메뉴 건너뛰기




Volumn 37, Issue 2, 2005, Pages 379-404

Regulation of cytochrome P450 by posttranslational modification

Author keywords

Cytochrome P450; Glycosylation; Nitration; Phosphorylation; Posttranslational modification; Ubiquitination

Indexed keywords

ADRENODOXIN; BILE ACID; CALCIUM; CARCINOGEN; CYTOCHROME P450; CYTOCHROME P450 1A2; CYTOCHROME P450 2B1; CYTOCHROME P450 2B2; CYTOCHROME P450 2C11; CYTOCHROME P450 2C12; CYTOCHROME P450 2E1; CYTOCHROME P450 3A1; CYTOCHROME P450 3A4; FATTY ACID; FERREDOXIN; GLUCOCORTICOID; ICOSANOID; MINERALOCORTICOID; NITRIC OXIDE; PREGNENOLONE; PROTEASOME; PROTEIN P450 11A1; PROTEIN P450 11B1; PROTEIN P450 17A1; PROTEIN P450 19A1; PROTEIN P450 27A1; PROTEIN P450 2C7; PROTEIN P450 3A6; PROTEIN P450 51; PROTEIN P450 7A1; STEROID; UNCLASSIFIED DRUG; VITAMIN D; XENOBIOTIC AGENT;

EID: 18744393086     PISSN: 03602532     EISSN: None     Source Type: Journal    
DOI: 10.1081/DMR-200046136     Document Type: Review
Times cited : (98)

References (132)
  • 2
    • 23444457486 scopus 로고
    • Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis
    • Amarneh, B., Corbin, C. J., Peterson, J. A., Simpson, E. R., Graham-Lorence, S. (1993). Functional domains of human aromatase cytochrome P450 characterized by linear alignment and site-directed mutagenesis. Mol. Endocrinol. 7(12):1617-1624.
    • (1993) Mol. Endocrinol. , vol.7 , Issue.12 , pp. 1617-1624
    • Amarneh, B.1    Corbin, C.J.2    Peterson, J.A.3    Simpson, E.R.4    Graham-Lorence, S.5
  • 3
    • 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., Avadhani, N. G. (1997). Localization of multiple forms of inducible cytochromes P450 in rat liver mitochondria: immunological characteristics and patterns of xenobiotic substrate metabolism. Arch. Biochem. Biophys. 339(1):136-150.
    • (1997) Arch. Biochem. Biophys. , vol.339 , Issue.1 , pp. 136-150
    • Anandatheerthavarada, H.K.1    Addya, S.2    Dwivedi, R.S.3    Biswas, G.4    Mullick, J.5    Avadhani, N.G.6
  • 4
    • 0033570145 scopus 로고    scopus 로고
    • Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP-dependent phosphorylation at Ser128
    • Anandatheerthavarada, H. K., Biswas, G., Mullick, J., Sepuri, N. B. V., Otvos, L., Pain, D., Avadhani, N. G. (1999). Dual targeting of cytochrome P4502B1 to endoplasmic reticulum and mitochondria involves a novel signal activation by cyclic AMP-dependent phosphorylation at Ser128. EMBO J. 18(20):5494-5504.
    • (1999) EMBO J. , vol.18 , Issue.20 , pp. 5494-5504
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Mullick, J.3    Sepuri, N.B.V.4    Otvos, L.5    Pain, D.6    Avadhani, N.G.7
  • 5
    • 0035710923 scopus 로고    scopus 로고
    • Phosphorylation processes mediate rapid changes of brain aromatase activity
    • Balthazart, J., Baillien, M., Ball, G. F. (2001a). Phosphorylation processes mediate rapid changes of brain aromatase activity. J. Steroid Biochem. Mol. Biol. 79(1-5):261-277.
    • (2001) J. Steroid Biochem. Mol. Biol. , vol.79 , Issue.1-5 , pp. 261-277
    • Balthazart, J.1    Baillien, M.2    Ball, G.F.3
  • 6
    • 0035172985 scopus 로고    scopus 로고
    • Rapid and reversible inhibition of brain aromatase activity
    • Balthazart, J., Baillien, M., Ball, G. F. (2001b). Rapid and reversible inhibition of brain aromatase activity. J. Neuroendocrinol. 13(1):63-73.
    • (2001) J. Neuroendocrinol. , vol.13 , Issue.1 , pp. 63-73
    • Balthazart, J.1    Baillien, M.2    Ball, G.F.3
  • 7
    • 0038694540 scopus 로고    scopus 로고
    • Calcium dependent phosphorylation processes control brain aromatase in quail
    • Balthazart, J., Baillien, M., Charlier, T. D., Ball, G. F. (2003). Calcium dependent phosphorylation processes control brain aromatase in quail. Eur. J. Neurosci. 17(8):1591-1606.
    • (2003) Eur. J. Neurosci. , vol.17 , Issue.8 , pp. 1591-1606
    • Balthazart, J.1    Baillien, M.2    Charlier, T.D.3    Ball, G.F.4
  • 8
    • 0033979374 scopus 로고    scopus 로고
    • Identification of a ubiquitination-target/substrate-interaction domain of cytochrome P-450 (CYP) 2E1
    • Banerjee, A., Kocarek, T. A., Novak, R. F. (2000). Identification of a ubiquitination-target/substrate-interaction domain of cytochrome P-450 (CYP) 2E1. Drug Metab. Dispos. 28(2):118-124.
    • (2000) Drug Metab. Dispos. , vol.28 , Issue.2 , pp. 118-124
    • Banerjee, A.1    Kocarek, T.A.2    Novak, R.F.3
  • 9
    • 0018978166 scopus 로고
    • Synthesis and insertion of cytochrome P-450 into endoplasmic reticulum membranes
    • Bar-Nun, S., Kreibich, G., Adesnik, M., Alterman, J., Negishi, M., Sabatini, D. D. (1980). Synthesis and insertion of cytochrome P-450 into endoplasmic reticulum membranes. PNAS 77(2):965-969.
    • (1980) PNAS , vol.77 , Issue.2 , pp. 965-969
    • Bar-Nun, S.1    Kreibich, G.2    Adesnik, M.3    Alterman, J.4    Negishi, M.5    Sabatini, D.D.6
  • 10
    • 0024379396 scopus 로고
    • Placental estrogen synthetase (aromatase): Evidence for phosphatase-dependent inactivation
    • Bellino, F. L., Holben, L. (1989). Placental estrogen synthetase (aromatase): evidence for phosphatase-dependent inactivation. Biochem. Biophys. Res. Commun. 162(1):498-504.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , Issue.1 , pp. 498-504
    • Bellino, F.L.1    Holben, L.2
  • 11
    • 0022742564 scopus 로고
    • Evidence against in vitro modulation of rat liver cholesterol 7 α-hydroxylase activity by phosphorylation-dephosphorylation: Comparison with hydroxymethylglutaryl CoA reductase
    • Berglund, L., Bjorkhem, I., Angelin, B., Einarsson, K. (1986). Evidence against in vitro modulation of rat liver cholesterol 7 α-hydroxylase activity by phosphorylation-dephosphorylation: comparison with hydroxymethylglutaryl CoA reductase. Acta Chem. Scand. B 40(6):457-461.
    • (1986) Acta Chem. Scand. B , vol.40 , Issue.6 , pp. 457-461
    • Berglund, L.1    Bjorkhem, I.2    Angelin, B.3    Einarsson, K.4
  • 12
    • 0033135469 scopus 로고    scopus 로고
    • Constitutive and inducible cytochromes P450 in rat lung mitochondria: Xenobiotic induction, relative abundance, and catalytic properties
    • Bhagwat, S. V., Mullick, J., Raza, H., Avadhani, N. G. (1999a). Constitutive and inducible cytochromes P450 in rat lung mitochondria: xenobiotic induction, relative abundance, and catalytic properties. Toxicol. Appl. Pharmacol. 156(3):231-240.
    • (1999) Toxicol. Appl. Pharmacol. , vol.156 , Issue.3 , pp. 231-240
    • Bhagwat, S.V.1    Mullick, J.2    Raza, H.3    Avadhani, N.G.4
  • 13
    • 0033588378 scopus 로고    scopus 로고
    • Dual targeting property of the N-terminal signal sequence of P4501 A1. Targeting of heterologous proteins to endoplasmic reticulum and mitochondria
    • Bhagwat, S. V., Biswas, G., Anandatheerthavarada, H. K., Addya, S., Pandak, W., Avadhani, N. G. (1999b). Dual targeting property of the N-terminal signal sequence of P4501 A1. Targeting of heterologous proteins to endoplasmic reticulum and mitochondria. J. Biol. Chem. 274(34):24014-24022.
    • (1999) J. Biol. Chem. , vol.274 , Issue.34 , pp. 24014-24022
    • Bhagwat, S.V.1    Biswas, G.2    Anandatheerthavarada, H.K.3    Addya, S.4    Pandak, W.5    Avadhani, N.G.6
  • 14
    • 0034456536 scopus 로고    scopus 로고
    • Effect of leptin on CYP17 enzymatic activities in human adrenal cells: New insight in the onset of adrenarche
    • Biason-Lauber, A., Zachmann, M., Schoenle, E. J. (2000). Effect of leptin on CYP17 enzymatic activities in human adrenal cells: new insight in the onset of adrenarche. Endocrinology 141(4):1446-1454.
    • (2000) Endocrinology , vol.141 , Issue.4 , pp. 1446-1454
    • Biason-Lauber, A.1    Zachmann, M.2    Schoenle, E.J.3
  • 15
    • 0022496911 scopus 로고
    • Solubilization and reconstitution of chick renal mitochondrial 25-hydroxyvitamin D3 24-hydroxylase
    • Burgos-Trinidad, M., Brown, A. J., DeLuca, H. F. (1986). Solubilization and reconstitution of chick renal mitochondrial 25-hydroxyvitamin D3 24-hydroxylase. Biochemistry 25(9):2692-2696.
    • (1986) Biochemistry , vol.25 , Issue.9 , pp. 2692-2696
    • Burgos-Trinidad, M.1    Brown, A.J.2    DeLuca, H.F.3
  • 16
    • 0016690354 scopus 로고
    • Protein kinase stimulation of a reconstituted cholesterol side chain cleavage enzyme system in the bovine corpus luteum
    • Caron, M. G., Goldstein, S., Savard, K., Marsh, J. M. (1975). Protein kinase stimulation of a reconstituted cholesterol side chain cleavage enzyme system in the bovine corpus luteum. J. Biol. Chem. 250(13):5137-5143.
    • (1975) J. Biol. Chem. , vol.250 , Issue.13 , pp. 5137-5143
    • Caron, M.G.1    Goldstein, S.2    Savard, K.3    Marsh, J.M.4
  • 17
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • Cohen, P. (2002). Protein kinases - the major drug targets of the twenty-first century? Nat. Rev. 1(4):309-315.
    • (2002) Nat. Rev. , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 18
    • 0042357403 scopus 로고    scopus 로고
    • Hepatic cytochrome P450 degradation: Mechanistic diversity of the cellular sanitation brigade
    • Correia, M. A. (2003). Hepatic cytochrome P450 degradation: mechanistic diversity of the cellular sanitation brigade. Drug Metab. Rev. 35(2,3):107-143.
    • (2003) Drug Metab. Rev. , vol.35 , Issue.2-3 , pp. 107-143
    • Correia, M.A.1
  • 19
    • 0026989765 scopus 로고
    • Degradation of rat liver cytochromes P450 3A after their inactivation by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1, 4-dihydropyridine: Characterization of the proteolytic system
    • Correia, M. A., Davoll, S. H., Wrighton, S. A., Thomas, P. E. (1992). Degradation of rat liver cytochromes P450 3A after their inactivation by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1, 4-dihydropyridine: characterization of the proteolytic system. Arch. Biochem. Biophys. 297(2):228-238.
    • (1992) Arch. Biochem. Biophys. , vol.297 , Issue.2 , pp. 228-238
    • Correia, M.A.1    Davoll, S.H.2    Wrighton, S.A.3    Thomas, P.E.4
  • 20
    • 0033127741 scopus 로고    scopus 로고
    • 17β-estradiol rapidly facilitates chemoinvestigation and mounting in castrated male rats
    • Cross, E., Roselli, C. E. (1999). 17β-estradiol rapidly facilitates chemoinvestigation and mounting in castrated male rats. Am. J. Physiol., Regul. Integr. Comp. Physiol. 276(5 pt. 2):R1346-R1350.
    • (1999) Am. J. Physiol., Regul. Integr. Comp. Physiol. , vol.276 , Issue.5 PART 2
    • Cross, E.1    Roselli, C.E.2
  • 24
    • 0019949905 scopus 로고
    • Phosphorylation of purified mitochondrial cytochromes P-450 (cholesterol desmolase and 11 β-hydroxylase) from bovine adrenal cortex
    • Defaye, G., Monnier, N., Guidicelli, C., Chambaz, E. M. (1982). Phosphorylation of purified mitochondrial cytochromes P-450 (cholesterol desmolase and 11 β-hydroxylase) from bovine adrenal cortex. Mol. Cell. Endocrinol. 27(2):157-168.
    • (1982) Mol. Cell. Endocrinol. , vol.27 , Issue.2 , pp. 157-168
    • Defaye, G.1    Monnier, N.2    Guidicelli, C.3    Chambaz, E.M.4
  • 25
    • 0023766578 scopus 로고
    • Regulation of bile acid synthesis. Isolation and characterization of microsomal phosphatases
    • Diven, W. F., Sweeney, J., Warty, V., Sanghvi, A. (1988). Regulation of bile acid synthesis. Isolation and characterization of microsomal phosphatases. Biochem. Biophys. Res. Commun. 155(1):7-13.
    • (1988) Biochem. Biophys. Res. Commun. , vol.155 , Issue.1 , pp. 7-13
    • Diven, W.F.1    Sweeney, J.2    Warty, V.3    Sanghvi, A.4
  • 26
    • 0037200671 scopus 로고    scopus 로고
    • Nitric oxide potently inhibits the rate-limiting enzymatic step in steroidogenesis
    • Drewett, J. G., Adams-Hays, R. L., Ho, B. Y., Hegge, D. J. (2002). Nitric oxide potently inhibits the rate-limiting enzymatic step in steroidogenesis. Mol. Cell. Endocrinol. 194(1,2):39-50.
    • (2002) Mol. Cell. Endocrinol. , vol.194 , Issue.1-2 , pp. 39-50
    • Drewett, J.G.1    Adams-Hays, R.L.2    Ho, B.Y.3    Hegge, D.J.4
  • 27
    • 0022462380 scopus 로고
    • Bile acid synthesis in man: Assay of hepatic microsomal cholesterol 7 α-hydroxylase activity by isotope dilution-mass spectrometry
    • Einarsson, K., Angelin, B., Ewerth, S., Nilsell, K., Bjorkhem, I. (1986). Bile acid synthesis in man: assay of hepatic microsomal cholesterol 7 α-hydroxylase activity by isotope dilution-mass spectrometry. J. Lipid. Res. 27(1):82-88.
    • (1986) J. Lipid. Res. , vol.27 , Issue.1 , pp. 82-88
    • Einarsson, K.1    Angelin, B.2    Ewerth, S.3    Nilsell, K.4    Bjorkhem, I.5
  • 28
    • 0028277268 scopus 로고
    • Substrate-regulated. cAMP-dependent phosphorylation, denaturation, and degradation of glucocorticoid-inducible rat liver cytochrome P450 3A1
    • Eliasson, E., Mkrtchian, S., Halpert, J. R., Ingelman-Sundberg, M. (1994). Substrate-regulated. cAMP-dependent phosphorylation, denaturation, and degradation of glucocorticoid-inducible rat liver cytochrome P450 3A1. J. Biol. Chem. 269(28):18378-18383.
    • (1994) J. Biol. Chem. , vol.269 , Issue.28 , pp. 18378-18383
    • Eliasson, E.1    Mkrtchian, S.2    Halpert, J.R.3    Ingelman-Sundberg, M.4
  • 30
    • 0015459188 scopus 로고
    • Oxygenated cytochrome P-450 as an intermediate in hydroxylation reactions
    • Estabrook, R. W., Baron, J., Peterson, J., Ishimura, Y. (1972). Oxygenated cytochrome P-450 as an intermediate in hydroxylation reactions. Biochem. Soc. Symp. 34:159-185.
    • (1972) Biochem. Soc. Symp. , vol.34 , pp. 159-185
    • Estabrook, R.W.1    Baron, J.2    Peterson, J.3    Ishimura, Y.4
  • 31
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans, R. M. (1988). The steroid and thyroid hormone receptor superfamily. Science 240(4854):889-895.
    • (1988) Science , vol.240 , Issue.4854 , pp. 889-895
    • Evans, R.M.1
  • 32
    • 0028149146 scopus 로고
    • Evidence against a role for serine 129 in determining murine cytochrome P450 Cyp2e-1 protein levels
    • Freeman, J. E., Wolf, C. R. (1994). Evidence against a role for serine 129 in determining murine cytochrome P450 Cyp2e-1 protein levels. Biochemistry 33(47):13963-13966.
    • (1994) Biochemistry , vol.33 , Issue.47 , pp. 13963-13966
    • Freeman, J.E.1    Wolf, C.R.2
  • 33
    • 0022340726 scopus 로고
    • Inhibition of 25-hydroxyvitamin D 1 α-hydroxylase by renal mitochondrial protein kinase-catalyzed phosphorylation
    • Ghazarian, J. G., Yanda, D. M. (1985). Inhibition of 25-hydroxyvitamin D 1 α-hydroxylase by renal mitochondrial protein kinase-catalyzed phosphorylation. Biochem. Biophys. Res. Commun. 132(3):1095-1102.
    • (1985) Biochem. Biophys. Res. Commun. , vol.132 , Issue.3 , pp. 1095-1102
    • Ghazarian, J.G.1    Yanda, D.M.2
  • 34
    • 0020413603 scopus 로고
    • Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor
    • Gilmore, R., Walter, P., Blobel, G. (1982). Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor. J. Cell. Biol. 95 (2 pt. 1):470-477.
    • (1982) J. Cell. Biol. , vol.95 , Issue.2 PART 1 , pp. 470-477
    • Gilmore, R.1    Walter, P.2    Blobel, G.3
  • 35
    • 0024605266 scopus 로고
    • Solubilization and reconstitution of kidney 25-hydroxyvitamin D3 1 α- and 24-hydroxylases from vitamin D-replete pigs
    • Gray, R. W., Ghazarian, J. G. (1989). Solubilization and reconstitution of kidney 25-hydroxyvitamin D3 1 α- and 24-hydroxylases from vitamin D-replete pigs. Biochem. J. 259(2):561-568.
    • (1989) Biochem. J. , vol.259 , Issue.2 , pp. 561-568
    • Gray, R.W.1    Ghazarian, J.G.2
  • 36
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich, F. P. (2001). Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity. Chem. Res. Toxicol. 14(6):611-650.
    • (2001) Chem. Res. Toxicol. , vol.14 , Issue.6 , pp. 611-650
    • Guengerich, F.P.1
  • 37
    • 0026791936 scopus 로고
    • Post-translational chemical modification(s) of proteins
    • Han, K. K., Martinage, A. (1992). Post-translational chemical modification(s) of proteins. Int. J. Biochem. 24(1):19-28.
    • (1992) Int. J. Biochem. , vol.24 , Issue.1 , pp. 19-28
    • Han, K.K.1    Martinage, A.2
  • 38
    • 0017057951 scopus 로고
    • Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450
    • Haugen, D. A., Coon, M. J. (1976). Properties of electrophoretically homogeneous phenobarbital-inducible and beta-naphthoflavone-inducible forms of liver microsomal cytochrome P-450. J. Biol. Chem. 251(24):7929-7939.
    • (1976) J. Biol. Chem. , vol.251 , Issue.24 , pp. 7929-7939
    • Haugen, D.A.1    Coon, M.J.2
  • 39
    • 2642667462 scopus 로고    scopus 로고
    • Calcium-regulating hormones
    • Conn, P. M., Melmed, S., eds. Totowa, NJ: Humana Press
    • Hendy, G. N. (1997). Calcium-regulating hormones. In: Conn, P. M., Melmed, S., eds. Endocrinology: Basic and Clinical Principles. Totowa, NJ: Humana Press, pp. 307-323.
    • (1997) Endocrinology: Basic and Clinical Principles , pp. 307-323
    • Hendy, G.N.1
  • 41
    • 0019336903 scopus 로고
    • Purification and organ-specific properties of cholecalciferol 25-hydroxylase system: Cytochrome P-450D25-linked mixed function oxidase system
    • Hiwatashi, A., Ichikawa, Y. (1980). Purification and organ-specific properties of cholecalciferol 25-hydroxylase system: cytochrome P-450D25-linked mixed function oxidase system. Biochem. Biophys. Res. Commun. 97(4):1443-1449.
    • (1980) Biochem. Biophys. Res. Commun. , vol.97 , Issue.4 , pp. 1443-1449
    • Hiwatashi, A.1    Ichikawa, Y.2
  • 42
    • 49049146545 scopus 로고
    • Purification and reconstitution of the steroid 21-hydroxylase system (cytochrome P-450-linked mixed function oxidase system) of bovine adrenocortical microsomes
    • Hiwatashi, A., Ichikawa, Y. (1981). Purification and reconstitution of the steroid 21-hydroxylase system (cytochrome P-450-linked mixed function oxidase system) of bovine adrenocortical microsomes. Biochim. Biophys. Acta 664(1):33-48.
    • (1981) Biochim. Biophys. Acta , vol.664 , Issue.1 , pp. 33-48
    • Hiwatashi, A.1    Ichikawa, Y.2
  • 43
    • 0034800477 scopus 로고    scopus 로고
    • Allosteric phenomena in cytochrome P450-catalyzed monooxygenations
    • Hlavica, P., Lewis, D. F. V. (2001). Allosteric phenomena in cytochrome P450-catalyzed monooxygenations. Eur. J. Biochem. 268(18):4817-4832.
    • (2001) Eur. J. Biochem. , vol.268 , Issue.18 , pp. 4817-4832
    • Hlavica, P.1    Lewis, D.F.V.2
  • 44
    • 0023266341 scopus 로고
    • Cytochrome P-450 cholesterol 7 α-hydroxylase: Inhibition of enzyme deactivation by structurally diverse calmodulin antagonists and phosphatase inhibitors
    • Holsztynska, E. J., Waxman, D. J. (1987). Cytochrome P-450 cholesterol 7 α-hydroxylase: inhibition of enzyme deactivation by structurally diverse calmodulin antagonists and phosphatase inhibitors. Arch. Biochem. Biophys. 256(2):543-559.
    • (1987) Arch. Biochem. Biophys. , vol.256 , Issue.2 , pp. 543-559
    • Holsztynska, E.J.1    Waxman, D.J.2
  • 45
    • 0020481215 scopus 로고
    • The role of the sugar regions of components of the cytochrome P-450-linked mixed-function oxidase (monooxygenase) system of bovine adrenocortical mitochondria
    • Ichikawa, Y., Hiwatashi, A. (1982). The role of the sugar regions of components of the cytochrome P-450-linked mixed-function oxidase (monooxygenase) system of bovine adrenocortical mitochondria. Biochim. Biophys. Acta 705(1):82-91.
    • (1982) Biochim. Biophys. Acta , vol.705 , Issue.1 , pp. 82-91
    • Ichikawa, Y.1    Hiwatashi, A.2
  • 47
    • 0027423004 scopus 로고
    • Nitric oxide is a mediator of the decrease in cytochrome P450-dependent metabolism caused by immunostimulants
    • Khatsenko, O. G., Gross, S. S., Rifkind, A. B., Vane, J. R. (1993). Nitric oxide is a mediator of the decrease in cytochrome P450-dependent metabolism caused by immunostimulants. PNAS 90(23):11147-11151.
    • (1993) PNAS , vol.90 , Issue.23 , pp. 11147-11151
    • Khatsenko, O.G.1    Gross, S.S.2    Rifkind, A.B.3    Vane, J.R.4
  • 48
    • 0024507004 scopus 로고
    • Posttranslational modification of hepatic cytochrome P-450. Phosphorylation of phenobarbital-inducible P-450 forms PB-4 (IIB1) and PB-5 (IIB2) in isolated rat hepatocytes and in vivo
    • Koch, J. A., Waxman, D. J. (1989). Posttranslational modification of hepatic cytochrome P-450. Phosphorylation of phenobarbital-inducible P-450 forms PB-4 (IIB1) and PB-5 (IIB2) in isolated rat hepatocytes and in vivo. Biochemistry 28(8):3145-3152.
    • (1989) Biochemistry , vol.28 , Issue.8 , pp. 3145-3152
    • Koch, J.A.1    Waxman, D.J.2
  • 49
    • 0033134224 scopus 로고    scopus 로고
    • Proteolytic degradation of heme-modified hepatic cytochromes P450: A role for phosphorylation, ubiquitination, and the 26S proteasome?
    • Korsmeyer, K. K., Davoll, S., Figueiredo-Pereira, M. E., Correia, M. A. (1999). Proteolytic degradation of heme-modified hepatic cytochromes P450: a role for phosphorylation, ubiquitination, and the 26S proteasome? Arch. Biochem. Biophys. 365(1):31-44.
    • (1999) Arch. Biochem. Biophys. , vol.365 , Issue.1 , pp. 31-44
    • Korsmeyer, K.K.1    Davoll, S.2    Figueiredo-Pereira, M.E.3    Correia, M.A.4
  • 50
    • 0017161935 scopus 로고
    • Dehydroepiandrosterone sulfate (DS) levels, a rapid test for abnormal adrenal androgen secretion
    • Korth-Schutz, S., Levine, L. S., New, M. I. (1976). Dehydroepiandrosterone sulfate (DS) levels, a rapid test for abnormal adrenal androgen secretion. J. Clin. Endocrinol. Metab. 42(6):1005-1013.
    • (1976) J. Clin. Endocrinol. Metab. , vol.42 , Issue.6 , pp. 1005-1013
    • Korth-Schutz, S.1    Levine, L.S.2    New, M.I.3
  • 52
    • 0037330482 scopus 로고    scopus 로고
    • Mutation of tyrosine 190 to alanine eliminates the inactivation of cytochrome P450 2B1 by peroxynitrite
    • Lin, H. L., Kent, U. M., Zhang, H., Waskell, L., Hollenberg, P. F. (2003). Mutation of tyrosine 190 to alanine eliminates the inactivation of cytochrome P450 2B1 by peroxynitrite. Chem. Res. Toxicol. 16(2):129-136.
    • (2003) Chem. Res. Toxicol. , vol.16 , Issue.2 , pp. 129-136
    • Lin, H.L.1    Kent, U.M.2    Zhang, H.3    Waskell, L.4    Hollenberg, P.F.5
  • 53
    • 0031566244 scopus 로고    scopus 로고
    • Protein phosphorylation changes ligand-binding efficiency of cytochrome P450c17 (CYP17) and accelerates its proteolytic degradation: Putative relevance for hormonal regulation of CYP17 activity
    • Löhr, J. B., Kühn-Velten, W. N. (1997). Protein phosphorylation changes ligand-binding efficiency of cytochrome P450c17 (CYP17) and accelerates its proteolytic degradation: putative relevance for hormonal regulation of CYP17 activity. Biochem. Biophys. Res. Commun. 231(2):403-408.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , Issue.2 , pp. 403-408
    • Löhr, J.B.1    Kühn-Velten, W.N.2
  • 55
    • 0025373333 scopus 로고
    • Reciprocal post-translational regulation of renal 1 α- and 24-hydroxylases of 25-hydroxyvitamin D3 by phosphorylation of ferredoxin. mRNA-directed cell-free synthesis and immunoisolation of ferredoxin
    • Mandel, M. L., Moorthy, B., Ghazarian, J. G. (1990). Reciprocal post-translational regulation of renal 1 α- and 24-hydroxylases of 25-hydroxyvitamin D3 by phosphorylation of ferredoxin. mRNA-directed cell-free synthesis and immunoisolation of ferredoxin. Biochem. J. 266(2):385-392.
    • (1990) Biochem. J. , vol.266 , Issue.2 , pp. 385-392
    • Mandel, M.L.1    Moorthy, B.2    Ghazarian, J.G.3
  • 56
    • 0023202836 scopus 로고
    • Cytochrome P-450 and NADPH-cytochrome P-450 reductase are degraded in the autolysosomes in rat liver
    • Masaki, R., Yamamoto, A., Tashiro, Y. (1987). Cytochrome P-450 and NADPH-cytochrome P-450 reductase are degraded in the autolysosomes in rat liver. J. Cell. Biol. 104(5):1207-1215.
    • (1987) J. Cell. Biol. , vol.104 , Issue.5 , pp. 1207-1215
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 58
    • 0027186367 scopus 로고
    • Phosphorylation of cytochrome P4502E1 (CYP2E1) by calmodulin dependent protein kinase, protein kinase C and cAMP dependent protein kinase
    • Menez, J. F., Machu, T. K., Song, B. J., Browning, M. D., Deitrich, R. A. (1993). Phosphorylation of cytochrome P4502E1 (CYP2E1) by calmodulin dependent protein kinase, protein kinase C and cAMP dependent protein kinase. Alcohol Alcohol. 28(4):445-451.
    • (1993) Alcohol Alcohol. , vol.28 , Issue.4 , pp. 445-451
    • Menez, J.F.1    Machu, T.K.2    Song, B.J.3    Browning, M.D.4    Deitrich, R.A.5
  • 60
    • 0023770976 scopus 로고
    • Signals for the incorporation and orientation of cytochrome P450 in the endoplasmic reticulum membrane
    • Monier, S., Van Luc, P., Kreibich, G., Sabatini, D. D., Adesnik, M. (1988). Signals for the incorporation and orientation of cytochrome P450 in the endoplasmic reticulum membrane. J. Cell. Biol. 107(2):457-470.
    • (1988) J. Cell. Biol. , vol.107 , Issue.2 , pp. 457-470
    • Monier, S.1    Van Luc, P.2    Kreibich, G.3    Sabatini, D.D.4    Adesnik, M.5
  • 61
    • 0023657947 scopus 로고
    • Phosphorylation of bovine adrenodoxin. Structural study and enzymatic activity
    • Monnier, N., Defaye, G., Chambaz, E. M. (1987). Phosphorylation of bovine adrenodoxin. Structural study and enzymatic activity. Eur. J. Biochem. 169(1):147-153.
    • (1987) Eur. J. Biochem. , vol.169 , Issue.1 , pp. 147-153
    • Monnier, N.1    Defaye, G.2    Chambaz, E.M.3
  • 62
    • 0031409592 scopus 로고    scopus 로고
    • Regulation of cytochromes P450 during inflammation and infection
    • Morgan, E. T. (1997). Regulation of cytochromes P450 during inflammation and infection. Drug Metab. Rev. 29(3):1129-1188.
    • (1997) Drug Metab. Rev. , vol.29 , Issue.3 , pp. 1129-1188
    • Morgan, E.T.1
  • 63
    • 0035119064 scopus 로고    scopus 로고
    • Regulation of cytochrome P450 by inflammatory mediators: Why and how?
    • Morgan, E. T. (2001). Regulation of cytochrome P450 by inflammatory mediators: why and how? Drug Metab. Dispos. 29(4):207-212.
    • (2001) Drug Metab. Dispos. , vol.29 , Issue.4 , pp. 207-212
    • Morgan, E.T.1
  • 66
    • 0035450192 scopus 로고    scopus 로고
    • Ubiquitin-dependent 26S proteasomal pathway: A role in the degradation of native human liver CYP3A4 expressed in Saccharomyces cerevisiae?
    • Murray, B. P., Correia, M. A. (2001). Ubiquitin-dependent 26S proteasomal pathway: a role in the degradation of native human liver CYP3A4 expressed in Saccharomyces cerevisiae? Arch. Biochem. Biophys. 393(1):106-116.
    • (2001) Arch. Biochem. Biophys. , vol.393 , Issue.1 , pp. 106-116
    • Murray, B.P.1    Correia, M.A.2
  • 67
    • 0036233468 scopus 로고    scopus 로고
    • Native CYP2C11: Heterologous expression in Saccharomyces cerevisiae reveals a role for vacuolar proteases rather than the proteasome system in the degradation of this endoplasmic reticulum
    • Murray, B. P., Zgoda, V. G., Correia, M. A. (2002). Native CYP2C11: heterologous expression in Saccharomyces cerevisiae reveals a role for vacuolar proteases rather than the proteasome system in the degradation of this endoplasmic reticulum. Protein Mol. Pharmacol. 61(5):1146-1153.
    • (2002) Protein Mol. Pharmacol. , vol.61 , Issue.5 , pp. 1146-1153
    • Murray, B.P.1    Zgoda, V.G.2    Correia, M.A.3
  • 68
    • 0017600531 scopus 로고
    • Cholesterol 7 α-hydroxylase
    • Myant, N. B., Mitropoulos, K. A. (1977). Cholesterol 7 α-hydroxylase. J. Lipid Res. 18(2):135-153.
    • (1977) J. Lipid Res. , vol.18 , Issue.2 , pp. 135-153
    • Myant, N.B.1    Mitropoulos, K.A.2
  • 69
    • 0019887951 scopus 로고
    • Microsomal cytochrome P-450 from neonatal pig testis. Purification and properties of a C21 steroid side-chain cleavage system (17 α-hydroxylase- C17,20 lyase)
    • Nakajin, S., Hall, P. F. (1981). Microsomal cytochrome P-450 from neonatal pig testis. Purification and properties of A C21 steroid side-chain cleavage system (17 α-hydroxylase-C17,20 lyase). J. Biol. Chem. 256(8):3871-3876.
    • (1981) J. Biol. Chem. , vol.256 , Issue.8 , pp. 3871-3876
    • Nakajin, S.1    Hall, P.F.2
  • 70
    • 0019888152 scopus 로고
    • Testicular microsomal cytochrome P-450 for C21 steroid side chain cleavage. Spectral and binding studies
    • Nakajin, S., Hall, P. F., Onoda, M. (1981). Testicular microsomal cytochrome P-450 for C21 steroid side chain cleavage. Spectral and binding studies. J. Biol. Chem. 256(12):6134-6139.
    • (1981) J. Biol. Chem. , vol.256 , Issue.12 , pp. 6134-6139
    • Nakajin, S.1    Hall, P.F.2    Onoda, M.3
  • 71
    • 0019504239 scopus 로고
    • The role of autoradiographic and immunocytochemical techniques in the clarification of sites of metabolism and action of vitamin D
    • Narbaitz, R., Stumpf, W. E., Sar, M. (1981). The role of autoradiographic and immunocytochemical techniques in the clarification of sites of metabolism and action of vitamin D. J. Histochem. Cytochem. 29(1):91-100.
    • (1981) J. Histochem. Cytochem. , vol.29 , Issue.1 , pp. 91-100
    • Narbaitz, R.1    Stumpf, W.E.2    Sar, M.3
  • 72
    • 0019559416 scopus 로고
    • Structural gene products of the murine Ah complex. Differences in ontogenesis and glucosamine incorporation between liver microsomal cytochromes P1-450 and P-448 induced by polycyclic aromatic compounds
    • Negishi, M., Jensen, N. M., Garcia, G. S., Nebert, D. W. (1981). Structural gene products of the murine Ah complex. Differences in ontogenesis and glucosamine incorporation between liver microsomal cytochromes P1-450 and P-448 induced by polycyclic aromatic compounds. Eur. J. Biochem. 115(3):585-594.
    • (1981) Eur. J. Biochem. , vol.115 , Issue.3 , pp. 585-594
    • Negishi, M.1    Jensen, N.M.2    Garcia, G.S.3    Nebert, D.W.4
  • 74
    • 0842312531 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants
    • Nelson, D. R., Zeldin, D. C., Hoffman, S. M., Maltais, L. J., Wain, H. M., Nebert, D. W. (2004). Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14(1):1-18.
    • (2004) Pharmacogenetics , vol.14 , Issue.1 , 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
  • 75
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert, W. (1997). Protein import into mitochondria. Annu. Rev. Biochem. 66:863-917.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 863-917
    • Neupert, W.1
  • 76
    • 0029658444 scopus 로고    scopus 로고
    • Cholesterol 7α-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation
    • Nguyen, L. B., Shefer, S., Salen, G., Chiang, J. Y., Patel, M. (1996). Cholesterol 7α-hydroxylase activities from human and rat liver are modulated in vitro posttranslationally by phosphorylation/dephosphorylation. Hepatology 24(6):1468-1474.
    • (1996) Hepatology , vol.24 , Issue.6 , pp. 1468-1474
    • Nguyen, L.B.1    Shefer, S.2    Salen, G.3    Chiang, J.Y.4    Patel, M.5
  • 77
    • 0025312690 scopus 로고
    • Phosphorylation of cytochrome P450 isoenzymes in intact hepatocytes and its importance for their function in metabolic processes
    • Oesch-Bartlomowicz, B., Oesch, F. (1990). Phosphorylation of cytochrome P450 isoenzymes in intact hepatocytes and its importance for their function in metabolic processes. Arch. Toxicol. 64(4):257-261.
    • (1990) Arch. Toxicol. , vol.64 , Issue.4 , pp. 257-261
    • Oesch-Bartlomowicz, B.1    Oesch, F.2
  • 79
    • 0035545910 scopus 로고    scopus 로고
    • cAMP-dependent phosphorylation of CYP2B1 as a functional switch for cyclophosphamide activation and its hormonal control in vitro and in vivo
    • Oesch-Bartlomowicz, B., Richter, B., Becker, R., Vogel, S., Padma, P. R., Hengstler, J. G., Oesch, F. (2001). cAMP-dependent phosphorylation of CYP2B1 as a functional switch for cyclophosphamide activation and its hormonal control in vitro and in vivo. Int. J. Cancer 94(5):733-742.
    • (2001) Int. J. Cancer , vol.94 , Issue.5 , pp. 733-742
    • Oesch-Bartlomowicz, B.1    Richter, B.2    Becker, R.3    Vogel, S.4    Padma, P.R.5    Hengstler, J.G.6    Oesch, F.7
  • 80
    • 0021181906 scopus 로고
    • Age changes and sex differences in serum dehydroepiandrosterone sulfate concentrations throughout adulthood
    • Orentreich, N., Brind, J. L., Rizer, R. L., Vogelman, J. H. (1984). Age changes and sex differences in serum dehydroepiandrosterone sulfate concentrations throughout adulthood. J. Clin. Endocrinol. Metab. 59(3):551-555.
    • (1984) J. Clin. Endocrinol. Metab. , vol.59 , Issue.3 , pp. 551-555
    • Orentreich, N.1    Brind, J.L.2    Rizer, R.L.3    Vogelman, J.H.4
  • 82
    • 0019066328 scopus 로고
    • Control of adrenal androgen secretion
    • Parker, L. N., Odell, W. D. (1980). Control of adrenal androgen secretion. Endocr. Rev. 1(4):392-410.
    • (1980) Endocr. Rev. , vol.1 , Issue.4 , pp. 392-410
    • Parker, L.N.1    Odell, W.D.2
  • 83
    • 0027534442 scopus 로고
    • Transcriptional regulation of the adrenal steroidogenic enzymes
    • Parker, K. L., Schimmer, B. P. (1993). Transcriptional regulation of the adrenal steroidogenic enzymes. Trends Endocrinol. Metab. 4(2):46-50.
    • (1993) Trends Endocrinol. Metab. , vol.4 , Issue.2 , pp. 46-50
    • Parker, K.L.1    Schimmer, B.P.2
  • 84
    • 0030218934 scopus 로고    scopus 로고
    • The roles of the nuclear receptor steroidogenic factor 1 in endocrine differentiation and development
    • Parker, K. L., Schimmer, B. P. (1996). The roles of the nuclear receptor steroidogenic factor 1 in endocrine differentiation and development. Trends Endocrinol. Metab. 7(6):203-207.
    • (1996) Trends Endocrinol. Metab. , vol.7 , Issue.6 , pp. 203-207
    • Parker, K.L.1    Schimmer, B.P.2
  • 85
    • 0031010818 scopus 로고    scopus 로고
    • Steroidogenic factor 1: A key determinant of endocrine development and function
    • Parker, K. L., Schimmer, B. P. (1997). Steroidogenic factor 1: a key determinant of endocrine development and function. Endocr. Rev. 18(3):361-377.
    • (1997) Endocr. Rev. , vol.18 , Issue.3 , pp. 361-377
    • Parker, K.L.1    Schimmer, B.P.2
  • 86
    • 0025784027 scopus 로고
    • Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms
    • Porter, T. D., Coon, M. J. (1991). Cytochrome P-450. Multiplicity of isoforms, substrates, and catalytic and regulatory mechanisms. J. Biol. Chem. 266(21):13469-13472.
    • (1991) J. Biol. Chem. , vol.266 , Issue.21 , pp. 13469-13472
    • Porter, T.D.1    Coon, M.J.2
  • 87
    • 0344824425 scopus 로고    scopus 로고
    • Cytochrome P450 flexibility
    • Poulos, T. L. (2003). Cytochrome P450 flexibility. PNAS 100(23):13121-13122.
    • (2003) PNAS , vol.100 , Issue.23 , pp. 13121-13122
    • Poulos, T.L.1
  • 88
    • 0024401458 scopus 로고
    • Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450
    • Pyerin, W., Taniguchi, H. (1989). Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450. EMBO J. 8(10):3003-3010.
    • (1989) EMBO J. , vol.8 , Issue.10 , pp. 3003-3010
    • Pyerin, W.1    Taniguchi, H.2
  • 90
    • 0030986960 scopus 로고    scopus 로고
    • Evidence of proteasome-mediated cytochrome P-450 degradation
    • Roberts, B. J. (1997). Evidence of proteasome-mediated cytochrome P-450 degradation. J. Biol. Chem. 272(15):9771-9778.
    • (1997) J. Biol. Chem. , vol.272 , Issue.15 , pp. 9771-9778
    • Roberts, B.J.1
  • 91
    • 0029618909 scopus 로고
    • Ethanol induces CYP2E1 by protein stabilization
    • Roberts, B. J., Song, B., Soh, Y., Park, S. S., Shoaf, S. E. (1995). Ethanol induces CYP2E1 by protein stabilization. J. Biol. Chem. 270(50):29632-29635.
    • (1995) J. Biol. Chem. , vol.270 , Issue.50 , pp. 29632-29635
    • Roberts, B.J.1    Song, B.2    Soh, Y.3    Park, S.S.4    Shoaf, S.E.5
  • 92
    • 0031670445 scopus 로고    scopus 로고
    • Peroxynitrite-mediated nitration of tyrosine and inactivation of the catalytic activity of cytochrome P450 2B1
    • Roberts, E. S., Lin, H., Crowley, J. R., Vuletich, J. L., Osawa, Y., Hollenberg, P. F. (1998). Peroxynitrite-mediated nitration of tyrosine and inactivation of the catalytic activity of cytochrome P450 2B1. Chem. Res. Toxicol. 11(9):1067-1074.
    • (1998) Chem. Res. Toxicol. , vol.11 , Issue.9 , pp. 1067-1074
    • Roberts, E.S.1    Lin, H.2    Crowley, J.R.3    Vuletich, J.L.4    Osawa, Y.5    Hollenberg, P.F.6
  • 93
    • 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., Anandatheerthavarada, H. K., Fang, J., Cudic, M., Otvos, L., Avadhani, N. G. (2001). 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(27):24680-24689.
    • (2001) J. Biol. Chem. , vol.276 , Issue.27 , pp. 24680-24689
    • Robin, M.1    Anandatheerthavarada, H.K.2    Fang, J.3    Cudic, M.4    Otvos, L.5    Avadhani, N.G.6
  • 94
    • 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., Anandatheerthavarada, H. K., Biswas, G., Sepuri, N. B. V., Gordon, D. M., Pain, D., Avadhani, N. G. (2002). Bimodal targeting of microsomal CYP2E1 to mitochondria through activation of an N-terminal chimeric signal by cAMP-mediated phosphorylation. J. Biol. Chem. 277(43):40583-40593.
    • (2002) J. Biol. Chem. , vol.277 , Issue.43 , pp. 40583-40593
    • Robin, M.1    Anandatheerthavarada, H.K.2    Biswas, G.3    Sepuri, N.B.V.4    Gordon, D.M.5    Pain, D.6    Avadhani, N.G.7
  • 95
  • 96
    • 0011270386 scopus 로고
    • Signal recognition particle is required for cotranslational insertion of cytochrome P-450 into microsomal membranes
    • Sakaguchi, M., Mihara, K., Sato, R. (1984). Signal recognition particle is required for cotranslational insertion of cytochrome P-450 into microsomal membranes. PNAS 81(11):3361-3364.
    • (1984) PNAS , vol.81 , Issue.11 , pp. 3361-3364
    • Sakaguchi, M.1    Mihara, K.2    Sato, R.3
  • 97
    • 0023390030 scopus 로고
    • A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence
    • Sakaguchi, M., Mihara, K., Sato, R. (1987). A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence. EMBO J. 6(8):2425-2431.
    • (1987) EMBO J. , vol.6 , Issue.8 , pp. 2425-2431
    • Sakaguchi, M.1    Mihara, K.2    Sato, R.3
  • 98
    • 0038305949 scopus 로고    scopus 로고
    • Specific nitration at tyrosine 430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase
    • Schmidt, P., Youhnovski, N., Daiber, A., Balan, A., Arsic, M., Bachschmid, M., Przybylski, M., Ullrich, V. (2003). Specific nitration at tyrosine 430 revealed by high resolution mass spectrometry as basis for redox regulation of bovine prostacyclin synthase. J. Biol. Chem. 278(15):12813-12819.
    • (2003) J. Biol. Chem. , vol.278 , Issue.15 , pp. 12813-12819
    • Schmidt, P.1    Youhnovski, N.2    Daiber, A.3    Balan, A.4    Arsic, M.5    Bachschmid, M.6    Przybylski, M.7    Ullrich, V.8
  • 99
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site
    • Schoch, G. A., Yano, J. K., Wester, M. R., Griffin, K. J., Stout, C. D., Johnson, E. F. (2004). Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site. J. Biol. Chem. 279(10):9497-9503.
    • (2004) J. Biol. Chem. , vol.279 , Issue.10 , pp. 9497-9503
    • Schoch, G.A.1    Yano, J.K.2    Wester, M.R.3    Griffin, K.J.4    Stout, C.D.5    Johnson, E.F.6
  • 101
    • 3042553224 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9 Å resolution: Insight into the range of P450 conformations and coordination of redox partner binding
    • Scott, E. E., White, M. A., He, Y. A., Johnson, E. F., Stout, C. D., Halpert, J. R. (2004). Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9 Å resolution: insight into the range of P450 conformations and coordination of redox partner binding. J. Biol. Chem. 279(26):27294-27301.
    • (2004) J. Biol. Chem. , vol.279 , Issue.26 , 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
  • 102
    • 0025754264 scopus 로고
    • Estrogen synthetase (aromatase). The cytochrome P-450 component of the human placental enzyme is a glycoprotein
    • Sethumadhavan, K., Bellino, F. L., Thotakura, N. R. (1991). Estrogen synthetase (aromatase). The cytochrome P-450 component of the human placental enzyme is a glycoprotein. Mol. Cell. Endocrinol. 78(1,2):25-32.
    • (1991) Mol. Cell. Endocrinol. , vol.78 , Issue.1-2 , pp. 25-32
    • Sethumadhavan, K.1    Bellino, F.L.2    Thotakura, N.R.3
  • 103
    • 0027382279 scopus 로고
    • Core glycosylation of cytochrome P-450 (arom). Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen
    • Shimozawa, O., Sakaguchi, M., Ogawa, H., Harada, N., Mihara, K., Omura, T. (1993). Core glycosylation of cytochrome P-450 (arom). Evidence for localization of N terminus of microsomal cytochrome P-450 in the lumen. J. Biol. Chem. 268(28):21399-21402.
    • (1993) J. Biol. Chem. , vol.268 , Issue.28 , pp. 21399-21402
    • Shimozawa, O.1    Sakaguchi, M.2    Ogawa, H.3    Harada, N.4    Mihara, K.5    Omura, T.6
  • 104
    • 0022992997 scopus 로고
    • Parathyroid hormone stimulates dephosphorylation of the renoredoxin component of the 25-hydroxyvitamin D3-1 α-hydroxylase from rat renal cortex
    • Siegel, N., Wongsurawat, N., Armbrecht, H. J. (1986). Parathyroid hormone stimulates dephosphorylation of the renoredoxin component of the 25-hydroxyvitamin D3-1 α-hydroxylase from rat renal cortex. J. Biol. Chem. 261(36):16998-17003.
    • (1986) J. Biol. Chem. , vol.261 , Issue.36 , pp. 16998-17003
    • Siegel, N.1    Wongsurawat, N.2    Armbrecht, H.J.3
  • 105
    • 0029165311 scopus 로고
    • Lanosterol 14-α-demethylase (cytochrome P-45014DM): Modulation of its enzyme activity by cholesterol feeding
    • Sonoda, Y., Amano, C., Endo, M., Sato, Y., Sekigawa, Y., Fukuhara, M. (1995). Lanosterol 14-α-demethylase (cytochrome P-45014DM): modulation of its enzyme activity by cholesterol feeding. Biol. Pharm. Bull. 18(7):1009-1011.
    • (1995) Biol. Pharm. Bull. , vol.18 , Issue.7 , pp. 1009-1011
    • Sonoda, Y.1    Amano, C.2    Endo, M.3    Sato, Y.4    Sekigawa, Y.5    Fukuhara, M.6
  • 107
    • 0034119678 scopus 로고    scopus 로고
    • The role of the StAR protein in steroidogenesis: Challenges for the future
    • Stocco, D. M. (2000). The role of the StAR protein in steroidogenesis: challenges for the future. J. Endocrinol. 164(3):247-253.
    • (2000) J. Endocrinol. , vol.164 , Issue.3 , pp. 247-253
    • Stocco, D.M.1
  • 108
    • 0024478250 scopus 로고
    • NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2
    • Szczesna-Skorupa, E., Kemper, B. (1989). NH2-terminal substitutions of basic amino acids induce translocation across the microsomal membrane and glycosylation of rabbit cytochrome P450IIC2. J. Cell. Biol. 108(4):1237-1243.
    • (1989) J. Cell. Biol. , vol.108 , Issue.4 , pp. 1237-1243
    • Szczesna-Skorupa, E.1    Kemper, B.2
  • 109
    • 0023955730 scopus 로고
    • Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide
    • Szczesna-Skorupa, E., Browne, N., Mead, D., Kemper, B. (1988). Positive charges at the NH2 terminus convert the membrane-anchor signal peptide of cytochrome P-450 to a secretory signal peptide. PNAS 85(3):738-742.
    • (1988) PNAS , vol.85 , Issue.3 , pp. 738-742
    • Szczesna-Skorupa, E.1    Browne, N.2    Mead, D.3    Kemper, B.4
  • 110
    • 0022510474 scopus 로고
    • Modulation of reconstituted cholesterol 7 α-hydroxylase by phosphatase and protein kinase
    • Tang, P. M., Chiang, J. Y. (1986). Modulation of reconstituted cholesterol 7 α-hydroxylase by phosphatase and protein kinase. Biochem. Biophys. Res. Commun. 134(2):797-802.
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , Issue.2 , pp. 797-802
    • Tang, P.M.1    Chiang, J.Y.2
  • 111
    • 0026546019 scopus 로고
    • Degradation of cytochrome P450 2E1: Selective loss after labilization of the enzyme
    • Tierney, D. J., Haas, A. L., Koop, D. R. (1992). Degradation of cytochrome P450 2E1: selective loss after labilization of the enzyme. Arch. Biochem. Biophys. 293(1):9-16.
    • (1992) Arch. Biochem. Biophys. , vol.293 , Issue.1 , pp. 9-16
    • Tierney, D.J.1    Haas, A.L.2    Koop, D.R.3
  • 112
    • 0034638622 scopus 로고    scopus 로고
    • Superoxide as a messenger of endothelial function
    • Ullrich, V., Bachschmid, M. (2000). Superoxide as a messenger of endothelial function. Biochem. Biophys. Res. Commun. 278(1):1-8.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , Issue.1 , pp. 1-8
    • Ullrich, V.1    Bachschmid, M.2
  • 113
    • 0021676906 scopus 로고
    • Adrenocortical cytochrome P-450 responsible for cholesterol side chain cleavage (P-450scc) is phosphorylated by the calcium-activated, phospholipid-sensitive protein kinase (protein kinase C)
    • Vilgrain, I., Defaye, G., Chambaz, E. M. (1984). Adrenocortical cytochrome P-450 responsible for cholesterol side chain cleavage (P-450scc) is phosphorylated by the calcium-activated, phospholipid-sensitive protein kinase (protein kinase C). Biochem. Biophys. Res. Commun. 125(2):554-561.
    • (1984) Biochem. Biophys. Res. Commun. , vol.125 , Issue.2 , pp. 554-561
    • Vilgrain, I.1    Defaye, G.2    Chambaz, E.M.3
  • 114
    • 0004062227 scopus 로고    scopus 로고
    • Cytochrome P450 3A degradation in isolated rat hepatocytes: 26S proteasome inhibitors as probes
    • Wang, H. F., Figueiredo Pereira, M. E., Correia, M. A. (1999). Cytochrome P450 3A degradation in isolated rat hepatocytes: 26S proteasome inhibitors as probes. Arch. Biochem. Biophys. 365(1):45-53.
    • (1999) Arch. Biochem. Biophys. , vol.365 , Issue.1 , pp. 45-53
    • Wang, H.F.1    Figueiredo Pereira, M.E.2    Correia, M.A.3
  • 115
    • 0035949711 scopus 로고    scopus 로고
    • Phosphorylation of native and heme-modified CYP3A4 by protein kinase C: A mass spectrometric characterization of the phosphorylated peptides
    • Wang, X., Medzihradszky, K. F., Maltby, D., Correia, M. A. (2001). Phosphorylation of native and heme-modified CYP3A4 by protein kinase C: a mass spectrometric characterization of the phosphorylated peptides. Biochemistry 40(38):11318-11326.
    • (2001) Biochemistry , vol.40 , Issue.38 , pp. 11318-11326
    • Wang, X.1    Medzihradszky, K.F.2    Maltby, D.3    Correia, M.A.4
  • 116
    • 0035292759 scopus 로고    scopus 로고
    • Ubiquitin and proteasomes: Themes and variations on ubiquitylation
    • Weissman, A. M. (2001). Ubiquitin and proteasomes: themes and variations on ubiquitylation. Nat. Rev. Mol. Cell. Biol. 2(3):169-178.
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , Issue.3 , pp. 169-178
    • Weissman, A.M.1
  • 117
    • 0037672866 scopus 로고    scopus 로고
    • Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: Evidence for multiple substrate binding modes
    • Wester, M. R., Johnson, E. F., Marques-Soares, C., Dansette, P. M., Mansuy, D., Stout, C. D. (2003a). Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 A resolution: evidence for multiple substrate binding modes. Biochemistry 42(21):6370-6379.
    • (2003) Biochemistry , vol.42 , Issue.21 , pp. 6370-6379
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dansette, P.M.4    Mansuy, D.5    Stout, C.D.6
  • 118
    • 0042573727 scopus 로고    scopus 로고
    • Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: Evidence for an induced fit model of substrate binding
    • Wester, M. R., Johnson, E. F., Marques-Soares, C., Dijols, S., Dansette, P. M., Mansuy, D., Stout, C. D. (2003b). Structure of mammalian cytochrome P450 2C5 complexed with diclofenac at 2.1 A resolution: evidence for an induced fit model of substrate binding. Biochemistry 42(31):9335-9345.
    • (2003) Biochemistry , vol.42 , Issue.31 , pp. 9335-9345
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dijols, S.4    Dansette, P.M.5    Mansuy, D.6    Stout, C.D.7
  • 119
    • 4143143372 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 2C9 complexed with flurbiprofen at 2.0 A resolution
    • Wester, M. R., Yano, J. K., Schoch, G. A., Yang, C., Griffin, K. J., Stout, C. D., Johnson, E. F. (2004). The structure of human microsomal cytochrome P450 2C9 complexed with flurbiprofen at 2.0 A resolution. J. Biol. Chem. 279(34):35630-35637.
    • (2004) J. Biol. Chem. , vol.279 , Issue.34 , pp. 35630-35637
    • Wester, M.R.1    Yano, J.K.2    Schoch, G.A.3    Yang, C.4    Griffin, K.J.5    Stout, C.D.6    Johnson, E.F.7
  • 120
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., McRee, D. E. (2000). Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell. 5(1):121-131.
    • (2000) Mol. Cell. , vol.5 , Issue.1 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 121
    • 0042265520 scopus 로고    scopus 로고
    • Crystal structure of human cytochrome P450 2C9 with bound warfarin
    • Williams, P. A., Cosme, J., Ward, A., Angove, H. C., Matak Vinkovic, D., Jhoti, H. (2003). Crystal structure of human cytochrome P450 2C9 with bound warfarin. Nature 424(6947):464-468.
    • (2003) Nature , vol.424 , Issue.6947 , pp. 464-468
    • Williams, P.A.1    Cosme, J.2    Ward, A.3    Angove, H.C.4    Matak Vinkovic, D.5    Jhoti, H.6
  • 125
    • 0031149527 scopus 로고    scopus 로고
    • Characterization of cytochrome P4502E1 turnover in transfected HepG2 cells expressing human CYP2E1
    • Yang, M. X., Cederbaum, A. I. (1997). Characterization of cytochrome P4502E1 turnover in transfected HepG2 cells expressing human CYP2E1. Arch. Biochem. Biophys. 341(1):25-33.
    • (1997) Arch. Biochem. Biophys. , vol.341 , Issue.1 , pp. 25-33
    • Yang, M.X.1    Cederbaum, A.I.2
  • 126
    • 18744409884 scopus 로고    scopus 로고
    • The crystal structure of human microsomal cytochrome P450 2A6 (CYP2A6): The principle nicotine oxidase
    • Mainz, Germany, July 4-9, P4-CH-11
    • Yano, J. K., Griffin, K., Stout, D. C., Johnson, E. F. (2004a). The crystal structure of human microsomal cytochrome P450 2A6 (CYP2A6): the principle nicotine oxidase, In: Abstracts, Microsomes and Drug Oxidations, Mainz, Germany, July 4-9, P4-CH-11.
    • (2004) Abstracts, Microsomes and Drug Oxidations
    • Yano, J.K.1    Griffin, K.2    Stout, D.C.3    Johnson, E.F.4
  • 127
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05′ resolution
    • Yano, J. K., Wester, M. R., Schoch, G. A., Griffin, K. J., Stout, C. D., Johnson, E. F. (2004b). The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05′ resolution. J. Biol. Chem. 279(37):38091 -38094.
    • (2004) J. Biol. Chem. , vol.279 , Issue.37 , 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
  • 129
    • 0242710208 scopus 로고    scopus 로고
    • Adaptive hypersensitivity following long-term estrogen deprivation: Involvement of multiple signal pathways
    • Yue, W., Wang, J. P., Conaway, M. R., Li, Y., Santen, R. J. (2003). Adaptive hypersensitivity following long-term estrogen deprivation: involvement of multiple signal pathways. J. Steroid Biochem. Mol. Biol. 86(3-5):265-274.
    • (2003) J. Steroid Biochem. Mol. Biol. , vol.86 , Issue.3-5 , pp. 265-274
    • Yue, W.1    Wang, J.P.2    Conaway, M.R.3    Li, Y.4    Santen, R.J.5
  • 130
    • 0028786656 scopus 로고
    • Serine phosphorylation of human P450c17 increases 17,20-lyase activity: Implications for adrenarche and the polycystic ovary syndrome
    • Zhang, L., Rodriguez, H., Ohno, S., Miller, W. L. (1995). Serine phosphorylation of human P450c17 increases 17,20-lyase activity: implications for adrenarche and the polycystic ovary syndrome. PNAS 92(23):10619-10623.
    • (1995) PNAS , vol.92 , Issue.23 , pp. 10619-10623
    • Zhang, L.1    Rodriguez, H.2    Ohno, S.3    Miller, W.L.4
  • 131
    • 0027485120 scopus 로고
    • Purification and characterization of two membrane bound serine proteinases from rat liver microsomes active in degradation of cytochrome P450
    • Zhukov, A., Werlinder, V., Ingelman-Sundberg, M. (1993). Purification and characterization of two membrane bound serine proteinases from rat liver microsomes active in degradation of cytochrome P450. Biochem. Biophys. Res. Commun. 197(1):221-228.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , Issue.1 , pp. 221-228
    • Zhukov, A.1    Werlinder, V.2    Ingelman-Sundberg, M.3
  • 132
    • 0030877284 scopus 로고    scopus 로고
    • Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite
    • Zou, M., Martin, C., Ullrich, V. (1997). Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite. Biol. Chem. 378(7):707-713.
    • (1997) Biol. Chem. , vol.378 , Issue.7 , pp. 707-713
    • Zou, M.1    Martin, C.2    Ullrich, V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.