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Volumn 21, Issue 10, 2007, Pages 2579-2595

Modulation of human CYP19A1 activity by mutant NADPH P450 oxidoreductase

Author keywords

[No Author keywords available]

Indexed keywords

ANDROSTENEDIONE; AROMATASE; CYTOCHROME P450 CYP19A1; OCTANOL; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; UNCLASSIFIED DRUG;

EID: 34948830894     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2007-0245     Document Type: Article
Times cited : (109)

References (90)
  • 1
    • 0024447464 scopus 로고
    • Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2
    • Shephard EA, Phillips IR, Santisteban I, West LF, Palmer CN, Ashworth A, Povey S 1989 Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2. Ann Hum Genet 53:291-301
    • (1989) Ann Hum Genet , vol.53 , pp. 291-301
    • Shephard, E.A.1    Phillips, I.R.2    Santisteban, I.3    West, L.F.4    Palmer, C.N.5    Ashworth, A.6    Povey, S.7
  • 2
    • 34347219795 scopus 로고    scopus 로고
    • Apparent manifesting heterozygosity in p450 oxidoreductase deficiency and its effect on coexisting 21-hydroxylase deficiency
    • Scott RR, Gomes LG, Huang N, Van Vliet G, Miller WL 2007 Apparent manifesting heterozygosity in p450 oxidoreductase deficiency and its effect on coexisting 21-hydroxylase deficiency. J Clin Endocrinol Metab 92:2318-2322
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 2318-2322
    • Scott, R.R.1    Gomes, L.G.2    Huang, N.3    Van Vliet, G.4    Miller, W.L.5
  • 3
    • 0024420756 scopus 로고
    • Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: Complete sequence of human enzyme and NADPH-binding sites
    • Haniu M, McManus ME, Birkett DJ, Lee TD, Shively JE 1989 Structural and functional analysis of NADPH-cytochrome P-450 reductase from human liver: complete sequence of human enzyme and NADPH-binding sites. Biochemistry 28:8639-8645
    • (1989) Biochemistry , vol.28 , pp. 8639-8645
    • Haniu, M.1    McManus, M.E.2    Birkett, D.J.3    Lee, T.D.4    Shively, J.E.5
  • 4
    • 0000305842 scopus 로고
    • The reduction of cytochrome c by xanthine oxidase
    • Horecker BL, Heppel LA 1949 The reduction of cytochrome c by xanthine oxidase. J Biol Chem 178:683-690
    • (1949) J Biol Chem , vol.178 , pp. 683-690
    • Horecker, B.L.1    Heppel, L.A.2
  • 5
    • 0004563140 scopus 로고
    • Triphosphate nucleotide-cytochrome c reductase in liver
    • Horecker BL 1950 Triphosphate nucleotide-cytochrome c reductase in liver. J Biol Chem 183:593-605
    • (1950) J Biol Chem , vol.183 , pp. 593-605
    • Horecker, B.L.1
  • 6
    • 73649173283 scopus 로고
    • Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver
    • Williams Jr CH, Kamin H 1962 Microsomal triphosphopyridine nucleotide-cytochrome c reductase of liver. J Biol Chem 237:587-595
    • (1962) J Biol Chem , vol.237 , pp. 587-595
    • Williams Jr, C.H.1    Kamin, H.2
  • 7
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization, and kinetic studies
    • Phillips AH, Langdon RG 1962 Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization, and kinetic studies. J Biol Chem 237:2652-2660
    • (1962) J Biol Chem , vol.237 , pp. 2652-2660
    • Phillips, A.H.1    Langdon, R.G.2
  • 8
    • 0014670327 scopus 로고
    • Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components
    • Lu AY, Junk KW, Coon MJ 1969 Resolution of the cytochrome P-450-containing ω-hydroxylation system of liver microsomes into three components. J Biol Chem 244:3714-3721
    • (1969) J Biol Chem , vol.244 , pp. 3714-3721
    • Lu, A.Y.1    Junk, K.W.2    Coon, M.J.3
  • 9
    • 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, Shea TM, Masters BSS, Kim JJ 1997 Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. Proc Natl Acad Sci USA 94:8411-8416
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8411-8416
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.S.5    Kim, J.J.6
  • 11
    • 0038152781 scopus 로고    scopus 로고
    • Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences
    • Roman LJ, McLain J, Masters BSS 2003 Chimeric enzymes of cytochrome P450 oxidoreductase and neuronal nitric-oxide synthase reductase domain reveal structural and functional differences. J Biol Chem 278:25700-25707
    • (2003) J Biol Chem , vol.278 , pp. 25700-25707
    • Roman, L.J.1    McLain, J.2    Masters, B.S.S.3
  • 12
    • 0035916295 scopus 로고    scopus 로고
    • Determination of the redox properties of human NADPH-cytochrome P450 reductase
    • Munro AW, Noble MA, Robledo L, Daff SN, Chapman SK 2001 Determination of the redox properties of human NADPH-cytochrome P450 reductase. Biochemistry 40:1956-1963
    • (2001) Biochemistry , vol.40 , pp. 1956-1963
    • Munro, A.W.1    Noble, M.A.2    Robledo, L.3    Daff, S.N.4    Chapman, S.K.5
  • 13
    • 0035800760 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer
    • Hubbard PA, Shen AL, Paschke R, Kasper CB, Kim JJ 2001 NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride and electron transfer. J Biol Chem 276:29163-29170
    • (2001) J Biol Chem , vol.276 , pp. 29163-29170
    • Hubbard, P.A.1    Shen, A.L.2    Paschke, R.3    Kasper, C.B.4    Kim, J.J.5
  • 14
    • 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 DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, Nebert DW 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
  • 15
    • 18844367746 scopus 로고    scopus 로고
    • Minireview: Regulation of steroidogenesis by electron transfer
    • Miller WL 2005 Minireview: regulation of steroidogenesis by electron transfer. Endocrinology 146:2544-2550
    • (2005) Endocrinology , vol.146 , pp. 2544-2550
    • Miller, W.L.1
  • 16
    • 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 2002 Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase. J Biol Chem 277:6536-6541
    • (2002) J Biol Chem , vol.277 , pp. 6536-6541
    • Shen, A.L.1    O'Leary, K.A.2    Kasper, C.B.3
  • 17
    • 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, Davey M, Gundersen TE, Blomhoff R, Adams RH, Tickle C, Wolf CR 2003 Identification of novel roles of the cytochrome P450 system in early embryogenesis: effects on vasculogenesis and retinoic acid homeostasis. Mol Cell Biol 23:6103-6116
    • (2003) Mol Cell Biol , vol.23 , pp. 6103-6116
    • Otto, D.M.1    Henderson, C.J.2    Carrie, D.3    Davey, M.4    Gundersen, T.E.5    Blomhoff, R.6    Adams, R.H.7    Tickle, C.8    Wolf, C.R.9
  • 20
    • 11244288204 scopus 로고    scopus 로고
    • P450 oxidoreductase deficiency: A new disorder of steroidogenesis affecting all microsomal P450 enzymes
    • Pandey AV, Flück CE, Huang N, Tajima T, Fujieda K, Miller WL 2004 P450 oxidoreductase deficiency: a new disorder of steroidogenesis affecting all microsomal P450 enzymes. Endocr Res 30:881-888
    • (2004) Endocr Res , vol.30 , pp. 881-888
    • Pandey, A.V.1    Flück, C.E.2    Huang, N.3    Tajima, T.4    Fujieda, K.5    Miller, W.L.6
  • 21
    • 34248631685 scopus 로고    scopus 로고
    • Biochemical analysis of mutations in P450 oxidoreductase
    • Pandey AV 2006 Biochemical analysis of mutations in P450 oxidoreductase. Biochem Soc Trans 34:1186-1191
    • (2006) Biochem Soc Trans , vol.34 , pp. 1186-1191
    • Pandey, A.V.1
  • 22
    • 4444379764 scopus 로고    scopus 로고
    • P450 oxidoreductase deficiency: A new disorder of steroidogenesis with multiple clinical manifestations
    • Miller WL 2004 P450 oxidoreductase deficiency: a new disorder of steroidogenesis with multiple clinical manifestations. Trends Endocrinol Metab 15:311-315
    • (2004) Trends Endocrinol Metab , vol.15 , pp. 311-315
    • Miller, W.L.1
  • 26
    • 3342918965 scopus 로고    scopus 로고
    • Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome
    • Adachi M, Tachibana K, Asakura Y, Yamamoto T, Hanaki K, Oka A 2004 Compound heterozygous mutations of cytochrome P450 oxidoreductase gene (POR) in two patients with Antley-Bixler syndrome. Am J Med Genet 128A:333-339
    • (2004) Am J Med Genet , vol.128 A , pp. 333-339
    • Adachi, M.1    Tachibana, K.2    Asakura, Y.3    Yamamoto, T.4    Hanaki, K.5    Oka, A.6
  • 28
    • 33644862230 scopus 로고    scopus 로고
    • POR R457H is a global founder mutation causing Antley-Bixler syndrome with autosomal recessive trait
    • Adachi M, Asakura Y, Matsuo M, Yamamoto T, Hanaki K, Arlt W 2006 POR R457H is a global founder mutation causing Antley-Bixler syndrome with autosomal recessive trait. Am J Med Genet A 140:633-635
    • (2006) Am J Med Genet A , vol.140 , pp. 633-635
    • Adachi, M.1    Asakura, Y.2    Matsuo, M.3    Yamamoto, T.4    Hanaki, K.5    Arlt, W.6
  • 30
    • 33646691530 scopus 로고    scopus 로고
    • Cytochrome P450 oxidoreductase deficiency in three patients initially regarded as having 21-hydroxylase deficiency and/or aromatase deficiency: Diagnostic value of urine steroid hormone analysis
    • Fukami M, Hasegawa T, Horikawa R, Ohashi T, Nishimura G, Homma K, Ogata T 2006 Cytochrome P450 oxidoreductase deficiency in three patients initially regarded as having 21-hydroxylase deficiency and/or aromatase deficiency: diagnostic value of urine steroid hormone analysis. Pediatr Res 59:276-280
    • (2006) Pediatr Res , vol.59 , pp. 276-280
    • Fukami, M.1    Hasegawa, T.2    Horikawa, R.3    Ohashi, T.4    Nishimura, G.5    Homma, K.6    Ogata, T.7
  • 32
    • 0024064517 scopus 로고
    • Molecular biology of steroid hormone synthesis
    • Miller WL 1988 Molecular biology of steroid hormone synthesis. Endocr Rev 9:295-318
    • (1988) Endocr Rev , vol.9 , pp. 295-318
    • Miller, W.L.1
  • 33
    • 1942422264 scopus 로고    scopus 로고
    • Aromatase: Biologic relevance of tissue-specific expression
    • Simpson ER 2004 Aromatase: biologic relevance of tissue-specific expression. Semin Reprod Med 22:11-23
    • (2004) Semin Reprod Med , vol.22 , pp. 11-23
    • Simpson, E.R.1
  • 36
    • 0026341320 scopus 로고
    • Assay of aromatase activity
    • Waterman MR, Johnson EF, eds, San Diego: Academic Press;
    • Lephart ED, Simpson ER 1991 Assay of aromatase activity. In: Waterman MR, Johnson EF, eds. Methods in enzymology. San Diego: Academic Press; 477-483
    • (1991) Methods in enzymology , pp. 477-483
    • Lephart, E.D.1    Simpson, E.R.2
  • 37
    • 0032488666 scopus 로고    scopus 로고
    • Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer
    • Auchus RJ, Lee TC, Miller WL 1998 Cytochrome b5 augments the 17,20-lyase activity of human P450c17 without direct electron transfer. J Biol Chem 273:3158-3165
    • (1998) J Biol Chem , vol.273 , pp. 3158-3165
    • Auchus, R.J.1    Lee, T.C.2    Miller, W.L.3
  • 38
    • 33645101080 scopus 로고    scopus 로고
    • An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles
    • Reed JR, Kelley RW, Backes WL 2006 An evaluation of methods for the reconstitution of cytochromes P450 and NADPH P450 reductase into lipid vesicles. Drug Metab Dispos 34:660-666
    • (2006) Drug Metab Dispos , vol.34 , pp. 660-666
    • Reed, J.R.1    Kelley, R.W.2    Backes, W.L.3
  • 39
    • 0028916567 scopus 로고
    • Expression of a recombinant derivative of human aromatase P450 in insect cells utilizing the baculovirus vector system
    • Amarneh B, Simpson ER 1995 Expression of a recombinant derivative of human aromatase P450 in insect cells utilizing the baculovirus vector system. Mol Cell Endocrinol 109:R1-R5
    • (1995) Mol Cell Endocrinol , vol.109
    • Amarneh, B.1    Simpson, E.R.2
  • 40
    • 2942595904 scopus 로고    scopus 로고
    • Characterization of stable human aromatase expressed in E. coli
    • Kagawa N, Hori H, Waterman MR, Yoshioka S 2004 Characterization of stable human aromatase expressed in E. coli. Steroids 69:235-243
    • (2004) Steroids , vol.69 , pp. 235-243
    • Kagawa, N.1    Hori, H.2    Waterman, M.R.3    Yoshioka, S.4
  • 41
    • 34447532545 scopus 로고    scopus 로고
    • Clinical, structural and functional implications of mutations and polymorphisms in human NADPH P450 oxidoreductase
    • Flück CE, Nicolo C, Pandey AV 2007 Clinical, structural and functional implications of mutations and polymorphisms in human NADPH P450 oxidoreductase. Fundam Clin Pharmacol 21:399-410
    • (2007) Fundam Clin Pharmacol , vol.21 , pp. 399-410
    • Flück, C.E.1    Nicolo, C.2    Pandey, A.V.3
  • 42
    • 0034731525 scopus 로고    scopus 로고
    • Differential contributions of NADPH-cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis
    • Shen AL, Kasper CB 2000 Differential contributions of NADPH-cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis. J Biol Chem 275:41087-41091
    • (2000) J Biol Chem , vol.275 , pp. 41087-41091
    • Shen, A.L.1    Kasper, C.B.2
  • 43
    • 0029759441 scopus 로고    scopus 로고
    • Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential
    • Shen AL, Kasper CB 1996 Role of Ser457 of NADPH-cytochrome P450 oxidoreductase in catalysis and control of FAD oxidation-reduction potential. Biochemistry 35:9451-9459
    • (1996) Biochemistry , vol.35 , pp. 9451-9459
    • Shen, A.L.1    Kasper, C.B.2
  • 44
    • 0033605237 scopus 로고    scopus 로고
    • Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase
    • Shen AL, Sem DS, Kasper CB 1999 Mechanistic studies on the reductive half-reaction of NADPH-cytochrome P450 oxidoreductase. J Biol Chem 274:5391-5398
    • (1999) J Biol Chem , vol.274 , pp. 5391-5398
    • Shen, A.L.1    Sem, D.S.2    Kasper, C.B.3
  • 45
    • 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 2006 Diminished FAD binding in the Y459H and V492E Antley-Bixler syndrome mutants of human cytochrome P450 reductase. J Biol Chem 281:35975-35982
    • (2006) J Biol Chem , vol.281 , pp. 35975-35982
    • Marohnic, C.C.1    Panda, S.P.2    Martasek, P.3    Masters, B.S.4
  • 46
    • 0025955439 scopus 로고
    • Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis
    • Graham-Lorence S, Khalil MW, Lorence MC, Mendelson CR, Simpson ER 1991 Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis. J Biol Chem 266:11939-11946
    • (1991) J Biol Chem , vol.266 , pp. 11939-11946
    • Graham-Lorence, S.1    Khalil, M.W.2    Lorence, M.C.3    Mendelson, C.R.4    Simpson, E.R.5
  • 49
    • 33644836657 scopus 로고    scopus 로고
    • Three-dimensional model of the human aromatase enzyme and density functional parameterization of the iron-containing protoporphyrin IX for a molecular dynamics study of heme-cysteinato cytochromes
    • Favia AD, Cavalli A, Masetti M, Carotti A, Recanatini M 2006 Three-dimensional model of the human aromatase enzyme and density functional parameterization of the iron-containing protoporphyrin IX for a molecular dynamics study of heme-cysteinato cytochromes. Proteins 62:1074-1087
    • (2006) Proteins , vol.62 , pp. 1074-1087
    • Favia, A.D.1    Cavalli, A.2    Masetti, M.3    Carotti, A.4    Recanatini, M.5
  • 50
    • 0033346398 scopus 로고    scopus 로고
    • Molecular modeling of human P450c17 (17α-hydroxylase/17,20-lyase): Insights into reaction mechanisms and effects of mutations
    • Auchus RJ, Miller WL 1999 Molecular modeling of human P450c17 (17α-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations. Mol Endocrinol 13:1169-1182
    • (1999) Mol Endocrinol , vol.13 , pp. 1169-1182
    • Auchus, R.J.1    Miller, W.L.2
  • 51
    • 0027375791 scopus 로고
    • Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 α-hydroxylase deficiency
    • Monno S, Ogawa H, Date T, Fujioka M, Miller WL, Kobayashi M 1993 Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 α-hydroxylase deficiency. J Biol Chem 268:25811-25817
    • (1993) J Biol Chem , vol.268 , pp. 25811-25817
    • Monno, S.1    Ogawa, H.2    Date, T.3    Fujioka, M.4    Miller, W.L.5    Kobayashi, M.6
  • 52
    • 33746296018 scopus 로고    scopus 로고
    • Clinical and biochemical description of a novel CYP21A2 gene mutation 962_963insA using a new 3D model for the P450c21 protein
    • Janner M, Pandey AV, Mullis PE, Fluck CE 2006 Clinical and biochemical description of a novel CYP21A2 gene mutation 962_963insA using a new 3D model for the P450c21 protein. Eur J Endocrinol 155:143-151
    • (2006) Eur J Endocrinol , vol.155 , pp. 143-151
    • Janner, M.1    Pandey, A.V.2    Mullis, P.E.3    Fluck, C.E.4
  • 53
    • 0024516824 scopus 로고
    • cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases
    • Hanukoglu I, Gutfinger T 1989 cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. Eur J Biochem 180:479-484
    • (1989) Eur J Biochem , vol.180 , pp. 479-484
    • Hanukoglu, I.1    Gutfinger, T.2
  • 54
    • 0025019734 scopus 로고
    • Redesign of the coenzyme specificity of a dehydrogenase by protein engineering
    • Scrutton NS, Berry A, Perham RN 1990 Redesign of the coenzyme specificity of a dehydrogenase by protein engineering. Nature 343:38-43
    • (1990) Nature , vol.343 , pp. 38-43
    • Scrutton, N.S.1    Berry, A.2    Perham, R.N.3
  • 55
    • 0025885546 scopus 로고
    • NADPH-cytochrome P-450 oxidoreductase. The role of cysteine 566 in catalysis and cofactor binding
    • Shen AL, Christensen MJ, Kasper CB 1991 NADPH-cytochrome P-450 oxidoreductase. The role of cysteine 566 in catalysis and cofactor binding. J Biol Chem 266:19976-19980
    • (1991) J Biol Chem , vol.266 , pp. 19976-19980
    • Shen, A.L.1    Christensen, M.J.2    Kasper, C.B.3
  • 56
    • 0021739143 scopus 로고
    • Structural analysis of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes. Sequences of proteolytic fragments, cysteine-containing peptides, and a NADPH-protected cysteine peptide
    • Haniu M, Iyanagi T, Legesse K, Shively JE 1984 Structural analysis of NADPH-cytochrome P-450 reductase from porcine hepatic microsomes. Sequences of proteolytic fragments, cysteine-containing peptides, and a NADPH-protected cysteine peptide. J Biol Chem 259:13703-13711
    • (1984) J Biol Chem , vol.259 , pp. 13703-13711
    • Haniu, M.1    Iyanagi, T.2    Legesse, K.3    Shively, J.E.4
  • 57
    • 0027366973 scopus 로고
    • Use of aromatase (CYP19) metabolite ratios to characterize electron transfer from NADPH-cytochrome P450 reductase
    • Grogan J, Shou M, Zhou D, Chen S, Korzekwa KR 1993 Use of aromatase (CYP19) metabolite ratios to characterize electron transfer from NADPH-cytochrome P450 reductase. Biochemistry 32:12007-12012
    • (1993) Biochemistry , vol.32 , pp. 12007-12012
    • Grogan, J.1    Shou, M.2    Zhou, D.3    Chen, S.4    Korzekwa, K.R.5
  • 58
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • Backes WL, Kelley RW 2003 Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. Pharmacol Ther 98:221-233
    • (2003) Pharmacol Ther , vol.98 , pp. 221-233
    • Backes, W.L.1    Kelley, R.W.2
  • 59
    • 0028805425 scopus 로고
    • Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c
    • Shen AL, Kasper CB 1995 Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c. J Biol Chem 270:27475-27480
    • (1995) J Biol Chem , vol.270 , pp. 27475-27480
    • Shen, A.L.1    Kasper, C.B.2
  • 60
    • 0030249221 scopus 로고    scopus 로고
    • The interaction of NADPH-P450 reductase with P450: An electrochemical study of the role of the flavin mononucleotide-binding domain
    • Estabrook RW, Shet MS, Fisher CW, Jenkins CM, Waterman MR 1996 The interaction of NADPH-P450 reductase with P450: an electrochemical study of the role of the flavin mononucleotide-binding domain. Arch Biochem Biophys 333:308-315
    • (1996) Arch Biochem Biophys , vol.333 , pp. 308-315
    • Estabrook, R.W.1    Shet, M.S.2    Fisher, C.W.3    Jenkins, C.M.4    Waterman, M.R.5
  • 62
    • 0029738284 scopus 로고    scopus 로고
    • Construction of plasmids and expression in Escherichia coli of enzymatically active fusion proteins containing the heme-domain of a P450 linked to NADPH-P450 reductase
    • Fisher CW, Shet MS, Estabrook RW 1996 Construction of plasmids and expression in Escherichia coli of enzymatically active fusion proteins containing the heme-domain of a P450 linked to NADPH-P450 reductase. Methods Enzymol 272:15-25
    • (1996) Methods Enzymol , vol.272 , pp. 15-25
    • Fisher, C.W.1    Shet, M.S.2    Estabrook, R.W.3
  • 63
    • 0034733026 scopus 로고    scopus 로고
    • Association of cytochromes P450 with their reductases: Opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system
    • Davydov DR, Kariakin AA, Petushkova NA, Peterson JA 2000 Association of cytochromes P450 with their reductases: opposite sign of the electrostatic interactions in P450BM-3 as compared with the microsomal 2B4 system. Biochemistry 39:6489-6497
    • (2000) Biochemistry , vol.39 , pp. 6489-6497
    • Davydov, D.R.1    Kariakin, A.A.2    Petushkova, N.A.3    Peterson, J.A.4
  • 64
    • 0025939628 scopus 로고
    • Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450
    • Nadler SG, Strobel HW 1991 Identification and characterization of an NADPH-cytochrome P450 reductase derived peptide involved in binding to cytochrome P450. Arch Biochem Biophys 290:277-284
    • (1991) Arch Biochem Biophys , vol.290 , pp. 277-284
    • Nadler, S.G.1    Strobel, H.W.2
  • 65
    • 0027216444 scopus 로고
    • Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase
    • Shen S, Strobel HW 1993 Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase. Arch Biochem Biophys 304:257-265
    • (1993) Arch Biochem Biophys , vol.304 , pp. 257-265
    • Shen, S.1    Strobel, H.W.2
  • 66
    • 0026589172 scopus 로고
    • The role of cytochrome P450 lysine residues in the interaction between cytochrome P450IA1 and NADPH-cytochrome P450 reductase
    • Shen S, Strobel HW 1992 The role of cytochrome P450 lysine residues in the interaction between cytochrome P450IA1 and NADPH-cytochrome P450 reductase. Arch Biochem Biophys 294:83-90
    • (1992) Arch Biochem Biophys , vol.294 , pp. 83-90
    • Shen, S.1    Strobel, H.W.2
  • 67
    • 0025755694 scopus 로고
    • Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagen-esis. Interaction with NADPH-cytochrome P450 reductase
    • Shimizu T, Tateishi T, Hatano M, Fujii-Kuriyama Y 1991 Probing the role of lysines and arginines in the catalytic function of cytochrome P450d by site-directed mutagen-esis. Interaction with NADPH-cytochrome P450 reductase. J Biol Chem 266:3372-3375
    • (1991) J Biol Chem , vol.266 , pp. 3372-3375
    • Shimizu, T.1    Tateishi, T.2    Hatano, M.3    Fujii-Kuriyama, Y.4
  • 68
    • 0023972392 scopus 로고
    • Role of electrostatic interactions in the reaction of NADPH-cytochrome P-450 reductase with cytochromes P-450
    • Nadler SG, Strobel HW 1988 Role of electrostatic interactions in the reaction of NADPH-cytochrome P-450 reductase with cytochromes P-450. Arch Biochem Biophys 261:418-429
    • (1988) Arch Biochem Biophys , vol.261 , pp. 418-429
    • Nadler, S.G.1    Strobel, H.W.2
  • 69
    • 0024441228 scopus 로고
    • Cytochrome P-450: Cytochrome P-450 reductase interactions
    • Strobel HW, Nadler SG, Nelson DR 1989 Cytochrome P-450: cytochrome P-450 reductase interactions. Drug Metab Rev 20:519-533
    • (1989) Drug Metab Rev , vol.20 , pp. 519-533
    • Strobel, H.W.1    Nadler, S.G.2    Nelson, D.R.3
  • 71
    • 0029776005 scopus 로고    scopus 로고
    • Yeast expression of animal and plant P450s in optimized redox environments
    • Pompon D, Louerat B, Bronine A, Urban P 1996 Yeast expression of animal and plant P450s in optimized redox environments. Methods Enzymol 272:51-64
    • (1996) Methods Enzymol , vol.272 , pp. 51-64
    • Pompon, D.1    Louerat, B.2    Bronine, A.3    Urban, P.4
  • 72
    • 0027742081 scopus 로고
    • Xenobiotic metabolism in humanized yeast: Engineered yeast cells producing human NADPH-cytochrome P-450 reductase, cytochrome b5, epoxide hydrolase and P-450s
    • Urban P, Truan G, Gautier JC, Pompon D 1993 Xenobiotic metabolism in humanized yeast: engineered yeast cells producing human NADPH-cytochrome P-450 reductase, cytochrome b5, epoxide hydrolase and P-450s. Biochem Soc Trans 21:1028-1034
    • (1993) Biochem Soc Trans , vol.21 , pp. 1028-1034
    • Urban, P.1    Truan, G.2    Gautier, J.C.3    Pompon, D.4
  • 73
    • 0023949565 scopus 로고
    • Novel properties of human placental aromatase as cytochrome P-450: Purification and characterization of a unique form of aromatase
    • Harada N 1988 Novel properties of human placental aromatase as cytochrome P-450: purification and characterization of a unique form of aromatase. J Biochem (Tokyo) 103:106-133
    • (1988) J Biochem (Tokyo) , vol.103 , pp. 106-133
    • Harada, N.1
  • 74
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by x-ray crystallography to 2.05-A resolution
    • Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, Johnson EF 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
  • 75
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl) imidazole at 1.9-A resolution: Insight into the range of P450 conformations and the coordination of redox partner binding
    • Scott EE, White MA, He YA, Johnson EF, Stout CD, Halpert JR 2004 Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl) imidazole at 1.9-A 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
  • 77
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL 1993 Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 234:779-815
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 79
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • Eisenberg D, Luthy R, Bowie JU 1997 VERIFY3D: assessment of protein models with three-dimensional profiles. Methods Enzymol 277:396-404
    • (1997) Methods Enzymol , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 82
    • 0030870075 scopus 로고    scopus 로고
    • Objectively judging the quality of a protein structure from a Ramachandran plot
    • Hooft RW, Sander C, Vriend G 1997 Objectively judging the quality of a protein structure from a Ramachandran plot. Comput Appl Biosci 13:425-430
    • (1997) Comput Appl Biosci , vol.13 , pp. 425-430
    • Hooft, R.W.1    Sander, C.2    Vriend, G.3
  • 83
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J 2000 DaliLite workbench for protein structure comparison. Bioinformatics 16:566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 84
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N, Peitsch MC 1997 SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 85
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend G 1990 WHAT IF: a molecular modeling and drug design program. J Mol Graph 8:52- 56:29
    • (1990) J Mol Graph , vol.8 , Issue.52-56 , pp. 29
    • Vriend, G.1
  • 86
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: Force-field parameterization in crystal space
    • Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G 2004 Making optimal use of empirical energy functions: force-field parameterization in crystal space. Proteins 57:678-683
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 90
    • 21644460933 scopus 로고    scopus 로고
    • Docking essential dynamics eigenstructures
    • Mustard D, Ritchie DW 2005 Docking essential dynamics eigenstructures. Proteins 60:269-274
    • (2005) Proteins , vol.60 , pp. 269-274
    • Mustard, D.1    Ritchie, D.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.