메뉴 건너뛰기




Volumn 8, Issue , 2008, Pages

The P450 oxidoreductase, RedA, controls development beyond the mound stage in Dictyostelium discoideum

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450; OXIDOREDUCTASE; COMPLEMENTARY DNA; PROTOZOAL RNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

EID: 40049111839     PISSN: None     EISSN: 1471213X     Source Type: Journal    
DOI: 10.1186/1471-213X-8-8     Document Type: Article
Times cited : (5)

References (60)
  • 1
    • 0019876543 scopus 로고
    • Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase
    • 6778861
    • Separate roles for FMN and FAD in catalysis by liver microsomal NADPH-cytochrome P-450 reductase. JL Vermilion DP Ballou V Massey MJ Coon, J Biol Chem 1981 256 266 77 6778861
    • (1981) J Biol Chem , vol.256 , pp. 266-77
    • Vermilion, J.L.1    Ballou, D.P.2    Massey, V.3    Coon, M.J.4
  • 2
    • 0030873316 scopus 로고    scopus 로고
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
    • 9237990. 10.1073/pnas.94.16.8411
    • Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes. M Wang DL Roberts R Paschke TM Shea BS Masters JJ Kim, Proc Natl Acad Sci USA 1997 94 8411 6 9237990 10.1073/pnas.94.16.8411
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 8411-6
    • Wang, M.1    Roberts, D.L.2    Paschke, R.3    Shea, T.M.4    Masters, B.S.5    Kim, J.J.6
  • 3
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • 10.1021/tx0002583. 11409933
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. FP Guengerich, Chem Res Toxicol 2001 14 611 50 10.1021/tx0002583 11409933
    • (2001) Chem Res Toxicol , vol.14 , pp. 611-50
    • Guengerich, F.P.1
  • 4
    • 0033072718 scopus 로고    scopus 로고
    • Pharmacogenetics of cytochromes P450
    • 25-137. 10575648
    • Pharmacogenetics of cytochromes P450. JA Hasler, Mol Aspects Med 1999 20 12 24 25-137 10575648
    • (1999) Mol Aspects Med , vol.20 , pp. 12-24
    • Hasler, J.A.1
  • 5
    • 0025976756 scopus 로고
    • An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals
    • 10.1016/0968-0004(91)90059-5. 1908607
    • An unusual yet strongly conserved flavoprotein reductase in bacteria and mammals. TD Porter, Trends Biochem Sci 1991 16 154 8 10.1016/0968-0004(91)90059- 5 1908607
    • (1991) Trends Biochem Sci , vol.16 , pp. 154-8
    • Porter, T.D.1
  • 7
    • 0035929601 scopus 로고    scopus 로고
    • Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation
    • 10.1074/jbc.M103707200. 11466310
    • Human methionine synthase reductase, a soluble P-450 reductase-like dual flavoprotein, is sufficient for NADPH-dependent methionine synthase activation. H Olteanu R Banerjee, J Biol Chem 2001 276 35558 63 10.1074/jbc.M103707200 11466310
    • (2001) J Biol Chem , vol.276 , pp. 35558-63
    • Olteanu, H.1    Banerjee, R.2
  • 9
    • 0023044638 scopus 로고
    • NADPH-cytochrome P-450 oxidoreductase: Flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins
    • 10.1021/bi00355a036. 3085707
    • NADPH-cytochrome P-450 oxidoreductase: flavin mononucleotide and flavin adenine dinucleotide domains evolved from different flavoproteins. TD Porter CB Kasper, Biochemistry 1986 25 1682 7 10.1021/bi00355a036 3085707
    • (1986) Biochemistry , vol.25 , pp. 1682-7
    • Porter, T.D.1    Kasper, C.B.2
  • 10
    • 0015501157 scopus 로고
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
    • 4113125
    • Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. BA Schacter EB Nelson HS Marver BS Masters, J Biol Chem 1972 247 3601 7 4113125
    • (1972) J Biol Chem , vol.247 , pp. 3601-7
    • Schacter, B.A.1    Nelson, E.B.2    Marver, H.S.3    Masters, B.S.4
  • 11
    • 0018801347 scopus 로고
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase
    • 113406
    • Cytochrome b5 reduction by NADPH-cytochrome P-450 reductase. HG Enoch P Strittmatter, J Biol Chem 1979 254 8976 81 113406
    • (1979) J Biol Chem , vol.254 , pp. 8976-81
    • Enoch, H.G.1    Strittmatter, P.2
  • 12
    • 0017339034 scopus 로고
    • Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system
    • 403952
    • Involvement of NADPH-cytochrome c reductase in the rat liver squalene epoxidase system. T Ono S Ozasa F Hasegawa Y Imai, Biochim Biophys Acta 1977 486 401 7 403952
    • (1977) Biochim Biophys Acta , vol.486 , pp. 401-7
    • Ono, T.1    Ozasa, S.2    Hasegawa, F.3    Imai, Y.4
  • 13
    • 0033199227 scopus 로고    scopus 로고
    • Cytochrome P450 and the individuality of species
    • 10.1006/abbi.1999.1352. 10462435
    • Cytochrome P450 and the individuality of species. DR Nelson, Arch Biochem Biophys 1999 369 1 10 10.1006/abbi.1999.1352 10462435
    • (1999) Arch Biochem Biophys , vol.369 , pp. 1-10
    • Nelson, D.R.1
  • 14
    • 0021956406 scopus 로고
    • Chromosomal assignments of genes coding for components of the mixed-function oxidase system in mice. Genetic localization of the cytochrome P-450PCN and P-450PB gene families and the NADPH-cytochrome P-450 oxidoreductase and epoxide hydratase genes
    • 3917435
    • Chromosomal assignments of genes coding for components of the mixed-function oxidase system in mice. Genetic localization of the cytochrome P-450PCN and P-450PB gene families and the NADPH-cytochrome P-450 oxidoreductase and epoxide hydratase genes. DL Simmons PA Lalley CB Kasper, J Biol Chem 1985 260 515 21 3917435
    • (1985) J Biol Chem , vol.260 , pp. 515-21
    • Simmons, D.L.1    Lalley, P.A.2    Kasper, C.B.3
  • 15
    • 0024447464 scopus 로고
    • Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2
    • 10.1111/j.1469-1809.1989.tb01798.x. 2516426
    • Isolation of a human cytochrome P-450 reductase cDNA clone and localization of the corresponding gene to chromosome 7q11.2. EA Shephard IR Phillips I Santisteban LF West CN Palmer A Ashworth S Povey, Ann Hum Genet 1989 53 Pt 4 291 301 10.1111/j.1469-1809.1989.tb01798.x 2516426
    • (1989) Ann Hum Genet , vol.53 , Issue.PART 4 , 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
  • 16
    • 0024322441 scopus 로고
    • Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole
    • 10.1016/S0006-291X(89)80139-1. 2543395
    • Disruption of the Saccharomyces cerevisiae gene for NADPH-cytochrome P450 reductase causes increased sensitivity to ketoconazole. TR Sutter JC Loper, Biochem Biophys Res Commun 1989 160 1257 66 10.1016/S0006-291X(89)80139-1 2543395
    • (1989) Biochem Biophys Res Commun , vol.160 , pp. 1257-66
    • Sutter, T.R.1    Loper, J.C.2
  • 17
    • 0031000922 scopus 로고    scopus 로고
    • Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: Pronounced expression in antennae may be related to odorant clearance
    • 10.1016/S0378-1119(96)00851-7. 9168130
    • Drosophila melanogaster NADPH-cytochrome P450 oxidoreductase: pronounced expression in antennae may be related to odorant clearance. BT Hovemann F Sehlmeyer J Malz, Gene 1997 189 213 9 10.1016/S0378-1119(96)00851-7 9168130
    • (1997) Gene , vol.189 , pp. 213-9
    • Hovemann, B.T.1    Sehlmeyer, F.2    Malz, J.3
  • 18
    • 0034673278 scopus 로고    scopus 로고
    • Cloning and characterization of the cytochrome P450 oxidoreductase gene from the zygomycete fungus Cunninghamella
    • 10.1006/bbrc.2000.2124. 10679206
    • Cloning and characterization of the cytochrome P450 oxidoreductase gene from the zygomycete fungus Cunninghamella. JS Yadav JC Loper, Biochem Biophys Res Commun 2000 268 345 53 10.1006/bbrc.2000.2124 10679206
    • (2000) Biochem Biophys Res Commun , vol.268 , pp. 345-53
    • Yadav, J.S.1    Loper, J.C.2
  • 19
    • 0013569329 scopus 로고
    • Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains
    • 3919392. 10.1073/pnas.82.4.973
    • Coding nucleotide sequence of rat NADPH-cytochrome P-450 oxidoreductase cDNA and identification of flavin-binding domains. TD Porter CB Kasper, Proc Natl Acad Sci USA 1985 82 973 7 3919392 10.1073/pnas.82.4.973
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 973-7
    • Porter, T.D.1    Kasper, C.B.2
  • 20
    • 2942588530 scopus 로고    scopus 로고
    • The NADPH-cytochrome P450 reductase gene from Gibberella fujikuroi is essential for gibberellin biosynthesis
    • 10.1074/jbc.M308517200. 15037621
    • The NADPH-cytochrome P450 reductase gene from Gibberella fujikuroi is essential for gibberellin biosynthesis. S Malonek MC Rojas P Hedden P Gaskin P Hopkins B Tudzynski, J Biol Chem 2004 279 25075 84 10.1074/jbc.M308517200 15037621
    • (2004) J Biol Chem , vol.279 , pp. 25075-84
    • Malonek, S.1    Rojas, M.C.2    Hedden, P.3    Gaskin, P.4    Hopkins, P.5    Tudzynski, B.6
  • 21
    • 0031594283 scopus 로고    scopus 로고
    • Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation
    • 9449848. 10.1104/pp.116.1.357
    • Two isoforms of NADPH:cytochrome P450 reductase in Arabidopsis thaliana. Gene structure, heterologous expression in insect cells, and differential regulation. M Mizutani D Ohta, Plant Physiol 1998 116 357 67 9449848 10.1104/pp.116.1.357
    • (1998) Plant Physiol , vol.116 , pp. 357-67
    • Mizutani, M.1    Ohta, D.2
  • 22
    • 0034891682 scopus 로고    scopus 로고
    • Functional cloning, based on azole resistance in Saccharomyces cerevisiae, and characterization of Rhizopus nigricans redox carriers that are differentially involved in the P450-dependent response to progesterone stress
    • 10.1007/s004380100492. 11523811
    • Functional cloning, based on azole resistance in Saccharomyces cerevisiae, and characterization of Rhizopus nigricans redox carriers that are differentially involved in the P450-dependent response to progesterone stress. B Kunic G Truan K Breskvar D Pompon, Mol Genet Genomics 2001 265 930 40 10.1007/s004380100492 11523811
    • (2001) Mol Genet Genomics , vol.265 , pp. 930-40
    • Kunic, B.1    Truan, G.2    Breskvar, K.3    Pompon, D.4
  • 23
    • 34547863854 scopus 로고    scopus 로고
    • Cloning and characterization of the NADPH cytochrome P450 reductase gene (CPR) from Candida bombicola
    • 17559413
    • Cloning and characterization of the NADPH cytochrome P450 reductase gene (CPR) from Candida bombicola. IN Van Bogaert D Develter W Soetaert EJ Vandamme, FEMS Yeast Res 2007 17559413
    • (2007) FEMS Yeast Res
    • Van Bogaert, I.N.1    Develter, D.2    Soetaert, W.3    Vandamme, E.J.4
  • 24
    • 0032548924 scopus 로고    scopus 로고
    • The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity
    • 10.1074/jbc.273.8.4492. 9468503
    • The N-terminal membrane domain of yeast NADPH-cytochrome P450 (CYP) oxidoreductase is not required for catalytic activity in sterol biosynthesis or in reconstitution of CYP activity. K Venkateswarlu DC Lamb DE Kelly NJ Manning SL Kelly, J Biol Chem 1998 273 4492 6 10.1074/jbc.273.8.4492 9468503
    • (1998) J Biol Chem , vol.273 , pp. 4492-6
    • Venkateswarlu, K.1    Lamb, D.C.2    Kelly, D.E.3    Manning, N.J.4    Kelly, S.L.5
  • 25
    • 0028281964 scopus 로고
    • Cloning and characterization of a yeast cytochrome b5-encoding gene which suppresses ketoconazole hypersensitivity in a NADPH-P-450 reductase-deficient strain
    • 10.1016/0378-1119(94)90366-2. 8181746
    • Cloning and characterization of a yeast cytochrome b5-encoding gene which suppresses ketoconazole hypersensitivity in a NADPH-P-450 reductase-deficient strain. G Truan JC Epinat C Rougeulle C Cullin D Pompon, Gene 1994 142 123 7 10.1016/0378-1119(94)90366-2 8181746
    • (1994) Gene , vol.142 , pp. 123-7
    • Truan, G.1    Epinat, J.C.2    Rougeulle, C.3    Cullin, C.4    Pompon, D.5
  • 26
    • 0032750635 scopus 로고    scopus 로고
    • Biodiversity of the P450 catalytic cycle: Yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction
    • 10.1016/S0014-5793(99)01548-3. 10622712
    • Biodiversity of the P450 catalytic cycle: yeast cytochrome b5/NADH cytochrome b5 reductase complex efficiently drives the entire sterol 14-demethylation (CYP51) reaction. DC Lamb DE Kelly NJ Manning MA Kaderbhai SL Kelly, FEBS Lett 1999 462 283 8 10.1016/S0014-5793(99)01548-3 10622712
    • (1999) FEBS Lett , vol.462 , pp. 283-8
    • Lamb, D.C.1    Kelly, D.E.2    Manning, N.J.3    Kaderbhai, M.A.4    Kelly, S.L.5
  • 28
    • 0037155271 scopus 로고    scopus 로고
    • Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase
    • 10.1074/jbc.M111408200. 11742006
    • Association of multiple developmental defects and embryonic lethality with loss of microsomal NADPH-cytochrome P450 oxidoreductase. AL Shen KA O'Leary CB Kasper, J Biol Chem 2002 277 6536 41 10.1074/jbc.M111408200 11742006
    • (2002) J Biol Chem , vol.277 , pp. 6536-41
    • Shen, A.L.1    O'Leary, K.A.2    Kasper, C.B.3
  • 29
    • 0041468898 scopus 로고    scopus 로고
    • Identification of novel roles of the cytochrome p450 system in early embryogenesis: Effects on vasculogenesis and retinoic acid homeostasis
    • 12917333. 10.1128/MCB.23.17.6103-6116.2003
    • Identification of novel roles of the cytochrome p450 system in early embryogenesis: effects on vasculogenesis and retinoic acid homeostasis. DM Otto CJ Henderson D Carrie M Davey TE Gundersen R Blomhoff RH Adams C Tickle CR Wolf, Mol Cell Biol 2003 23 6103 16 12917333 10.1128/MCB.23.17.6103-6116.2003
    • (2003) Mol Cell Biol , vol.23 , pp. 6103-16
    • 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
  • 30
    • 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
    • 10.1016/j.ydbio.2006.10.032. 17126317
    • Rescue of cytochrome P450 oxidoreductase (Por) mouse mutants reveals functions in vasculogenesis, brain and limb patterning linked to retinoic acid homeostasis. V Ribes DM Otto L Dickmann K Schmidt B Schuhbaur C Henderson R Blomhoff CR Wolf C Tickle P Dolle, Dev Biol 2007 303 66 81 10.1016/j.ydbio.2006. 10.032 17126317
    • (2007) Dev Biol , vol.303 , pp. 66-81
    • Ribes, V.1    Otto, D.M.2    Dickmann, L.3    Schmidt, K.4    Schuhbaur, B.5    Henderson, C.6    Blomhoff, R.7    Wolf, C.R.8    Tickle, C.9    Dolle, P.10
  • 31
    • 0032757423 scopus 로고    scopus 로고
    • Two novel sites of expression of NADPH cytochrome P450 reductase during murine embryogenesis: Limb mesenchyme and developing olfactory neuroepithelia
    • 10.1002/(SICI)1097-0177(199912)216:4/5<511::AID-DVDY19>3.0.CO;2-H. 10633870
    • Two novel sites of expression of NADPH cytochrome P450 reductase during murine embryogenesis: limb mesenchyme and developing olfactory neuroepithelia. DS Keeney MR Waterman, Dev Dyn 1999 216 511 7 10.1002/(SICI)1097-0177(199912) 216:4/5<511::AID-DVDY19>3.0.CO;2-H 10633870
    • (1999) Dev Dyn , vol.216 , pp. 511-7
    • Keeney, D.S.1    Waterman, M.R.2
  • 32
    • 0033678971 scopus 로고    scopus 로고
    • Molecular cloning of NADPH-cytochrome P450 oxidoreductase from silkworm eggs. Its involvement in 20-hydroxyecdysone biosynthesis during embryonic development
    • 10.1046/j.1432-1033.2000.01796.x. 11082204
    • Molecular cloning of NADPH-cytochrome P450 oxidoreductase from silkworm eggs. Its involvement in 20-hydroxyecdysone biosynthesis during embryonic development. N Horike H Takemori Y Nonaka H Sonobe M Okamoto, Eur J Biochem 2000 267 6914 20 10.1046/j.1432-1033.2000.01796.x 11082204
    • (2000) Eur J Biochem , vol.267 , pp. 6914-20
    • Horike, N.1    Takemori, H.2    Nonaka, Y.3    Sonobe, H.4    Okamoto, M.5
  • 34
    • 0026646765 scopus 로고
    • Tagging developmental genes in Dictyostelium by restriction enzyme-mediated integration of plasmid DNA
    • 1326764. 10.1073/pnas.89.18.8803
    • Tagging developmental genes in Dictyostelium by restriction enzyme-mediated integration of plasmid DNA. A Kuspa WF Loomis, Proc Natl Acad Sci USA 1992 89 8803 7 1326764 10.1073/pnas.89.18.8803
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8803-7
    • Kuspa, A.1    Loomis, W.F.2
  • 35
    • 0028106174 scopus 로고
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains
    • 8078947. 10.1073/pnas.91.18.8710
    • Dissection of NADPH-cytochrome P450 oxidoreductase into distinct functional domains. GC Smith DG Tew CR Wolf, Proc Natl Acad Sci USA 1994 91 8710 4 8078947 10.1073/pnas.91.18.8710
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8710-4
    • Smith, G.C.1    Tew, D.G.2    Wolf, C.R.3
  • 36
    • 0035793117 scopus 로고    scopus 로고
    • Engineering of a functional human NADH-dependent cytochrome P450 system
    • 11136248. 10.1073/pnas.98.1.81
    • Engineering of a functional human NADH-dependent cytochrome P450 system. O Dohr MJ Paine T Friedberg GC Roberts CR Wolf, Proc Natl Acad Sci USA 2001 98 81 6 11136248 10.1073/pnas.98.1.81
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 81-6
    • Dohr, O.1    Paine, M.J.2    Friedberg, T.3    Roberts, G.C.4    Wolf, C.R.5
  • 37
    • 0034731525 scopus 로고    scopus 로고
    • Differential contributions of NADPH-cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis
    • 10.1074/jbc.M008380200. 11022049
    • Differential contributions of NADPH-cytochrome P450 oxidoreductase FAD binding site residues to flavin binding and catalysis. AL Shen CB Kasper, J Biol Chem 2000 275 41087 91 10.1074/jbc.M008380200 11022049
    • (2000) J Biol Chem , vol.275 , pp. 41087-91
    • Shen, A.L.1    Kasper, C.B.2
  • 38
    • 0027130428 scopus 로고
    • Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH
    • 10.1021/bi00094a011. 8218222
    • Interaction with arginine 597 of NADPH-cytochrome P-450 oxidoreductase is a primary source of the uniform binding energy used to discriminate between NADPH and NADH. DS Sem CB Kasper, Biochemistry 1993 32 11548 58 10.1021/bi00094a011 8218222
    • (1993) Biochemistry , vol.32 , pp. 11548-58
    • Sem, D.S.1    Kasper, C.B.2
  • 39
    • 0031240609 scopus 로고    scopus 로고
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • 10.1142/S0129065797000537. 10065837
    • A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. H Nielsen J Engelbrecht S Brunak G von Heijne, Int J Neural Syst 1997 8 581 99 10.1142/S0129065797000537 10065837
    • (1997) Int J Neural Syst , vol.8 , pp. 581-99
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 40
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • 10.1006/jmbi.2000.4315. 11152613
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. A Krogh B Larsson G von Heijne EL Sonnhammer, J Mol Biol 2001 305 567 80 10.1006/jmbi.2000.4315 11152613
    • (2001) J Mol Biol , vol.305 , pp. 567-80
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 41
    • 0036918780 scopus 로고    scopus 로고
    • Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar
    • 12481067. 10.1104/pp.008011
    • Cloning, functional expression, and subcellular localization of multiple NADPH-cytochrome P450 reductases from hybrid poplar. DK Ro J Ehlting CJ Douglas, Plant Physiol 2002 130 1837 51 12481067 10.1104/pp.008011
    • (2002) Plant Physiol , vol.130 , pp. 1837-51
    • Ro, D.K.1    Ehlting, J.2    Douglas, C.J.3
  • 42
    • 0033676030 scopus 로고    scopus 로고
    • Regulation of NADPH-cytochrome P450 reductase expressed during Douglas-fir germination and seedling development
    • 10.1023/A:1006425025702. 11117258
    • Regulation of NADPH-cytochrome P450 reductase expressed during Douglas-fir germination and seedling development. TJ Tranbarger BS Forward S Misra, Plant Mol Biol 2000 44 141 53 10.1023/A:1006425025702 11117258
    • (2000) Plant Mol Biol , vol.44 , pp. 141-53
    • Tranbarger, T.J.1    Forward, B.S.2    Misra, S.3
  • 43
    • 18944371940 scopus 로고    scopus 로고
    • Cloning and heterologous expression of the NADPH cytochrome P450 oxidoreductase genes from an industrial dicarboxylic acid-producing Candida tropicalis
    • 10.1002/yea.1227. 15849785
    • Cloning and heterologous expression of the NADPH cytochrome P450 oxidoreductase genes from an industrial dicarboxylic acid-producing Candida tropicalis. F He YT Chen, Yeast 2005 22 481 91 10.1002/yea.1227 15849785
    • (2005) Yeast , vol.22 , pp. 481-91
    • He, F.1    Chen, Y.T.2
  • 44
    • 0037408258 scopus 로고    scopus 로고
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes
    • 12725870. 10.1016/S0163-7258(03)00031-7
    • Organization of multiple cytochrome P450s with NADPH-cytochrome P450 reductase in membranes. WL Backes RW Kelley, Pharmacol Ther 2003 98 221 33 12725870 10.1016/S0163-7258(03)00031-7
    • (2003) Pharmacol Ther , vol.98 , pp. 221-33
    • Backes, W.L.1    Kelley, R.W.2
  • 45
    • 0029099231 scopus 로고
    • Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger
    • 7646819
    • Cloning and characterization of the NADPH cytochrome P450 oxidoreductase gene from the filamentous fungus Aspergillus niger. HJ van den Brink CM van Zeijl JF Brons CA van den Hondel RF van Gorcom, DNA Cell Biol 1995 14 719 29 7646819
    • (1995) DNA Cell Biol , vol.14 , pp. 719-29
    • Van Den Brink, H.J.1    Van Zeijl, C.M.2    Brons, J.F.3    Van Den Hondel, C.A.4    Van Gorcom, R.F.5
  • 46
    • 0025815253 scopus 로고
    • Multiple forms of NADPH-cytochrome P450 reductase in higher plants
    • 10.1016/0006-291X(91)91954-B. 1904216
    • Multiple forms of NADPH-cytochrome P450 reductase in higher plants. I Benveniste A Lesot MP Hasenfratz G Kochs F Durst, Biochem Biophys Res Commun 1991 177 105 12 10.1016/0006-291X(91)91954-B 1904216
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 105-12
    • Benveniste, I.1    Lesot, A.2    Hasenfratz, M.P.3    Kochs, G.4    Durst, F.5
  • 47
    • 0031464795 scopus 로고    scopus 로고
    • Differentially regulated NADPH:cytochrome P450 oxidoreductases in parsley
    • 9405720. 10.1073/pnas.94.26.14954
    • Differentially regulated NADPH:cytochrome P450 oxidoreductases in parsley. E Koopmann K Hahlbrock, Proc Natl Acad Sci USA 1997 94 14954 9 9405720 10.1073/pnas.94.26.14954
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14954-9
    • Koopmann, E.1    Hahlbrock, K.2
  • 48
    • 0042232109 scopus 로고    scopus 로고
    • Genome-wide expression analyses of gene regulation during early development of Dictyostelium discoideum
    • 12912885. 10.1128/EC.2.4.664-670.2003
    • Genome-wide expression analyses of gene regulation during early development of Dictyostelium discoideum. N Iranfar D Fuller WF Loomis, Eukaryot Cell 2003 2 664 70 12912885 10.1128/EC.2.4.664-670.2003
    • (2003) Eukaryot Cell , vol.2 , pp. 664-70
    • Iranfar, N.1    Fuller, D.2    Loomis, W.F.3
  • 49
    • 0025277656 scopus 로고
    • A pharmacologically distinct cyclic AMP receptor is responsible for the regulation of gp80 expression in Dictyostelium discoideum
    • 2162472
    • A pharmacologically distinct cyclic AMP receptor is responsible for the regulation of gp80 expression in Dictyostelium discoideum. PC Ma CH Siu, Mol Cell Biol 1990 10 3297 306 2162472
    • (1990) Mol Cell Biol , vol.10 , pp. 3297-306
    • Ma, P.C.1    Siu, C.H.2
  • 50
    • 0029851378 scopus 로고    scopus 로고
    • The Dictyostelium dual-specificity kinase splA is essential for spore differentiation
    • 8898241
    • The Dictyostelium dual-specificity kinase splA is essential for spore differentiation. GH Nuckolls N Osherov WF Loomis JA Spudich, Development 1996 122 3295 305 8898241
    • (1996) Development , vol.122 , pp. 3295-305
    • Nuckolls, G.H.1    Osherov, N.2    Loomis, W.F.3    Spudich, J.A.4
  • 51
    • 0034235862 scopus 로고    scopus 로고
    • Molecular basis for cell-specific regulation of the NADPH-cytochrome P450 oxidoreductase gene
    • 10.1006/abbi.2000.1862. 10864447
    • Molecular basis for cell-specific regulation of the NADPH-cytochrome P450 oxidoreductase gene. KA O'Leary CB Kasper, Arch Biochem Biophys 2000 379 97 108 10.1006/abbi.2000.1862 10864447
    • (2000) Arch Biochem Biophys , vol.379 , pp. 97-108
    • O'Leary, K.A.1    Kasper, C.B.2
  • 52
    • 0024539659 scopus 로고
    • Quantitation of mRNAs specific for the mixed-function oxidase system in rat liver and extrahepatic tissues during development
    • 10.1016/0003-9861(89)90250-6. 2469391
    • Quantitation of mRNAs specific for the mixed-function oxidase system in rat liver and extrahepatic tissues during development. DL Simmons CB Kasper, Arch Biochem Biophys 1989 271 10 20 10.1016/0003-9861(89)90250-6 2469391
    • (1989) Arch Biochem Biophys , vol.271 , pp. 10-20
    • Simmons, D.L.1    Kasper, C.B.2
  • 53
    • 0029892410 scopus 로고    scopus 로고
    • Preimplantation mouse blastocysts fail to express CYP genes required for estrogen biosynthesis
    • 10.1002/(SICI)1098-2795(199604)43:4<428::AID-MRD4>3.0.CO;2-R. 9052933
    • Preimplantation mouse blastocysts fail to express CYP genes required for estrogen biosynthesis. M Stromstedt DS Keeney MR Waterman BC Paria AJ Conley SK Dey, Mol Reprod Dev 1996 43 428 36 10.1002/(SICI)1098-2795(199604)43:4<428:: AID-MRD4>3.0.CO;2-R 9052933
    • (1996) Mol Reprod Dev , vol.43 , pp. 428-36
    • Stromstedt, M.1    Keeney, D.S.2    Waterman, M.R.3    Paria, B.C.4    Conley, A.J.5    Dey, S.K.6
  • 54
    • 0025217604 scopus 로고
    • Microsomal lipid peroxidation: The role of NADPH - cytochrome P450 reductase and cytochrome P450
    • 10.1016/0891-5849(90)90087-Y. 2110108
    • Microsomal lipid peroxidation: the role of NADPH - cytochrome P450 reductase and cytochrome P450. A Sevanian K Nordenbrand E Kim L Ernster P Hochstein, Free Radic Biol Med 1990 8 145 52 10.1016/0891-5849(90)90087-Y 2110108
    • (1990) Free Radic Biol Med , vol.8 , pp. 145-52
    • Sevanian, A.1    Nordenbrand, K.2    Kim, E.3    Ernster, L.4    Hochstein, P.5
  • 56
    • 0023073916 scopus 로고
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions
    • 3298997
    • Cultivation and synchronous morphogenesis of Dictyostelium under controlled experimental conditions. M Sussman, Methods Cell Biol 1987 28 9 29 3298997
    • (1987) Methods Cell Biol , vol.28 , pp. 9-29
    • Sussman, M.1
  • 57
    • 0029008282 scopus 로고
    • A multidrug resistance transporter/serine protease gene is required for prestalk specialization in Dictyostelium
    • 10.1101/gad.9.9.1111. 7744252
    • A multidrug resistance transporter/serine protease gene is required for prestalk specialization in Dictyostelium. G Shaulsky A Kuspa WF Loomis, Genes Dev 1995 9 1111 22 10.1101/gad.9.9.1111 7744252
    • (1995) Genes Dev , vol.9 , pp. 1111-22
    • Shaulsky, G.1    Kuspa, A.2    Loomis, W.F.3
  • 59
    • 0023805043 scopus 로고
    • A Dictyostelium prespore-specific gene is transcriptionally repressed by DIF in vitro
    • 3246222
    • A Dictyostelium prespore-specific gene is transcriptionally repressed by DIF in vitro. AE Early JG Williams, Development 1988 103 519 24 3246222
    • (1988) Development , vol.103 , pp. 519-24
    • Early, A.E.1    Williams, J.G.2
  • 60
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • 10.1006/meth.2001.1262. 11846609
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. KJ Livak TD Schmittgen, Methods 2001 25 402 8 10.1006/meth.2001.1262 11846609
    • (2001) Methods , vol.25 , pp. 402-8
    • Livak, K.J.1    Schmittgen, T.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.