메뉴 건너뛰기




Volumn 38, Issue 3, 2006, Pages 451-476

CYP4B1: An enigmatic P450 at the interface between xenobiotic and endobiotic metabolism

Author keywords

Bioactivation; Cytochrome P450; Gene regulation; Heme; Pharmacogenetics; Structure

Indexed keywords

1 AMINOBENZOTRIAZOLE; 2 AMINOANTHRACENE; 2 FLUORENYLAMINE; 3,3' DICHLOROBENZIDINE; 4 AMINO 3 METHOXYAZOBENZENE; 4 IPOMEANOL; ANTICONVULSIVE AGENT; AROMATIC AMINE; CYTOCHROME P450; CYTOCHROME P450 4B1; CYTOCHROME P450 INHIBITOR; HEME; N (2 FLUORENYL)ACETAMIDE; PROADIFEN; PRODRUG; SKATOLE; VALPROIC ACID; XENOBIOTIC AGENT;

EID: 33746713687     PISSN: 03602532     EISSN: 10979883     Source Type: Journal    
DOI: 10.1080/03602530600688503     Document Type: Review
Times cited : (84)

References (116)
  • 1
    • 0016685233 scopus 로고
    • Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test
    • Ames, B. N., McCann, J., Yamasaki, E. (1975). Methods for detecting carcinogens and mutagens with the Salmonella/mammalian-microsome mutagenicity test. Mutat. Res. 31:347-364.
    • (1975) Mutat. Res. , vol.31 , pp. 347-364
    • Ames, B.N.1    McCann, J.2    Yamasaki, E.3
  • 2
    • 0017116574 scopus 로고
    • Preparation and properties of partially purified pulmonary cytochrome P-450 from rabbits
    • Arinc, E., Philpot, M. (1976). Preparation and properties of partially purified pulmonary cytochrome P-450 from rabbits. J. Biol. Chem. 251:3213-3220.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3213-3220
    • Arinc, E.1    Philpot, M.2
  • 3
    • 1042277989 scopus 로고    scopus 로고
    • Retinoic acid induces corneal epithelial CYP4B1 gene expression and stimulates the synthesis of inflammatory 12-hydroxyeicosanoids
    • Ashkar, S., Mesentsev, A., Zhang, W. X., Mastyugin, V., Dunn, M. W., Laniado-Schwartzman, M. (2004). Retinoic acid induces corneal epithelial CYP4B1 gene expression and stimulates the synthesis of inflammatory 12-hydroxyeicosanoids. J. Ocul. Pharmacol. Ther. 20:65-74.
    • (2004) J. Ocul. Pharmacol. Ther. , vol.20 , pp. 65-74
    • Ashkar, S.1    Mesentsev, A.2    Zhang, W.X.3    Mastyugin, V.4    Dunn, M.W.5    Laniado-Schwartzman, M.6
  • 4
    • 18944393300 scopus 로고    scopus 로고
    • Bioactivation of 4-ipomeanol by CYP4B1: Adduct characterization and evidence for an enedial intermediate
    • Baer, B. R., Rettie, A. E., Henne, K. R. (2005). Bioactivation of 4-ipomeanol by CYP4B1: adduct characterization and evidence for an enedial intermediate. Chem. Res. Toxicol. 18:855-864.
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 855-864
    • Baer, B.R.1    Rettie, A.E.2    Henne, K.R.3
  • 5
    • 0022371070 scopus 로고
    • Immunochemical study on the contribution of hypolipidaemic-induced cytochrome P-452 to the metabolism of lauric acid and arachidonic acid
    • Bains, S. K., Gardiner, S. M., Mannweiler, K., Gillett, D., Gibson, G. G. (1985). Immunochemical study on the contribution of hypolipidaemic-induced cytochrome P-452 to the metabolism of lauric acid and arachidonic acid. Biochem. Pharmacol. 34:3221-3229.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3221-3229
    • Bains, S.K.1    Gardiner, S.M.2    Mannweiler, K.3    Gillett, D.4    Gibson, G.G.5
  • 6
    • 0021245440 scopus 로고
    • Autoradiographic evidence of 3-methylindole covalent binding to pulmonary epithelial cells in the goat
    • Becker, G. M., Breeze, R. G., Carlson, J. R. (1984). Autoradiographic evidence of 3-methylindole covalent binding to pulmonary epithelial cells in the goat. Toxicology 31:109-121.
    • (1984) Toxicology , vol.31 , pp. 109-121
    • Becker, G.M.1    Breeze, R.G.2    Carlson, J.R.3
  • 7
    • 0000037422 scopus 로고
    • Metabolic acitvation and DNA adducts of aromatic amines and nitroaromatic hydrocarbons
    • Couper, C., Grover, P., eds., New York: Springer
    • Beland, F., Kadlubar, F. (1990). Metabolic acitvation and DNA adducts of aromatic amines and nitroaromatic hydrocarbons. In: Couper, C., Grover, P., eds., Chemical Carcinogenesis and Mutagenesis I. New York: Springer, pp. 267-325.
    • (1990) Chemical Carcinogenesis and Mutagenesis I , pp. 267-325
    • Beland, F.1    Kadlubar, F.2
  • 8
    • 0343471998 scopus 로고    scopus 로고
    • Cytochrome P450 hydroxylation of carbon atoms of the alkyl chain of symmetrical N-nitrosodialkylamines by human liver microsomes
    • Bellec, G., Dreano, Y., Bail, J. P., Menez, J. F., Berthou, F. (1997). Cytochrome P450 hydroxylation of carbon atoms of the alkyl chain of symmetrical N-nitrosodialkylamines by human liver microsomes. Mutat. Res. 377:199-209.
    • (1997) Mutat. Res. , vol.377 , pp. 199-209
    • Bellec, G.1    Dreano, Y.2    Bail, J.P.3    Menez, J.F.4    Berthou, F.5
  • 9
    • 0034723274 scopus 로고    scopus 로고
    • Regulation of cyclooxygenase-2 by hypoxia and peroxisome proliferators in the corneal epithelium
    • Bonazzi, A., Mastyugin, V., Mieyal, P. A., Dunn, M. W., Laniado-Schwartzman, M. (2000). Regulation of cyclooxygenase-2 by hypoxia and peroxisome proliferators in the corneal epithelium. J. Biol. Chem. 275:2837-2844.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2837-2844
    • Bonazzi, A.1    Mastyugin, V.2    Mieyal, P.A.3    Dunn, M.W.4    Laniado-Schwartzman, M.5
  • 10
    • 0017741869 scopus 로고
    • Evidence for the Clara cell as a site of cytochrome P450-dependent mixed-unction oxidase activity in lung
    • Boyd, M. R. (1977). Evidence for the Clara cell as a site of cytochrome P450-dependent mixed-unction oxidase activity in lung. Nature 269:713-715.
    • (1977) Nature , vol.269 , pp. 713-715
    • Boyd, M.R.1
  • 11
    • 0019046677 scopus 로고
    • Biochemical mechanisms in chemical-induced lung injury: Roles of metabolic activation
    • Boyd, M. R. (1980). Biochemical mechanisms in chemical-induced lung injury: roles of metabolic activation. Crit. Rev. Toxicol. 7:103-176.
    • (1980) Crit. Rev. Toxicol. , vol.7 , pp. 103-176
    • Boyd, M.R.1
  • 12
    • 0015967889 scopus 로고
    • Lung-toxic furanoterpenoids produced by sweet potatoes (Ipomoea batatas) following microbial infection
    • Boyd, M. R., Burka, L. T., Harris, T. M., Wilson, B. J. (1974). Lung-toxic furanoterpenoids produced by sweet potatoes (Ipomoea batatas) following microbial infection. Biochim. Biophys. Acta. 337:184-195.
    • (1974) Biochim. Biophys. Acta , vol.337 , pp. 184-195
    • Boyd, M.R.1    Burka, L.T.2    Harris, T.M.3    Wilson, B.J.4
  • 13
    • 0033595160 scopus 로고    scopus 로고
    • Gene expression of a novel cytochrome P450 of the CYP4F subfamily in human seminal vesicles
    • Bylund, J., Finnstrom, N., Oliw, E. H. (1999). Gene expression of a novel cytochrome P450 of the CYP4F subfamily in human seminal vesicles. Biochem. Biophys. Res. Commun. 261:169-174.
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 169-174
    • Bylund, J.1    Finnstrom, N.2    Oliw, E.H.3
  • 14
    • 0038644585 scopus 로고    scopus 로고
    • Characterization of pulmonary CYP4B2, specific catalyst of methyl oxidation of 3-methylindole
    • Carr, B. A., Ramakanth, S., Dannan, G. A., Yost, G. S. (2003). Characterization of pulmonary CYP4B2, specific catalyst of methyl oxidation of 3-methylindole. Mol. Pharmacol. 63:1137-1147.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1137-1147
    • Carr, B.A.1    Ramakanth, S.2    Dannan, G.A.3    Yost, G.S.4
  • 15
    • 0030753035 scopus 로고    scopus 로고
    • Characterization of amino acid and glutathione adducts of cis-2-butene-1,4-dial, a reactive metabolite of furan
    • Chen, L. J., Hecht, S. S., Peterson, L. A. (1997). Characterization of amino acid and glutathione adducts of cis-2-butene-1,4-dial, a reactive metabolite of furan. Chem. Res. Toxicol. 10:866-874.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 866-874
    • Chen, L.J.1    Hecht, S.S.2    Peterson, L.A.3
  • 16
    • 14744302949 scopus 로고    scopus 로고
    • Expression patterns of mouse and human CYP orthologs (families 1-4) during development and in different adult tissues
    • Choudhary, D., Jansson, I., Stoilov, I., Sarfarazi, M., Schenkman, J. B. (2005). Expression patterns of mouse and human CYP orthologs (families 1-4) during development and in different adult tissues. Arch. Biochem. Biophys. 436:50-61.
    • (2005) Arch. Biochem. Biophys. , vol.436 , pp. 50-61
    • Choudhary, D.1    Jansson, I.2    Stoilov, I.3    Sarfarazi, M.4    Schenkman, J.B.5
  • 17
    • 0035851164 scopus 로고    scopus 로고
    • Alternative splicing determines the function of CYP4F3 by switching substrate specificity
    • Christmas, P., Jones, J. P., Patten, C. J., Rock, D. A., Zheng, Y., Cheng, S. M., et al. (2001). Alternative splicing determines the function of CYP4F3 by switching substrate specificity. J. Biol. Chem. 276:38166-38172.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38166-38172
    • Christmas, P.1    Jones, J.P.2    Patten, C.J.3    Rock, D.A.4    Zheng, Y.5    Cheng, S.M.6
  • 18
    • 0028315963 scopus 로고
    • Quantification of CYP2B7, CYP4B1, and CYPOR messenger RNAs in normal human lung and lung tumors
    • Czerwinski, M., McLemore, T. L., Gelboin, H. V., Gonzalez, F. J. (1994). Quantification of CYP2B7, CYP4B1, and CYPOR messenger RNAs in normal human lung and lung tumors. Cancer Res. 54:1085-1091.
    • (1994) Cancer Res. , vol.54 , pp. 1085-1091
    • Czerwinski, M.1    McLemore, T.L.2    Gelboin, H.V.3    Gonzalez, F.J.4
  • 19
    • 0025949636 scopus 로고
    • Metabolic activation of 4-ipomeanol by complementary DNA-expressed human cytochromes P-450: Evidence for species-specific metabolism
    • Czerwinski, M., McLemore, T. L., Philpot, R. M., Nhamburo, P. T., Korzekwa, K., Gelboin, H. V., et al. (1991). Metabolic activation of 4-ipomeanol by complementary DNA-expressed human cytochromes P-450: evidence for species-specific metabolism. Cancer Res. 51:4636-4638.
    • (1991) Cancer Res. , vol.51 , pp. 4636-4638
    • Czerwinski, M.1    McLemore, T.L.2    Philpot, R.M.3    Nhamburo, P.T.4    Korzekwa, K.5    Gelboin, H.V.6
  • 20
    • 0030910381 scopus 로고    scopus 로고
    • Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group
    • DePillis, G. D., Ozaki, S., Kuo, J. M., Maltby, D. A., Ortiz de Montellano, P. R. (1997). Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group. J. Biol. Chem. 272:8857-8860.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8857-8860
    • DePillis, G.D.1    Ozaki, S.2    Kuo, J.M.3    Maltby, D.A.4    Ortiz De Montellano, P.R.5
  • 21
    • 0019831185 scopus 로고
    • Identification of cytochrome P-450 isozymes in nonciliated bronchiolar epithelial (Clara) and alveolar type II cells isolated from rabbit lung
    • Devereux, T. R., Serabjit-Singh, C. J., Slaughter, S. R., Wolf, C. R., Philpot, R. M., Fouts, J. R. (1981). Identification of cytochrome P-450 isozymes in nonciliated bronchiolar epithelial (Clara) and alveolar type II cells isolated from rabbit lung. Exp. Lung. Res. 2:221-230.
    • (1981) Exp. Lung. Res. , vol.2 , pp. 221-230
    • Devereux, T.R.1    Serabjit-Singh, C.J.2    Slaughter, S.R.3    Wolf, C.R.4    Philpot, R.M.5    Fouts, J.R.6
  • 22
    • 0022523266 scopus 로고
    • The effect of substrate on the expression of activity catalyzed by cytochrome P-450: Metabolism mediated by rabbit isozyme 6 in pulmonary microsomal and reconstituted monooxygenase systems
    • Domin, B. A., Philpot, R. M. (1986). The effect of substrate on the expression of activity catalyzed by cytochrome P-450: metabolism mediated by rabbit isozyme 6 in pulmonary microsomal and reconstituted monooxygenase systems. Arch. Biochem. Biophys. 246:128-142.
    • (1986) Arch. Biochem. Biophys. , vol.246 , pp. 128-142
    • Domin, B.A.1    Philpot, R.M.2
  • 23
    • 33646586642 scopus 로고    scopus 로고
    • Effects of the differentiated keratinocyte phenotype on expression levels of CYP1-4 family genes in human skin cells
    • Du, L., Neis, M. M., Ladd, P. A., Lanza, D. L., Yost, G. S., Keeney, D. S. (2005). Effects of the differentiated keratinocyte phenotype on expression levels of CYP1-4 family genes in human skin cells. Toxicol. Appl. Pharmacol. 215:135-144.
    • (2005) Toxicol. Appl. Pharmacol. , vol.215 , pp. 135-144
    • Du, L.1    Neis, M.M.2    Ladd, P.A.3    Lanza, D.L.4    Yost, G.S.5    Keeney, D.S.6
  • 24
    • 0018595843 scopus 로고
    • Species and strain differences in target organ alkylation and toxicity by 4-ipomeanol. Predictive value of covalent binding in studies of target organ toxicities by reactive metabolites
    • Dutcher, J. S., Boyd, M. R. (1979). Species and strain differences in target organ alkylation and toxicity by 4-ipomeanol. Predictive value of covalent binding in studies of target organ toxicities by reactive metabolites. Biochem. Pharmacol. 28:3367-3372.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 3367-3372
    • Dutcher, J.S.1    Boyd, M.R.2
  • 25
    • 0028853285 scopus 로고
    • Structure of the green heme in myeloperoxidase
    • Fenna, R., Zeng, J., Davey, C. (1995). Structure of the green heme in myeloperoxidase. Arch. Biochem. Biophys. 316:653-656.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 653-656
    • Fenna, R.1    Zeng, J.2    Davey, C.3
  • 27
    • 0032551713 scopus 로고    scopus 로고
    • Positional specificity of rabbit CYP4B1 for omega-hydroxylation1 of short-medium chain fatty acids and hydrocarbons
    • Fisher, M. B., Zheng, Y. M., Rettie, A. E. (1998). Positional specificity of rabbit CYP4B1 for omega-hydroxylation1 of short-medium chain fatty acids and hydrocarbons. Biochem. Biophys. Res. Commun. 248:352-355.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 352-355
    • Fisher, M.B.1    Zheng, Y.M.2    Rettie, A.E.3
  • 28
    • 0018876795 scopus 로고
    • Quantitation of two forms of pulmonary cytochrome P-450 in microsomes, using substrate specificities
    • Franklin, M. R., Wolf, C. R., Serabjit-Singh, C., Philpot, R. M. (1980). Quantitation of two forms of pulmonary cytochrome P-450 in microsomes, using substrate specificities. Mol. Pharmacol. 17:415-420.
    • (1980) Mol. Pharmacol. , vol.17 , pp. 415-420
    • Franklin, M.R.1    Wolf, C.R.2    Serabjit-Singh, C.3    Philpot, R.M.4
  • 29
    • 3042688858 scopus 로고    scopus 로고
    • Cytochrome p450 gene expression levels in peripheral blood mononuclear cells in comparison with the liver
    • Furukawa, M., Nishimura, M., Ogino, D., Chiba, R., Ikai, I., Ueda, N., et al. (2004). Cytochrome p450 gene expression levels in peripheral blood mononuclear cells in comparison with the liver. Cancer Sci. 95:520-529.
    • (2004) Cancer Sci. , vol.95 , pp. 520-529
    • Furukawa, M.1    Nishimura, M.2    Ogino, D.3    Chiba, R.4    Ikai, I.5    Ueda, N.6
  • 30
    • 0024370045 scopus 로고
    • Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: Identification of cytochrome P-450 gene subfamily IVB
    • Gasser, R., Philpot, R. M. (1989). Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and regulation of species-dependent expression and induction in lung and liver: identification of cytochrome P-450 gene subfamily IVB. Mol. Pharmacol. 35:617-625.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 617-625
    • Gasser, R.1    Philpot, R.M.2
  • 31
    • 0026542989 scopus 로고
    • Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • Gotoh, O. (1992). Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J. Biol. Chem. 267:83-90.
    • (1992) J. Biol. Chem. , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 32
    • 0031918678 scopus 로고    scopus 로고
    • Cytochrome P450-dependent desaturation of lauric acid: Isoform selectivity and mechanism of formation of 11-dodecenoic acid
    • Guan, X., Fisher, M. B., Lang, D. H., Zheng, Y. M., Koop, D. R., Rettie, A. E. (1998). Cytochrome P450-dependent desaturation of lauric acid: isoform selectivity and mechanism of formation of 11-dodecenoic acid. Chem. Biol. Interact. 110:103-121.
    • (1998) Chem. Biol. Interact. , vol.110 , pp. 103-121
    • Guan, X.1    Fisher, M.B.2    Lang, D.H.3    Zheng, Y.M.4    Koop, D.R.5    Rettie, A.E.6
  • 33
    • 0017671864 scopus 로고
    • Preparation and properties of highly purified cytochrome p-450 and NADPH-cytochrome P-450 reductase from pulmonary microsomes of untreated rabbits
    • Guengerich, F. P. (1977). Preparation and properties of highly purified cytochrome p-450 and NADPH-cytochrome P-450 reductase from pulmonary microsomes of untreated rabbits. Mol. Pharmacol. 13:911-923.
    • (1977) Mol. Pharmacol. , vol.13 , pp. 911-923
    • Guengerich, F.P.1
  • 38
    • 0035815686 scopus 로고    scopus 로고
    • Covalently linked heme in cytochrome p4504a fatty acid hydroxylases
    • Hoch, U., Ortiz De Montellano, P. R. (2001). Covalently linked heme in cytochrome p4504a fatty acid hydroxylases. J. Biol. Chem. 276:11339-11346.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11339-11346
    • Hoch, U.1    Ortiz De Montellano, P.R.2
  • 39
    • 0033955218 scopus 로고    scopus 로고
    • Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid omega-hydroxylases
    • Hoch, U., Zhang, Z., Kroetz, D. L., Ortiz de Montellano, P. R. (2000). Structural determination of the substrate specificities and regioselectivities of the rat and human fatty acid omega-hydroxylases. Arch. Biochem. Biophys. 373:63-71.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 63-71
    • Hoch, U.1    Zhang, Z.2    Kroetz, D.L.3    Ortiz De Montellano, P.R.4
  • 40
    • 0042807479 scopus 로고    scopus 로고
    • Combined radiation and cytochrome CYP4B1/4-ipomeanol gene therapy using the EGR1 promoter
    • Hsu, H., Rainov, N. G., Quinones, A., Eling, D. J., Sakamoto, K. M., Spear, M. A. (2003). Combined radiation and cytochrome CYP4B1/4-ipomeanol gene therapy using the EGR1 promoter. Anticancer Res. 23:2723-2728.
    • (2003) Anticancer Res. , vol.23 , pp. 2723-2728
    • Hsu, H.1    Rainov, N.G.2    Quinones, A.3    Eling, D.J.4    Sakamoto, K.M.5    Spear, M.A.6
  • 41
    • 0024538329 scopus 로고
    • Inhibition of 3-methylindole bioactivation by the cytochrome P-450 suicide substrates 1-aminobenzotriazole and alpha-methylbenzylaminobenzotriazole
    • Huijzer, J. C., Adams, J. D., Jr., Jaw, J. Y., Yost, G. S. (1989). Inhibition of 3-methylindole bioactivation by the cytochrome P-450 suicide substrates 1-aminobenzotriazole and alpha-methylbenzylaminobenzotriazole. Drug Metab. Dispos. 17:37-42.
    • (1989) Drug Metab. Dispos. , vol.17 , pp. 37-42
    • Huijzer, J.C.1    Adams Jr., J.D.2    Jaw, J.Y.3    Yost, G.S.4
  • 42
    • 0025303399 scopus 로고
    • Purification and characterization of rat pulmonary cytochrome P-450
    • Imaoka, S., Funae, Y. (1990). Purification and characterization of rat pulmonary cytochrome P-450. J. Biochem. (Tokyo) 108:33-36.
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 33-36
    • Imaoka, S.1    Funae, Y.2
  • 44
    • 0029144726 scopus 로고
    • Mutagenic activation of 3-methoxy-4-aminoazobenzene by mouse renal cytochrome P450 CYP4B1: Cloning and characterization of mouse CYP4B1
    • Imaoka, S., Hiroi, T., Tamura, Y., Yamazaki, H., Shimada, T., Komori, M., et al. (1995). Mutagenic activation of 3-methoxy-4-aminoazobenzene by mouse renal cytochrome P450 CYP4B1: cloning and characterization of mouse CYP4B1. Arch. Biochem. Biophys. 321:255-262.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 255-262
    • Imaoka, S.1    Hiroi, T.2    Tamura, Y.3    Yamazaki, H.4    Shimada, T.5    Komori, M.6
  • 45
    • 0343471515 scopus 로고    scopus 로고
    • Mutagenic activation of urinary bladder carcinogens by CYP4B1 and the presence of CYP4B1 in bladder mucosa
    • Imaoka, S., Yoneda, Y., Matsuda, T., Degawa, M., Fukushima, S., Funae, Y. (1997). Mutagenic activation of urinary bladder carcinogens by CYP4B1 and the presence of CYP4B1 in bladder mucosa. Biochem. Pharmacol. 54:677-683.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 677-683
    • Imaoka, S.1    Yoneda, Y.2    Matsuda, T.3    Degawa, M.4    Fukushima, S.5    Funae, Y.6
  • 47
    • 0035954132 scopus 로고    scopus 로고
    • Androgen regulation of CYP4B1 responsible for mutagenic activation of bladder carcinogens in the rat bladder: Detection of CYP4B1 mRNA by competitive reverse transcription-polymerase chain reaction
    • Imaoka, S., Yoneda, Y., Sugimoto, T., Ikemoto, S., Hiroi, T., Yamamoto, K., Nakatani, T., et al. (2001b). Androgen regulation of CYP4B1 responsible for mutagenic activation of bladder carcinogens in the rat bladder: detection of CYP4B1 mRNA by competitive reverse transcription-polymerase chain reaction. Cancer Lett. 166:119-123.
    • (2001) Cancer Lett. , vol.166 , pp. 119-123
    • Imaoka, S.1    Yoneda, Y.2    Sugimoto, T.3    Ikemoto, S.4    Hiroi, T.5    Yamamoto, K.6    Nakatani, T.7
  • 48
    • 0014082654 scopus 로고
    • Carcinogenicity of 2-acetylaminofluorene and N-hydroxy-2- acetylaminofluorene in the rabbit
    • Irving, C. C., Wiseman, R., Jr., Young, J. M. (1967). Carcinogenicity of 2-acetylaminofluorene and N-hydroxy-2-acetylaminofluorene in the rabbit. Cancer Res. 27:838-848.
    • (1967) Cancer Res. , vol.27 , pp. 838-848
    • Irving, C.C.1    Wiseman Jr., R.2    Young, J.M.3
  • 50
    • 0037711701 scopus 로고    scopus 로고
    • Hormonal regulation and characterisation of the mouse Cyp4b1 gene 5′-flanking region
    • Isern, J., Meseguer, A. (2003). Hormonal regulation and characterisation of the mouse Cyp4b1 gene 5′-flanking region. Biochem. Biophys. Res. Commun. 307:139-147.
    • (2003) Biochem. Biophys. Res. Commun. , vol.307 , pp. 139-147
    • Isern, J.1    Meseguer, A.2
  • 51
    • 0025934202 scopus 로고
    • Mechanism of action of the urinary bladder carcinogen N-nitrosobutyl-3-carboxypropylamine
    • Janzowski, C., Jacob, D., Henn, I., Zankl, H., Pool-Zobel, B. L., Wiessler, M., et al. (1991). Mechanism of action of the urinary bladder carcinogen N-nitrosobutyl-3-carboxypropylamine. IARC Sci. Publ. 332-338.
    • (1991) IARC Sci. Publ. , pp. 332-338
    • Janzowski, C.1    Jacob, D.2    Henn, I.3    Zankl, H.4    Pool-Zobel, B.L.5    Wiessler, M.6
  • 53
    • 0023899024 scopus 로고
    • The essential role of microsomal deacetylase activity in the metabolic activation, DNA-(deoxyguanosin-8-yl)-2-aminofluorene adduct formation and initiation of liver tumors by N-hydroxy-2-acetylaminofluorene in the livers of infant male B6C3F1 mice
    • Lai, C. C., Miller, E. C., Miller, J. A., Liem, A. (1988). The essential role of microsomal deacetylase activity in the metabolic activation, DNA-(deoxyguanosin-8-yl)-2-aminofluorene adduct formation and initiation of liver tumors by N-hydroxy-2-acetylaminofluorene in the livers of infant male B6C3F1 mice. Carcinogenesis 9:1295-1302.
    • (1988) Carcinogenesis , vol.9 , pp. 1295-1302
    • Lai, C.C.1    Miller, E.C.2    Miller, J.A.3    Liem, A.4
  • 54
    • 0002203122 scopus 로고    scopus 로고
    • Cytochrome P450 and arachidonic acid metabolism in the corneal epithelium: Role in inflammation
    • Green, K., Edelhauser, H. F., Hackett, R. B., Hull, D. S., Potter, D. E., Tripathi, R. C., eds., New York: Plenum Press
    • Laniado-Schwartzman, M. (1997). Cytochrome P450 and arachidonic acid metabolism in the corneal epithelium: role in inflammation. In: Green, K., Edelhauser, H. F., Hackett, R. B., Hull, D. S., Potter, D. E., Tripathi, R. C., eds., Advances in Ocular Toxicology. New York: Plenum Press, pp. 3-20.
    • (1997) Advances in Ocular Toxicology , pp. 3-20
    • Laniado-Schwartzman, M.1
  • 55
    • 0034635521 scopus 로고    scopus 로고
    • Formation of 20-hydroxyeicosatetraenoic acid, a vasoactive and natriuretic eicosanoid, in human kidney. Role of Cyp4F2 and Cyp4A11
    • Lasker, J. M., Chen, W. B., Wolf, I., Bloswick, B. P., Wilson, P. D., Powell, P. K. (2000). Formation of 20-hydroxyeicosatetraenoic acid, a vasoactive and natriuretic eicosanoid, in human kidney. Role of Cyp4F2 and Cyp4A11. J. Biol. Chem. 275:4118-4126.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4118-4126
    • Lasker, J.M.1    Chen, W.B.2    Wolf, I.3    Bloswick, B.P.4    Wilson, P.D.5    Powell, P.K.6
  • 56
    • 0036020994 scopus 로고    scopus 로고
    • Genetic polymorphism of the human cytochrome P450 CYP4B1: Evidence for a non-functional allelic variant
    • Lo-Guidice, J. M., Allorge, D., Cauffiez, C., Chevalier, D., Lafitte, J. J., Lhermitte, M., et al. (2002). Genetic polymorphism of the human cytochrome P450 CYP4B1: evidence for a non-functional allelic variant. Pharmacogenetics 12:367-374.
    • (2002) Pharmacogenetics , vol.12 , pp. 367-374
    • Lo-Guidice, J.M.1    Allorge, D.2    Cauffiez, C.3    Chevalier, D.4    Lafitte, J.J.5    Lhermitte, M.6
  • 57
    • 0032993630 scopus 로고    scopus 로고
    • Hypoxia-induced production of 12-hydroxyeicosanoids in the corneal epithelium: Involvement of a cytochrome P-4504B1 isoform
    • Mastyugin, V., Aversa, E., Bonazzi, A., Vafaes, C., Mieyal, P., Schwartzman, M. L. (1999). Hypoxia-induced production of 12-hydroxyeicosanoids in the corneal epithelium: involvement of a cytochrome P-4504B1 isoform. J. Pharmacol. Exp. Ther. 289:1611-1619.
    • (1999) J. Pharmacol. Exp. Ther. , vol.289 , pp. 1611-1619
    • Mastyugin, V.1    Aversa, E.2    Bonazzi, A.3    Vafaes, C.4    Mieyal, P.5    Schwartzman, M.L.6
  • 59
    • 0036257467 scopus 로고    scopus 로고
    • Corneal epithelial VEGF and cytochrome P450 4B1 expression in a rabbit model of closed eye contact lens wear
    • Mastyugin, V., Mosaed, S., Bonazzi, A., Dunn, M. W., Schwartzman, M. L. (2001). Corneal epithelial VEGF and cytochrome P450 4B1 expression in a rabbit model of closed eye contact lens wear. Curr. Eye Res. 23:1-10.
    • (2001) Curr. Eye Res. , vol.23 , pp. 1-10
    • Mastyugin, V.1    Mosaed, S.2    Bonazzi, A.3    Dunn, M.W.4    Schwartzman, M.L.5
  • 60
    • 0028116354 scopus 로고
    • Species-specific expression of CYP4B1 in rabbit and human gastrointestinal tissues
    • McKinnon, R. A., Burgess, W. M., Gonzalez, F. J., Gasser, R., McManus, M. E. (1994). Species-specific expression of CYP4B1 in rabbit and human gastrointestinal tissues. Pharmacogenetics 4:260-270.
    • (1994) Pharmacogenetics , vol.4 , pp. 260-270
    • McKinnon, R.A.1    Burgess, W.M.2    Gonzalez, F.J.3    Gasser, R.4    McManus, M.E.5
  • 61
    • 0030440082 scopus 로고    scopus 로고
    • Localization of cytochromes P450 in human tissues: Implications for chemical toxicity
    • McKinnon, R. A., McManus, M. E. (1996). Localization of cytochromes P450 in human tissues: implications for chemical toxicity. Pathology 28:148-155.
    • (1996) Pathology , vol.28 , pp. 148-155
    • McKinnon, R.A.1    McManus, M.E.2
  • 62
    • 25644453560 scopus 로고    scopus 로고
    • Transfection of cytochrome P4504B1 into the cornea increases angiogenic activity of the limbal vessels
    • Mezentsev, A., Mastyugin, V., Seta, F., Ashkar, S., Kemp, R., Reddy, D. S., et al. (2005). Transfection of cytochrome P4504B1 into the cornea increases angiogenic activity of the limbal vessels. J. Pharmacol. Exp. Ther. 315:42-50.
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , pp. 42-50
    • Mezentsev, A.1    Mastyugin, V.2    Seta, F.3    Ashkar, S.4    Kemp, R.5    Reddy, D.S.6
  • 63
    • 0028326162 scopus 로고
    • Recent studies on the metabolic activation of chemical carcinogens
    • Miller, J. A. (1994). Recent studies on the metabolic activation of chemical carcinogens. Cancer Res. 54:1879s-1881s.
    • (1994) Cancer Res. , vol.54
    • Miller, J.A.1
  • 64
    • 0033914287 scopus 로고    scopus 로고
    • Rabbit cytochrome P450 4B1: A novel prodrug activating gene for pharmacogene therapy of hepatocellular carcinoma
    • Mohr, L., Rainov, N. G., Mohr, U. G., Wands, J. R. (2000). Rabbit cytochrome P450 4B1: a novel prodrug activating gene for pharmacogene therapy of hepatocellular carcinoma. Cancer Gene. Ther. 7:1008-1014.
    • (2000) Cancer Gene. Ther. , vol.7 , pp. 1008-1014
    • Mohr, L.1    Rainov, N.G.2    Mohr, U.G.3    Wands, J.R.4
  • 65
    • 0024501044 scopus 로고
    • Prostaglandin and fatty acid omega- and (omega-1)-oxidation in rabbit lung. Acetylenic fatty acid mechanism-based inactivators as specific inhibitors
    • Muerhoff, A. S., Williams, D. E., Reich, N. O., CaJacob, C. A., Ortiz de Montellano, P. R., Masters, B. S. (1989). Prostaglandin and fatty acid omega- and (omega-1)-oxidation in rabbit lung. Acetylenic fatty acid mechanism-based inactivators as specific inhibitors. J. Biol. Chem. 264:749-756.
    • (1989) J. Biol. Chem. , vol.264 , pp. 749-756
    • Muerhoff, A.S.1    Williams, D.E.2    Reich, N.O.3    CaJacob, C.A.4    Ortiz De Montellano, P.R.5    Masters, B.S.6
  • 66
    • 0842312531 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants
    • Nelson, D. R., Zeldin, D. C., Hoffman, S. M., Maltais, L. J., Wain, H. M., Nebert, D. W. (2004). Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14:1-18.
    • (2004) Pharmacogenetics , vol.14 , pp. 1-18
    • Nelson, D.R.1    Zeldin, D.C.2    Hoffman, S.M.3    Maltais, L.J.4    Wain, H.M.5    Nebert, D.W.6
  • 67
    • 0032997280 scopus 로고    scopus 로고
    • Kinetic profile of the rat CYP4A isoforms: Arachidonic acid metabolism and isoform-specific inhibitors
    • Nguyen, X., Wang, M. H., Reddy, K. M., Falck, J. R., Schwartzman, M. L. (1999). Kinetic profile of the rat CYP4A isoforms: arachidonic acid metabolism and isoform-specific inhibitors. Am. J. Physiol. 276:R1691-R1700.
    • (1999) Am. J. Physiol. , vol.276
    • Nguyen, X.1    Wang, M.H.2    Reddy, K.M.3    Falck, J.R.4    Schwartzman, M.L.5
  • 68
    • 0024425342 scopus 로고
    • Identification of a new P450 expressed in human lung: Complete cDNA sequence, cDNA-directed expression, and chromosome mapping
    • Nhamburo, P. T., Gonzalez, F. J., McBride, O. W., Gelboin, H. V., Kimura, S. (1989). Identification of a new P450 expressed in human lung: complete cDNA sequence, cDNA-directed expression, and chromosome mapping. Biochemistry 28:8060-8066.
    • (1989) Biochemistry , vol.28 , pp. 8060-8066
    • Nhamburo, P.T.1    Gonzalez, F.J.2    McBride, O.W.3    Gelboin, H.V.4    Kimura, S.5
  • 69
    • 0023144776 scopus 로고
    • Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of structure and inducibility
    • Parandoosh, Z., Fujita, V. S., Coon, M. J., Philpot, R. M. (1987). Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of structure and inducibility. Drug Metab. Dispos. 15:59-67.
    • (1987) Drug Metab. Dispos. , vol.15 , pp. 59-67
    • Parandoosh, Z.1    Fujita, V.S.2    Coon, M.J.3    Philpot, R.M.4
  • 70
    • 22944472719 scopus 로고    scopus 로고
    • Molecular mechanisms regulating human CYP4B1 lung-selective expression
    • Poch, M. T., Cutler, N. S., Yost, G. S., Hines, R. N. (2005). Molecular mechanisms regulating human CYP4B1 lung-selective expression. Drug Metab. Dispos. 33:1174-1184.
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 1174-1184
    • Poch, M.T.1    Cutler, N.S.2    Yost, G.S.3    Hines, R.N.4
  • 71
    • 0032561204 scopus 로고    scopus 로고
    • The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l-peptides
    • Rae, T. D., Goff, H. M. (1998). The heme prosthetic group of lactoperoxidase. Structural characteristics of heme l and heme l-peptides. J. Biol. Chem. 273:27968-27977.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27968-27977
    • Rae, T.D.1    Goff, H.M.2
  • 72
    • 0032503657 scopus 로고    scopus 로고
    • New prodrug activation gene therapy for cancer using cytochrome P450 4B1 and 2-aminoanthracene/4-ipomeanol
    • Rainov, N. G., Dobberstein, K. U., Sena-Esteves, M., Herrlinger, U., Kramm, C. M., Philpot, R. M., et al. (1998a). New prodrug activation gene therapy for cancer using cytochrome P450 4B1 and 2-aminoanthracene/4-ipomeanol. Hum. Gene. Ther. 9:1261-1273.
    • (1998) Hum. Gene. Ther. , vol.9 , pp. 1261-1273
    • Rainov, N.G.1    Dobberstein, K.U.2    Sena-Esteves, M.3    Herrlinger, U.4    Kramm, C.M.5    Philpot, R.M.6
  • 73
    • 0031784978 scopus 로고    scopus 로고
    • A chimeric fusion protein of cytochrome CYP4B1 and green fluorescent protein for detection of pro-drug activating gene delivery and for gene therapy in malignant glioma
    • Rainov, N. G., Sena-Esteves, M., Fraefel, C., Dobberstein, K. U., Chiocca, E. A., Breakefield, X. O. (1998b). A chimeric fusion protein of cytochrome CYP4B1 and green fluorescent protein for detection of pro-drug activating gene delivery and for gene therapy in malignant glioma. Adv. Exp. Med. Biol. 451:393-403.
    • (1998) Adv. Exp. Med. Biol. , vol.451 , pp. 393-403
    • Rainov, N.G.1    Sena-Esteves, M.2    Fraefel, C.3    Dobberstein, K.U.4    Chiocca, E.A.5    Breakefield, X.O.6
  • 74
    • 0028226524 scopus 로고
    • Correlation between pulmonary cytochrome P450 transcripts and the organ-selective pneumotoxicity of 3-methylindole
    • Ramakanth, S., Thornton-Manning, J. R., Wang, H., Maxwell, H., Yost, G. S. (1994). Correlation between pulmonary cytochrome P450 transcripts and the organ-selective pneumotoxicity of 3-methylindole. Toxicol. Lett. 71:77-85.
    • (1994) Toxicol. Lett. , vol.71 , pp. 77-85
    • Ramakanth, S.1    Thornton-Manning, J.R.2    Wang, H.3    Maxwell, H.4    Yost, G.S.5
  • 75
    • 0023697057 scopus 로고
    • Cytochrome P-450-catalyzed desaturation of valproic acid in vitro. Species differences, induction effects, and mechanistic studies
    • Rettie, A. E., Boberg, M., Rettenmeier, A. W., Baillie, T. A. (1988). Cytochrome P-450-catalyzed desaturation of valproic acid in vitro. Species differences, induction effects, and mechanistic studies. J. Biol. Chem. 263:13733-13738.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13733-13738
    • Rettie, A.E.1    Boberg, M.2    Rettenmeier, A.W.3    Baillie, T.A.4
  • 76
    • 0029079640 scopus 로고
    • CYP4 isozyme specificity and the relationship between omega-hydroxylation and terminal desaturation of valproic acid
    • Rettie, A. E., Sheffels, P. R., Korzekwa, K. R., Gonzalez, F. J., Philpot, R. M., Baillie, T. A. (1995). CYP4 isozyme specificity and the relationship between omega-hydroxylation and terminal desaturation of valproic acid. Biochemistry 34:7889-7895.
    • (1995) Biochemistry , vol.34 , pp. 7889-7895
    • Rettie, A.E.1    Sheffels, P.R.2    Korzekwa, K.R.3    Gonzalez, F.J.4    Philpot, R.M.5    Baillie, T.A.6
  • 77
    • 0020628670 scopus 로고
    • The relationship between increases in the hepatic content of cytochrome P-450, form 5, and in the metabolism of aromatic amines to mutagenic products following treatment of rabbits with phenobarbital
    • Robertson, I. G., Serabjit-Singh, C., Croft, J. E., Philpot, R. M. (1983). The relationship between increases in the hepatic content of cytochrome P-450, form 5, and in the metabolism of aromatic amines to mutagenic products following treatment of rabbits with phenobarbital. Mol. Pharmacol. 24:156-162.
    • (1983) Mol. Pharmacol. , vol.24 , pp. 156-162
    • Robertson, I.G.1    Serabjit-Singh, C.2    Croft, J.E.3    Philpot, R.M.4
  • 78
    • 0019851310 scopus 로고
    • Specificity of rabbit pulmonary cytochrome P-450 isozymes in the activation of several aromatic amines and aflatoxin B1
    • Robertson, L. G., Philpot, R. M., Zeiger, E., Wolf, C. R. (1981). Specificity of rabbit pulmonary cytochrome P-450 isozymes in the activation of several aromatic amines and aflatoxin B1. Mol. Pharmacol. 20:662-668.
    • (1981) Mol. Pharmacol. , vol.20 , pp. 662-668
    • Robertson, L.G.1    Philpot, R.M.2    Zeiger, E.3    Wolf, C.R.4
  • 79
    • 0027195106 scopus 로고
    • Phase I and pharmacological study of the pulmonary cytotoxin 4-ipomeanol on a single dose schedule in lung cancer patients: Hepatotoxicity is dose limiting in humans
    • Rowinsky, E. K., Noe, D. A., Ettinger, D. S., Christian, M. C., Lubejko, B. G., Fishman, E. K., et al. (1993). Phase I and pharmacological study of the pulmonary cytotoxin 4-ipomeanol on a single dose schedule in lung cancer patients: hepatotoxicity is dose limiting in humans. Cancer Res. 53:1794-1801.
    • (1993) Cancer Res. , vol.53 , pp. 1794-1801
    • Rowinsky, E.K.1    Noe, D.A.2    Ettinger, D.S.3    Christian, M.C.4    Lubejko, B.G.5    Fishman, E.K.6
  • 80
    • 0025298478 scopus 로고
    • Tissue, species, and substrate concentration differences in the position-selective hydroxylation of N-nitrosodibutylamine. Relationship to the distribution of cytochrome P-450 isozymes 2 (IIB) and 5 (IVB)
    • Schulze, J., Richter, E., Philpot, R. M. (1990). Tissue, species, and substrate concentration differences in the position-selective hydroxylation of N-nitrosodibutylamine. Relationship to the distribution of cytochrome P-450 isozymes 2 (IIB) and 5 (IVB). Drug Metab. Dispos. 18:398-402.
    • (1990) Drug Metab. Dispos. , vol.18 , pp. 398-402
    • Schulze, J.1    Richter, E.2    Philpot, R.M.3
  • 81
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • Scott, E. E., White, M. A., He, Y. A., Johnson, E. F., Stout, C. D., Halpert, J. R. (2004). Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-Å resolution: insight into the range of P450 conformations and the coordination of redox partner binding. J. Biol. Chem. 279:27294-27301.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3    Johnson, E.F.4    Stout, C.D.5    Halpert, J.R.6
  • 82
    • 0021054147 scopus 로고
    • Interactions between xenobiotics that increase or decrease the levels of cytochrome P-450 isozymes in rabbit lung and liver
    • Serabjit-Singh, C. J., Albro, P. W., Robertson, I. G., Philpot, R. M. (1983). Interactions between xenobiotics that increase or decrease the levels of cytochrome P-450 isozymes in rabbit lung and liver. J. Biol. Chem. 258:12827-12834.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12827-12834
    • Serabjit-Singh, C.J.1    Albro, P.W.2    Robertson, I.G.3    Philpot, R.M.4
  • 83
    • 0018714868 scopus 로고
    • The rabbit pulmonary monooxygenase system. Immunochemical and biochemical characterization of enzyme components
    • Serabjit-Singh, C. J., Wolf, C. R., Philpot, R. M. (1979). The rabbit pulmonary monooxygenase system. Immunochemical and biochemical characterization of enzyme components. J. Biol. Chem. 254:9901-9907.
    • (1979) J. Biol. Chem. , vol.254 , pp. 9901-9907
    • Serabjit-Singh, C.J.1    Wolf, C.R.2    Philpot, R.M.3
  • 84
    • 0024432048 scopus 로고
    • Role of hepatic and renal cytochrome P-450 IVA1 in the metabolism of lipid substrates
    • Sharma, R. K., Doig, M. V., Lewis, D. F., Gibson, G. G. (1989). Role of hepatic and renal cytochrome P-450 IVA1 in the metabolism of lipid substrates. Biochem. Pharmacol. 38:3621-3629.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 3621-3629
    • Sharma, R.K.1    Doig, M.V.2    Lewis, D.F.3    Gibson, G.G.4
  • 85
    • 0031049745 scopus 로고    scopus 로고
    • The cytochrome P450 4 (CYP4) family
    • Simpson, A. E. (1997). The cytochrome P450 4 (CYP4) family. Gen. Pharmacol. 28:351-359.
    • (1997) Gen. Pharmacol. , vol.28 , pp. 351-359
    • Simpson, A.E.1
  • 86
    • 0030050265 scopus 로고    scopus 로고
    • Mechanistic studies on the cytochrome P450-catalyzed dehydrogenation of 3-methylindole
    • Skiles, G. L., Yost, G. S. (1996). Mechanistic studies on the cytochrome P450-catalyzed dehydrogenation of 3-methylindole. Chem. Res. Toxicol. 9:291-297.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 291-297
    • Skiles, G.L.1    Yost, G.S.2
  • 87
    • 0020658239 scopus 로고
    • Covalent binding of metabolites of 4-ipomeanol to rabbit pulmonary and hepatic microsomal proteins and to the enzymes of the pulmonary cytochrome P-450-dependent monooxygenase system
    • Slaughter, S. R., Statham, C. N., Philpot, R. M., Boyd, M. R. (1983). Covalent binding of metabolites of 4-ipomeanol to rabbit pulmonary and hepatic microsomal proteins and to the enzymes of the pulmonary cytochrome P-450-dependent monooxygenase system. J. Pharmacol. Exp. Ther. 224:252-257.
    • (1983) J. Pharmacol. Exp. Ther. , vol.224 , pp. 252-257
    • Slaughter, S.R.1    Statham, C.N.2    Philpot, R.M.3    Boyd, M.R.4
  • 88
    • 0019876652 scopus 로고
    • The rabbit pulmonary monooxygenase system. partial structural characterization of the cytochrome P-450 components and comparison to the hepatic cytochrome P-450
    • Slaughter, S. R., Wolf, C. R., Marciniszyn, J. P., Philpot, R. M. (1981). The rabbit pulmonary monooxygenase system. partial structural characterization of the cytochrome P-450 components and comparison to the hepatic cytochrome P-450. J. Biol. Chem. 256:2499-2503.
    • (1981) J. Biol. Chem. , vol.256 , pp. 2499-2503
    • Slaughter, S.R.1    Wolf, C.R.2    Marciniszyn, J.P.3    Philpot, R.M.4
  • 89
    • 0020347918 scopus 로고
    • p-Xylene metabolism by rabbit lung and liver and its relationship to the selective destruction of pulmonary cytochrome P-450
    • Smith, B. R., Plummer, J. L., Wolf, C. R., Philpot, R. M., Bend, J. R. (1982). p-Xylene metabolism by rabbit lung and liver and its relationship to the selective destruction of pulmonary cytochrome P-450. J. Pharmacol. Exp. Ther. 223:736-742.
    • (1982) J. Pharmacol. Exp. Ther. , vol.223 , pp. 736-742
    • Smith, B.R.1    Plummer, J.L.2    Wolf, C.R.3    Philpot, R.M.4    Bend, J.R.5
  • 90
    • 0028834249 scopus 로고
    • 4-Ipomeanol and 2-aminoanthracene cytotoxicity in C3H/10T1/2 cells expressing rabbit cytochrome P450 4B1
    • Smith, P. B., Tiano, H. F., Nesnow, S., Boyd, M. R., Philpot, R. M., Langenbach, R. (1995). 4-Ipomeanol and 2-aminoanthracene cytotoxicity in C3H/10T1/2 cells expressing rabbit cytochrome P450 4B1. Biochem. Pharmacol. 50:1567-1575.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 1567-1575
    • Smith, P.B.1    Tiano, H.F.2    Nesnow, S.3    Boyd, M.R.4    Philpot, R.M.5    Langenbach, R.6
  • 91
    • 0034102736 scopus 로고    scopus 로고
    • Enhanced green fluorescent protein fusion proteins of herpes simplex virus type 1 thymidine kinase and cytochrome P450 4B1: Applications for prodrug-activating gene therapy
    • Steffens, S., Frank, S., Fischer, U., Heuser, C., Meyer, K. L., Dobberstein, K. U., et al. (2000). Enhanced green fluorescent protein fusion proteins of herpes simplex virus type 1 thymidine kinase and cytochrome P450 4B1: applications for prodrug-activating gene therapy. Cancer Gene. Ther. 7:806-812.
    • (2000) Cancer Gene. Ther. , vol.7 , pp. 806-812
    • Steffens, S.1    Frank, S.2    Fischer, U.3    Heuser, C.4    Meyer, K.L.5    Dobberstein, K.U.6
  • 92
    • 0029974584 scopus 로고    scopus 로고
    • Bioactivation of a toxic metabolite of valproic acid, (E)-2-propyl-2,4-pentadienoic acid, via glucuronidation. LC/MS/MS characterization of the GSH-glucuronide diconjugates
    • Tang, W., Abbott, F. S. (1996). Bioactivation of a toxic metabolite of valproic acid, (E)-2-propyl-2,4-pentadienoic acid, via glucuronidation. LC/MS/MS characterization of the GSH-glucuronide diconjugates. Chem. Res. Toxicol. 9:517-526.
    • (1996) Chem. Res. Toxicol. , vol.9 , pp. 517-526
    • Tang, W.1    Abbott, F.S.2
  • 93
    • 0029875880 scopus 로고    scopus 로고
    • Metabolism of 3-methylindole by vaccinia-expressed P450 enzymes: Correlation of 3-methyleneindolenine formation and protein-binding
    • Thornton-Manning, J., Appleton, M. L., Gonzalez, F. J., Yost, G. S. (1996). Metabolism of 3-methylindole by vaccinia-expressed P450 enzymes: correlation of 3-methyleneindolenine formation and protein-binding. J. Pharmacol. Exp. Ther. 276:21-29.
    • (1996) J. Pharmacol. Exp. Ther. , vol.276 , pp. 21-29
    • Thornton-Manning, J.1    Appleton, M.L.2    Gonzalez, F.J.3    Yost, G.S.4
  • 94
    • 0032245811 scopus 로고    scopus 로고
    • Hypoxia stimulates the synthesis of cytochrome P450-derived inflammatory eicosanoids in rabbit corneal epithelium
    • Vafeas, C., Mieyal, P. A., Urbano, F., Falck, J. R., Chauhan, K., Berman, M., et al. (1998). Hypoxia stimulates the synthesis of cytochrome P450-derived inflammatory eicosanoids in rabbit corneal epithelium. J. Pharmacol. Exp. Ther. 287:903-910.
    • (1998) J. Pharmacol. Exp. Ther. , vol.287 , pp. 903-910
    • Vafeas, C.1    Mieyal, P.A.2    Urbano, F.3    Falck, J.R.4    Chauhan, K.5    Berman, M.6
  • 95
    • 0022369235 scopus 로고
    • The cytochrome P-450 monooxygenase system of rabbit bladder mucosa: Enzyme components and isozyme 5-dependent metabolism of 2-aminofluorene
    • Vanderslice, R. R., Boyd, J. A., Eling, T. E., Philpot, R. M. (1985). The cytochrome P-450 monooxygenase system of rabbit bladder mucosa: enzyme components and isozyme 5-dependent metabolism of 2-aminofluorene. Cancer Res. 45:5851-5858.
    • (1985) Cancer Res. , vol.45 , pp. 5851-5858
    • Vanderslice, R.R.1    Boyd, J.A.2    Eling, T.E.3    Philpot, R.M.4
  • 96
    • 0023218991 scopus 로고
    • Species-dependent expression and induction of homologues of rabbit cytochrome P-450 isozyme 5 in liver and lung
    • Vanderslice, R. R., Domin, B. A., Carver, G. T., Philpot, R. M. (1987). Species-dependent expression and induction of homologues of rabbit cytochrome P-450 isozyme 5 in liver and lung. Mol. Pharmacol. 31:320-325.
    • (1987) Mol. Pharmacol. , vol.31 , pp. 320-325
    • Vanderslice, R.R.1    Domin, B.A.2    Carver, G.T.3    Philpot, R.M.4
  • 98
    • 0030589540 scopus 로고    scopus 로고
    • Cloning, sequencing, and cDNA-directed expression of the rat renal CYP4A2: Arachidonic acid omega-hydroxylation and 11,12-epoxidation by CYP4A2 protein
    • Wang, M. H., Stec, D. E., Balazy, M., Mastyugin, V., Yang, C. S., Roman, R. J., et al. (1996). Cloning, sequencing, and cDNA-directed expression of the rat renal CYP4A2: arachidonic acid omega-hydroxylation and 11,12-epoxidation by CYP4A2 protein. Arch. Biochem. Biophys. 336:240-250.
    • (1996) Arch. Biochem. Biophys. , vol.336 , pp. 240-250
    • Wang, M.H.1    Stec, D.E.2    Balazy, M.3    Mastyugin, V.4    Yang, C.S.5    Roman, R.J.6
  • 99
    • 0033199499 scopus 로고    scopus 로고
    • P450 gene induction by structurally diverse xenochemicals: Central role of nuclear receptors CAR, PXR, and PPAR
    • Waxman, D. J. (1999). P450 gene induction by structurally diverse xenochemicals: central role of nuclear receptors CAR, PXR, and PPAR. Arch. Biochem. Biophys. 369:11-23.
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 11-23
    • Waxman, D.J.1
  • 101
    • 4143143372 scopus 로고    scopus 로고
    • The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-Å resolution
    • Wester, M. R., Yano, J. K., Schoch, G. A., Yang, C., Griffin, K. J., Stout, C. D., et al. (2004). The structure of human cytochrome P450 2C9 complexed with flurbiprofen at 2.0-Å resolution. J. Biol. Chem. 279:35630-35637.
    • (2004) J. Biol. Chem. , vol.279 , pp. 35630-35637
    • Wester, M.R.1    Yano, J.K.2    Schoch, G.A.3    Yang, C.4    Griffin, K.J.5    Stout, C.D.6
  • 102
    • 0021674610 scopus 로고
    • A prostaglandin omega-hydroxylase cytochrome P-450 (P-450PG-omega) purified from lungs of pregnant rabbits
    • Williams, D. E., Hale, S. E., Okita, R. T., Masters, B. S. (1984). A prostaglandin omega-hydroxylase cytochrome P-450 (P-450PG-omega) purified from lungs of pregnant rabbits. J. Biol. Chem. 259:14600-14608.
    • (1984) J. Biol. Chem. , vol.259 , pp. 14600-14608
    • Williams, D.E.1    Hale, S.E.2    Okita, R.T.3    Masters, B.S.4
  • 103
    • 3442896773 scopus 로고    scopus 로고
    • Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone
    • Williams, P. A., Cosme, J., Vinkovic, D. M., Ward, A., Angove, H. C., Day, P. J., et al. (2004). Crystal structures of human cytochrome P450 3A4 bound to metyrapone and progesterone. Science 305:683-686.
    • (2004) Science , vol.305 , pp. 683-686
    • Williams, P.A.1    Cosme, J.2    Vinkovic, D.M.3    Ward, A.4    Angove, H.C.5    Day, P.J.6
  • 105
    • 0030995728 scopus 로고    scopus 로고
    • The role of xenobiotic metabolizing enzymes in arylamine toxicity and carcinogenesis: Functional and localization studies
    • Windmill, K. F., McKinnon, R. A., Zhu, X., Gaedigk, A., Grant, D. M., McManus, M. E. (1997). The role of xenobiotic metabolizing enzymes in arylamine toxicity and carcinogenesis: functional and localization studies. Mutat. Res. 376:153-160.
    • (1997) Mutat. Res. , vol.376 , pp. 153-160
    • Windmill, K.F.1    McKinnon, R.A.2    Zhu, X.3    Gaedigk, A.4    Grant, D.M.5    McManus, M.E.6
  • 106
    • 0018144257 scopus 로고
    • The rabbit pulmonary monooxygenase system: Characteristics and activities of two forms of pulmonary cytochrome P-450
    • Wolf, C. R., Szutowski, M. M., Ball, L. M., Philpot, R. M. (1978). The rabbit pulmonary monooxygenase system: characteristics and activities of two forms of pulmonary cytochrome P-450. Chem. Biol. Interact. 21:29-43.
    • (1978) Chem. Biol. Interact. , vol.21 , pp. 29-43
    • Wolf, C.R.1    Szutowski, M.M.2    Ball, L.M.3    Philpot, R.M.4
  • 107
    • 1342323347 scopus 로고    scopus 로고
    • Catalytic activity and isoform-specific inhibition of rat cytochrome p450 4F enzymes
    • Xu, F., Falck, J. R., Ortiz de Montellano, P. R., Kroetz, D. L. (2004). Catalytic activity and isoform-specific inhibition of rat cytochrome p450 4F enzymes. J. Pharmacol. Exp. Ther. 308:887-895.
    • (2004) J. Pharmacol. Exp. Ther. , vol.308 , pp. 887-895
    • Xu, F.1    Falck, J.R.2    Ortiz De Montellano, P.R.3    Kroetz, D.L.4
  • 108
    • 26944462419 scopus 로고    scopus 로고
    • Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen
    • Yano, J. K., Hsu, M. H., Griffin, K. J., Stout, C. D., Johnson, E. F. (2005). Structures of human microsomal cytochrome P450 2A6 complexed with coumarin and methoxsalen. Nat. Struct. Mol. Biol. 12:822-823.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 822-823
    • Yano, J.K.1    Hsu, M.H.2    Griffin, K.J.3    Stout, C.D.4    Johnson, E.F.5
  • 109
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution
    • Yano, J. K., Wester, M. R., Schoch, G. A., Griffin, K. J., Stout, C. D., Johnson, E. F. (2004). The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J. Biol. Chem. 279:38091-38094.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38091-38094
    • Yano, J.K.1    Wester, M.R.2    Schoch, G.A.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 110
    • 0025058298 scopus 로고
    • cDNA cloning of cytochrome P-450 related to P-450p-2 from the cDNA library of human placenta. Gene structure and expression
    • Yokotani, N., Sogawa, K., Matsubara, S., Gotoh, O., Kusunose, E., Kusunose, M., et al. (1990). cDNA cloning of cytochrome P-450 related to P-450p-2 from the cDNA library of human placenta. Gene structure and expression. Eur. J. Biochem. 187:23-29.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 23-29
    • Yokotani, N.1    Sogawa, K.2    Matsubara, S.3    Gotoh, O.4    Kusunose, E.5    Kusunose, M.6
  • 111
    • 0024416367 scopus 로고
    • Mechanisms of 3-methylindole pneumotoxicity
    • Yost, G. S. (1989). Mechanisms of 3-methylindole pneumotoxicity. Chem. Res. Toxicol. 2:273-279.
    • (1989) Chem. Res. Toxicol. , vol.2 , pp. 273-279
    • Yost, G.S.1
  • 112
    • 0028930148 scopus 로고
    • The rabbit pulmonary cytochrome P450 arachidonic acid metabolic pathway: Characterization and significance
    • Zeldin, D. C., Plitman, J. D., Kobayashi, J., Miller, R. F., Snapper, J. R., Falck, J. R., et al. (1995). The rabbit pulmonary cytochrome P450 arachidonic acid metabolic pathway: characterization and significance. J. Clin. Invest. 95:2150-2160.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2150-2160
    • Zeldin, D.C.1    Plitman, J.D.2    Kobayashi, J.3    Miller, R.F.4    Snapper, J.R.5    Falck, J.R.6
  • 113
    • 0032530321 scopus 로고    scopus 로고
    • Identification of a meander region proline residue critical for heme binding to cytochrome P450: Implications for the catalytic function of human CYP4B1
    • Zheng, Y. M., Fisher, M. B., Yokotani, N., Fujii-Kuriyama, Y., Rettie, A. E. (1998). Identification of a meander region proline residue critical for heme binding to cytochrome P450: implications for the catalytic function of human CYP4B1. Biochemistry 37:12847-12851.
    • (1998) Biochemistry , vol.37 , pp. 12847-12851
    • Zheng, Y.M.1    Fisher, M.B.2    Yokotani, N.3    Fujii-Kuriyama, Y.4    Rettie, A.E.5
  • 114
    • 0037461344 scopus 로고    scopus 로고
    • Covalent heme binding to CYP4B1 via Glu310 and a carbocation porphyrin intermediate
    • Zheng, Y. M., Baer, B. R., Kneller, M. B., Henne, K. R., Kunze, K. L., Rettie, A. E. (2003). Covalent heme binding to CYP4B1 via Glu310 and a carbocation porphyrin intermediate. Biochemistry. 42:4601-4606.
    • (2003) Biochemistry , vol.42 , pp. 4601-4606
    • Zheng, Y.M.1    Baer, B.R.2    Kneller, M.B.3    Henne, K.R.4    Kunze, K.L.5    Rettie, A.E.6
  • 115
    • 0037438020 scopus 로고    scopus 로고
    • Genotyping and site-directed mutagenesis of a cytochrome P450 meander Pro-X-Arg motif critical to CYP4B1 catalysis
    • Zheng, Y. M., Henne, K. R., Charmley, P., Kim, R. B., McCarver, D. G., Cabacungan, E. T., et al. (2003). Genotyping and site-directed mutagenesis of a cytochrome P450 meander Pro-X-Arg motif critical to CYP4B1 catalysis. Toxicol. Appl. Pharmacol. 186:119-126.
    • (2003) Toxicol. Appl. Pharmacol. , vol.186 , pp. 119-126
    • Zheng, Y.M.1    Henne, K.R.2    Charmley, P.3    Kim, R.B.4    McCarver, D.G.5    Cabacungan, E.T.6
  • 116
    • 0020420283 scopus 로고
    • Valproate-induced hepatic injury: Analyses of 23 fatal cases
    • Zimmerman, H. J., Ishak, K. G. (1982). Valproate-induced hepatic injury: analyses of 23 fatal cases. Hepatology 2:591-597.
    • (1982) Hepatology , vol.2 , pp. 591-597
    • Zimmerman, H.J.1    Ishak, K.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.