, Comparison of epoxide hydrases in the soluble and microsomal fractions of mammalian liver, in Molecular Basis of Environmental Toxicity, ed. by Bhatnagar RS. Ann Arbor Science Publishers, Ann Arbor, MI, pp. 229-272 (1980).
    • (1980) Molecular Basis of Environmental Toxicity , pp. 229-272
    • Hammock, B.D.1    Gill, S.S.2    Mumby, S.M.3    Ota, K.4
  • 93
    • 0018857823 scopus 로고
    • Distribution and properties of a mammalian soluble epoxide hydrase
    • Gill S and Hammock BD, Distribution and properties of a mammalian soluble epoxide hydrase. Biochem Pharmacol 29:389-395 (1980).
    • (1980) Biochem Pharmacol , vol.29 , pp. 389-395
    • Gill, S.1    Hammock, B.D.2
  • 94
    • 0018832988 scopus 로고
    • Cytosolic and microsomal epoxide hydrolases: Differential properties in mammalian liver
    • Ota K and Hammock BD, Cytosolic and microsomal epoxide hydrolases: differential properties in mammalian liver. Science (Washington) 207:1479-1481 (1980).
    • (1980) Science (Washington) , vol.207 , pp. 1479-1481
    • Ota, K.1    Hammock, B.D.2
  • 96
    • 0001185242 scopus 로고
    • On the conversion of squalene to lanosterol in vitro
    • Tchen TT and Bloch K, On the conversion of squalene to lanosterol in vitro. J Biol Chem 226:921-930 (1957).
    • (1957) J Biol Chem , vol.226 , pp. 921-930
    • Tchen, T.T.1    Bloch, K.2
  • 97
    • 0000041673 scopus 로고    scopus 로고
    • Corey EJ, Lin K and Jautelat M, Studies on the action of 2,3-epoxysqualene-sterol cyclase on unnatural substrates produced by alkylidene transfer from sulfonium alkylides to 4,8,13,17,21-pentamethyldocosa-4,8,12,16, 20-pentaenal. J Am Chem Soc 90:2724-2726 (1968).
    • Corey EJ, Lin K and Jautelat M, Studies on the action of 2,3-epoxysqualene-sterol cyclase on unnatural substrates produced by alkylidene transfer from sulfonium alkylides to 4,8,13,17,21-pentamethyldocosa-4,8,12,16, 20-pentaenal. J Am Chem Soc 90:2724-2726 (1968).
  • 99
    • 0018424829 scopus 로고
    • Substrate selectivity and stereochemistry of enzymatic epoxide hydration in the soluble fraction of mouse liver
    • Mumby SM and Hammock BD, Substrate selectivity and stereochemistry of enzymatic epoxide hydration in the soluble fraction of mouse liver. Pestic Biochem Physiol 11:275-284 (1979).
    • (1979) Pestic Biochem Physiol , vol.11 , pp. 275-284
    • Mumby, S.M.1    Hammock, B.D.2
  • 101
    • 0345420607 scopus 로고
    • Peroxisomal proliferation and subcellular localization of soluble epoxide hydrolase: Role of peroxisomal targeting sequences
    • ed. by Moody DE. CRC Press, Inc, Boca Raton, FL, pp
    • Gill SJ, Grant DF, Beetham JK, Chang C and Hammock BD, Peroxisomal proliferation and subcellular localization of soluble epoxide hydrolase: role of peroxisomal targeting sequences, in Peroxisome Proliferators: Unique Inducers of Drug-Metabolizing Enzymes, ed. by Moody DE. CRC Press, Inc., Boca Raton, FL, pp. 113-121 (1994).
    • (1994) Peroxisome Proliferators: Unique Inducers of Drug-Metabolizing Enzymes , pp. 113-121
    • Gill, S.J.1    Grant, D.F.2    Beetham, J.K.3    Chang, C.4    Hammock, B.D.5
  • 102
    • 33344460020 scopus 로고    scopus 로고
    • Cell-specific subcellular localization of soluble epoxide hydrolase inhuman tissues
    • Enayetallah AE, French RA, Barber M and Grant DF, Cell-specific subcellular localization of soluble epoxide hydrolase inhuman tissues. J Histochem Cytochem 54:329-335 (2006).
    • (2006) J Histochem Cytochem , vol.54 , pp. 329-335
    • Enayetallah, A.E.1    French, R.A.2    Barber, M.3    Grant, D.F.4
  • 103
    • 15544383250 scopus 로고    scopus 로고
    • Identification and characterization of an ovary-selective isoform of epoxide hydrolase
    • Hennebold JD, Mah K, Perez W, Vance JE, Stouffer RL, Morisseau C et al, Identification and characterization of an ovary-selective isoform of epoxide hydrolase. Biol Reprod 72:968-975 (2005).
    • (2005) Biol Reprod , vol.72 , pp. 968-975
    • Hennebold, J.D.1    Mah, K.2    Perez, W.3    Vance, J.E.4    Stouffer, R.L.5    Morisseau, C.6
  • 104
    • 0021073537 scopus 로고
    • Differential induction of cytosolic epoxide hydrolase, microsomal epoxide hydrolase, and glutathione S-transferase activities
    • Hammock BD and Ota K, Differential induction of cytosolic epoxide hydrolase, microsomal epoxide hydrolase, and glutathione S-transferase activities. Toxicol App Pharmacol 71:254-265 (1983).
    • (1983) Toxicol App Pharmacol , vol.71 , pp. 254-265
    • Hammock, B.D.1    Ota, K.2
  • 106
    • 34547468357 scopus 로고    scopus 로고
    • Angiotensin II up-regulates soluble epoxide hydrolase in vascular endothelium in vitro and in vivo
    • Ai D, Fu Y, Guo D, Tanaka H, Wang N, Tang C et al, Angiotensin II up-regulates soluble epoxide hydrolase in vascular endothelium in vitro and in vivo. Proc Natl Acad Sci USA 104:9018-9023 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 9018-9023
    • Ai, D.1    Fu, Y.2    Guo, D.3    Tanaka, H.4    Wang, N.5    Tang, C.6
  • 107
    • 0018424829 scopus 로고
    • Substrate selectivity and stereochemistry of enzymatic epoxide hydration in the soluble fraction of mouse liver
    • Mumby SM and Hammock BD, Substrate selectivity and stereochemistry of enzymatic epoxide hydration in the soluble fraction of mouse liver. Pestic Biochem Physiol 11:275-284 (1979).
    • (1979) Pestic Biochem Physiol , vol.11 , pp. 275-284
    • Mumby, S.M.1    Hammock, B.D.2
  • 108
    • 0018789450 scopus 로고
    • Hydration of cis- and trans-epoxymethyl stearates by the cytosolic epoxide hydrase of mouse liver
    • Gill SS and Hammock BD, Hydration of cis- and trans-epoxymethyl stearates by the cytosolic epoxide hydrase of mouse liver. Biochem Biophys Res Commun 89:965-971 (1979).
    • (1979) Biochem Biophys Res Commun , vol.89 , pp. 965-971
    • Gill, S.S.1    Hammock, B.D.2
  • 109
    • 0024361188 scopus 로고
    • Catabolism of epoxy fatty esters by the purified epoxide hydrolase from mouse and human liver
    • Halarnkar PP, Wixtrom RN, Silva MH and Hammock BD, Catabolism of epoxy fatty esters by the purified epoxide hydrolase from mouse and human liver. Arch Biochem Biophys 272:226-236 (1989).
    • (1989) Arch Biochem Biophys , vol.272 , pp. 226-236
    • Halarnkar, P.P.1    Wixtrom, R.N.2    Silva, M.H.3    Hammock, B.D.4
  • 110
    • 0027512995 scopus 로고
    • Regio- and enantiofacial selectivity of epoxyeicosatrienoic acid hydration by cytosolic epoxide hydrolase
    • Zeldin DC, Kobayashi J, Falck JR, Winder BS, Hammock BD, Snapper JR et al, Regio- and enantiofacial selectivity of epoxyeicosatrienoic acid hydration by cytosolic epoxide hydrolase. J Biol Chem 268:6402-6407 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 6402-6407
    • Zeldin, D.C.1    Kobayashi, J.2    Falck, J.R.3    Winder, B.S.4    Hammock, B.D.5    Snapper, J.R.6
  • 111
    • 33947375240 scopus 로고    scopus 로고
    • Action of epoxyeicosatrienoic acids on cellular function
    • Spector AA and Norris AW, Action of epoxyeicosatrienoic acids on cellular function. Am J Physiol Cell Physiol 292:C996-C1012 (2007).
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Spector, A.A.1    Norris, A.W.2
  • 112
    • 0032529615 scopus 로고    scopus 로고
    • Mechanism of mammalian soluble epoxide hydrolase inhibition by chalcone oxide derivatives
    • Morisseau C, Du G, Newman JW and Hammock BD, Mechanism of mammalian soluble epoxide hydrolase inhibition by chalcone oxide derivatives. Arch Biochem Biophys 356:214-228 (1998).
    • (1998) Arch Biochem Biophys , vol.356 , pp. 214-228
    • Morisseau, C.1    Du, G.2    Newman, J.W.3    Hammock, B.D.4
  • 113
    • 0033798373 scopus 로고    scopus 로고
    • 3-D QSAR analysis of inhibition of murine soluble epoxide hydrolase (MsEH) by benzoylureas, arylureas, and their analogues
    • Nakagawa Y, Wheelock CE, Morisseau C, Goodrow MH, Hammock BG and Hammock BD, 3-D QSAR analysis of inhibition of murine soluble epoxide hydrolase (MsEH) by benzoylureas, arylureas, and their analogues. Bioorg Med Chem 8:2663-2673 (2000).
    • (2000) Bioorg Med Chem , vol.8 , pp. 2663-2673
    • Nakagawa, Y.1    Wheelock, C.E.2    Morisseau, C.3    Goodrow, M.H.4    Hammock, B.G.5    Hammock, B.D.6
  • 115
    • 0034711488 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase regulates hydrolysis of vasoactive epoxyeicosatrienoic acids
    • Yu Z, Xu F, Huse LM, Morisseau C, Draper AJ, Newman JW et al, Soluble epoxide hydrolase regulates hydrolysis of vasoactive epoxyeicosatrienoic acids. Circ Res 87:992-998 (2000).
    • (2000) Circ Res , vol.87 , pp. 992-998
    • Yu, Z.1    Xu, F.2    Huse, L.M.3    Morisseau, C.4    Draper, A.J.5    Newman, J.W.6
  • 117
    • 28044434102 scopus 로고    scopus 로고
    • The anti-inflammatory effect of laminar flow: The role of PPARγ, epoxyeicosatrienoic acids, and soluble epoxide hydrolase
    • Liu Y, Zhang Y, Schmelzer K, Lee TS, Fang X, Zhu Y et al, The anti-inflammatory effect of laminar flow: the role of PPARγ, epoxyeicosatrienoic acids, and soluble epoxide hydrolase. Proc Natl Acad Sci USA 102:16747-16752 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16747-16752
    • Liu, Y.1    Zhang, Y.2    Schmelzer, K.3    Lee, T.S.4    Fang, X.5    Zhu, Y.6
  • 118
    • 33750529521 scopus 로고    scopus 로고
    • Inhibition of soluble epoxide hydrolase reduces LPS-induced thermal hyperalgesia and mechanical allodynia in a rat model of inflammatory pain
    • Inceoglu B, Jinks SL, Schmelzer KR, Waite T, Kim IH and Hammock BD, Inhibition of soluble epoxide hydrolase reduces LPS-induced thermal hyperalgesia and mechanical allodynia in a rat model of inflammatory pain. Life Sci 79:2311-2319 (2006).
    • (2006) Life Sci , vol.79 , pp. 2311-2319
    • Inceoglu, B.1    Jinks, S.L.2    Schmelzer, K.R.3    Waite, T.4    Kim, I.H.5    Hammock, B.D.6
  • 119
    • 33748797975 scopus 로고    scopus 로고
    • Enhancement of antinociception by coadministration of nonsteroidal anti-inflammatory drugs and soluble epoxide hydrolase inhibitors
    • Schmelzer KR, Inceoglu B, Kubala L, Kim IH, Jinks SL, Eiserich JP et al, Enhancement of antinociception by coadministration of nonsteroidal anti-inflammatory drugs and soluble epoxide hydrolase inhibitors. Proc Natl Acad Sci USA 103:13646-13651 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13646-13651
    • Schmelzer, K.R.1    Inceoglu, B.2    Kubala, L.3    Kim, I.H.4    Jinks, S.L.5    Eiserich, J.P.6
  • 120
    • 33845474465 scopus 로고    scopus 로고
    • Prevention and reversal of cardiac hypertrophy by soluble epoxide hydrolase inhibitors
    • Xu D, Li N, He Y, Timofeyev V, Lu L, Tsai HJ et al, Prevention and reversal of cardiac hypertrophy by soluble epoxide hydrolase inhibitors. Proc Natl Acad Sci USA 103:18733-18738 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18733-18738
    • Xu, D.1    Li, N.2    He, Y.3    Timofeyev, V.4    Lu, L.5    Tsai, H.J.6
  • 122
    • 1842555060 scopus 로고    scopus 로고
    • Design, synthesis, and biological activity of 1,3-disubstituted ureas as potent inhibitors of the soluble epoxide hydrolase of increased water solubility
    • Kim IH, Morisseau C, Watanabe T and Hammock BD, Design, synthesis, and biological activity of 1,3-disubstituted ureas as potent inhibitors of the soluble epoxide hydrolase of increased water solubility. J Med Chem 47:110-2122 (2004).
    • (2004) J Med Chem , vol.47 , pp. 110-2122
    • Kim, I.H.1    Morisseau, C.2    Watanabe, T.3    Hammock, B.D.4
  • 123
    • 33747331141 scopus 로고    scopus 로고
    • Synthesis and SAR of conformationally restricted inhibitors of soluble epoxide hydrolase
    • Jones PD, Tsai H-J, Do ZN, Morisseau C and Hammock BD, Synthesis and SAR of conformationally restricted inhibitors of soluble epoxide hydrolase. Bioorg Med Chem Lett 16:5212-5216 (2006).
    • (2006) Bioorg Med Chem Lett , vol.16 , pp. 5212-5216
    • Jones, P.D.1    Tsai, H.-J.2    Do, Z.N.3    Morisseau, C.4    Hammock, B.D.5
  • 124
    • 34548070313 scopus 로고    scopus 로고
    • Orally bioavailable potent soluble epoxide hydrolase (sEH) inhibitors
    • Hwang SH, Tsai H-J, Liu J-Y, Morisseau C and Hammock BD, Orally bioavailable potent soluble epoxide hydrolase (sEH) inhibitors. J Med Chem 50:3825-3840 (2007).
    • (2007) J Med Chem , vol.50 , pp. 3825-3840
    • Hwang, S.H.1    Tsai, H.-J.2    Liu, J.-Y.3    Morisseau, C.4    Hammock, B.D.5
  • 126
    • 0032170424 scopus 로고    scopus 로고
    • Characterization of a tobacco epoxide hydrolase gene induced during the resistance response to TMV
    • Guo A, Durner J and Klessig DF, Characterization of a tobacco epoxide hydrolase gene induced during the resistance response to TMV. Plant J 15:647-656 (1998).
    • (1998) Plant J , vol.15 , pp. 647-656
    • Guo, A.1    Durner, J.2    Klessig, D.F.3
  • 127
    • 0016753292 scopus 로고
    • Biosynthesis of hydroxy fatty acid polymers. Enzymatic hydration of 18-hydroxy-cis-9,10-epoxystearic acid to threo-9,10,18-trihydroxystearic acid by a particulate preparation from apple (Malus pumila)
    • Croteau R and Kolattukudy PE, Biosynthesis of hydroxy fatty acid polymers. Enzymatic hydration of 18-hydroxy-cis-9,10-epoxystearic acid to threo-9,10,18-trihydroxystearic acid by a particulate preparation from apple (Malus pumila). Arch Biochem Biophys 170:73-81 (1975).
    • (1975) Arch Biochem Biophys , vol.170 , pp. 73-81
    • Croteau, R.1    Kolattukudy, P.E.2
  • 128
    • 0026574135 scopus 로고
    • Occurrence of fatty acid epoxide hydrolases in soybean (Glycine max)
    • Blée E and Schuber F, Occurrence of fatty acid epoxide hydrolases in soybean (Glycine max). Biochem J 282:711-714 (1992).
    • (1992) Biochem J , vol.282 , pp. 711-714
    • Blée, E.1    Schuber, F.2
  • 129
    • 0028485440 scopus 로고
    • Characterization of an Aradibopsis cDNA for a soluble epoxide hydrolase gene that is inducible by auxin and water stress
    • Kiyosue T, Beetham JK, Pinot F, Hammock BD, Yamaguchi-Shinozaki K and Shinozaki K, Characterization of an Aradibopsis cDNA for a soluble epoxide hydrolase gene that is inducible by auxin and water stress. Plant J 6:259-269 (1994).
    • (1994) Plant J , vol.6 , pp. 259-269
    • Kiyosue, T.1    Beetham, J.K.2    Pinot, F.3    Hammock, B.D.4    Yamaguchi-Shinozaki, K.5    Shinozaki, K.6
  • 130
    • 33846917437 scopus 로고    scopus 로고
    • Effect of ionic liquids on epoxide hydrolase-catalyzed synthesis of chiral 1,2-diols
    • Chiappe C, Leandri E, Hammock BD and Morisseau C, Effect of ionic liquids on epoxide hydrolase-catalyzed synthesis of chiral 1,2-diols. Green Chem 9:162-168 (2007).
    • (2007) Green Chem , vol.9 , pp. 162-168
    • Chiappe, C.1    Leandri, E.2    Hammock, B.D.3    Morisseau, C.4
  • 131
    • 0032924489 scopus 로고    scopus 로고
    • Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene
    • Van der Werf MJ, Swans HJ and Bont JA, Rhodococcus erythropolis DCL14 contains a novel degradation pathway for limonene. Appl Environ Microbiol 65:2095-2102 (1999).
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2095-2102
    • Van der Werf, M.J.1    Swans, H.J.2    Bont, J.A.3
  • 132
    • 0026348175 scopus 로고
    • Characterization of the epoxide hydrolase from epichlorohydrin-degrading Pseudomonas sp
    • Jacobs MHJ, Wijngaard AJ, Pentenga M and Janssen DB, Characterization of the epoxide hydrolase from epichlorohydrin-degrading Pseudomonas sp. Eur J Biochem 202:1217-1222 (1991).
    • (1991) Eur J Biochem , vol.202 , pp. 1217-1222
    • Jacobs, M.H.J.1    Wijngaard, A.J.2    Pentenga, M.3    Janssen, D.B.4
  • 133
    • 33745744218 scopus 로고    scopus 로고
    • Diversity of epoxide hydrolase biocatalysts
    • Smit MS and Labuschagné M, Diversity of epoxide hydrolase biocatalysts. Curr Org Chem 10:1145-1161 (2006).
    • (2006) Curr Org Chem , vol.10 , pp. 1145-1161
    • Smit, M.S.1    Labuschagné, M.2
  • 134
    • 0033565356 scopus 로고    scopus 로고
    • Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger
    • Morisseau C, Archelas A, Guitton C, Faucher D, Furstoss R and Baratti JC, Purification and characterization of a highly enantioselective epoxide hydrolase from Aspergillus niger. Eur J Biochem 263:386-395 (1999).
    • (1999) Eur J Biochem , vol.263 , pp. 386-395
    • Morisseau, C.1    Archelas, A.2    Guitton, C.3    Faucher, D.4    Furstoss, R.5    Baratti, J.C.6
  • 135
    • 0029090931 scopus 로고
    • Isolation of a highly enantioselective epoxide hydrolase from Rhodococcus sp. NCIMB 11216
    • Mischitz M, Faber K and Willetts A, Isolation of a highly enantioselective epoxide hydrolase from Rhodococcus sp. NCIMB 11216. Biotech Lett 17:893-898 (1995).
    • (1995) Biotech Lett , vol.17 , pp. 893-898
    • Mischitz, M.1    Faber, K.2    Willetts, A.3
  • 136
    • 0037863737 scopus 로고    scopus 로고
    • Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site
    • Arand M, Haalberg BM, Zou J, Bergfors T, Oesch F, van der Werf MJ et al, Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site. EMBO J 22:2583-2592 (2003).
    • (2003) EMBO J , vol.22 , pp. 2583-2592
    • Arand, M.1    Haalberg, B.M.2    Zou, J.3    Bergfors, T.4    Oesch, F.5    van der Werf, M.J.6


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