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Volumn 4, Issue 4, 2008, Pages 439-452

P450 oxidoreductase: Genetic polymorphisms and implications for drug metabolism and toxicity

Author keywords

Cytochrome P450 oxidoreductase; Drug metabolism; Genetic polymorphism; Pharmacogenetics; POR; Toxicity

Indexed keywords

ANTINEOPLASTIC AGENT; APAZIQUONE; CYTOCHROME P450 REDUCTASE; MENADIONE; MITOMYCIN C; PARAQUAT; QUINONE DERIVATIVE; TIRAPAZAMINE;

EID: 44349094918     PISSN: 17425255     EISSN: None     Source Type: Journal    
DOI: 10.1517/17425255.4.4.439     Document Type: Review
Times cited : (51)

References (83)
  • 1
    • 0033569516 scopus 로고    scopus 로고
    • Pharmacogenomics: Translating functional genomics into rational therapeutics
    • Evans WE, Relling MV. Pharmacogenomics: translating functional genomics into rational therapeutics. Science 1999;286:487-91
    • (1999) Science , vol.286 , pp. 487-491
    • Evans, W.E.1    Relling, M.V.2
  • 2
    • 4344574336 scopus 로고    scopus 로고
    • Pharmacogenetics: Five decades of therapeutic lessons from genetic diversity
    • Meyer UA. Pharmacogenetics: five decades of therapeutic lessons from genetic diversity. Nat Rev Genet 2004;5:669-76
    • (2004) Nat Rev Genet , vol.5 , pp. 669-676
    • Meyer, U.A.1
  • 4
    • 0000783041 scopus 로고    scopus 로고
    • Evaluation of the genetic component of variability in CYP3A4 activity: A repeated drug administration method
    • Ozdemir V, Kalow W, Tang BK, et al. Evaluation of the genetic component of variability in CYP3A4 activity: a repeated drug administration method. Pharmacogenetics 2000; 10:373-88
    • (2000) Pharmacogenetics , vol.10 , pp. 373-388
    • Ozdemir, V.1    Kalow, W.2    Tang, B.K.3
  • 5
    • 34147162376 scopus 로고    scopus 로고
    • Pharmacogenetics of warfarin: Current status and future challenges
    • Wadelius M, Pirmohamed M. Pharmacogenetics of warfarin: current status and future challenges. Pharmacogenomics J 2007;7:99-111
    • (2007) Pharmacogenomics J , vol.7 , pp. 99-111
    • Wadelius, M.1    Pirmohamed, M.2
  • 6
    • 13844315559 scopus 로고    scopus 로고
    • CYP2C9 gene variants, drug dose, and bleeding risk in warfarin-treated patients: A HuGEnet systematic review and meta-analysis
    • Sanderson S, Emery J, Higgins J. CYP2C9 gene variants, drug dose, and bleeding risk in warfarin-treated patients: a HuGEnet systematic review and meta-analysis. Genet Med 2005;7:97-104
    • (2005) Genet Med , vol.7 , pp. 97-104
    • Sanderson, S.1    Emery, J.2    Higgins, J.3
  • 7
    • 0028210729 scopus 로고
    • Impaired (S)-warfarin metabolism catalysed by the R144C allelic variant of CYP2C9
    • Rettie AE, Wienkers LC, Gonzalez FJ, et al. Impaired (S)-warfarin metabolism catalysed by the R144C allelic variant of CYP2C9. Pharmacogenetics 1994;4:39-42
    • (1994) Pharmacogenetics , vol.4 , pp. 39-42
    • Rettie, A.E.1    Wienkers, L.C.2    Gonzalez, F.J.3
  • 8
    • 0029658591 scopus 로고    scopus 로고
    • The role of the CYP2C9-Leu359 allelic variant in the tolbutamide polymorphism
    • Sullivan-Klose TH, Ghanayem BI, Bell DA, et al. The role of the CYP2C9-Leu359 allelic variant in the tolbutamide polymorphism. Pharmacogenetics 1996;6:341-9
    • (1996) Pharmacogenetics , vol.6 , pp. 341-349
    • Sullivan-Klose, T.H.1    Ghanayem, B.I.2    Bell, D.A.3
  • 9
    • 0028260641 scopus 로고
    • The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans
    • de Morais SM, Wilkinson GR, Blaisdell J, et al. The major genetic defect responsible for the polymorphism of S-mephenytoin metabolism in humans. J Biol Chem 1994;269:15419-22
    • (1994) J Biol Chem , vol.269 , pp. 15419-15422
    • de Morais, S.M.1    Wilkinson, G.R.2    Blaisdell, J.3
  • 10
    • 0028044085 scopus 로고
    • Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese
    • De Movais SM, Wilkinson GR, Blaisdell J, et al. Identification of a new genetic defect responsible for the polymorphism of (S)-mephenytoin metabolism in Japanese. Mol Pharmacol 1994;46:594-8
    • (1994) Mol Pharmacol , vol.46 , pp. 594-598
    • De Movais, S.M.1    Wilkinson, G.R.2    Blaisdell, J.3
  • 11
    • 0028271144 scopus 로고
    • CYP2D6 genotyping and the association with lung cancer susceptibility
    • Wolf CR, Smith CA, Bishop T, et al. CYP2D6 genotyping and the association with lung cancer susceptibility. Pharmacogenetics 1994;4:104-6
    • (1994) Pharmacogenetics , vol.4 , pp. 104-106
    • Wolf, C.R.1    Smith, C.A.2    Bishop, T.3
  • 12
    • 36148976077 scopus 로고    scopus 로고
    • Influence of cytochrome P450 polymorphisms on drug therapies: Pharmacogenetic, pharmacoepigenetic and clinical aspects
    • Ingelman-Sundberg M, Sim SC, Gomez A, Rodriguez-Antona C. Influence of cytochrome P450 polymorphisms on drug therapies: pharmacogenetic, pharmacoepigenetic and clinical aspects. Pharmacol Ther 2007; 116:496-526
    • (2007) Pharmacol Ther , vol.116 , pp. 496-526
    • Ingelman-Sundberg, M.1    Sim, S.C.2    Gomez, A.3    Rodriguez-Antona, C.4
  • 13
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • Wrighton SA, Stevens JC. The human hepatic cytochromes P450 involved in drug metabolism. Crit Rev Toxicol 1992;22:1-21
    • (1992) Crit Rev Toxicol , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 14
    • 0031958417 scopus 로고    scopus 로고
    • Metabolism of Zaleplon by human hepatic microsomal cytochrome P450 isoforms
    • Renwick AB, Mistry H, Ball SE, et al. Metabolism of Zaleplon by human hepatic microsomal cytochrome P450 isoforms. Xenobiotica 1998;28:337-48
    • (1998) Xenobiotica , vol.28 , pp. 337-348
    • Renwick, A.B.1    Mistry, H.2    Ball, S.E.3
  • 15
    • 0023943652 scopus 로고
    • Lack of bimodality in nifedipine plasma kinetics in a large population of healthy subjects
    • Schellens JH, Soons PA, Breimer DD. Lack of bimodality in nifedipine plasma kinetics in a large population of healthy subjects. Biochem Pharmacol 1988;37:2507-10
    • (1988) Biochem Pharmacol , vol.37 , pp. 2507-2510
    • Schellens, J.H.1    Soons, P.A.2    Breimer, D.D.3
  • 17
    • 1642498313 scopus 로고    scopus 로고
    • Functional characterization of four naturally occurring variants of human pregnane X receptor (PXR): One variant causes dramatic loss of both DNA binding activity and the transactivation of the CYP3A4 promoter/enhancer region
    • Koyano S, Kurose K, Saito Y, et al. Functional characterization of four naturally occurring variants of human pregnane X receptor (PXR): one variant causes dramatic loss of both DNA binding activity and the transactivation of the CYP3A4 promoter/enhancer region. Drug Metabol Dispos 2004;32:149-54
    • (2004) Drug Metabol Dispos , vol.32 , pp. 149-154
    • Koyano, S.1    Kurose, K.2    Saito, Y.3
  • 18
    • 23144435169 scopus 로고    scopus 로고
    • Genetic variants of PXR (NR1I2) and CAR (NRID) and their implications in drug metabolism and pharmacogenetics
    • Lamba J, Lamba V, Schuetz E. Genetic variants of PXR (NR1I2) and CAR (NRID) and their implications in drug metabolism and pharmacogenetics. Curr Drug Metab 2005;6:369-83
    • (2005) Curr Drug Metab , vol.6 , pp. 369-383
    • Lamba, J.1    Lamba, V.2    Schuetz, E.3
  • 19
    • 26244454187 scopus 로고    scopus 로고
    • Functional analysis of four naturally occurring variants of human constitutive androstane receptor
    • Ikeda S, Kurose K, Jinno H, et al. Functional analysis of four naturally occurring variants of human constitutive androstane receptor. Mol Genet Metab 2005;86:314-9
    • (2005) Mol Genet Metab , vol.86 , pp. 314-319
    • Ikeda, S.1    Kurose, K.2    Jinno, H.3
  • 20
    • 33645876468 scopus 로고    scopus 로고
    • MDR1 genotype is associated with hepatic cytochrome P450 3A4 basal and induction phenotype
    • Lamba J, Strom S, Venkatammanan R, et al. MDR1 genotype is associated with hepatic cytochrome P450 3A4 basal and induction phenotype. Clin Pharmacol Ther 2006;79:325-38
    • (2006) Clin Pharmacol Ther , vol.79 , pp. 325-338
    • Lamba, J.1    Strom, S.2    Venkatammanan, R.3
  • 21
    • 3242765929 scopus 로고    scopus 로고
    • Mutations in the SLCO1B3 gene affecting the substrate specificity of the hepatocellular uptake transporter OATP1B3 (OATP8)
    • Letschert K, Keppler D, Konig J. Mutations in the SLCO1B3 gene affecting the substrate specificity of the hepatocellular uptake transporter OATP1B3 (OATP8). Pharmacogenetics 2004;14:441-52
    • (2004) Pharmacogenetics , vol.14 , pp. 441-452
    • Letschert, K.1    Keppler, D.2    Konig, J.3
  • 22
    • 18644368162 scopus 로고    scopus 로고
    • A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter
    • Michalski C, Cui Y, Nies AT, et al. A naturally occurring mutation in the SLC21A6 gene causing impaired membrane localization of the hepatocyte uptake transporter. J Biol Chem 2002;277:43058-63
    • (2002) J Biol Chem , vol.277 , pp. 43058-43063
    • Michalski, C.1    Cui, Y.2    Nies, A.T.3
  • 23
    • 0036073404 scopus 로고    scopus 로고
    • Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): Allele frequencies in the Japanese population and functional analysis
    • Nozawa T, Nakajima M, Tamai I, et al. Genetic polymorphisms of human organic anion transporters OATP-C (SLC21A6) and OATP-B (SLC21A9): allele frequencies in the Japanese population and functional analysis. J Pharmacol Exp Ther 2002;302:804-13
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 804-813
    • Nozawa, T.1    Nakajima, M.2    Tamai, I.3
  • 24
    • 0035929574 scopus 로고    scopus 로고
    • Polymorphisms in OATP-C: Identification of multiple allelic variants associated with altered transport activity among European- and African-Americans
    • Tirona RG, Leake BF, Merino G, Kim RB. Polymorphisms in OATP-C: identification of multiple allelic variants associated with altered transport activity among European- and African-Americans. J Biol Chemi 2001;276:35669-75
    • (2001) J Biol Chemi , vol.276 , pp. 35669-35675
    • Tirona, R.G.1    Leake, B.F.2    Merino, G.3    Kim, R.B.4
  • 25
    • 0004563140 scopus 로고
    • Triphosphopyridine nucleotide-cytochrome c reductase in liver
    • Horecker B. Triphosphopyridine nucleotide-cytochrome c reductase in liver. J Biol Chem 1950;183:593-605
    • (1950) J Biol Chem , vol.183 , pp. 593-605
    • Horecker, B.1
  • 26
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleoride-cytochrome c reductase of liver
    • Williams CH Jr, Kamin H. Microsomal triphosphopyridine nucleoride-cytochrome c reductase of liver. J Biol Chem 1962;237:587-95
    • (1962) J Biol Chem , vol.237 , pp. 587-595
    • Williams Jr, C.H.1    Kamin, H.2
  • 27
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • Schacter BA, Nelson EB, Marver HS, Masters BS. Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. J Biol Chem 1972;247:5601-7
    • (1972) J Biol Chem , vol.247 , pp. 5601-5607
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.4
  • 28
    • 0016641043 scopus 로고
    • Solubilization and partial characterization of rat liver squalene epoxidase
    • Ono T, Bloch K. Solubilization and partial characterization of rat liver squalene epoxidase. J Biol Chem 1975;250:1571-9
    • (1975) J Biol Chem , vol.250 , pp. 1571-1579
    • Ono, T.1    Bloch, K.2
  • 29
    • 0034652106 scopus 로고    scopus 로고
    • Evidence for requirement of NADPH-cytochrome P450 oxidoreductase in the microsomal NADPH-sterol Delta7-reductase system
    • Nishino H, Ishibashi T. Evidence for requirement of NADPH-cytochrome P450 oxidoreductase in the microsomal NADPH-sterol Delta7-reductase system. Arch Biochem Biophys 2000;374:293-8
    • (2000) Arch Biochem Biophys , vol.374 , pp. 293-298
    • Nishino, H.1    Ishibashi, T.2
  • 30
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • Enoch HG, Strittmatter P. Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase. J Biol Chem 1979;254:8976-81
    • (1979) J Biol Chem , vol.254 , pp. 8976-8981
    • Enoch, H.G.1    Strittmatter, P.2
  • 31
    • 0019876543 scopus 로고
    • Separate mies for FMN and FAD in catalysis by liver microsomal NADPH-cytochmme P450 reductase
    • Vennilion JL BD, Massey V, Coon MJ. Separate mies for FMN and FAD in catalysis by liver microsomal NADPH-cytochmme P450 reductase. J Biol Chem 1981;256:266-77
    • (1981) J Biol Chem , vol.256 , pp. 266-277
    • Vennilion, J.B.1    Massey, V.2    Coon, M.J.3
  • 32
    • 0030781147 scopus 로고    scopus 로고
    • Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: Rapid reduction in the absence of substrate and variations among cytochrome P450 systems
    • Guengerich FP, Johnson WW. Kinetics of ferric cytochrome P450 reduction by NADPH-cytochrome P450 reductase: rapid reduction in the absence of substrate and variations among cytochrome P450 systems. Biochemistry 1997;36:14741-50
    • (1997) Biochemistry , vol.36 , pp. 14741-14750
    • Guengerich, F.P.1    Johnson, W.W.2
  • 33
    • 0015032258 scopus 로고
    • Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions
    • Hildebrandt A, Estabrook RW. Evidence for the participation of cytochrome b 5 in hepatic microsomal mixed-function oxidation reactions. Arch Biochem Biophys 1971;143:66-79
    • (1971) Arch Biochem Biophys , vol.143 , pp. 66-79
    • Hildebrandt, A.1    Estabrook, R.W.2
  • 34
    • 0019573721 scopus 로고
    • Cytochrome b5 as electron donor for oxy-cytochrome P450
    • Noshiro M, Ullrich V, Omura T. Cytochrome b5 as electron donor for oxy-cytochrome P450. Eur J Biochem 1981;116:521-6
    • (1981) Eur J Biochem , vol.116 , pp. 521-526
    • Noshiro, M.1    Ullrich, V.2    Omura, T.3
  • 35
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich FP. Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem Res Toxicol 2001;14:611-50
    • (2001) Chem Res Toxicol , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 36
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • Wang M, Roberts DL, Paschke R, et al. Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc Nad Acad Sci USA 1997;94:8411-6
    • (1997) Proc Nad Acad Sci USA , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3
  • 37
    • 0035800760 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard PA, Shen AL, Paschke R, et al. NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer. J Biol Chem 2001;276:29163-70
    • (2001) J Biol Chem , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3
  • 38
    • 0035916251 scopus 로고    scopus 로고
    • Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains
    • Gutierrez A, Lian LY, Wolf CR, et al. Stopped-flow kinetic studies of flavin reduction in human cytochrome P450 reductase and its component domains. Biochemistry 2001;40:1964-75
    • (2001) Biochemistry , vol.40 , pp. 1964-1975
    • Gutierrez, A.1    Lian, L.Y.2    Wolf, C.R.3
  • 39
    • 0037046154 scopus 로고    scopus 로고
    • Relaxation kinetics of cytochrome P450 reductase: Internal electron transfer is limited by conformational change and regulated by coenzyme binding
    • Gutierrez A, Paine M, Wolf CR, et al. Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding. Biochemistry 2002;41:4626-37
    • (2002) Biochemistry , vol.41 , pp. 4626-4637
    • Gutierrez, A.1    Paine, M.2    Wolf, C.R.3
  • 40
    • 32244437847 scopus 로고    scopus 로고
    • Global effects of the energetics of coenzyme binding: NADPH controls the protein interaction properties of human cytochrome P450 reductase
    • Grunau A, Paine MJ, Ladbury JE, Gutierrez A. Global effects of the energetics of coenzyme binding: NADPH controls the protein interaction properties of human cytochrome P450 reductase. Biochemistry 2006;45:1421-34
    • (2006) Biochemistry , vol.45 , pp. 1421-1434
    • Grunau, A.1    Paine, M.J.2    Ladbury, J.E.3    Gutierrez, A.4
  • 41
    • 33646681244 scopus 로고    scopus 로고
    • Cytochromes P450: A family of proteins and scientists - understanding their relationships
    • Sue Masters B, Marohnic CC. Cytochromes P450: a family of proteins and scientists - understanding their relationships. Drug Metab Rev 2006;38:209-25
    • (2006) Drug Metab Rev , vol.38 , pp. 209-225
    • Sue Masters, B.1    Marohnic, C.C.2
  • 42
    • 0037527821 scopus 로고    scopus 로고
    • Electron transfer in human cytochrome P450 reductase
    • Gutierrez A, Grunau A, Paine M, et al. Electron transfer in human cytochrome P450 reductase. Biochem Soc Trans 2003;31:497-501
    • (2003) Biochem Soc Trans , vol.31 , pp. 497-501
    • Gutierrez, A.1    Grunau, A.2    Paine, M.3
  • 43
    • 0014485104 scopus 로고
    • Studies on the rate of reduction of hepatic microsomal cytochrome P-450 by reduced nicotinamide adenine dinucleotide phosphate: Effect of drug substrates
    • Gigon PL, Gram TE, Gillette JR. Studies on the rate of reduction of hepatic microsomal cytochrome P-450 by reduced nicotinamide adenine dinucleotide phosphate: effect of drug substrates. Mol Pharmacol 1969;5:109-22
    • (1969) Mol Pharmacol , vol.5 , pp. 109-122
    • Gigon, P.L.1    Gram, T.E.2    Gillette, J.R.3
  • 45
    • 0041468898 scopus 로고    scopus 로고
    • Identification of novel roles of the cytochrome p450 system in early embryogenesis: Effects on vasculogenesis and retinoic acid homeostasis
    • Otto DM, Henderson CJ, Carrie D, et al. Identification of novel roles of the cytochrome p450 system in early embryogenesis: effects on vasculogenesis and retinoic acid homeostasis. Mol Cell Biol 2003;23:6103-16
    • (2003) Mol Cell Biol , vol.23 , pp. 6103-6116
    • Otto, D.M.1    Henderson, C.J.2    Carrie, D.3
  • 46
    • 0037155271 scopus 로고    scopus 로고
    • Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase
    • Shen AL, O'Leary KA, Kasper CB. Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase. J Biol Chem 2002;277:6536-41
    • (2002) J Biol Chem , vol.277 , pp. 6536-6541
    • Shen, A.L.1    O'Leary, K.A.2    Kasper, C.B.3
  • 47
    • 33847018823 scopus 로고    scopus 로고
    • Rescue of cytochrome P450 oxidoreductase (Por) mouse mutants reveals functions in vasculogenesis, brain and limb patterning linked to retinoic acid homeostasis
    • Ribes V, Otto DM, Dickmann L, et al. Rescue of cytochrome P450 oxidoreductase (Por) mouse mutants reveals functions in vasculogenesis, brain and limb patterning linked to retinoic acid homeostasis. Dev Biol 2007;303:66-81
    • (2007) Dev Biol , vol.303 , pp. 66-81
    • Ribes, V.1    Otto, D.M.2    Dickmann, L.3
  • 48
    • 0038507099 scopus 로고    scopus 로고
    • Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: Impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase
    • Gu J, Weng Y, Zhang QY, et al. Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase. J Biol Chem 2003;278:25895-901
    • (2003) J Biol Chem , vol.278 , pp. 25895-25901
    • Gu, J.1    Weng, Y.2    Zhang, Q.Y.3
  • 49
    • 0037790603 scopus 로고    scopus 로고
    • Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase
    • Henderson CJ, Otto DM, Carrie D, et al. Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase. J Biol Chem 2003;278:13480-6
    • (2003) J Biol Chem , vol.278 , pp. 13480-13486
    • Henderson, C.J.1    Otto, D.M.2    Carrie, D.3
  • 50
    • 35649019357 scopus 로고    scopus 로고
    • The disruption of hepatic cytochrome P450 reductase alters mouse lipid metabolism
    • Mutch DM, Klocke B, Morrison P, et al. The disruption of hepatic cytochrome P450 reductase alters mouse lipid metabolism. J Proteome Res 2007;6:3976-84
    • (2007) J Proteome Res , vol.6 , pp. 3976-3984
    • Mutch, D.M.1    Klocke, B.2    Morrison, P.3
  • 51
    • 0024447464 scopus 로고
    • Isolation of a human cytochrome P450 reductase cDNA clone and localization of the corresponding gene to chromosome 7ql1.2
    • Shephard EA, Phillips IR, Santisteban I, et al. Isolation of a human cytochrome P450 reductase cDNA clone and localization of the corresponding gene to chromosome 7ql1.2. Ann Hum Genet 1989;53:291-301
    • (1989) Ann Hum Genet , vol.53 , pp. 291-301
    • Shephard, E.A.1    Phillips, I.R.2    Santisteban, I.3
  • 52
    • 0141541805 scopus 로고    scopus 로고
    • Investigating single nucleotide polymorphism (SNP) density in the human genome and its implications for molecular evolution
    • Zhao Z, Fu YX, Hewett-Emmett D, Boenvinkle E. Investigating single nucleotide polymorphism (SNP) density in the human genome and its implications for molecular evolution. Gene 2003;312:207-13
    • (2003) Gene , vol.312 , pp. 207-213
    • Zhao, Z.1    Fu, Y.X.2    Hewett-Emmett, D.3    Boenvinkle, E.4
  • 53
    • 44349086618 scopus 로고    scopus 로고
    • Available from: http://www.ncbi.nlm.nih.gov/SNP/ snp_ref.cgi?locusId=5447&chooseRs=all [Build 128, revised by May 25, 2006]
    • Available from: http://www.ncbi.nlm.nih.gov/SNP/ snp_ref.cgi?locusId=5447&chooseRs=all [Build 128, revised by May 25, 2006]
  • 54
    • 33747495541 scopus 로고    scopus 로고
    • P450 oxidoreductase deficiency: A new form of congenital adrenal hyperplasia
    • Flück CE, Miller WL. P450 oxidoreductase deficiency: a new form of congenital adrenal hyperplasia. Curr Opin Pediatr 2006;18:435-41
    • (2006) Curr Opin Pediatr , vol.18 , pp. 435-441
    • Flück, C.E.1    Miller, W.L.2
  • 55
    • 20244367932 scopus 로고    scopus 로고
    • Diversity and function of mutations in p450 oxidoreductase in patients with Antley-Bixler syndrome and disordered steroidogenesis
    • Huang N, Pandey AV, Agrawal V, et al. Diversity and function of mutations in p450 oxidoreductase in patients with Antley-Bixler syndrome and disordered steroidogenesis. Am J Hum Genet 2005;76:729-49
    • (2005) Am J Hum Genet , vol.76 , pp. 729-749
    • Huang, N.1    Pandey, A.V.2    Agrawal, V.3
  • 56
    • 33846214395 scopus 로고    scopus 로고
    • Congenital adrenal hyperplasia and P450 oxidoreductase deficiency
    • Krone N, Dhir V, Ivison HE, Arlt W. Congenital adrenal hyperplasia and P450 oxidoreductase deficiency. Clin Endocrinol 2007;66:162-72
    • (2007) Clin Endocrinol , vol.66 , pp. 162-172
    • Krone, N.1    Dhir, V.2    Ivison, H.E.3    Arlt, W.4
  • 57
    • 38049075709 scopus 로고    scopus 로고
    • P450 oxidoreductase deficiency and Andey-Bixler syndrome
    • Arlt W. P450 oxidoreductase deficiency and Andey-Bixler syndrome. Rev Endocr Metab Dis 2007;8:301-7
    • (2007) Rev Endocr Metab Dis , vol.8 , pp. 301-307
    • Arlt, W.1
  • 58
    • 0032996258 scopus 로고    scopus 로고
    • A male patient presenting with major clinical symptoms of glucocorticoid deficiency and skeletal dysplasia, showing a steroid pattern compatible with 17alpha-hydroxylase/ 17,20-1yase deficiency, but without obvious CYP17 gene mutations
    • Adachi M, Tachibana K, Asakura Y, et al. A male patient presenting with major clinical symptoms of glucocorticoid deficiency and skeletal dysplasia, showing a steroid pattern compatible with 17alpha-hydroxylase/ 17,20-1yase deficiency, but without obvious CYP17 gene mutations. Endocr J 1999;46:285-92
    • (1999) Endocr J , vol.46 , pp. 285-292
    • Adachi, M.1    Tachibana, K.2    Asakura, Y.3
  • 59
    • 0034059969 scopus 로고    scopus 로고
    • Evidence for digenic inheritance in some cases of Antley-Bixler syndrome?
    • Reardon W, Smith A, Honour JW, et al. Evidence for digenic inheritance in some cases of Antley-Bixler syndrome? J Med Genet 2000;37:26-32
    • (2000) J Med Genet , vol.37 , pp. 26-32
    • Reardon, W.1    Smith, A.2    Honour, J.W.3
  • 60
    • 0022590907 scopus 로고
    • Congenital adrenal hyperplasia
    • Miller WL. Congenital adrenal hyperplasia. N Engl J Med 1986;314:1521-2
    • (1986) N Engl J Med , vol.314 , pp. 1521-1522
    • Miller, W.L.1
  • 61
    • 10744224515 scopus 로고    scopus 로고
    • Mutant P450 oxidoreductase causes disordered steroidngenesis with and without Antley-Bixler syndrome
    • Flück CE, Tajima T, Pandey AV, et al. Mutant P450 oxidoreductase causes disordered steroidngenesis with and without Antley-Bixler syndrome. Nature Genet 2004;36:228-50
    • (2004) Nature Genet , vol.36 , pp. 228-250
    • Flück, C.E.1    Tajima, T.2    Pandey, A.V.3
  • 62
    • 3042613405 scopus 로고    scopus 로고
    • Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: Analytical study
    • Arlt W, Walker EA, Draper N, et al. Congenital adrenal hyperplasia caused by mutant P450 oxidoreductase and human androgen synthesis: analytical study. Lancet 2004;363:2128-35
    • (2004) Lancet , vol.363 , pp. 2128-2135
    • Arlt, W.1    Walker, E.A.2    Draper, N.3
  • 63
    • 19944429961 scopus 로고    scopus 로고
    • Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: Molecular and clinical studies in 10 patients
    • Fukami M, Horikawa R, Nagai T, et al. Cytochrome P450 oxidoreductase gene mutations and Antley-Bixler syndrome with abnormal genitalia and/or impaired steroidogenesis: molecular and clinical studies in 10 patients. J Clin Endocrin Metab 2005;90:414-26
    • (2005) J Clin Endocrin Metab , vol.90 , pp. 414-426
    • Fukami, M.1    Horikawa, R.2    Nagai, T.3
  • 64
    • 34248582836 scopus 로고    scopus 로고
    • A variant in the cytochrome p450 oxidoreductase gene is associated with breast cancer risk in African Americans
    • Haiman CA, Setiawan VW, Xia LY, et al. A variant in the cytochrome p450 oxidoreductase gene is associated with breast cancer risk in African Americans. Cancer Res 2007;67:3565-8
    • (2007) Cancer Res , vol.67 , pp. 3565-3568
    • Haiman, C.A.1    Setiawan, V.W.2    Xia, L.Y.3
  • 65
    • 19944426178 scopus 로고    scopus 로고
    • Transgenic mice with a hypomorphic NADPH-cytochrome P450 reductase gene: Effects on development, reproduction, and microsomal cytochrome P450
    • Wu L, Gu J, Cui H, et al. Transgenic mice with a hypomorphic NADPH-cytochrome P450 reductase gene: effects on development, reproduction, and microsomal cytochrome P450. J Pharmacol Exp Ther 2005;312:35-43
    • (2005) J Pharmacol Exp Ther , vol.312 , pp. 35-43
    • Wu, L.1    Gu, J.2    Cui, H.3
  • 66
  • 67
    • 38549085263 scopus 로고    scopus 로고
    • Genetic polymorphisms in cytochrome P450 oxidoreductase influence microsomal P450-catalyzed drug metabolism
    • Hart S, Wang S, Nakamoto K, et al. Genetic polymorphisms in cytochrome P450 oxidoreductase influence microsomal P450-catalyzed drug metabolism. Pharmacogenet Genom 2008;18:11-24
    • (2008) Pharmacogenet Genom , vol.18 , pp. 11-24
    • Hart, S.1    Wang, S.2    Nakamoto, K.3
  • 68
    • 40349092943 scopus 로고    scopus 로고
    • Genetics of P450 oxidoreductase, sequence variation in 842 individuals of four ethnicities and activities of 15 missense mutations
    • Huang N, Agrawal V, Giacomini KM, Miller WL. Genetics of P450 oxidoreductase, sequence variation in 842 individuals of four ethnicities and activities of 15 missense mutations. Proc Natl Acad Sci USA 2008;105:1733-8
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 1733-1738
    • Huang, N.1    Agrawal, V.2    Giacomini, K.M.3    Miller, W.L.4
  • 69
    • 33845967142 scopus 로고    scopus 로고
    • Diminished FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase
    • Marohnic CC, Panda SP, Martasek P, Masters BS. Diminished FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase. J Biol Chemi 2006;281:35975-82
    • (2006) J Biol Chemi , vol.281 , pp. 35975-35982
    • Marohnic, C.C.1    Panda, S.P.2    Martasek, P.3    Masters, B.S.4
  • 70
    • 34547465321 scopus 로고    scopus 로고
    • Differential inhibition of CYPI7AI and CYP21A2 activities by the P450 oxidoreductase mutant A287P
    • Dhir V, Ivison HE, Krone N, et al. Differential inhibition of CYPI7AI and CYP21A2 activities by the P450 oxidoreductase mutant A287P. Mol Endocrinol 2007;21:1958-68
    • (2007) Mol Endocrinol , vol.21 , pp. 1958-1968
    • Dhir, V.1    Ivison, H.E.2    Krone, N.3
  • 71
    • 33645818541 scopus 로고    scopus 로고
    • Effect of genetic variation on human cytochrome p450 reductase-mediated paraquat cytotoxicity
    • Han JF, Wang SL, He XY, et al. Effect of genetic variation on human cytochrome p450 reductase-mediated paraquat cytotoxicity. Toxicol Sci 2006;91:42-8
    • (2006) Toxicol Sci , vol.91 , pp. 42-48
    • Han, J.F.1    Wang, S.L.2    He, X.Y.3
  • 72
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P450-containing omega-hydroxylation system of liver microsomes into three components
    • Lu AY, Junk KW, Coon MJ. Resolution of the cytochrome P450-containing omega-hydroxylation system of liver microsomes into three components. J Biol Chemi 1969;244:3714-21
    • (1969) J Biol Chemi , vol.244 , pp. 3714-3721
    • Lu, A.Y.1    Junk, K.W.2    Coon, M.J.3
  • 73
    • 0013791038 scopus 로고
    • Studies on menadione reductase of baker's yeast. II. Inhibition of the enzyme activity by NAD and stimulation of that by p-chloromercuribenzoate
    • Misaka E, Nakanishi K. Studies on menadione reductase of baker's yeast. II. Inhibition of the enzyme activity by NAD and stimulation of that by p-chloromercuribenzoate. J Biochem 1965;58:1-6
    • (1965) J Biochem , vol.58 , pp. 1-6
    • Misaka, E.1    Nakanishi, K.2
  • 74
    • 0018741206 scopus 로고
    • NADPH cytochrome P450 reductase activation of quinone anticancer agents to free radicals
    • Bachur NR GS, Gee MV, Kon H. NADPH cytochrome P450 reductase activation of quinone anticancer agents to free radicals. Proc Natl Acad Sci USA 1979;76:954-7
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 954-957
    • Bachur, N.G.1    Gee, M.V.2    Kon, H.3
  • 75
    • 0024324086 scopus 로고
    • Molecular enzymology of the reductive bioactivation of hypoxic cell cytotoxins
    • Walton MI, Wolf CR, Workman P. Molecular enzymology of the reductive bioactivation of hypoxic cell cytotoxins. Int J Radiat Oncol Biol Phys 1989;16:983-6
    • (1989) Int J Radiat Oncol Biol Phys , vol.16 , pp. 983-986
    • Walton, M.I.1    Wolf, C.R.2    Workman, P.3
  • 76
    • 0033961216 scopus 로고    scopus 로고
    • The relative importance of NADPH: Cytochrome c (P450) reductase for determining the sensitivity of human tumour cells to the indolequinone EO9 and related analogues lacking functionality at the C-2 and C-3 positions
    • Saunders MP, Jaffar M, Patterson AV, Nolan J, et al. The relative importance of NADPH: cytochrome c (P450) reductase for determining the sensitivity of human tumour cells to the indolequinone EO9 and related analogues lacking functionality at the C-2 and C-3 positions. Biochem Pharmacol 2000;59:993-6
    • (2000) Biochem Pharmacol , vol.59 , pp. 993-996
    • Saunders, M.P.1    Jaffar, M.2    Patterson, A.V.3    Nolan, J.4
  • 77
    • 0028867912 scopus 로고
    • Importance of P450 reductase activity in determining sensitivity of breast tumour cells to the bioreductive drug, tirapazamine (SR 4233)
    • Pattersoa AV, Barham HM, Chinje EC, et al. Importance of P450 reductase activity in determining sensitivity of breast tumour cells to the bioreductive drug, tirapazamine (SR 4233). Br J Cancer 1995;72:1144-50
    • (1995) Br J Cancer , vol.72 , pp. 1144-1150
    • Pattersoa, A.V.1    Barham, H.M.2    Chinje, E.C.3
  • 78
    • 0026642263 scopus 로고
    • The role of cytochrome P450 and cytochrome P450 reductase in the reductive bioactivation of the novel benzotriazine di-N-oxide hypoxic cytotoxin 3-amino-1,2,4-benzotriazine-1,4-dioxide (SR 4233, WIN 59075) by mouse liver
    • Walton MI, Wolf CR, Workman P. The role of cytochrome P450 and cytochrome P450 reductase in the reductive bioactivation of the novel benzotriazine di-N-oxide hypoxic cytotoxin 3-amino-1,2,4-benzotriazine-1,4-dioxide (SR 4233, WIN 59075) by mouse liver. Biochem Pharmacol 1992;44:251-9
    • (1992) Biochem Pharmacol , vol.44 , pp. 251-259
    • Walton, M.I.1    Wolf, C.R.2    Workman, P.3
  • 79
    • 0030738399 scopus 로고    scopus 로고
    • Adaptation of human tumor cells to tirapazamine under aerobic conditions: Implications of increased antioxidant enzyme activity to mechanism of aerobic cytotoxicity
    • Elwell JH, Siim BG, Evans JW, Brown JM. Adaptation of human tumor cells to tirapazamine under aerobic conditions: implications of increased antioxidant enzyme activity to mechanism of aerobic cytotoxicity. Biochem Pharmacol 1997;54:249-57
    • (1997) Biochem Pharmacol , vol.54 , pp. 249-257
    • Elwell, J.H.1    Siim, B.G.2    Evans, J.W.3    Brown, J.M.4
  • 80
    • 0033653205 scopus 로고    scopus 로고
    • Tirapazamine: A bioreductive anticancer drug that exploits tumour hypoxia
    • Denny WA, Wilson WR. Tirapazamine: a bioreductive anticancer drug that exploits tumour hypoxia. Expert Opin Investig Drugs 2000;9:2889-901
    • (2000) Expert Opin Investig Drugs , vol.9 , pp. 2889-2901
    • Denny, W.A.1    Wilson, W.R.2
  • 81
    • 33845936862 scopus 로고    scopus 로고
    • Genetic variation of human cytochrome p450 reductase as a potential biomarker for mitomycin C-induced cytotoxicity
    • Wang SL, Han JF, He XY, et al. Genetic variation of human cytochrome p450 reductase as a potential biomarker for mitomycin C-induced cytotoxicity. Drug Metab Dispos 2007;35:176-9
    • (2007) Drug Metab Dispos , vol.35 , pp. 176-179
    • Wang, S.L.1    Han, J.F.2    He, X.Y.3
  • 82
    • 0019193338 scopus 로고
    • Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids
    • Benedetti A, Comporti M, Esterbauer H. Identification of 4-hydroxynonenal as a cytotoxic product originating from the peroxidation of liver microsomal lipids. Biochim Biophys Acta 1980;620:281-96
    • (1980) Biochim Biophys Acta , vol.620 , pp. 281-296
    • Benedetti, A.1    Comporti, M.2    Esterbauer, H.3
  • 83
    • 0022392099 scopus 로고
    • Paraquat and ferritin-dependent lipid peroxidation
    • Saito M, Thomas CE, Aust SD. Paraquat and ferritin-dependent lipid peroxidation. J Free Rad Biol Med 1985;1:179-85
    • (1985) J Free Rad Biol Med , vol.1 , pp. 179-185
    • Saito, M.1    Thomas, C.E.2    Aust, S.D.3


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