메뉴 건너뛰기




Volumn 163, Issue 1-2, 2006, Pages 86-93

Mitochondrial P450s

Author keywords

Intracellular sorting of P450s; Microsomal P450s; Mitochondrial P450s; Steroid metabolism

Indexed keywords

CYTOCHROME P450; REACTIVE OXYGEN METABOLITE; UNSPECIFIC MONOOXYGENASE; XENOBIOTIC AGENT;

EID: 33750010974     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2006.06.008     Document Type: Article
Times cited : (110)

References (55)
  • 1
  • 2
    • 0033616138 scopus 로고    scopus 로고
    • Forty years of cytochrome P450
    • Omura T. Forty years of cytochrome P450. Biochem. Biophys. Res. Commun. 266 (1999) 690-698
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 690-698
    • Omura, T.1
  • 4
    • 0017617311 scopus 로고
    • Photochemical action spectrum of the CO-inhibited 5β-cholestane-3α,7α,12α-triol 26-hydroxylase system
    • Okuda K., Weber P., and Ullrich V. Photochemical action spectrum of the CO-inhibited 5β-cholestane-3α,7α,12α-triol 26-hydroxylase system. Biochem. Biophys. Res. Commun. 74 (1977) 1071-1076
    • (1977) Biochem. Biophys. Res. Commun. , vol.74 , pp. 1071-1076
    • Okuda, K.1    Weber, P.2    Ullrich, V.3
  • 5
    • 0024394549 scopus 로고
    • Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme
    • Andersson S., Davis D.L., Dahlbäck H., Jörnvall H., and Russell D.W. Cloning, structure, and expression of the mitochondrial cytochrome P-450 sterol 26-hydroxylase, a bile acid biosynthetic enzyme. J. Biol. Chem. 264 (1989) 8222-8229
    • (1989) J. Biol. Chem. , vol.264 , pp. 8222-8229
    • Andersson, S.1    Davis, D.L.2    Dahlbäck, H.3    Jörnvall, H.4    Russell, D.W.5
  • 6
    • 0023752569 scopus 로고
    • Purification and characterization of Vitamin D 25-hydroxylase from rat liver mitochondria
    • Masumoto O., Okayama Y., and Okuda K. Purification and characterization of Vitamin D 25-hydroxylase from rat liver mitochondria. J. Biol. Chem. 263 (1988) 14256-14260
    • (1988) J. Biol. Chem. , vol.263 , pp. 14256-14260
    • Masumoto, O.1    Okayama, Y.2    Okuda, K.3
  • 8
    • 0026070652 scopus 로고
    • Cloning and expression of cDNA encoding 25-hydroxyvitamin D3 24-hydroxylase
    • Ohyama Y., Noshiro M., and Okuda K. Cloning and expression of cDNA encoding 25-hydroxyvitamin D3 24-hydroxylase. FEBS Lett. 278 (1991) 195-198
    • (1991) FEBS Lett. , vol.278 , pp. 195-198
    • Ohyama, Y.1    Noshiro, M.2    Okuda, K.3
  • 9
    • 0001507078 scopus 로고
    • Isolation from adrenal cortex of a non-heme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P450 reductase
    • Omura T., Sanders E., Estabrook R.W., Cooper D.Y., and Rosenthal O. Isolation from adrenal cortex of a non-heme iron protein and a flavoprotein functional as a reduced triphosphopyridine nucleotide-cytochrome P450 reductase. Arch. Biochem. Biophys. 117 (1966) 660-673
    • (1966) Arch. Biochem. Biophys. , vol.117 , pp. 660-673
    • Omura, T.1    Sanders, E.2    Estabrook, R.W.3    Cooper, D.Y.4    Rosenthal, O.5
  • 10
    • 0014429758 scopus 로고
    • A soluble cytochrome P450 functional in methylene hydroxylation
    • Katagiri M., Ganguli B.N., and Gunsalus I.C. A soluble cytochrome P450 functional in methylene hydroxylation. J. Biol. Chem. 243 (1968) 3543-3546
    • (1968) J. Biol. Chem. , vol.243 , pp. 3543-3546
    • Katagiri, M.1    Ganguli, B.N.2    Gunsalus, I.C.3
  • 11
    • 0021680784 scopus 로고
    • Hepatic mitochondrial cytochrome P450 system. Distinctive features of cytochrome P450 involved in the activation of aflatoxin B1 and benzo(a)pyrene
    • Niranjan B.G., Wilson N.M., Jefcoate C.R., and Avadhani N.G. Hepatic mitochondrial cytochrome P450 system. Distinctive features of cytochrome P450 involved in the activation of aflatoxin B1 and benzo(a)pyrene. J. Biol. Chem. 259 (1984) 12495-12501
    • (1984) J. Biol. Chem. , vol.259 , pp. 12495-12501
    • Niranjan, B.G.1    Wilson, N.M.2    Jefcoate, C.R.3    Avadhani, N.G.4
  • 13
    • 0023930428 scopus 로고
    • Hepatic mitochondrial cytochrome P450 system. Identification and characterization of a precursor form of mitochondrial cytochrome P450 induced by 3-methylcholanthrene
    • Niranjan B.G., Raza H., Shayig R.M., Jefcoate C.R., and Avadhani N.G. Hepatic mitochondrial cytochrome P450 system. Identification and characterization of a precursor form of mitochondrial cytochrome P450 induced by 3-methylcholanthrene. J. Biol. Chem. 263 (1988) 575-580
    • (1988) J. Biol. Chem. , vol.263 , pp. 575-580
    • Niranjan, B.G.1    Raza, H.2    Shayig, R.M.3    Jefcoate, C.R.4    Avadhani, N.G.5
  • 14
    • 0024428983 scopus 로고
    • Purification and characterization of a hepatic mitochondrial cytochrome P450 active in aflatoxin B1 metabolism
    • Shayig R.M., and Avadhani N.G. Purification and characterization of a hepatic mitochondrial cytochrome P450 active in aflatoxin B1 metabolism. Biochemistry 28 (1989) 7546-7554
    • (1989) Biochemistry , vol.28 , pp. 7546-7554
    • Shayig, R.M.1    Avadhani, N.G.2
  • 15
    • 0029077901 scopus 로고
    • Brain mitochondrial cytochrome P450: xenobiotic metabolism, presence of multiple forms and their selective inducibility
    • Bhagwat S.V., Boyd M.R., and Ravindranath V. Brain mitochondrial cytochrome P450: xenobiotic metabolism, presence of multiple forms and their selective inducibility. Arch. Biochem. Biophys. 320 (1995) 73-83
    • (1995) Arch. Biochem. Biophys. , vol.320 , pp. 73-83
    • Bhagwat, S.V.1    Boyd, M.R.2    Ravindranath, V.3
  • 16
    • 0032744250 scopus 로고    scopus 로고
    • A soluble amino-teminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria
    • Neve E.P.A., and Ingelman-Sundberg M. A soluble amino-teminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria. FEBS Lett. 460 (1999) 309-314
    • (1999) FEBS Lett. , vol.460 , pp. 309-314
    • Neve, E.P.A.1    Ingelman-Sundberg, M.2
  • 17
    • 0011270386 scopus 로고
    • Signal recognition particle is required for co-translational insertion of cytochrome P-450 into microsomal membrane
    • Sakaguchi M., Mihara K., and Sato R. Signal recognition particle is required for co-translational insertion of cytochrome P-450 into microsomal membrane. Proc. Natl. Acad. Sci. U.S.A. 81 (1984) 3361-3364
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 3361-3364
    • Sakaguchi, M.1    Mihara, K.2    Sato, R.3
  • 18
    • 0022817092 scopus 로고
    • Processing-independnet in vitro translocation of cytochrome P-450(SCC) precursor across mitochondrial membranes
    • Ou W., Ito A., Morohashi K., Fujii-Kuriyama Y., and Omura T. Processing-independnet in vitro translocation of cytochrome P-450(SCC) precursor across mitochondrial membranes. J. Biochem. 100 (1986) 1287-1296
    • (1986) J. Biochem. , vol.100 , pp. 1287-1296
    • Ou, W.1    Ito, A.2    Morohashi, K.3    Fujii-Kuriyama, Y.4    Omura, T.5
  • 19
    • 0025360792 scopus 로고
    • The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane
    • Sato T., Sakaguchi M., Mihara K., and Omura T. The amino-terminal structures that determine topological orientation of cytochrome P-450 in microsomal membrane. EMBO J. 9 (1990) 2391-2397
    • (1990) EMBO J. , vol.9 , pp. 2391-2397
    • Sato, T.1    Sakaguchi, M.2    Mihara, K.3    Omura, T.4
  • 20
    • 0027376024 scopus 로고
    • Importance of the proline-rich region following signal-anchor sequence in the formation of correct conformation of microsomal cytochorme P-450s
    • Yamazaki S., Sato K., Suhara K., Sakaguchi M., Mihara K., and Omura T. Importance of the proline-rich region following signal-anchor sequence in the formation of correct conformation of microsomal cytochorme P-450s. J. Biochem. 114 (1993) 652-657
    • (1993) J. Biochem. , vol.114 , pp. 652-657
    • Yamazaki, S.1    Sato, K.2    Suhara, K.3    Sakaguchi, M.4    Mihara, K.5    Omura, T.6
  • 21
    • 0027217892 scopus 로고
    • Deletion of a conserved tetrapeptide, PPGP, in P450 2C2 results in loss of enzymatic activity without a change in the cellular location
    • Szczesna-Skorupa E., Straub P., and Kemper B. Deletion of a conserved tetrapeptide, PPGP, in P450 2C2 results in loss of enzymatic activity without a change in the cellular location. Arch. Biochem. Biophys. 304 (1993) 170-175
    • (1993) Arch. Biochem. Biophys. , vol.304 , pp. 170-175
    • Szczesna-Skorupa, E.1    Straub, P.2    Kemper, B.3
  • 23
    • 0042939577 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex
    • Morohashi K., Fujii-Kuriyama Y., Okada Y., Sogawa K., Hirose T., Inayama S., and Omura T. Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex. Proc. Natl. Acad. Sci. U.S.A. 81 (1984) 4647-4651
    • (1984) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4647-4651
    • Morohashi, K.1    Fujii-Kuriyama, Y.2    Okada, Y.3    Sogawa, K.4    Hirose, T.5    Inayama, S.6    Omura, T.7
  • 24
    • 0026501551 scopus 로고
    • Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge
    • Sakaguchi M., Tomiyoshi R., Kuroiwa T., Mihara K., and Omura T. Functions of signal and signal-anchor sequences are determined by the balance between the hydrophobic segment and the N-terminal charge. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 16-19
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 16-19
    • Sakaguchi, M.1    Tomiyoshi, R.2    Kuroiwa, T.3    Mihara, K.4    Omura, T.5
  • 25
    • 0035110289 scopus 로고    scopus 로고
    • Microsomal P450s use specific proline-rich sequences for efficient folding, but not for maintenance of the folded protein
    • Kusano K., Sakaguchi M., Kagawa N., Waterman M.R., and Omura T. Microsomal P450s use specific proline-rich sequences for efficient folding, but not for maintenance of the folded protein. J. Biochem. 129 (2001) 259-269
    • (2001) J. Biochem. , vol.129 , pp. 259-269
    • Kusano, K.1    Sakaguchi, M.2    Kagawa, N.3    Waterman, M.R.4    Omura, T.5
  • 26
    • 0027382279 scopus 로고
    • Core Glycosylation of cytochrome P450(arom). Evidence for localization of N terminus of microsomal cytochrome P450 in the lumen
    • Shimozawa O., Sakaguchi M., Ogawa H., Harada N., Mihara K., and Omura T. Core Glycosylation of cytochrome P450(arom). Evidence for localization of N terminus of microsomal cytochrome P450 in the lumen. J. Biol. Chem. 268 (1993) 21399-21402
    • (1993) J. Biol. Chem. , vol.268 , pp. 21399-21402
    • Shimozawa, O.1    Sakaguchi, M.2    Ogawa, H.3    Harada, N.4    Mihara, K.5    Omura, T.6
  • 27
    • 0033534789 scopus 로고    scopus 로고
    • Some properties of mitochondrial adrenodoxin associated with its nonconventional electron donor function toward rabbit liver microsomal cytochrome P450 2B4
    • Lehnerer M., Schulze J., Bernhardt R., and Hlavica P. Some properties of mitochondrial adrenodoxin associated with its nonconventional electron donor function toward rabbit liver microsomal cytochrome P450 2B4. Biochem. Biophys. Res. Commun. 254 (1999) 83-87
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 83-87
    • Lehnerer, M.1    Schulze, J.2    Bernhardt, R.3    Hlavica, P.4
  • 28
    • 0032570255 scopus 로고    scopus 로고
    • Interaction of adrenodoxin with P450 1A1 and its truncated form P450MT2 through different domains: differential modulation of enzyme activities
    • Anandatheerthavarada H.K., Addya S., Mullick J., and Avadhani N.G. Interaction of adrenodoxin with P450 1A1 and its truncated form P450MT2 through different domains: differential modulation of enzyme activities. Biochemistry 37 (1998) 1150-1160
    • (1998) Biochemistry , vol.37 , pp. 1150-1160
    • Anandatheerthavarada, H.K.1    Addya, S.2    Mullick, J.3    Avadhani, N.G.4
  • 29
    • 0035815726 scopus 로고    scopus 로고
    • Identification and characterizaion of a mitochondrial targeting signal in rat cytochrome P450 2E1 (CYP2E1)
    • Neve E.P.A., and Ingelman-Sundberg M. Identification and characterizaion of a mitochondrial targeting signal in rat cytochrome P450 2E1 (CYP2E1). J. Biol. Chem. 276 (2001) 11317-11322
    • (2001) J. Biol. Chem. , vol.276 , pp. 11317-11322
    • Neve, E.P.A.1    Ingelman-Sundberg, M.2
  • 30
    • 0029859961 scopus 로고    scopus 로고
    • Molecular engineering study on electron transfer from NADPH-P450 reductase to rat mitochondrial P450c27 in yeast microsomes
    • Sakaki T., Kominami S., Hayashi K., Akiyoshi-Shibata M., and Yabusaki Y. Molecular engineering study on electron transfer from NADPH-P450 reductase to rat mitochondrial P450c27 in yeast microsomes. J. Biol. Chem. 271 (1996) 26209-26213
    • (1996) J. Biol. Chem. , vol.271 , pp. 26209-26213
    • Sakaki, T.1    Kominami, S.2    Hayashi, K.3    Akiyoshi-Shibata, M.4    Yabusaki, Y.5
  • 31
    • 0028104977 scopus 로고
    • Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities
    • Jenkins C.M., and Waterman M.R. Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities. J. Biol. Chem. 269 (1994) 27401-27408
    • (1994) J. Biol. Chem. , vol.269 , pp. 27401-27408
    • Jenkins, C.M.1    Waterman, M.R.2
  • 32
    • 0018342988 scopus 로고
    • Immunohistochemical localization of adrenodoxin and adrenodoxin reductase in bovine adrenal cortex
    • Mitani F., Ishimura Y., Izumi S., and Watanabe K. Immunohistochemical localization of adrenodoxin and adrenodoxin reductase in bovine adrenal cortex. Acta Endocrinol. 90 (1979) 317-327
    • (1979) Acta Endocrinol. , vol.90 , pp. 317-327
    • Mitani, F.1    Ishimura, Y.2    Izumi, S.3    Watanabe, K.4
  • 33
    • 0024478462 scopus 로고
    • Immunohistochemical localization of adrenodoxin in bovine adrenal cortex by protein A-gold technique
    • Hatano O., Sagara Y., Omura T., and Takakusu A. Immunohistochemical localization of adrenodoxin in bovine adrenal cortex by protein A-gold technique. Histochemistry 91 (1989) 89-97
    • (1989) Histochemistry , vol.91 , pp. 89-97
    • Hatano, O.1    Sagara, Y.2    Omura, T.3    Takakusu, A.4
  • 34
    • 0023049739 scopus 로고
    • Stoichiometry of mitochondrial cytochrome P450, adrenodoxin, and adrenodoxin reductase in adrenal cortex and corpus luteum
    • Hanukoglu I., and Hanukoglu Z. Stoichiometry of mitochondrial cytochrome P450, adrenodoxin, and adrenodoxin reductase in adrenal cortex and corpus luteum. Eur. J. Biochem. 157 (1986) 27-31
    • (1986) Eur. J. Biochem. , vol.157 , pp. 27-31
    • Hanukoglu, I.1    Hanukoglu, Z.2
  • 36
    • 0024539032 scopus 로고
    • Active complex between adrenodoxin reductase and adrenodoxin in the cytochrome P450scc reduction reaction
    • Hara T., and Kimura T. Active complex between adrenodoxin reductase and adrenodoxin in the cytochrome P450scc reduction reaction. J. Biochem. 105 (1989) 601-605
    • (1989) J. Biochem. , vol.105 , pp. 601-605
    • Hara, T.1    Kimura, T.2
  • 37
    • 0032508616 scopus 로고    scopus 로고
    • Characterization of recombinant adrenodoxin reductase homologue (Arh1p) from yeast
    • Lacourt T., Achstetter T., and Dumas B. Characterization of recombinant adrenodoxin reductase homologue (Arh1p) from yeast. J. Biol. Chem. 273 (1998) 23984-23992
    • (1998) J. Biol. Chem. , vol.273 , pp. 23984-23992
    • Lacourt, T.1    Achstetter, T.2    Dumas, B.3
  • 38
    • 0033953353 scopus 로고    scopus 로고
    • A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins
    • Lange H., Kraut A., Kispal G., and Lill R. A mitochondrial ferredoxin is essential for biogenesis of cellular iron-sulfur proteins. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 1050-1055
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1050-1055
    • Lange, H.1    Kraut, A.2    Kispal, G.3    Lill, R.4
  • 39
    • 0033527754 scopus 로고    scopus 로고
    • Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly repair protein
    • Jung Y.S., Gao-Sheridan H.S., Christiansen J., Dean D.R., and Burgess B.K. Purification and biophysical characterization of a new [2Fe-2S] ferredoxin from Azotobacter vinelandii, a putative [Fe-S] cluster assembly repair protein. J. Biol. Chem. 274 (1999) 32402-32410
    • (1999) J. Biol. Chem. , vol.274 , pp. 32402-32410
    • Jung, Y.S.1    Gao-Sheridan, H.S.2    Christiansen, J.3    Dean, D.R.4    Burgess, B.K.5
  • 40
    • 0034672689 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein (StAR) and the intramitochondrial translocation of cholesterol
    • Christenson L.K., and Strauss J.F. Steroidogenic acute regulatory protein (StAR) and the intramitochondrial translocation of cholesterol. Biochim. Biophys. Acta 1529 (2000) 175-187
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 175-187
    • Christenson, L.K.1    Strauss, J.F.2
  • 41
    • 0035076216 scopus 로고    scopus 로고
    • Genes involved in initial steps of bile acid synthesis
    • Björkhem I., and Eggertsen G. Genes involved in initial steps of bile acid synthesis. Curr. Opin. Lipidol. 12 (2001) 97-103
    • (2001) Curr. Opin. Lipidol. , vol.12 , pp. 97-103
    • Björkhem, I.1    Eggertsen, G.2
  • 42
    • 0036668184 scopus 로고    scopus 로고
    • Bile acid regulation of gene expression: role of nuclear hormone receptors
    • Chiang J.Y. Bile acid regulation of gene expression: role of nuclear hormone receptors. Endocrinol. Rev. 23 (2002) 443-463
    • (2002) Endocrinol. Rev. , vol.23 , pp. 443-463
    • Chiang, J.Y.1
  • 43
    • 0034672672 scopus 로고    scopus 로고
    • Oxysterol biosynthetic enzymes
    • Russell D.W. Oxysterol biosynthetic enzymes. Biochim. Biophys. Acta 1529 (2000) 126-135
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 126-135
    • Russell, D.W.1
  • 44
    • 8544284075 scopus 로고    scopus 로고
    • Enzymes involved in the activation and inactivation of Vitamin D
    • Prosser D.E., and Jones G. Enzymes involved in the activation and inactivation of Vitamin D. Trends Biochem. Sci. 29 (2004) 664-673
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 664-673
    • Prosser, D.E.1    Jones, G.2
  • 45
    • 0842312531 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes, and alternative-splice variants
    • Nelson D.R., Zeldin D.C., Hoffman S.M.G., Maltais L.J., Wain H.M., and Nebert D.W. Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes, and alternative-splice variants. Pharmacogenetics 14 (2004) 1-18
    • (2004) Pharmacogenetics , vol.14 , pp. 1-18
    • Nelson, D.R.1    Zeldin, D.C.2    Hoffman, S.M.G.3    Maltais, L.J.4    Wain, H.M.5    Nebert, D.W.6
  • 46
    • 0018908672 scopus 로고
    • Activation of aflatoxin B1 by a mono-oxygenase system localized in rat liver mitochondria
    • Niranjan B.G., and Avadhani N.G. Activation of aflatoxin B1 by a mono-oxygenase system localized in rat liver mitochondria. J. Biol. Chem. 255 (1980) 6575-6578
    • (1980) J. Biol. Chem. , vol.255 , pp. 6575-6578
    • Niranjan, B.G.1    Avadhani, N.G.2
  • 47
    • 0020367149 scopus 로고
    • Aryl hydrocarbon hydroxylase of rat brain mitochondria: properties of, and effects of inhibitors and inducers on, enzyme activity
    • Das M., Seth P.K., Dixit R., and Mukhtar H. Aryl hydrocarbon hydroxylase of rat brain mitochondria: properties of, and effects of inhibitors and inducers on, enzyme activity. Arch. Biochem. Biophys. 217 (1982) 205-215
    • (1982) Arch. Biochem. Biophys. , vol.217 , pp. 205-215
    • Das, M.1    Seth, P.K.2    Dixit, R.3    Mukhtar, H.4
  • 48
    • 0030611669 scopus 로고    scopus 로고
    • Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450 MT2
    • Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V., Mullick J., and Avadhani N.G. Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450 MT2. J. Cell Biol. 139 (1997) 589-599
    • (1997) J. Cell Biol. , vol.139 , pp. 589-599
    • Addya, S.1    Anandatheerthavarada, H.K.2    Biswas, G.3    Bhagwat, S.V.4    Mullick, J.5    Avadhani, N.G.6
  • 49
    • 0035816554 scopus 로고    scopus 로고
    • Mitochondrial targeted cytochrome P450 2E1 (P450 MT5) contains an intact N-terminus and requires mitochondrial specific electron transfer proteins for activity
    • Robin M.A., Anandatheerthavarada H.K., Fang J.K., Cudic M., Otvos L., and Avadhani N.G. Mitochondrial targeted cytochrome P450 2E1 (P450 MT5) contains an intact N-terminus and requires mitochondrial specific electron transfer proteins for activity. J. Biol. Chem. 276 (2001) 24680-24689
    • (2001) J. Biol. Chem. , vol.276 , pp. 24680-24689
    • Robin, M.A.1    Anandatheerthavarada, H.K.2    Fang, J.K.3    Cudic, M.4    Otvos, L.5    Avadhani, N.G.6
  • 50
    • 0031106254 scopus 로고    scopus 로고
    • Localization of multiple forms of inducible cytochromes P450 in rat liver mitochondria: immunological characteristics and patterns of xenobiotic substrate metabolism
    • Anandatheerthavarada H.K., Addya S., Dwivedi R.S., Biswas G., Mullick J., and Avadhani N.G. Localization of multiple forms of inducible cytochromes P450 in rat liver mitochondria: immunological characteristics and patterns of xenobiotic substrate metabolism. Arch. Biochem. Biophys. 339 (1997) 136-150
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 136-150
    • Anandatheerthavarada, H.K.1    Addya, S.2    Dwivedi, R.S.3    Biswas, G.4    Mullick, J.5    Avadhani, N.G.6
  • 51
    • 0033135469 scopus 로고    scopus 로고
    • Constitutive and inducible cytochrome P450 in rat lung mitochondria: xenobiotic induction, relative abundance, and catalytic properties
    • Bhagwat S.V., Mullick J., Raza H., and Avadhani N.G. Constitutive and inducible cytochrome P450 in rat lung mitochondria: xenobiotic induction, relative abundance, and catalytic properties. Toxicol. Appl. Pharmacol. 156 (1999) 231-240
    • (1999) Toxicol. Appl. Pharmacol. , vol.156 , pp. 231-240
    • Bhagwat, S.V.1    Mullick, J.2    Raza, H.3    Avadhani, N.G.4
  • 52
  • 53
    • 0037174926 scopus 로고    scopus 로고
    • Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation
    • Robin M.A., Anandatheerhavarada H.K., Biswas G., Babu N., Sepuri V., Gordon D.M., Pain D., and Avadhani N.G. Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation. J. Biol. Chem. 277 (2002) 40583-40593
    • (2002) J. Biol. Chem. , vol.277 , pp. 40583-40593
    • Robin, M.A.1    Anandatheerhavarada, H.K.2    Biswas, G.3    Babu, N.4    Sepuri, V.5    Gordon, D.M.6    Pain, D.7    Avadhani, N.G.8
  • 54
    • 0028923332 scopus 로고
    • Electron leakage from the adrenal cortex mitochondrial P450scc and P450c11 systems: NADPH and steroid dependence
    • Rapoport R., Sklam D., and Hanukoglu I. Electron leakage from the adrenal cortex mitochondrial P450scc and P450c11 systems: NADPH and steroid dependence. Arch. Biochem. Biophys. 317 (1995) 412-416
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 412-416
    • Rapoport, R.1    Sklam, D.2    Hanukoglu, I.3
  • 55
    • 0027328115 scopus 로고
    • Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system
    • Hanukoglu I., Rapoport R., Weiner L., and Sklan D. Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system. Arch. Biochem. Biophys. 305 (1993) 489-498
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 489-498
    • Hanukoglu, I.1    Rapoport, R.2    Weiner, L.3    Sklan, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.