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Volumn , Issue , 2010, Pages 363-406

Cytochrome P450 Degradation and Its Clinical Relevance

Author keywords

Cytochrome P450 degradation and clinical relevance; P450 degradation pathological relevance in autoimmune hepatitis and drug induced hepatitis; Pharmacokinetic drug interactions and P450 turnover and drug interactions

Indexed keywords


EID: 84884445011     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470538951.ch11     Document Type: Chapter
Times cited : (4)

References (231)
  • 1
    • 34247371476 scopus 로고    scopus 로고
    • Regulation of CYP2A5 gene by the transcription factor nuclear factor (erythroid-derived 2)-like 2
    • Abu-Bakar A, Lämsä V, Arpiainen S, Moore MR, Lang MA, Hakkola J. Regulation of CYP2A5 gene by the transcription factor nuclear factor (erythroid-derived 2)-like 2. Drug Metab Dispos 2007; 35: 787-794.
    • (2007) Drug Metab Dispos , vol.35 , pp. 787-794
    • Abu-Bakar, A.1    Lämsä, V.2    Arpiainen, S.3    Moore, M.R.4    Lang, M.A.5    Hakkola, J.6
  • 2
    • 0036217332 scopus 로고    scopus 로고
    • Proteasome inhibition: a novel approach to cancer therapy
    • Adams J. Proteasome inhibition: a novel approach to cancer therapy. Trends Mol Med 2002; 8 (4 Suppl):S 49-S 54.
    • (2002) Trends Mol Med , vol.8 , Issue.4 SUPPL.
    • Adams, J.1
  • 3
    • 18744393086 scopus 로고    scopus 로고
    • Regulation of cytochrome P450 by posttranslational modification
    • Aguiar M, Masse R, Gibbs BF. Regulation of cytochrome P450 by posttranslational modification. Drug Metab Rev 2005; 37: 379-404.
    • (2005) Drug Metab Rev , vol.37 , pp. 379-404
    • Aguiar, M.1    Masse, R.2    Gibbs, B.F.3
  • 4
    • 39949083392 scopus 로고    scopus 로고
    • Roles of nitric oxide in inflammatory downregulation of human cytochromes P450
    • Aitken AE, Lee CM, Morgan ET. Roles of nitric oxide in inflammatory downregulation of human cytochromes P450. Free Radic Biol Med 2008; 44: 1161-1168.
    • (2008) Free Radic Biol Med , vol.44 , pp. 1161-1168
    • Aitken, A.E.1    Lee, C.M.2    Morgan, E.T.3
  • 5
    • 13744263015 scopus 로고    scopus 로고
    • Novel interaction between Apc5p and Rsp5p in an intracellular signaling pathway in Saccharomyces cerevisiae
    • Arnason TG, Pisclevich MG, Dash MD, Davies GF, Harkness TA. Novel interaction between Apc5p and Rsp5p in an intracellular signaling pathway in Saccharomyces cerevisiae. Eukaryot Cell 2005; 4: 134-146.
    • (2005) Eukaryot Cell , vol.4 , pp. 134-146
    • Arnason, T.G.1    Pisclevich, M.G.2    Dash, M.D.3    Davies, G.F.4    Harkness, T.A.5
  • 6
    • 0024562943 scopus 로고
    • The degradation signal in a short-lived protein
    • Bachmair A, Varshavsky A. The degradation signal in a short-lived protein. Cell 1989; 56: 1019-1032.
    • (1989) Cell , vol.56 , pp. 1019-1032
    • Bachmair, A.1    Varshavsky, A.2
  • 8
    • 13444288378 scopus 로고    scopus 로고
    • Proteasomal degradation of human CYP1B1: effect of the Asn453Ser polymorphism on the post-translational regulation of CYP1B1 expression
    • Bandiera S, Weidlich S, Harth V, Broede P, Ko Y, Friedberg T. Proteasomal degradation of human CYP1B1: effect of the Asn453Ser polymorphism on the post-translational regulation of CYP1B1 expression. Mol Pharmacol 2005; 67: 435-443.
    • (2005) Mol Pharmacol , vol.67 , pp. 435-443
    • Bandiera, S.1    Weidlich, S.2    Harth, V.3    Broede, P.4    Ko, Y.5    Friedberg, T.6
  • 9
    • 0033979374 scopus 로고    scopus 로고
    • Identification of a ubiquitination target/ substrate-interaction domain of cytochrome P-450 (CYP) 2E1
    • Banerjee A, Kocarek TA, Novak RF. Identification of a ubiquitination target/ substrate-interaction domain of cytochrome P-450 (CYP) 2E1. Drug Metab Dispos 2000; 28: 118-124.
    • (2000) Drug Metab Dispos , vol.28 , pp. 118-124
    • Banerjee, A.1    Kocarek, T.A.2    Novak, R.F.3
  • 10
    • 0036139602 scopus 로고    scopus 로고
    • Ethanol withdrawal induced CYP2e1 degradation in vivo blocked by proteasome inhibitor PS-341
    • Bardag-Gorce F, Li J, French BA, French SW. Ethanol withdrawal induced CYP2e1 degradation in vivo blocked by proteasome inhibitor PS-341. Free Radic Biol Med 2002; 32: 17-21.
    • (2002) Free Radic Biol Med , vol.32 , pp. 17-21
    • Bardag-Gorce, F.1    Li, J.2    French, B.A.3    French, S.W.4
  • 11
    • 0028900699 scopus 로고
    • Rabbit P450 2E1 expressed in CHO-K1 cells has a short half-life
    • Barmada S, Kienle E, Koop DR. Rabbit P450 2E1 expressed in CHO-K1 cells has a short half-life. Biochem Biophys Res Commun 1995; 206: 601-607.
    • (1995) Biochem Biophys Res Commun , vol.206 , pp. 601-607
    • Barmada, S.1    Kienle, E.2    Koop, D.R.3
  • 12
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY. Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 2001a; 3: 24-29.
    • (2001) Nat Cell Biol , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 14
    • 14744293006 scopus 로고    scopus 로고
    • Cdc48-Ufd2-Rad23: the road less ubiquitinated?
    • Bazirgan OA, Hampton RY. Cdc48-Ufd2-Rad23: the road less ubiquitinated? Nat Cell Biol 2005; 7: 207-209.
    • (2005) Nat Cell Biol , vol.7 , pp. 207-209
    • Bazirgan, O.A.1    Hampton, R.Y.2
  • 16
    • 0030822761 scopus 로고    scopus 로고
    • Epitope mapping of human CYP1A2 in dihydralazine-induced autoimmune hepatitis
    • Belloc C, Gauffre A, André C, Beaune PH. Epitope mapping of human CYP1A2 in dihydralazine-induced autoimmune hepatitis. Pharmacogenetics 1997; 7: 181-186.
    • (1997) Pharmacogenetics , vol.7 , pp. 181-186
    • Belloc, C.1    Gauffre, A.2    André, C.3    Beaune, P.H.4
  • 17
    • 76549170813 scopus 로고
    • Influence of turnover rates on the responses of enzymes to cortisone
    • Berlin CM, Schimke RT. Influence of turnover rates on the responses of enzymes to cortisone. Mol Pharmacol 1965; 1: 149-156.
    • (1965) Mol Pharmacol , vol.1 , pp. 149-156
    • Berlin, C.M.1    Schimke, R.T.2
  • 18
    • 45849153870 scopus 로고    scopus 로고
    • The HECT family of E3 ubiquitin ligases: multiple players in cancer development
    • Bernassola F, Karin M, Ciechanover A, Melino G. The HECT family of E3 ubiquitin ligases: multiple players in cancer development. Cancer Cell 2008; 14: 10-21.
    • (2008) Cancer Cell , vol.14 , pp. 10-21
    • Bernassola, F.1    Karin, M.2    Ciechanover, A.3    Melino, G.4
  • 19
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cue1p in ubiquitination and degradation at the ER surface
    • Biederer T, Volkwein C, Sommer T. Role of Cue1p in ubiquitination and degradation at the ER surface. Science 1997; 278: 1806-1809.
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 20
    • 0015592534 scopus 로고
    • A morphometric study of the removal of phenobarbital induced membranes from hepatocytes after cessation of treatment
    • Bolender R, Weibel E. A morphometric study of the removal of phenobarbital induced membranes from hepatocytes after cessation of treatment. J Cell Biol 1973; 56: 746-761.
    • (1973) J Cell Biol , vol.56 , pp. 746-761
    • Bolender, R.1    Weibel, E.2
  • 22
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 2003; 72: 395-447.
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 25
    • 0029816947 scopus 로고    scopus 로고
    • Characterization of the human cytochrome P4502D6 promoter: A potential role for antagonistic interactions between members of the nuclear receptor family
    • Cairns W, Smith CA, McLaren AW, Wolf CR. Characterization of the human cytochrome P4502D6 promoter: A potential role for antagonistic interactions between members of the nuclear receptor family. J Biol Chem 1996; 271: 25269-25276.
    • (1996) J Biol Chem , vol.271 , pp. 25269-25276
    • Cairns, W.1    Smith, C.A.2    McLaren, A.W.3    Wolf, C.R.4
  • 26
    • 0035192944 scopus 로고    scopus 로고
    • Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: evidence for mechanism-based inactivation of CYP1A2
    • Chang TK, Chen J, Lee WB. Differential inhibition and inactivation of human CYP1 enzymes by trans-resveratrol: evidence for mechanism-based inactivation of CYP1A2. J Pharmacol Exp Ther 2001; 299: 874-882.
    • (2001) J Pharmacol Exp Ther , vol.299 , pp. 874-882
    • Chang, T.K.1    Chen, J.2    Lee, W.B.3
  • 27
    • 0142181023 scopus 로고    scopus 로고
    • Human cytochrome P450 inhibition and metabolic-intermediate complex formation by goldenseal extract and its methylenedioxyphenyl components
    • Chatterjee P, Franklin MR. Human cytochrome P450 inhibition and metabolic-intermediate complex formation by goldenseal extract and its methylenedioxyphenyl components. Drug Metab Dispos 2003; 31: 1391-1397.
    • (2003) Drug Metab Dispos , vol.31 , pp. 1391-1397
    • Chatterjee, P.1    Franklin, M.R.2
  • 28
    • 0029146930 scopus 로고
    • Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway
    • Chen Z, Hagler J, Palombella VJ, Melandri F, Scherer D. Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway. Genes Dev 1995; 9: 1586-1597.
    • (1995) Genes Dev , vol.9 , pp. 1586-1597
    • Chen, Z.1    Hagler, J.2    Palombella, V.J.3    Melandri, F.4    Scherer, D.5
  • 29
    • 0030802792 scopus 로고    scopus 로고
    • Pharmacokinetic consequences of induction of CYP2E1 by ligand stabilization
    • Chien JY, Thummel KE, Slattery JT. Pharmacokinetic consequences of induction of CYP2E1 by ligand stabilization. Drug Metab Dispos 1997; 25: 1165-1175.
    • (1997) Drug Metab Dispos , vol.25 , pp. 1165-1175
    • Chien, J.Y.1    Thummel, K.E.2    Slattery, J.T.3
  • 30
    • 1442323729 scopus 로고    scopus 로고
    • N-terminal ubiquitination: more protein substrates join in
    • Ciechanover A, Ben-Saadon R. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol 2004; 14: 103-106.
    • (2004) Trends Cell Biol , vol.14 , pp. 103-106
    • Ciechanover, A.1    Ben-Saadon, R.2
  • 31
    • 0018992813 scopus 로고
    • ATP dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation
    • Ciechanover A, Heller H, Elias S, Haas AL, Hershko A. ATP dependent conjugation of reticulocyte proteins with the polypeptide required for protein degradation. Proc Natl Acad Sci USA 1980; 77: 1365-1368.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 1365-1368
    • Ciechanover, A.1    Heller, H.2    Elias, S.3    Haas, A.L.4    Hershko, A.5
  • 32
    • 0026356874 scopus 로고
    • Cytochrome P450 turnover
    • Correia MA. Cytochrome P450 turnover. Methods Enzymol 1991; 206: 315-325.
    • (1991) Methods Enzymol , vol.206 , pp. 315-325
    • Correia, M.A.1
  • 33
    • 0042357403 scopus 로고    scopus 로고
    • Hepatic cytochrome P450 degradation: mechanistic diversity of the cellular sanitation brigade
    • Correia MA. Hepatic cytochrome P450 degradation: mechanistic diversity of the cellular sanitation brigade. Drug Metab Rev 2003; 35: 107-143.
    • (2003) Drug Metab Rev , vol.35 , pp. 107-143
    • Correia, M.A.1
  • 34
    • 33745819422 scopus 로고    scopus 로고
    • Human and rat liver cytochromes P450: functional markers, diagnostic inhibitor probes and parameters frequently used in P450 studies
    • Ortiz de Montellano P, editor New York: Kluwer-Academic/Plenum Press
    • Correia MA. Human and rat liver cytochromes P450: functional markers, diagnostic inhibitor probes and parameters frequently used in P450 studies. In: Ortiz de Montellano P, editor. Cytochrome P450: Structure, Mechanism and Biochemistry. New York: Kluwer-Academic/Plenum Press, 2005, pp. 619-657.
    • (2005) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 619-657
    • Correia, M.A.1
  • 35
    • 34250314575 scopus 로고    scopus 로고
    • Cellular proteolytic systems in P450 degradation: evolutionary conservation from Saccharomyces cerevisiae to mammalian liver
    • Correia MA, Liao M. Cellular proteolytic systems in P450 degradation: evolutionary conservation from Saccharomyces cerevisiae to mammalian liver. Expert Opin Drug Metab Toxicol 2007; 3: 33-49.
    • (2007) Expert Opin Drug Metab Toxicol , vol.3 , pp. 33-49
    • Correia, M.A.1    Liao, M.2
  • 37
    • 84908722494 scopus 로고
    • Effect of cimetidine on phenobarbitone-induced changes in hepatic cytochrome P450 and d-aminolaevulinic acid synthase
    • Correia MA, Litman DA, McColl KEL, Schmid R, Thompson GC. Effect of cimetidine on phenobarbitone-induced changes in hepatic cytochrome P450 and d-aminolaevulinic acid synthase. Proc Br Pharmacol 1983;C 24.
    • (1983) Proc Br Pharmacol
    • Correia, M.A.1    Litman, D.A.2    McColl, K.E.L.3    Schmid, R.4    Thompson, G.C.5
  • 38
    • 0023447289 scopus 로고
    • Degradation of rat hepatic cytochrome P-450 heme by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine to irreversibly bound protein adducts
    • Correia MA, Decker C, Sugiyama K, Caldera P, Bornheim L, Wrighton SA, Rettie AE, Trager WF. Degradation of rat hepatic cytochrome P-450 heme by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine to irreversibly bound protein adducts. Arch Biochem Biophys 1987; 258: 436-451.
    • (1987) Arch Biochem Biophys , vol.258 , pp. 436-451
    • Correia, M.A.1    Decker, C.2    Sugiyama, K.3    Caldera, P.4    Bornheim, L.5    Wrighton, S.A.6    Rettie, A.E.7    Trager, W.F.8
  • 39
    • 0024448249 scopus 로고
    • Degradation of rat hepatic cytochrome P-450p
    • Correia MA, Sugiyama K, Yao KQ. Degradation of rat hepatic cytochrome P-450p. Drug Metab Rev 1989; 20: 615-628.
    • (1989) Drug Metab Rev , vol.20 , pp. 615-628
    • Correia, M.A.1    Sugiyama, K.2    Yao, K.Q.3
  • 40
    • 0026989765 scopus 로고
    • Degradation of rat liver cytochromes P-450 3A after their inactivation by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine: Characterization of the proteolytic system
    • Correia MA, Davoll SH, Wrighton SA, Thomas PE. Degradation of rat liver cytochromes P-450 3A after their inactivation by 3,5-dicarbethoxy-2,6-dimethyl-4-ethyl-1,4-dihydropyridine: Characterization of the proteolytic system. Arch Biochem Biophys 1992; 297: 228-238.
    • (1992) Arch Biochem Biophys , vol.297 , pp. 228-238
    • Correia, M.A.1    Davoll, S.H.2    Wrighton, S.A.3    Thomas, P.E.4
  • 41
    • 13844314200 scopus 로고    scopus 로고
    • Cytochrome P450 ubiquitination: branding for the proteolytic slaughter?
    • Correia MA, Sadeghi S, Mundo-Paredes E. Cytochrome P450 ubiquitination: branding for the proteolytic slaughter? Annu Rev Pharmacol Toxicol 2005; 45: 439-464.
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 439-464
    • Correia, M.A.1    Sadeghi, S.2    Mundo-Paredes, E.3
  • 42
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem Biochem 1996; 65: 801-847.
    • (1996) Annu Rev Biochem Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 43
    • 0031883733 scopus 로고    scopus 로고
    • Lysosomes, a meeting point of proteins, chaperones, and proteases
    • Cuervo AM, Dice JF. Lysosomes, a meeting point of proteins, chaperones, and proteases. J Mol Med 1998; 76: 6-12.
    • (1998) J Mol Med , vol.76 , pp. 6-12
    • Cuervo, A.M.1    Dice, J.F.2
  • 44
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D. Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004; 305: 1292-1295.
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 45
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • Cyr DM, Höhfeld J, Patterson C. Protein quality control: U-box-containing E3 ubiquitin ligases join the fold. Trends Biochem Sci 2002; 27: 368-375.
    • (2002) Trends Biochem Sci , vol.27 , pp. 368-375
    • Cyr, D.M.1    Höhfeld, J.2    Patterson, C.3
  • 46
    • 0034907973 scopus 로고    scopus 로고
    • Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation
    • Dai RM, Li CC. Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat Cell Biol 2001; 3: 740-744.
    • (2001) Nat Cell Biol , vol.3 , pp. 740-744
    • Dai, R.M.1    Li, C.C.2
  • 47
    • 0029553016 scopus 로고
    • Inactivation and degradation of human cytochrome P4502E1 by CCl4 in a transfected HepG2 cell line
    • Dai Y, Cederbaum A. Inactivation and degradation of human cytochrome P4502E1 by CCl4 in a transfected HepG2 cell line. J Pharmacol Exp Ther 1995; 275: 1614-1622.
    • (1995) J Pharmacol Exp Ther , vol.275 , pp. 1614-1622
    • Dai, Y.1    Cederbaum, A.2
  • 48
    • 11244257361 scopus 로고
    • Enzymic content of the mitochondria fraction
    • London
    • de Duve C, Gianetto R, Appelmans F, Wattiaux R. Enzymic content of the mitochondria fraction. Nature (London) 1953; 172: 1143-1144.
    • (1953) Nature , vol.172 , pp. 1143-1144
    • de Duve, C.1    Gianetto, R.2    Appelmans, F.3    Wattiaux, R.4
  • 50
    • 34250167524 scopus 로고    scopus 로고
    • Rates of processing determine the immunogenicity of immunoproteasome-generated epitopes
    • Deol P, Zaiss DM, Monaco JJ, Sijts AJ. Rates of processing determine the immunogenicity of immunoproteasome-generated epitopes. J Immunol 2007; 178: 7557-7562.
    • (2007) J Immunol , vol.178 , pp. 7557-7562
    • Deol, P.1    Zaiss, D.M.2    Monaco, J.J.3    Sijts, A.J.4
  • 51
    • 0023545339 scopus 로고
    • Molecular determinants of protein half-lives in eukaryotic cells
    • Dice JF. Molecular determinants of protein half-lives in eukaryotic cells. FASEB J 1987; 1: 349-357.
    • (1987) FASEB J , vol.1 , pp. 349-357
    • Dice, J.F.1
  • 53
    • 0029937677 scopus 로고    scopus 로고
    • Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone
    • Dick LR, Cruikshank AA, Grenier L, Melandri FD, Nunes SL, Stein RL. Mechanistic studies on the inactivation of the proteasome by lactacystin: a central role for clasto-lactacystin beta-lactone. J Biol Chem 1996; 271: 7273-7276.
    • (1996) J Biol Chem , vol.271 , pp. 7273-7276
    • Dick, L.R.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Stein, R.L.6
  • 54
    • 4644243461 scopus 로고    scopus 로고
    • Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for sterol-regulated enzyme degradation
    • Doolman R, Leichner GS, Avner R, Roitelman J. Ubiquitin is conjugated by membrane ubiquitin ligase to three sites, including the N terminus, in transmembrane region of mammalian 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for sterol-regulated enzyme degradation. J Biol Chem 2004; 279: 38184-38193.
    • (2004) J Biol Chem , vol.279 , pp. 38184-38193
    • Doolman, R.1    Leichner, G.S.2    Avner, R.3    Roitelman, J.4
  • 55
    • 0036802227 scopus 로고    scopus 로고
    • Recent developments in the intracellular degradation of oxidized proteins
    • Dunlop RA, Rodgers KJ, Dean RT. Recent developments in the intracellular degradation of oxidized proteins. Free Radic Biol Med 2002; 33: 894-906.
    • (2002) Free Radic Biol Med , vol.33 , pp. 894-906
    • Dunlop, R.A.1    Rodgers, K.J.2    Dean, R.T.3
  • 56
    • 0029786269 scopus 로고    scopus 로고
    • Cytochrome P450 2E1 is a cell surface autoantigen in halothane hepatitis
    • Eliasson E, Kenna JG. Cytochrome P450 2E1 is a cell surface autoantigen in halothane hepatitis. Mol Pharmacol 1996; 50: 573-582.
    • (1996) Mol Pharmacol , vol.50 , pp. 573-582
    • Eliasson, E.1    Kenna, J.G.2
  • 57
  • 58
    • 0026773423 scopus 로고
    • Hormone-and substrate-regulated intracellular degradation of cytochrome P450 (2E1) involving MgATP-activated rapid proteolysis in the endoplasmic reticulum membranes
    • Eliasson E, Mkrtchian S, Ingelman-Sundberg M. Hormone-and substrate-regulated intracellular degradation of cytochrome P450 (2E1) involving MgATP-activated rapid proteolysis in the endoplasmic reticulum membranes. J Biol Chem 1992; 267: 15765-15769.
    • (1992) J Biol Chem , vol.267 , pp. 15765-15769
    • Eliasson, E.1    Mkrtchian, S.2    Ingelman-Sundberg, M.3
  • 59
    • 0028277268 scopus 로고
    • Substrate-regulated, cAMP-dependent phosphorylation, denaturation, and degradation of glucocorticoid-inducible rat liver cytochrome P450 3A1
    • Eliasson E, Mkrtchian S, Halpert JR, Ingelman-Sundberg M. Substrate-regulated, cAMP-dependent phosphorylation, denaturation, and degradation of glucocorticoid-inducible rat liver cytochrome P450 3A1. J Biol Chem 1994; 269: 18378-18383.
    • (1994) J Biol Chem , vol.269 , pp. 18378-18383
    • Eliasson, E.1    Mkrtchian, S.2    Halpert, J.R.3    Ingelman-Sundberg, M.4
  • 60
    • 13244299150 scopus 로고    scopus 로고
    • Mechanism-based inactivation of CYP3A by HIV protease inhibitors
    • Ernest CS 2nd, Hall SD, Jones DR. Mechanism-based inactivation of CYP3A by HIV protease inhibitors. J Pharmacol Exptl Ther 2005; 312: 583-591.
    • (2005) J Pharmacol Exptl Ther , vol.312 , pp. 583-591
    • Ernest II, C.S.1    Hall, S.D.2    Jones, D.R.3
  • 61
    • 0033569516 scopus 로고    scopus 로고
    • Pharmacogenomics: translating functional genomics into rational therapeutics
    • Evans WE, Relling MV. Pharmacogenomics: translating functional genomics into rational therapeutics. Science 1999; 286: 487-491.
    • (1999) Science , vol.286 , pp. 487-491
    • Evans, W.E.1    Relling, M.V.2
  • 62
    • 34347354365 scopus 로고    scopus 로고
    • Characterization of the physiological turnover of native and inactivated cytochromes P450 3A in cultured rat hepatocytes: a role for the cytosolic AAA ATPase P97?
    • Faouzi S, Medzihradszky KF, Hefner C, Maher JJ, Correia MA. Characterization of the physiological turnover of native and inactivated cytochromes P450 3A in cultured rat hepatocytes: a role for the cytosolic AAA ATPase P97? Biochemistry 2007; 46: 7793-7803.
    • (2007) Biochemistry , vol.46 , pp. 7793-7803
    • Faouzi, S.1    Medzihradszky, K.F.2    Hefner, C.3    Maher, J.J.4    Correia, M.A.5
  • 63
    • 0036091895 scopus 로고    scopus 로고
    • Ubiquitin chained and crosslinked
    • Finley D. Ubiquitin chained and crosslinked. Nat Cell Biol 2002; 4 :E 121-E 123.
    • (2002) Nat Cell Biol , vol.4
    • Finley, D.1
  • 64
    • 48249104628 scopus 로고    scopus 로고
    • Induction effects of ritonavir: implications for drug interactions
    • Foisy MM, Yakiwchuk EM, Hughes CA. Induction effects of ritonavir: implications for drug interactions. Ann Pharmacother 2008; 42: 1048-1059.
    • (2008) Ann Pharmacother , vol.42 , pp. 1048-1059
    • Foisy, M.M.1    Yakiwchuk, E.M.2    Hughes, C.A.3
  • 65
    • 0028149146 scopus 로고
    • Evidence against a role for serine 129 in determining murine cytochrome P450 Cyp2E-1 protein levels
    • Freeman JE, Wolf CR. Evidence against a role for serine 129 in determining murine cytochrome P450 Cyp2E-1 protein levels. Biochemistry 1994; 33: 13963-13966.
    • (1994) Biochemistry , vol.33 , pp. 13963-13966
    • Freeman, J.E.1    Wolf, C.R.2
  • 66
    • 0033961923 scopus 로고    scopus 로고
    • RING for destruction?
    • Freemont PS. RING for destruction? Curr Biol 2000; 10 :R 84-R 87.
    • (2000) Curr Biol , vol.10
    • Freemont, P.S.1
  • 67
    • 0033231014 scopus 로고    scopus 로고
    • A " distributed degron " allows regulated entry into the ER degradation pathway
    • Gardner RG, Hampton RY. A " distributed degron " allows regulated entry into the ER degradation pathway. EMBO J 1999; 18: 5994-6004.
    • (1999) EMBO J , vol.18 , pp. 5994-6004
    • Gardner, R.G.1    Hampton, R.Y.2
  • 68
    • 58149347476 scopus 로고    scopus 로고
    • Grapefruit juice-drug interaction studies as a method to assess the extent of intestinal availability: utility and limitations
    • Gertz M, Davis JD, Harrison A, Houston JB, Galetin A. Grapefruit juice-drug interaction studies as a method to assess the extent of intestinal availability: utility and limitations. Curr Drug Metab 2008; 9: 785-795.
    • (2008) Curr Drug Metab , vol.9 , pp. 785-795
    • Gertz, M.1    Davis, J.D.2    Harrison, A.3    Houston, J.B.4    Galetin, A.5
  • 69
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome pathway: Destruction for the sake of construction. Physiol Rev 2002; 82: 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 70
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman MH, Rubin DM, Fried VA, Finley D. The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol 1998; 18: 3149-3162.
    • (1998) Mol Cell Biol , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 71
    • 0026089183 scopus 로고
    • Cyclin is degraded by the ubiquitin pathway
    • Glotzer M, Murray AW, Kirschner MW. Cyclin is degraded by the ubiquitin pathway. Nature 1991; 349: 132-138.
    • (1991) Nature , vol.349 , pp. 132-138
    • Glotzer, M.1    Murray, A.W.2    Kirschner, M.W.3
  • 72
    • 0033570101 scopus 로고    scopus 로고
    • NADP H-dependent microsomal electron transfer increases degradation of CYP2E1 by the proteasome complex: role of reactive oxygen species
    • Goasduff T, Cederbaum AI. NADP H-dependent microsomal electron transfer increases degradation of CYP2E1 by the proteasome complex: role of reactive oxygen species. Arch Biochem Biophys 1999; 370: 258-270.
    • (1999) Arch Biochem Biophys , vol.370 , pp. 258-270
    • Goasduff, T.1    Cederbaum, A.I.2
  • 73
    • 0034661466 scopus 로고    scopus 로고
    • CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90
    • Goasduff T, Cederbaum AI. CYP2E1 degradation by in vitro reconstituted systems: role of the molecular chaperone hsp90. Arch Biochem Biophys 2000; 379: 321-330.
    • (2000) Arch Biochem Biophys , vol.379 , pp. 321-330
    • Goasduff, T.1    Cederbaum, A.I.2
  • 74
    • 0016908233 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells: Part 2
    • Goldberg AL, St. John AC. Intracellular protein degradation in mammalian and bacterial cells: Part 2. Annu Rev Biochem 1976; 45: 747-803.
    • (1976) Annu Rev Biochem , vol.45 , pp. 747-803
    • Goldberg, A.L.1    St. John, A.C.2
  • 75
    • 0025690898 scopus 로고
    • ATP-dependent proteases in prokaryotic and eukaryotic cells
    • Goldberg AL. ATP-dependent proteases in prokaryotic and eukaryotic cells. Semin Cell Biol 1991; 1: 423-432.
    • (1991) Semin Cell Biol , vol.1 , pp. 423-432
    • Goldberg, A.L.1
  • 76
    • 33847066706 scopus 로고    scopus 로고
    • Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy
    • Goldberg AL. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem Soc Trans 2007; 35: 12-17.
    • (2007) Biochem Soc Trans , vol.35 , pp. 12-17
    • Goldberg, A.L.1
  • 77
    • 0022971547 scopus 로고
    • Depression of cytochrome P-450 and alterations of protein metabolism in mice treated with the interferon inducer polyriboinosinic acid: polyribocytidylic acid
    • Gooderham NJ, Mannering GJ. Depression of cytochrome P-450 and alterations of protein metabolism in mice treated with the interferon inducer polyriboinosinic acid: polyribocytidylic acid. Arch Biochem Biophys 1986; 250: 418-425.
    • (1986) Arch Biochem Biophys , vol.250 , pp. 418-425
    • Gooderham, N.J.1    Mannering, G.J.2
  • 78
    • 84892246340 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes
    • Ortiz de Montellano P, editor New York: Kluwer-Academic/Plenum Press
    • Guengerich FP. Human cytochrome P450 enzymes. In: Ortiz de Montellano P, editor. Cytochrome P450: Structure, Mechanism and Biochemistry. New York: Kluwer-Academic/Plenum Press, 2005, pp. 377-530.
    • (2005) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 377-530
    • Guengerich, F.P.1
  • 79
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas AL, Siepmann TJ. Pathways of ubiquitin conjugation. FASEB J 1997; 11: 1257-1268.
    • (1997) FASEB J , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 80
    • 0021810622 scopus 로고
    • The inactivation of ubiquitin accounts for the inability to demonstrate ATP, ubiquitin-dependent proteolysis in liver extracts
    • Haas AL, Murphy KE, Bright PM. The inactivation of ubiquitin accounts for the inability to demonstrate ATP, ubiquitin-dependent proteolysis in liver extracts. J Biol Chem 1985; 260: 4694-4703.
    • (1985) J Biol Chem , vol.260 , pp. 4694-4703
    • Haas, A.L.1    Murphy, K.E.2    Bright, P.M.3
  • 81
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton RY. ER-associated degradation in protein quality control and cellular regulation. Curr Opin Cell Biol 2002; 14: 476-482.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 82
    • 0028213166 scopus 로고
    • Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast
    • Hampton RY, Rine J. Regulated degradation of HMG-CoA reductase, an integral membrane protein of the endoplasmic reticulum, in yeast. J Cell Biol 1994; 125: 299-312.
    • (1994) J Cell Biol , vol.125 , pp. 299-312
    • Hampton, R.Y.1    Rine, J.2
  • 83
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton RY, Gardner RG, Rine J. Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol Biol Cell 1996; 7: 2029-2044.
    • (1996) Mol Biol Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 84
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DERindependent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • Haynes CM, Caldwell S, Cooper AA. An HRD/DERindependent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J Cell Biol 2002; 158: 91-101.
    • (2002) J Cell Biol , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 85
    • 0037905938 scopus 로고    scopus 로고
    • Secobarbital-mediated in activation of cytochrome P450 2B1 and its active site mutants: partitioning between heme and protein alkylation and epoxidation
    • He K, He YA, Szklarz GD, Halpert JR, Correia MA. Secobarbital-mediated in activation of cytochrome P450 2B1 and its active site mutants: partitioning between heme and protein alkylation and epoxidation. J Biol Chem 1996; 271: 25864-25872.
    • (1996) J Biol Chem , vol.271 , pp. 25864-25872
    • He, K.1    He, Y.A.2    Szklarz, G.D.3    Halpert, J.R.4    Correia, M.A.5
  • 86
    • 0032534908 scopus 로고    scopus 로고
    • Identification of the heme-modified peptides from cumene hydroperoxide-inactivated cytochrome P450 3A4
    • He K, Bornheim LM, Falick AM, Maltby D, Yin H, Correia MA. Identification of the heme-modified peptides from cumene hydroperoxide-inactivated cytochrome P450 3A4. Biochemistry 1998; 37: 17448-17457.
    • (1998) Biochemistry , vol.37 , pp. 17448-17457
    • He, K.1    Bornheim, L.M.2    Falick, A.M.3    Maltby, D.4    Yin, H.5    Correia, M.A.6
  • 87
    • 21544475903 scopus 로고    scopus 로고
    • IFN γ-induced immune adaptation of the proteasome system is an accelerated and transient response
    • Heink S, Ludwig D, Kloetzel P, Kruger E. IFN γ-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc Natl Acad Sci USA 2005; 102: 9241-9246.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9241-9246
    • Heink, S.1    Ludwig, D.2    Kloetzel, P.3    Kruger, E.4
  • 88
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko A, Ciechanover A. The ubiquitin system for protein degradation. Annu Rev Biochem 1992; 61: 761-807.
    • (1992) Annu Rev Biochem , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 91
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2001; 2: 195-201.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 195-201
    • Hicke, L.1
  • 92
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor
    • Hochstrasser M, Varshavsky A. In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor. Cell 1990; 61: 697-708.
    • (1990) Cell , vol.61 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 94
    • 38949099990 scopus 로고    scopus 로고
    • Mechanism-based inactivation of human cytochromes P450s: experimental characterization, reactive intermediates, and clinical implications
    • Hollenberg PF, Kent UM, Bumpus NN. Mechanism-based inactivation of human cytochromes P450s: experimental characterization, reactive intermediates, and clinical implications. Chem Res Toxicol 2008; 21: 189-205.
    • (2008) Chem Res Toxicol , vol.21 , pp. 189-205
    • Hollenberg, P.F.1    Kent, U.M.2    Bumpus, N.N.3
  • 95
    • 0032893473 scopus 로고    scopus 로고
    • Tightly regulated and inducible expression of rabbit CYP2E1 using a tetracycline-controlled expression system
    • Huan JY, Koop DR. Tightly regulated and inducible expression of rabbit CYP2E1 using a tetracycline-controlled expression system. Drug Metab Dispos 1999; 27: 549-554.
    • (1999) Drug Metab Dispos , vol.27 , pp. 549-554
    • Huan, J.Y.1    Koop, D.R.2
  • 96
    • 4444283077 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of cytochromes P450 2E1 and 2B1 expressed in tetracycline-regulated HeLa cells
    • Huan JY, Streicher JM, Bleyle LA, Koop DR. Proteasome-dependent degradation of cytochromes P450 2E1 and 2B1 expressed in tetracycline-regulated HeLa cells. Toxicol Appl Pharmacol 2004; 199: 332-343.
    • (2004) Toxicol Appl Pharmacol , vol.199 , pp. 332-343
    • Huan, J.Y.1    Streicher, J.M.2    Bleyle, L.A.3    Koop, D.R.4
  • 97
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
    • Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S. Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 2004; 279: 38369-38378.
    • (2004) J Biol Chem , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 98
    • 28744449655 scopus 로고    scopus 로고
    • A new epitope of CYP2D6 recognized by liver kidney microsomal autoantibody from japanese patients with autoimmune hepatitis
    • Imaoka S, Obata N, Hiroi T, Osada-Oka M, Hara R, Nishiguchi S, Funae Y. A new epitope of CYP2D6 recognized by liver kidney microsomal autoantibody from japanese patients with autoimmune hepatitis. Biol Pharm Bull 2005; 28: 2240-2243.
    • (2005) Biol Pharm Bull , vol.28 , pp. 2240-2243
    • Imaoka, S.1    Obata, N.2    Hiroi, T.3    Osada-Oka, M.4    Hara, R.5    Nishiguchi, S.6    Funae, Y.7
  • 99
    • 0036023402 scopus 로고    scopus 로고
    • Differential effect of IFN a-2b on the cytochrome P450 enzyme system: a potential basis of IFN toxicity and its modulation by other drugs
    • Islam M, Frye RF, Richards TJ, Sbeitan I, Donnelly SS, Glue P, Agarwala SS, Kirkwood JM. Differential effect of IFN a-2b on the cytochrome P450 enzyme system: a potential basis of IFN toxicity and its modulation by other drugs. Clin Cancer Res 2002; 8: 2480-2487.
    • (2002) Clin Cancer Res , vol.8 , pp. 2480-2487
    • Islam, M.1    Frye, R.F.2    Richards, T.J.3    Sbeitan, I.4    Donnelly, S.S.5    Glue, P.6    Agarwala, S.S.7    Kirkwood, J.M.8
  • 100
    • 0027179010 scopus 로고
    • Effects of interferon-a monotherapy on hepatic drug metabolism in cancer patients
    • Israel BC, Blouin RA, McIntyre W, Shedlofsky SI. Effects of interferon-a monotherapy on hepatic drug metabolism in cancer patients. Br J Clin Pharmacol 1993; 36: 229-235.
    • (1993) Br J Clin Pharmacol , vol.36 , pp. 229-235
    • Israel, B.C.1    Blouin, R.A.2    McIntyre, W.3    Shedlofsky, S.I.4
  • 103
    • 55449134163 scopus 로고    scopus 로고
    • Lysosomal targeting and trafficking of acid sphingomyelinase to lipid raft platforms in coronary endothelial cells
    • Jin S, Yi F, Zhang F, Poklis JL, Li PL. Lysosomal targeting and trafficking of acid sphingomyelinase to lipid raft platforms in coronary endothelial cells. Arterioscler Thromb Vasc Biol 2008; 28: 2056-2062.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 2056-2062
    • Jin, S.1    Yi, F.2    Zhang, F.3    Poklis, J.L.4    Li, P.L.5
  • 104
    • 0034266806 scopus 로고    scopus 로고
    • RING finger proteins: mediators of ubiquitin ligase activity
    • Joazeiro CA, Weissman AM. RING finger proteins: mediators of ubiquitin ligase activity. Cell 2000; 102: 549-552.
    • (2000) Cell , vol.102 , pp. 549-552
    • Joazeiro, C.A.1    Weissman, A.M.2
  • 105
    • 49149088172 scopus 로고    scopus 로고
    • Endothelin receptor antagonism: role in the treatment of pulmonary arterial hypertension related to scleroderma
    • Kabunga P, Coghlan G. Endothelin receptor antagonism: role in the treatment of pulmonary arterial hypertension related to scleroderma. Drugs 2008; 68: 1635-1645.
    • (2008) Drugs , vol.68 , pp. 1635-1645
    • Kabunga, P.1    Coghlan, G.2
  • 106
    • 40949102296 scopus 로고    scopus 로고
    • CYP3A4-Mediated carbamazepine (CBZ) metabolism: formation of a covalent CBZ-CYP3A4 adduct and alteration of the enzyme kinetic profile
    • Kang P, Liao M, Wester MR, Leeder JS, Pearce RE, Correia MA. CYP3A4-Mediated carbamazepine (CBZ) metabolism: formation of a covalent CBZ-CYP3A4 adduct and alteration of the enzyme kinetic profile. Drug Metab Dispos 2008; 36: 490-499.
    • (2008) Drug Metab Dispos , vol.36 , pp. 490-499
    • Kang, P.1    Liao, M.2    Wester, M.R.3    Leeder, J.S.4    Pearce, R.E.5    Correia, M.A.6
  • 107
    • 33646498651 scopus 로고    scopus 로고
    • The quantitative prediction of in vivo enzyme-induction caused by drug exposure from in vitro information on human hepatocytes
    • Kato M, Chiba K, Horikawa M, Sugiyama Y. The quantitative prediction of in vivo enzyme-induction caused by drug exposure from in vitro information on human hepatocytes. Drug Metab Pharmacokinet 2005; 20: 236-243.
    • (2005) Drug Metab Pharmacokinet , vol.20 , pp. 236-243
    • Kato, M.1    Chiba, K.2    Horikawa, M.3    Sugiyama, Y.4
  • 109
    • 4344680011 scopus 로고    scopus 로고
    • Influence of hepatic and intestinal cytochrome P4503A activity on the acute disposition and effects of oral transmucosal fentanyl citrate
    • Kharasch ED, Whittington D, Hoffer C. Influence of hepatic and intestinal cytochrome P4503A activity on the acute disposition and effects of oral transmucosal fentanyl citrate. Anesthesiology 2004; 101: 729-737.
    • (2004) Anesthesiology , vol.101 , pp. 729-737
    • Kharasch, E.D.1    Whittington, D.2    Hoffer, C.3
  • 111
    • 0242349770 scopus 로고    scopus 로고
    • Hydroperoxy-10,12-octadecadienoic acid stimulates cytochrome P450 3A protein aggregation by a mechanism that is inhibited by substrate
    • Kimzey AL, Weitz KK, Guengerich FP, Zangar RC. Hydroperoxy-10,12-octadecadienoic acid stimulates cytochrome P450 3A protein aggregation by a mechanism that is inhibited by substrate. Biochemistry 2003; 42: 12691-12699.
    • (2003) Biochemistry , vol.42 , pp. 12691-12699
    • Kimzey, A.L.1    Weitz, K.K.2    Guengerich, F.P.3    Zangar, R.C.4
  • 112
    • 0029787091 scopus 로고    scopus 로고
    • Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates
    • King RW, Glotzer M, Kirschner MW. Mutagenic analysis of the destruction signal of mitotic cyclins and structural characterization of ubiquitinated intermediates. Mol Biol Cell 1996; 7: 1343-1357.
    • (1996) Mol Biol Cell , vol.7 , pp. 1343-1357
    • King, R.W.1    Glotzer, M.2    Kirschner, M.W.3
  • 113
    • 14044277429 scopus 로고    scopus 로고
    • The molecular machinery of autophagy: unanswered questions
    • Klionsky DJ. The molecular machinery of autophagy: unanswered questions. J Cell Sci 2005; 118: 7-18.
    • (2005) J Cell Sci , vol.118 , pp. 7-18
    • Klionsky, D.J.1
  • 114
    • 35448981935 scopus 로고    scopus 로고
    • Autophagy: from phenomenology to molecular understanding in less than a decade
    • Klionsky DJ. Autophagy: from phenomenology to molecular understanding in less than a decade. Nat Rev Mol Cell Biol 2007; 8: 931-937.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 931-937
    • Klionsky, D.J.1
  • 115
    • 0032516469 scopus 로고    scopus 로고
    • Mechanism-based inactivation of P450 2A6 by furanocoumarins
    • Koenigs LL, Trager WF. Mechanism-based inactivation of P450 2A6 by furanocoumarins. Biochemistry 1998; 37: 10047-10061.
    • (1998) Biochemistry , vol.37 , pp. 10047-10061
    • Koenigs, L.L.1    Trager, W.F.2
  • 117
    • 0025051251 scopus 로고
    • Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes
    • Kopitz J, Kisen GO, Gordon PB, Bohley P, Seglen PO. Nonselective autophagy of cytosolic enzymes by isolated rat hepatocytes. J Cell Biol 1990; 111: 941-953.
    • (1990) J Cell Biol , vol.111 , pp. 941-953
    • Kopitz, J.1    Kisen, G.O.2    Gordon, P.B.3    Bohley, P.4    Seglen, P.O.5
  • 118
    • 0033134224 scopus 로고    scopus 로고
    • Proteolytic degradation of heme-modified hepatic cytochromes P450: a role for phosphorylation, ubiquitination and the 26S proteasome?
    • Korsmeyer KK, Davoll S, Figueiredo-Pereira ME, Correia MA. Proteolytic degradation of heme-modified hepatic cytochromes P450: a role for phosphorylation, ubiquitination and the 26S proteasome? Arch Biochem Biophys 1999; 365: 31-44.
    • (1999) Arch Biochem Biophys , vol.365 , pp. 31-44
    • Korsmeyer, K.K.1    Davoll, S.2    Figueiredo-Pereira, M.E.3    Correia, M.A.4
  • 120
    • 0029790276 scopus 로고    scopus 로고
    • Tienilic acid-induced autoimmune hepatitis: anti-liver and-kidney microsomal type 2 autoantibodies recognize a three-site conformational epitope on cytochrome P4502C9
    • Lecoeur S, André C, Beaune PH. Tienilic acid-induced autoimmune hepatitis: anti-liver and-kidney microsomal type 2 autoantibodies recognize a three-site conformational epitope on cytochrome P4502C9. Mol Pharmacol 1996; 50: 326-333.
    • (1996) Mol Pharmacol , vol.50 , pp. 326-333
    • Lecoeur, S.1    André, C.2    Beaune, P.H.3
  • 121
    • 38149062111 scopus 로고    scopus 로고
    • Nitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins
    • Lee C, Kim B, Li L, Morgan ET. Nitric oxide-dependent proteasomal degradation of cytochrome P450 2B proteins. J Biol Chem 2008; 283: 889-898.
    • (2008) J Biol Chem , vol.283 , pp. 889-898
    • Lee, C.1    Kim, B.2    Li, L.3    Morgan, E.T.4
  • 122
    • 0026727963 scopus 로고
    • Human anti-cytochrome P450 antibodies in aromatic anticonvulsant-induced hypersensitivity
    • Leeder JS, Riley RJ, Cook VA, Spielberg SP. Human anti-cytochrome P450 antibodies in aromatic anticonvulsant-induced hypersensitivity. J Pharmacol Exp Ther 1992; 263: 360-367.
    • (1992) J Pharmacol Exp Ther , vol.263 , pp. 360-367
    • Leeder, J.S.1    Riley, R.J.2    Cook, V.A.3    Spielberg, S.P.4
  • 123
    • 0030063547 scopus 로고    scopus 로고
    • Epitope mapping studies with human anti-cytochrome P450 3A antibodies
    • Leeder JS, Gaedigk A, Lu X, Cook VA. Epitope mapping studies with human anti-cytochrome P450 3A antibodies. Mol Pharmacol 1996; 49: 234-243.
    • (1996) Mol Pharmacol , vol.49 , pp. 234-243
    • Leeder, J.S.1    Gaedigk, A.2    Lu, X.3    Cook, V.A.4
  • 124
    • 33745143290 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated degradation of cytochrome P450 CYP3A4 in Saccharomyces cerevisiae: Further characterization of cellular participants and structural determinants
    • Liao M, Faouzi S, Karyakin A, Correia MA. Endoplasmic reticulum-associated degradation of cytochrome P450 CYP3A4 in Saccharomyces cerevisiae: Further characterization of cellular participants and structural determinants. Mol Pharmacol 2006; 69: 1897-1904.
    • (2006) Mol Pharmacol , vol.69 , pp. 1897-1904
    • Liao, M.1    Faouzi, S.2    Karyakin, A.3    Correia, M.A.4
  • 125
    • 17844376185 scopus 로고    scopus 로고
    • Vacuolar degradation of rat liver CYP2B1 in Saccharomyces cerevisiae: Further validation of the yeast model and structural implications for the degradation of mammalian endoplasmic reticulum P450 proteins
    • Liao M, Zgoda VG, Murray BP, Correia MA. Vacuolar degradation of rat liver CYP2B1 in Saccharomyces cerevisiae: Further validation of the yeast model and structural implications for the degradation of mammalian endoplasmic reticulum P450 proteins. Mol Pharmacol 2005; 67: 1460-1469.
    • (2005) Mol Pharmacol , vol.67 , pp. 1460-1469
    • Liao, M.1    Zgoda, V.G.2    Murray, B.P.3    Correia, M.A.4
  • 126
    • 0036164027 scopus 로고    scopus 로고
    • Epitope mapping of cytochrome P450 cholesterol side-chain cleavage enzyme by sera from patients with autoimmune polyglandular syndrome type 1
    • Liiv I, Teesalu K, Peterson P, Clemente MG, Perheentupa J, Uibo R. Epitope mapping of cytochrome P450 cholesterol side-chain cleavage enzyme by sera from patients with autoimmune polyglandular syndrome type 1. Eur J Endocrinol 2002; 146: 113-119.
    • (2002) Eur J Endocrinol , vol.146 , pp. 113-119
    • Liiv, I.1    Teesalu, K.2    Peterson, P.3    Clemente, M.G.4    Perheentupa, J.5    Uibo, R.6
  • 127
    • 0023749075 scopus 로고
    • Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins
    • Lippincott-Schwartz J, Bonifacino JS, Yuan LC, Klausner RD. Degradation from the endoplasmic reticulum: disposing of newly synthesized proteins. Cell 1988; 54: 209-220.
    • (1988) Cell , vol.54 , pp. 209-220
    • Lippincott-Schwartz, J.1    Bonifacino, J.S.2    Yuan, L.C.3    Klausner, R.D.4
  • 128
    • 0036695061 scopus 로고    scopus 로고
    • Immune-mediated drug-induced liver disease
    • Liu ZX, Kaplowitz N. Immune-mediated drug-induced liver disease. Clin Liver Dis 2002; 6: 755-774.
    • (2002) Clin Liver Dis , vol.6 , pp. 755-774
    • Liu, Z.X.1    Kaplowitz, N.2
  • 129
    • 34249895621 scopus 로고    scopus 로고
    • Cytochrome P450IID6-specific CD8 T cell immune responses mirror disease activity in autoimmune hepatitis type 2
    • Longhi MS, Hussain MJ, Bogdanos DP, Quaglia A, Mieli-Vergani G, Ma Y, Vergani D. Cytochrome P450IID6-specific CD8 T cell immune responses mirror disease activity in autoimmune hepatitis type 2. Hepatology 2007; 46: 472-484.
    • (2007) Hepatology , vol.46 , pp. 472-484
    • Longhi, M.S.1    Hussain, M.J.2    Bogdanos, D.P.3    Quaglia, A.4    Mieli-Vergani, G.5    Ma, Y.6    Vergani, D.7
  • 132
    • 0040017910 scopus 로고    scopus 로고
    • Function of WW domains as phosphoserine-or phosphothreonine-binding modules
    • Lu P, Zhou X, Shen M, Lu K. Function of WW domains as phosphoserine-or phosphothreonine-binding modules. Science 1999; 283: 1325-1328.
    • (1999) Science , vol.283 , pp. 1325-1328
    • Lu, P.1    Zhou, X.2    Shen, M.3    Lu, K.4
  • 133
    • 34347392672 scopus 로고    scopus 로고
    • Aryl hydrocarbon receptor degradation-promoting factor (ADPF) and the control of the xenobiotic response
    • Ma Q. Aryl hydrocarbon receptor degradation-promoting factor (ADPF) and the control of the xenobiotic response. Mol Intervent 2007; 7: 133-137.
    • (2007) Mol Intervent , vol.7 , pp. 133-137
    • Ma, Q.1
  • 136
    • 0025992973 scopus 로고
    • LKM-1 autoantibodies recognize a short linear sequence in P450IID6, a cytochrome P-450 monooxygenase
    • Manns MP, Griffin KJ, Sullivan KF, Johnson EF. LKM-1 autoantibodies recognize a short linear sequence in P450IID6, a cytochrome P-450 monooxygenase. J Clin Invest 1991; 88: 1370-1378.
    • (1991) J Clin Invest , vol.88 , pp. 1370-1378
    • Manns, M.P.1    Griffin, K.J.2    Sullivan, K.F.3    Johnson, E.F.4
  • 137
    • 0023202836 scopus 로고
    • Cytochrome P450 and NADPH-cytochrome P450 reductase are degraded in the autolysosomes in rat liver
    • Masaki R, Yamamoto A, Tashiro Y. Cytochrome P450 and NADPH-cytochrome P450 reductase are degraded in the autolysosomes in rat liver. J Cell Biol 1987; 104: 1207-1215.
    • (1987) J Cell Biol , vol.104 , pp. 1207-1215
    • Masaki, R.1    Yamamoto, A.2    Tashiro, Y.3
  • 138
    • 0032706108 scopus 로고    scopus 로고
    • Mechanism-based inactivation of cytochrome P450s 1A2 and 3A4 by dihydralazine in human liver microsomes
    • Masubuchi Y, Horie T. Mechanism-based inactivation of cytochrome P450s 1A2 and 3A4 by dihydralazine in human liver microsomes. Chem Res Toxicol 1999; 12: 1028-1032.
    • (1999) Chem Res Toxicol , vol.12 , pp. 1028-1032
    • Masubuchi, Y.1    Horie, T.2
  • 139
    • 0036144190 scopus 로고    scopus 로고
    • Ligands have various potential effects on the degradation of pregnane X receptor by proteasome
    • Masuyama H, Inoshita H, Hiramatsu Y, Kudo T. Ligands have various potential effects on the degradation of pregnane X receptor by proteasome. Endocrinology 2002; 143: 55-61.
    • (2002) Endocrinology , vol.143 , pp. 55-61
    • Masuyama, H.1    Inoshita, H.2    Hiramatsu, Y.3    Kudo, T.4
  • 140
    • 0033831197 scopus 로고    scopus 로고
    • An in vitro model for predicting in vivo inhibition of cytochrome P450 3A4 by metabolic intermediate complex formation
    • Mayhew BS, Jones DR, Hall SD. An in vitro model for predicting in vivo inhibition of cytochrome P450 3A4 by metabolic intermediate complex formation. Drug Metab Dispos 2000; 28: 1031-1037.
    • (2000) Drug Metab Dispos , vol.28 , pp. 1031-1037
    • Mayhew, B.S.1    Jones, D.R.2    Hall, S.D.3
  • 141
    • 0034658270 scopus 로고    scopus 로고
    • A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways
    • Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J 2000; 19: 2181-2192.
    • (2000) EMBO J , vol.19 , pp. 2181-2192
    • Meyer, H.H.1    Shorter, J.G.2    Seemann, J.3    Pappin, D.4    Warren, G.5
  • 142
    • 0028557348 scopus 로고
    • Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B
    • Miyamoto S, Maki M, Schmitt MJ, Hatanaka M, Verma IM. Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B. Proc Natl Acad Sci USA 1994; 91: 12740-12744.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12740-12744
    • Miyamoto, S.1    Maki, M.2    Schmitt, M.J.3    Hatanaka, M.4    Verma, I.M.5
  • 143
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: from protein metabolism to bactericide
    • Mizushima N. The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell Death Differ 2005; 12 (Suppl 2 ): 1535-1541.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1535-1541
    • Mizushima, N.1
  • 144
    • 34250864795 scopus 로고    scopus 로고
    • Protein turnover via autophagy: implications for metabolism
    • Mizushima N, Klionsky DJ. Protein turnover via autophagy: implications for metabolism. Annu Rev Nutr 2007; 27: 19-40.
    • (2007) Annu Rev Nutr , vol.27 , pp. 19-40
    • Mizushima, N.1    Klionsky, D.J.2
  • 146
    • 39749171761 scopus 로고    scopus 로고
    • Xenoreceptors CAR and PXR activation and consequences on lipid metabolism, glucose homeostasis, and inflammatory response
    • Moreau A, Vilarem MJ, Maurel P, Pascussi JM. Xenoreceptors CAR and PXR activation and consequences on lipid metabolism, glucose homeostasis, and inflammatory response. Mol Pharm 2008; 5: 35-41.
    • (2008) Mol Pharm , vol.5 , pp. 35-41
    • Moreau, A.1    Vilarem, M.J.2    Maurel, P.3    Pascussi, J.M.4
  • 148
    • 28944446728 scopus 로고    scopus 로고
    • Regulation of cytochrome P450 2E1 by heat shock protein 90-dependent stabilization and CHIP-dependent proteasomal degradation
    • Morishima Y, Peng HM, Lin HL, Hollenberg PF, Sunahara RK, Osawa Y, Pratt WB. Regulation of cytochrome P450 2E1 by heat shock protein 90-dependent stabilization and CHIP-dependent proteasomal degradation. Biochemistry 2005; 44: 16333-16340.
    • (2005) Biochemistry , vol.44 , pp. 16333-16340
    • Morishima, Y.1    Peng, H.M.2    Lin, H.L.3    Hollenberg, P.F.4    Sunahara, R.K.5    Osawa, Y.6    Pratt, W.B.7
  • 149
    • 0037401714 scopus 로고    scopus 로고
    • CHIP: a quality-control E3 ligase collaborating with molecular chaperones
    • Murata S, Chiba T, Tanaka K. CHIP: a quality-control E3 ligase collaborating with molecular chaperones. Int J Biochem Cell Biol 2003; 35: 572-578.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 572-578
    • Murata, S.1    Chiba, T.2    Tanaka, K.3
  • 150
    • 0035450192 scopus 로고    scopus 로고
    • Ubiquitin-dependent 26S proteasomal pathway: A role in the degradation of the native human liver CYP3A4 expressed in Saccharomyces cerevisiae ?
    • Murray BP, Correia MA. Ubiquitin-dependent 26S proteasomal pathway: A role in the degradation of the native human liver CYP3A4 expressed in Saccharomyces cerevisiae ? Arch Biochem Biophys 2001; 393: 106-116.
    • (2001) Arch Biochem Biophys , vol.393 , pp. 106-116
    • Murray, B.P.1    Correia, M.A.2
  • 151
    • 0036233468 scopus 로고    scopus 로고
    • Native CYP2C11: heterologous expression in Saccharomyces cerevisiae reveals a role for vacuolar proteases rather than the ubiquitin-26S proteasome system in the degradation of this endoplasmic reticulum enzyme
    • Murray BP, Zgoda VG, Correia MA. Native CYP2C11: heterologous expression in Saccharomyces cerevisiae reveals a role for vacuolar proteases rather than the ubiquitin-26S proteasome system in the degradation of this endoplasmic reticulum enzyme. Mol Pharmacol 2002; 61: 1146-1153.
    • (2002) Mol Pharmacol , vol.61 , pp. 1146-1153
    • Murray, B.P.1    Zgoda, V.G.2    Correia, M.A.3
  • 152
    • 0034932451 scopus 로고    scopus 로고
    • Inhibition and inactivation of human cytochrome P450 isoforms by phenethyl isothiocyanate
    • Nakajima M, Yoshida R, Shimada N, Yamazaki H, Yokoi T. Inhibition and inactivation of human cytochrome P450 isoforms by phenethyl isothiocyanate. Drug Metab Dispos 2001; 29: 1110-1113.
    • (2001) Drug Metab Dispos , vol.29 , pp. 1110-1113
    • Nakajima, M.1    Yoshida, R.2    Shimada, N.3    Yamazaki, H.4    Yokoi, T.5
  • 153
    • 0014216707 scopus 로고
    • Turnover of constituents of the endoplasmic reticulum membranes of rat hepatocytes
    • Omura T, Siekevitz P, Palade GE. Turnover of constituents of the endoplasmic reticulum membranes of rat hepatocytes. J Biol Chem 1967; 242: 2389-2239.
    • (1967) J Biol Chem , vol.242 , pp. 2389-2239
    • Omura, T.1    Siekevitz, P.2    Palade, G.E.3
  • 154
    • 59849092071 scopus 로고    scopus 로고
    • CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases
    • Pabarcus MK, Hoe N, Sadeghi S, Patterson C, Wiertz E, Correia MA. CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases. Arch Biochem Biophys 2009; 483: 66-74.
    • (2009) Arch Biochem Biophys , vol.483 , pp. 66-74
    • Pabarcus, M.K.1    Hoe, N.2    Sadeghi, S.3    Patterson, C.4    Wiertz, E.5    Correia, M.A.6
  • 155
    • 34249875093 scopus 로고    scopus 로고
    • Clinical relevance of the small intestine as an organ of drug elimination: drug-fruit juice interactions
    • Paine MF, Oberlies NH. Clinical relevance of the small intestine as an organ of drug elimination: drug-fruit juice interactions. Expert Opin Drug Metab Toxicol 2007; 3: 67-80.
    • (2007) Expert Opin Drug Metab Toxicol , vol.3 , pp. 67-80
    • Paine, M.F.1    Oberlies, N.H.2
  • 156
    • 0020565558 scopus 로고
    • Differential time course of induction of rat liver microsomal cytochrome P-450 isozymes and epoxide hydrolase by Aroclor 1254
    • Parkinson A, Thomas PE, Ryan DE, Levin W. Differential time course of induction of rat liver microsomal cytochrome P-450 isozymes and epoxide hydrolase by Aroclor 1254. Arch Biochem Biophys 1983; 225: 203-215.
    • (1983) Arch Biochem Biophys , vol.225 , pp. 203-215
    • Parkinson, A.1    Thomas, P.E.2    Ryan, D.E.3    Levin, W.4
  • 157
    • 8744225764 scopus 로고    scopus 로고
    • The anaphase-promoting complex (APC): the sum of its parts?
    • Passmore LA. The anaphase-promoting complex (APC): the sum of its parts? Biochem Soc Trans 2004; 32: 724-727.
    • (2004) Biochem Soc Trans , vol.32 , pp. 724-727
    • Passmore, L.A.1
  • 158
    • 21744438514 scopus 로고    scopus 로고
    • Bosentan decreases the plasma concentration of sildenafil when coprescribed in pulmonary hypertension
    • Paul GA, Gibbs JS, Boobis AR, Abbas A, Wilkins MR. Bosentan decreases the plasma concentration of sildenafil when coprescribed in pulmonary hypertension. Br J Clin Pharmacol 2005; 60: 107-112.
    • (2005) Br J Clin Pharmacol , vol.60 , pp. 107-112
    • Paul, G.A.1    Gibbs, J.S.2    Boobis, A.R.3    Abbas, A.4    Wilkins, M.R.5
  • 159
    • 42049091467 scopus 로고    scopus 로고
    • Evaluation of proteomic strategies for analyzing ubiquitinated proteins
    • Peng J. Evaluation of proteomic strategies for analyzing ubiquitinated proteins. BMB Rep 2008; 41: 177-183.
    • (2008) BMB Rep , vol.41 , pp. 177-183
    • Peng, J.1
  • 160
    • 0001802845 scopus 로고
    • Toxic and immune mechanisms leading to acute and subacute drug induced liver injury
    • Miguet JP, Dhumeaux D, editors Paris: John Libbey Eurotext
    • Pessayre D. Toxic and immune mechanisms leading to acute and subacute drug induced liver injury. In: Miguet JP, Dhumeaux D, editors. Progress in Hepatology. Paris: John Libbey Eurotext, 1993, pp. 23-39.
    • (1993) Progress in Hepatology , pp. 23-39
    • Pessayre, D.1
  • 162
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • Pickart CM. Mechanisms underlying ubiquitination. Annu Rev Biochem 2001; 70: 503-533.
    • (2001) Annu Rev Biochem , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 163
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: proteases in the machine age
    • Pickart CM, Cohen RE. Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 2004; 5: 177-187.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 164
    • 17144413347 scopus 로고    scopus 로고
    • Diltiazem inhibits human intestinal cytochrome P450 3A (CYP3A) activity in vivo without altering the expression of intestinal mRNA or protein
    • Pinto AG, Horlander J, Chalasani N, Hamman M, Asghar A, Kolwankar D, Hall SD. Diltiazem inhibits human intestinal cytochrome P450 3A (CYP3A) activity in vivo without altering the expression of intestinal mRNA or protein. Br J Clin Pharmacol 2005; 59: 440-446.
    • (2005) Br J Clin Pharmacol , vol.59 , pp. 440-446
    • Pinto, A.G.1    Horlander, J.2    Chalasani, N.3    Hamman, M.4    Asghar, A.5    Kolwankar, D.6    Hall, S.D.7
  • 165
    • 0017262111 scopus 로고
    • Pharmacokinetic model to describe self-induced decreases in steady-state concentrations of carbamazepine
    • Pitlick WH, Levy RH, Tropin AS, Green JR. Pharmacokinetic model to describe self-induced decreases in steady-state concentrations of carbamazepine. J Pharm Sci 1976; 65: 462-463.
    • (1976) J Pharm Sci , vol.65 , pp. 462-463
    • Pitlick, W.H.1    Levy, R.H.2    Tropin, A.S.3    Green, J.R.4
  • 166
    • 36249022073 scopus 로고    scopus 로고
    • Ubiquitin receptors and ERAD: a network of pathways to the proteasome
    • Raasi S, Wolf DH. Ubiquitin receptors and ERAD: a network of pathways to the proteasome. Semin Cell Dev Biol 2007; 18: 780-791.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 780-791
    • Raasi, S.1    Wolf, D.H.2
  • 167
    • 50149086108 scopus 로고    scopus 로고
    • Diversity of degradation signals in the ubiquitin-proteasome system
    • Ravid T, Hochstrasser M. Diversity of degradation signals in the ubiquitin-proteasome system. Nat Rev Mol Cell Biol 2008; 9: 679-690.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 679-690
    • Ravid, T.1    Hochstrasser, M.2
  • 168
    • 32544437041 scopus 로고    scopus 로고
    • Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways
    • Ravid T, Kreft SG, Hochstrasser M. Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathways. EMBO J 2006; 25: 533-543.
    • (2006) EMBO J , vol.25 , pp. 533-543
    • Ravid, T.1    Kreft, S.G.2    Hochstrasser, M.3
  • 170
    • 0030986960 scopus 로고    scopus 로고
    • Evidence of proteasome-mediated cytochrome P450 degradation
    • Roberts BJ. Evidence of proteasome-mediated cytochrome P450 degradation. J Biol Chem 1997; 272: 9771-9778.
    • (1997) J Biol Chem , vol.272 , pp. 9771-9778
    • Roberts, B.J.1
  • 172
    • 0029778819 scopus 로고    scopus 로고
    • Antigenic targets in tienilic acid hepatitis Both cytochrome P450 2C11 and 2C11-tienilic acid adducts are transported to the plasma membrane of rat hepatocytes and recognized by human sera
    • Robin MA, Maratrat M, Le Roy M, Le Breton FP, Bonierbale E, Dansette P, Ballet F, Mansuy D, Pessayre D. Antigenic targets in tienilic acid hepatitis. Both cytochrome P450 2C11 and 2C11-tienilic acid adducts are transported to the plasma membrane of rat hepatocytes and recognized by human sera. J Clin Invest 1996; 98: 1471-1480.
    • (1996) J Clin Invest , vol.98 , pp. 1471-1480
    • Robin, M.A.1    Maratrat, M.2    Le Roy, M.3    Le Breton, F.P.4    Bonierbale, E.5    Dansette, P.6    Ballet, F.7    Mansuy, D.8    Pessayre, D.9
  • 175
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, Hwang D, Goldberg AL. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994; 78: 761-771.
    • (1994) Cell , vol.78 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 176
    • 0024444168 scopus 로고
    • Acetone-dependent regulation of cytochrome P450j (IIE1) and P450b (IIB1) in rat liver
    • Ronis MJ, Ingelman-Sundberg M. Acetone-dependent regulation of cytochrome P450j (IIE1) and P450b (IIB1) in rat liver. Xenobiotica 1989; 19: 1161-1165.
    • (1989) Xenobiotica , vol.19 , pp. 1161-1165
    • Ronis, M.J.1    Ingelman-Sundberg, M.2
  • 179
    • 20344384024 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated protein quality control and degradation: screen for ERAD mutants after ethylmethane sulfonate mutagenesis
    • Schafer A, Wolf DH. Endoplasmic reticulum-associated protein quality control and degradation: screen for ERAD mutants after ethylmethane sulfonate mutagenesis. Methods Mol Biol 2005; 301: 283-288.
    • (2005) Methods Mol Biol , vol.301 , pp. 283-288
    • Schafer, A.1    Wolf, D.H.2
  • 181
    • 0002697457 scopus 로고
    • Regulation of autophagic protein degradation in isolated liver cells
    • Glaumann H, Ballard FJ, editors. London: Academic Press
    • Seglen PO. Regulation of autophagic protein degradation in isolated liver cells. In: Glaumann H, Ballard FJ, editors. Lysosomes: Their Role in Protein Breakdown. London: Academic Press, 1987, pp. 371-414.
    • (1987) Lysosomes: Their Role in Protein Breakdown , pp. 371-414
    • Seglen, P.O.1
  • 182
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: a double-edged sword
    • Shintani T, Klionsky DJ. Autophagy in health and disease: a double-edged sword. Science 2004; 306: 990-995.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 183
    • 0021703594 scopus 로고
    • Turnover of membrane proteins: kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPH-cytochrome P-450 reductase and epoxide hydrolase
    • Shiraki H, Guengerich FP. Turnover of membrane proteins: kinetics of induction and degradation of seven forms of rat liver microsomal cytochrome P-450, NADPH-cytochrome P-450 reductase and epoxide hydrolase. Arch Biochem Biophys 1984; 235: 86-96.
    • (1984) Arch Biochem Biophys , vol.235 , pp. 86-96
    • Shiraki, H.1    Guengerich, F.P.2
  • 184
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome dependent proteolysis in mammalian cells
    • Shringarpure R, Grune T, Davies KJA. Protein oxidation and 20S proteasome dependent proteolysis in mammalian cells. Cell Mol Life Sci 2001; 58: 1442-1450.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.A.3
  • 186
    • 0026544514 scopus 로고
    • Ubiquitin conjugation to cytochromes c.Structure of the yeast iso-1 conjugate and possible recognition determinants
    • Sokolik CW, Cohen RE. Ubiquitin conjugation to cytochromes c. Structure of the yeast iso-1 conjugate and possible recognition determinants. J Biol Chem 1992; 267: 1067-1071.
    • (1992) J Biol Chem , vol.267 , pp. 1067-1071
    • Sokolik, C.W.1    Cohen, R.E.2
  • 187
    • 0024521525 scopus 로고
    • Induction of rat hepatic N-nitrosodimethylamine demethylase by acetone is due to protein stabilization
    • Song BJ, Veech RL, Park SS, Gelboin HV, Gonzalez FJ. Induction of rat hepatic N-nitrosodimethylamine demethylase by acetone is due to protein stabilization. J Biol Chem 1989; 264: 3568-3572.
    • (1989) J Biol Chem , vol.264 , pp. 3568-3572
    • Song, B.J.1    Veech, R.L.2    Park, S.S.3    Gelboin, H.V.4    Gonzalez, F.J.5
  • 188
    • 0016812238 scopus 로고
    • Kinetics of steroid induction and deinduction of tyrosine aminotransferase synthesis in cultured hepatoma cells
    • Steinberg RA, Levinson BB, Tomkins GM. Kinetics of steroid induction and deinduction of tyrosine aminotransferase synthesis in cultured hepatoma cells. Proc Natl Acad Sci USA 1975; 72: 2007-2011.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 2007-2011
    • Steinberg, R.A.1    Levinson, B.B.2    Tomkins, G.M.3
  • 189
    • 0021813986 scopus 로고
    • Synthesis and degradation of 3-methylcholanthrene-inducible cytochromes P-450 and their mRNAs in primary monolayer cultures of adult rat hepatocytes
    • Steward AR, Wrighton SA, Pasco DS, Fagan JB, Li D, Guzelian PS. Synthesis and degradation of 3-methylcholanthrene-inducible cytochromes P-450 and their mRNAs in primary monolayer cultures of adult rat hepatocytes. Arch Biochem Biophys 1985; 241: 494-508.
    • (1985) Arch Biochem Biophys , vol.241 , pp. 494-508
    • Steward, A.R.1    Wrighton, S.A.2    Pasco, D.S.3    Fagan, J.B.4    Li, D.5    Guzelian, P.S.6
  • 190
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson R, Locher M, Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev 2001; 15: 2660-2674.
    • (2001) Genes Dev , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 191
    • 54249158324 scopus 로고    scopus 로고
    • Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction
    • Tai HC, Schuman EM. Ubiquitin, the proteasome and protein degradation in neuronal function and dysfunction. Nat Rev Neurosci 2008; 9: 826-838.
    • (2008) Nat Rev Neurosci , vol.9 , pp. 826-838
    • Tai, H.C.1    Schuman, E.M.2
  • 192
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • Teckman JH, Perlmutter DH. Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am J Physiol Gastrointest Liver Physiol 2000; 279 :G 961-G 974.
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.279
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 194
    • 33750885465 scopus 로고    scopus 로고
    • Expression of xenobiotic metabolizing enzymes in different lung compartments of smokers and nonsmokers
    • Thum T, Erpenbeck VJ, Moeller J, Hohlfeld JM, Krug N, Borlak J. Expression of xenobiotic metabolizing enzymes in different lung compartments of smokers and nonsmokers. Environ Health Perspect 2006; 114: 1655-1661.
    • (2006) Environ Health Perspect , vol.114 , pp. 1655-1661
    • Thum, T.1    Erpenbeck, V.J.2    Moeller, J.3    Hohlfeld, J.M.4    Krug, N.5    Borlak, J.6
  • 195
    • 0026546019 scopus 로고
    • Degradation of cytochrome P450 2E1: Selective loss after labilization of the enzyme
    • Tierney DJ, Haas AL, Koop DR. Degradation of cytochrome P450 2E1: Selective loss after labilization of the enzyme. Arch Biochem Biophys 1992; 29: 9-16.
    • (1992) Arch Biochem Biophys , vol.29 , pp. 9-16
    • Tierney, D.J.1    Haas, A.L.2    Koop, D.R.3
  • 197
    • 0028362930 scopus 로고
    • Identification and characterization of lysosomal enzymes involved in the proteolysis of phenobarbital-inducible cytochrome P450
    • Tsuji H, Akasaki K. Identification and characterization of lysosomal enzymes involved in the proteolysis of phenobarbital-inducible cytochrome P450. Biol Pharm Bull 1994; 17: 568-571.
    • (1994) Biol Pharm Bull , vol.17 , pp. 568-571
    • Tsuji, H.1    Akasaki, K.2
  • 198
    • 0026059280 scopus 로고
    • Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver
    • Ueno T, Muno D, Kominami E. Membrane markers of endoplasmic reticulum preserved in autophagic vacuolar membranes isolated from leupeptin-administered rat liver. J Biol Chem 1991; 266: 18995-18999.
    • (1991) J Biol Chem , vol.266 , pp. 18995-18999
    • Ueno, T.1    Muno, D.2    Kominami, E.3
  • 199
    • 21244468587 scopus 로고    scopus 로고
    • Current trends in drug-induced autoimmunity
    • Uetrecht J. Current trends in drug-induced autoimmunity. Autoimmun Rev 2005; 4: 309-314.
    • (2005) Autoimmun Rev , vol.4 , pp. 309-314
    • Uetrecht, J.1
  • 200
    • 33847081148 scopus 로고    scopus 로고
    • Idiosyncratic drug reactions: current understanding
    • Uetrecht J. Idiosyncratic drug reactions: current understanding. Annu Rev Pharmacol Toxicol 2007; 47: 513-539.
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 513-539
    • Uetrecht, J.1
  • 201
    • 84995870568 scopus 로고
    • Autoantibodies to cytochrome P450 enzymes P450scc, P450c17, and P450c21 in autoimmune polyglandular disease types I and II and in isolated Addison's disease
    • Uibo R, Aavik E, Peterson P, Perheentupa J, Aranko S, Pelkonen R, Krohn KJ. Autoantibodies to cytochrome P450 enzymes P450scc, P450c17, and P450c21 in autoimmune polyglandular disease types I and II and in isolated Addison's disease. J Clin Endocrinol Metab 1994; 78: 23-28.
    • (1994) J Clin Endocrinol Metab , vol.78 , pp. 23-28
    • Uibo, R.1    Aavik, E.2    Peterson, P.3    Perheentupa, J.4    Aranko, S.5    Pelkonen, R.6    Krohn, K.J.7
  • 202
  • 203
    • 0026068805 scopus 로고
    • Naming a targeting signal
    • Varshavsky A. Naming a targeting signal. Cell 1991; 64: 13-15.
    • (1991) Cell , vol.64 , pp. 13-15
    • Varshavsky, A.1
  • 204
    • 0029861143 scopus 로고    scopus 로고
    • The N-end rule: functions, mysteries, uses
    • Varshavsky A. The N-end rule: functions, mysteries, uses. Proc Natl Acad Sci USA 1996; 93: 12142-12149.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12142-12149
    • Varshavsky, A.1
  • 206
    • 0346099111 scopus 로고    scopus 로고
    • Role of orphan nuclear receptors in the regulation of drug-metabolising enzymes
    • Wang H, LeCluyse EL. Role of orphan nuclear receptors in the regulation of drug-metabolising enzymes. Clin Pharmacokinet 2003; 42: 1331-1357.
    • (2003) Clin Pharmacokinet , vol.42 , pp. 1331-1357
    • Wang, H.1    LeCluyse, E.L.2
  • 208
    • 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 KF, Maltby D, Correia MA. Phosphorylation of native and heme-modified CYP3A4 by protein kinase C: a mass spectrometric characterization of the phosphorylated peptides. Biochemistry 2001; 40: 11318-11326.
    • (2001) Biochemistry , vol.40 , pp. 11318-11326
    • Wang, X.1    Medzihradszky, K.F.2    Maltby, D.3    Correia, M.A.4
  • 209
    • 65549106478 scopus 로고    scopus 로고
    • A role for protein phosphorylation in cytochrome P450 3A4 ubiquitin-dependent proteasomal degradation
    • Wang Y, Liao M, Hoe N, Acharya P, Deng C, Krutchinsky AN, Correia MA. A role for protein phosphorylation in cytochrome P450 3A4 ubiquitin-dependent proteasomal degradation. J Biol Chem 2009; 284: 5671-5684.
    • (2009) J Biol Chem , vol.284 , pp. 5671-5684
    • Wang, Y.1    Liao, M.2    Hoe, N.3    Acharya, P.4    Deng, C.5    Krutchinsky, A.N.6    Correia, M.A.7
  • 210
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitinproteasome pathway
    • Ward CL, Omura S, Kopito RR. Degradation of CFTR by the ubiquitinproteasome pathway. Cell 1995; 83: 121-127.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 211
    • 0023024338 scopus 로고
    • Macrolide antibiotics inhibit the degradation of the glucocorticoid-responsive cytochrome P-450p in rat hepatocytes in vivo and in primary monolayer culture
    • Watkins PB, Wrighton SA, Schuetz EG, Maurel P, Guzelian PS. Macrolide antibiotics inhibit the degradation of the glucocorticoid-responsive cytochrome P-450p in rat hepatocytes in vivo and in primary monolayer culture. J Biol Chem 1986; 261: 6264-6271.
    • (1986) J Biol Chem , vol.261 , pp. 6264-6271
    • Watkins, P.B.1    Wrighton, S.A.2    Schuetz, E.G.3    Maurel, P.4    Guzelian, P.S.5
  • 212
    • 0023588109 scopus 로고
    • Identification of glucocorticoid-inducible cytochromes P-450 in the intestinal mucosa of rats and man
    • Watkins PB, Wrighton SA, Schuetz EG, Molowa DT, Guzelian PS. Identification of glucocorticoid-inducible cytochromes P-450 in the intestinal mucosa of rats and man. J Clin Invest 1987; 80: 1029-1036.
    • (1987) J Clin Invest , vol.80 , pp. 1029-1036
    • Watkins, P.B.1    Wrighton, S.A.2    Schuetz, E.G.3    Molowa, D.T.4    Guzelian, P.S.5
  • 213
    • 0019443468 scopus 로고
    • Genetic determination of kinetic parameters in beta-glucuronidase induction by androgen
    • Watson G, Davey RA, Labarca C, Paigen K. Genetic determination of kinetic parameters in beta-glucuronidase induction by androgen. J Biol Chem 1981; 256: 3005-3011.
    • (1981) J Biol Chem , vol.256 , pp. 3005-3011
    • Watson, G.1    Davey, R.A.2    Labarca, C.3    Paigen, K.4
  • 214
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman A. Themes and variations on ubiquitylation. Nat Rev Mol Cell Biol 2001; 2: 169-178.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 169-178
    • Weissman, A.1
  • 215
    • 0029122799 scopus 로고
    • N-and C-terminal sequences control degradation of MAD3/I kappa B alpha in response to inducers of NF-kappa B activity
    • Whiteside S, Ernst M, LeBail O, Laurent-Winter C, Rice N, Israel A. N-and C-terminal sequences control degradation of MAD3/I kappa B alpha in response to inducers of NF-kappa B activity. Mol Cell Biol 1995; 15: 5339-5345.
    • (1995) Mol Cell Biol , vol.15 , pp. 5339-5345
    • Whiteside, S.1    Ernst, M.2    LeBail, O.3    Laurent-Winter, C.4    Rice, N.5    Israel, A.6
  • 216
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • Wilkinson KD. Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB J 1997; 11: 1245-1256.
    • (1997) FASEB J , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 217
    • 3242730192 scopus 로고    scopus 로고
    • From lysosome to proteasome: the power of yeast in the dissection of proteinase function in cellular regulation and waste disposal
    • Wolf DH. From lysosome to proteasome: the power of yeast in the dissection of proteinase function in cellular regulation and waste disposal. Cell Mol Life Sci 2004; 61: 1601-1604.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1601-1604
    • Wolf, D.H.1
  • 218
    • 0022340785 scopus 로고
    • Is cytochrome P-450 transported from the endoplasmic reticulum to the Golgi apparatus in rat hepatocytes?
    • Yamamoto A, Masaki R, Tashiro Y. Is cytochrome P-450 transported from the endoplasmic reticulum to the Golgi apparatus in rat hepatocytes? J Cell Biol 1985; 101: 1733-1740.
    • (1985) J Cell Biol , vol.101 , pp. 1733-1740
    • Yamamoto, A.1    Masaki, R.2    Tashiro, Y.3
  • 219
    • 0027414305 scopus 로고
    • Identification and analysis of cytochrome P450IID6 antigenic sites recognized by anti-liver-kidney microsome type-1 antibodies (LKM1)
    • Yamamoto AM, Cresteil D, Boniface O, Clerc FF, Alvarez F. Identification and analysis of cytochrome P450IID6 antigenic sites recognized by anti-liver-kidney microsome type-1 antibodies (LKM1). Eur J Immunol 1993; 23: 1105-1111.
    • (1993) Eur J Immunol , vol.23 , pp. 1105-1111
    • Yamamoto, A.M.1    Cresteil, D.2    Boniface, O.3    Clerc, F.F.4    Alvarez, F.5
  • 220
    • 47749122616 scopus 로고    scopus 로고
    • Cytochrome P450 turnover: regulation of synthesis and degradation, methods for determining rates, and implications for the prediction of drug interactions
    • Yang J, Liao M, Shou M, Jamei M, Yeo KR, Tucker GT, Rostami-Hodjegan A. Cytochrome P450 turnover: regulation of synthesis and degradation, methods for determining rates, and implications for the prediction of drug interactions. Curr Drug Metab 2008; 9: 384-394.
    • (2008) Curr Drug Metab , vol.9 , pp. 384-394
    • Yang, J.1    Liao, M.2    Shou, M.3    Jamei, M.4    Yeo, K.R.5    Tucker, G.T.6    Rostami-Hodjegan, A.7
  • 221
    • 0030600404 scopus 로고    scopus 로고
    • Role of the proteasome complex in degradation of human CYP2E1 in transfected HepG2 cells
    • Yang MX, Cederbaum AI. Role of the proteasome complex in degradation of human CYP2E1 in transfected HepG2 cells. Biochem Biophys Res Commun 1996; 226: 711-716.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 711-716
    • Yang, M.X.1    Cederbaum, A.I.2
  • 222
    • 0031149527 scopus 로고    scopus 로고
    • Characterization of cytochrome P4502E1 turnover in transfected HepG2 cells expressing human CYP2E1
    • Yang MX, Cederbaum AI. Characterization of cytochrome P4502E1 turnover in transfected HepG2 cells expressing human CYP2E1. Arch Biochem Biophys 1997; 341: 25-33.
    • (1997) Arch Biochem Biophys , vol.341 , pp. 25-33
    • Yang, M.X.1    Cederbaum, A.I.2
  • 223
    • 21544452226 scopus 로고    scopus 로고
    • Immunoproteasomes: regulating the regulator
    • Yewdell JW. Immunoproteasomes: regulating the regulator. Proc Natl Acad Sci USA 2005; 102: 9089-9090.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9089-9090
    • Yewdell, J.W.1
  • 224
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: molecular machinery for self-eating
    • Yorimitsu T, Klionsky DJ. Autophagy: molecular machinery for self-eating. Cell Death Differ 2005; 12 (Suppl 2 ): 1542-1552.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 225
  • 226
    • 33845442925 scopus 로고    scopus 로고
    • Mechanistic studies of the Nrf2-Keap1 pathway
    • Zhang DD. Mechanistic studies of the Nrf2-Keap1 pathway. Drug Metab Rev 2006; 38: 769-789.
    • (2006) Drug Metab Rev , vol.38 , pp. 769-789
    • Zhang, D.D.1
  • 227
    • 1942469598 scopus 로고    scopus 로고
    • Characterization of the acetaminophen-induced degradation of cytochrome P450-3A4 and the proteolytic pathway
    • Zhang QX, Melnikov Z, Feierman DE. Characterization of the acetaminophen-induced degradation of cytochrome P450-3A4 and the proteolytic pathway. Basic Clin Pharmacol Toxicol 2004; 94: 191-200.
    • (2004) Basic Clin Pharmacol Toxicol , vol.94 , pp. 191-200
    • Zhang, Q.X.1    Melnikov, Z.2    Feierman, D.E.3
  • 228
    • 47349094025 scopus 로고    scopus 로고
    • An update on clinical drug interactions with the herbal antidepressant St John's wort
    • Zhou SF, Lai X. An update on clinical drug interactions with the herbal antidepressant St John's wort. Curr Drug Metab 2008; 9: 394-409.
    • (2008) Curr Drug Metab , vol.9 , pp. 394-409
    • Zhou, S.F.1    Lai, X.2
  • 229
    • 0030841119 scopus 로고    scopus 로고
    • Selective fast degradation of cytochrome P450 2E1 in serum-deprived hepatoma cells by a mechanism sensitive to inhibitors of vesicular transport
    • Zhukov A, Ingelman-Sundberg M. Selective fast degradation of cytochrome P450 2E1 in serum-deprived hepatoma cells by a mechanism sensitive to inhibitors of vesicular transport. Eur J Biochem 1997; 247: 37-43.
    • (1997) Eur J Biochem , vol.247 , pp. 37-43
    • Zhukov, A.1    Ingelman-Sundberg, M.2
  • 230
    • 0033151930 scopus 로고    scopus 로고
    • Relationship between cytochrome P450 catalytic cycling and stability: fast degradation of ethanol-inducible cytochrome P450 2E1 (CYP2E1) in hepatoma cells is abolished by inactivation of its electron donor NADPH-cytochrome P450 reductase
    • Zhukov A, Ingelman-Sundberg M. Relationship between cytochrome P450 catalytic cycling and stability: fast degradation of ethanol-inducible cytochrome P450 2E1 (CYP2E1) in hepatoma cells is abolished by inactivation of its electron donor NADPH-cytochrome P450 reductase. Biochem J 1999; 340: 453-458.
    • (1999) Biochem J , vol.340 , pp. 453-458
    • Zhukov, A.1    Ingelman-Sundberg, M.2
  • 231
    • 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. Purification and characterization of two membrane bound serine proteinases from rat liver microsomes active in degradation of cytochrome P450. Biochem Biophys Res Commun 1993; 197: 221-228.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 221-228
    • Zhukov, A.1    Werlinder, V.2    Ingelman-Sundberg, M.3


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