메뉴 건너뛰기




Volumn 42, Issue 1, 2014, Pages 9-22

Correlating structure and function of drug-metabolizing enzymes: Progress and ongoing challenges

Author keywords

[No Author keywords available]

Indexed keywords

AJMALICINE; AMLODIPINE; AROMATASE INHIBITOR; ATAZANAVIR; COBICISTAT; COBICISTAT PLUS ELVITEGRAVIR PLUS EMTRICITABINE PLUS TENOFOVIR DISOPROXIL; CYTOCHROME B5; CYTOCHROME P450; CYTOCHROME P450 17A1; CYTOCHROME P450 1A2; CYTOCHROME P450 2B4; CYTOCHROME P450 2C19; CYTOCHROME P450 2D6; CYTOCHROME P450 3A4; CYTOCHROME P450 3A5; ELVITEGRAVIR; FLURBIPROFEN; HUMAN IMMUNODEFICIENCY VIRUS PROTEINASE INHIBITOR; PRINOMASTAT; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE FERRIHEMOPROTEIN REDUCTASE; RITONAVIR; THIORIDAZINE; UNCLASSIFIED DRUG;

EID: 84890721702     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.113.054627     Document Type: Conference Paper
Times cited : (21)

References (96)
  • 2
    • 28044470748 scopus 로고    scopus 로고
    • 5 modulation of 17 hydroxylase and 17-20 lyase (CYP17) activities in steroidogenesis
    • DOI 10.1677/joe.1.06375
    • Akhtar MK, Kelly SL, and Kaderbhai MA (2005) Cytochrome b(5) modulation of 17alpha hydroxylase and 17-20 lyase (CYP17) activities in steroidogenesis. J Endocrinol 187:267-274. (Pubitemid 41685186)
    • (2005) Journal of Endocrinology , vol.187 , Issue.2 , pp. 267-274
    • Akhtar, M.K.1    Kelly, S.L.2    Kaderbhai, M.A.3
  • 4
    • 0032530282 scopus 로고    scopus 로고
    • Interactions among P450 enzymes when combined in reconstituted systems: Formation of a 2B4-1A2 complex with a high affinity for NADPH-cytochrome P450 reductase
    • DOI 10.1021/bi980674a
    • Backes WL, Batie CJ, and Cawley GF (1998) Interactions among P450 enzymes when combined in reconstituted systems: formation of a 2B4-1A2 complex with a high affinity for NADPH-cytochrome P450 reductase. Biochemistry 37:12852-12859. (Pubitemid 28433517)
    • (1998) Biochemistry , vol.37 , Issue.37 , pp. 12852-12859
    • Backes, W.L.1    Batie, C.J.2    Cawley, G.F.3
  • 5
    • 0026708585 scopus 로고
    • Substrate mobility in a deeply buried active site: Analysis of norcamphor bound to cytochrome P-450cam as determined by a 201-psec molecular dynamics simulation
    • Bass MB, Paulsen MD, and Ornstein RL (1992) Substrate mobility in a deeply buried active site: analysis of norcamphor bound to cytochrome P-450cam as determined by a 201-psec molecular dynamics simulation. Proteins 13:26-37.
    • (1992) Proteins , vol.13 , pp. 26-37
    • Bass, M.B.1    Paulsen, M.D.2    Ornstein, R.L.3
  • 6
    • 80054709526 scopus 로고    scopus 로고
    • Membrane position of ibu-profen agrees with suggested access path entrance to cytochrome P450 2C9 active site
    • Berka K, Hendrychová T, Anzenbacher P, and Otyepka M (2011) Membrane position of ibu-profen agrees with suggested access path entrance to cytochrome P450 2C9 active site. J Phys Chem A 115:11248-11255.
    • (2011) J Phys Chem A , vol.115 , pp. 11248-11255
    • Berka, K.1    Hendrychová, T.2    Anzenbacher, P.3    Otyepka, M.4
  • 11
    • 0023865160 scopus 로고
    • Theoretical study of the product specificity in the hydroxylation of camphor, norcamphor, 5,5-difluorocamphor, and pericyclocamphanone by cytochrome P-450(cam)
    • Collins JR and Loew GH (1988) Theoretical study of the product specificity in the hydroxylation of camphor, norcamphor, 5, 5-difluorocamphor, and pericyclocamphanone by cytochrome P-450cam. J Biol Chem 263:3164-3170. (Pubitemid 18072766)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.7 , pp. 3164-3170
    • Collins, J.R.1    Loew, G.H.2
  • 13
    • 79955099060 scopus 로고    scopus 로고
    • Microsomal monooxygenase as a multienzyme system: The role of P450-P450 interactions
    • Davydov DR (2011) Microsomal monooxygenase as a multienzyme system: the role of P450-P450 interactions. Expert Opin Drug Metab Toxicol 7:543-558.
    • (2011) Expert Opin Drug Metab Toxicol , vol.7 , pp. 543-558
    • Davydov, D.R.1
  • 14
    • 0026492443 scopus 로고
    • High pressure induced inactivation of ferrous cytochrome P-450 LM2 (IIB4) CO complex: Evidence for the presence of two conformers in the oligomer
    • Davydov DR, Knyushko TV, and Hoa GH (1992) High pressure induced inactivation of ferrous cytochrome P-450 LM2 (IIB4) CO complex: evidence for the presence of two conformers in the oligomer. Biochem Biophys Res Commun 188:216-221.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 216-221
    • Davydov, D.R.1    Knyushko, T.V.2    Hoa, G.H.3
  • 15
    • 75649112318 scopus 로고    scopus 로고
    • Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: The effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium
    • Davydov DR, Sineva EV, Sistla S, Davydova NY, Frank DJ, Sligar SG, and Halpert JR (2010) Electron transfer in the complex of membrane-bound human cytochrome P450 3A4 with the flavin domain of P450BM-3: the effect of oligomerization of the heme protein and intermittent modulation of the spin equilibrium. Biochim Biophys Acta 1797:378-390.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 378-390
    • Davydov, D.R.1    Sineva, E.V.2    Sistla, S.3    Davydova, N.Y.4    Frank, D.J.5    Sligar, S.G.6    Halpert, J.R.7
  • 16
    • 33745216665 scopus 로고    scopus 로고
    • Designing better drugs: Predicting cytochrome P450 metabolism
    • de Groot MJ (2006) Designing better drugs: predicting cytochrome P450 metabolism. Drug Discov Today 11:601-606.
    • (2006) Drug Discov Today , vol.11 , pp. 601-606
    • De Groot, M.J.1
  • 17
    • 84862843404 scopus 로고    scopus 로고
    • Co-formulated elvite-gravir, cobicistat, emtricitabine, and tenofovir disoproxil fumarate versus ritonavir-boosted atazanavir plus co-formulated emtricitabine and tenofovir disoproxil fumarate for initial treatment of HIV-1 infection: A randomised, double-blind, phase 3, non-inferiority trial
    • GS-236-0103 Study Team
    • DeJesus E, Rockstroh JK, Henry K, Molina JM, Gathe J, Ramanathan S, Wei X, Yale K, Szwarcberg J, and White K, et al.; GS-236-0103 Study Team (2012) Co-formulated elvite-gravir, cobicistat, emtricitabine, and tenofovir disoproxil fumarate versus ritonavir-boosted atazanavir plus co-formulated emtricitabine and tenofovir disoproxil fumarate for initial treatment of HIV-1 infection: a randomised, double-blind, phase 3, non-inferiority trial. Lancet 379:2429-2438.
    • (2012) Lancet , vol.379 , pp. 2429-2438
    • Dejesus, E.1    Rockstroh, J.K.2    Henry, K.3    Molina, J.M.4    Gathe, J.5    Ramanathan, S.6    Wei, X.7    Yale, K.8    Szwarcberg, J.9    White, K.10
  • 18
    • 84856477784 scopus 로고    scopus 로고
    • Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001
    • DeVore NM and Scott EE (2012) Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001. Nature 482:116-119.
    • (2012) Nature , vol.482 , pp. 116-119
    • Devore, N.M.1    Scott, E.E.2
  • 21
    • 84878750608 scopus 로고    scopus 로고
    • Substrate-modulated cytochrome P450 17A1 and cytochrome b5 interactions revealed by NMR
    • Estrada DF, Laurence JS, and Scott EE (2013) Substrate-modulated cytochrome P450 17A1 and cytochrome b5 interactions revealed by NMR. J Biol Chem 288:17008-17018.
    • (2013) J Biol Chem , vol.288 , pp. 17008-17018
    • Estrada, D.F.1    Laurence, J.S.2    Scott, E.E.3
  • 22
    • 84878525908 scopus 로고    scopus 로고
    • Cobicistat versus ritonavir as a pharmacoenhancer of atazanavir plus emtricitabine/tenofovir disoproxil fumarate in treatment-naive HIV type 1-infected patients: Week 48 results
    • Gallant JE, Koenig E, Andrade-Villanueva J, Chetchotisakd P, DeJesus E, Antunes F, Arastéh K, Moyle G, Rizzardini G, and Fehr J (2013) Cobicistat versus ritonavir as a pharmacoenhancer of atazanavir plus emtricitabine/ tenofovir disoproxil fumarate in treatment-naive HIV type 1-infected patients: week 48 results. J Infect Dis 208(1):32-9.
    • (2013) J Infect Dis , vol.208 , Issue.1 , pp. 32-39
    • Gallant, J.E.1    Koenig, E.2    Andrade-Villanueva, J.3    Chetchotisakd, P.4    Dejesus, E.5    Antunes, F.6    Arastéh, K.7    Moyle, G.8    Rizzardini, G.9    Fehr, J.10
  • 23
    • 13644249455 scopus 로고    scopus 로고
    • Protease-inhibitor boosting in the treatment-experienced patient
    • Gallant JE (2004) Protease-inhibitor boosting in the treatment- experienced patient. AIDS Rev 6: 226-233. (Pubitemid 40227884)
    • (2004) AIDS Reviews , vol.6 , Issue.4 , pp. 226-233
    • Gallant, J.E.1
  • 24
  • 25
    • 0032893922 scopus 로고    scopus 로고
    • 5
    • DOI 10.1210/me.13.1.167
    • Geller DH, Auchus RJ, and Miller WL (1999) P450c17 mutations R347H and R358Q selectively disrupt 17, 20-lyase activity by disrupting interactions with P450 oxidoreductase and cyto-chrome b5. Mol Endocrinol 13:167-175. (Pubitemid 29022289)
    • (1999) Molecular Endocrinology , vol.13 , Issue.1 , pp. 167-175
    • Geller, D.H.1    Auchus, R.J.2    Miller, W.L.3
  • 27
    • 79959385330 scopus 로고    scopus 로고
    • Structure and function of cytochromes P450 2B: From mechanism-based inactivators to X-ray crystal structures and back
    • Halpert JR (2011) Structure and function of cytochromes P450 2B: from mechanism-based inactivators to X-ray crystal structures and back. Drug Metab Dispos 39:1113-1121.
    • (2011) Drug Metab Dispos , vol.39 , pp. 1113-1121
    • Halpert, J.R.1
  • 28
  • 29
    • 11144328243 scopus 로고    scopus 로고
    • Interactions between CYP2C9 and CYP2C19 in reconstituted binary systems influence their catalytic activity: Possible rationale for the inability of CYP2C19 to catalyze methoxychlor demethylation in human liver microsomes
    • DOI 10.1124/dmd.104.001578
    • Hazai E and Kupfer D (2005) Interactions between CYP2C9 and CYP2C19 in reconstituted binary systems influence their catalytic activity: possible rationale for the inability of CYP2C19 to catalyze methoxychlor demethylation in human liver microsomes. Drug Metab Dispos 33: 157-164. (Pubitemid 40023527)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.1 , pp. 157-164
    • Hazai, E.1    Kupfer, D.2
  • 30
    • 85080846545 scopus 로고    scopus 로고
    • The structure of the cytochrome P450cam-putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography
    • DOI:10.1124/pr.55.3.4 [published ahead of print]
    • Hiruma Y, Hass MA, Kikui Y, Liu WM, Olmez B, Skinner SP, Blok A, Kloosterman A, Koteishi H, and Löhr F, et al. (2013) The structure of the cytochrome P450cam-putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography. J Mol Biol DOI:10.1124/pr.55.3.4 [published ahead of print].
    • (2013) J Mol Biol
    • Hiruma, Y.1    Hass, M.A.2    Kikui, Y.3    Liu, W.M.4    Olmez, B.5    Skinner, S.P.6    Blok, A.7    Kloosterman, A.8    Koteishi, H.9    Löhr, F.10
  • 31
    • 78049388318 scopus 로고    scopus 로고
    • CYP2C8 exists as a dimer in natural membranes
    • Hu G, Johnson EF, and Kemper B (2010) CYP2C8 exists as a dimer in natural membranes. Drug Metab Dispos 38:1976-1983.
    • (2010) Drug Metab Dispos , vol.38 , pp. 1976-1983
    • Hu, G.1    Johnson, E.F.2    Kemper, B.3
  • 32
    • 15844394255 scopus 로고    scopus 로고
    • Identification of residues 99, 220, and 221 of human cytochrome P450 2C19 as key determinants of omeprazole hydroxylase activity
    • DOI 10.1074/jbc.271.21.12496
    • Ibeanu GC, Ghanayem BI, Linko P, Li L, Pederson LG, and Goldstein JA (1996) Identification of residues 99, 220, and 221 of human cytochrome P450 2C19 as key determinants of omeprazole activity. J Biol Chem 271:12496-12501. (Pubitemid 26160921)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.21 , pp. 12496-12501
    • Ibeanu, G.C.1    Ghanayem, B.I.2    Linko, P.3    Li, L.4    Pedersen, L.G.5    Goldstein, J.A.6
  • 33
    • 79951561142 scopus 로고    scopus 로고
    • The interaction of microsomal cytochrome P450 2B4 with its redox partners, cytochrome P450 reductase and cytochrome b(5)
    • Im SC and Waskell L (2011) The interaction of microsomal cytochrome P450 2B4 with its redox partners, cytochrome P450 reductase and cytochrome b(5). Arch Biochem Biophys 507:144-153.
    • (2011) Arch Biochem Biophys , vol.507 , pp. 144-153
    • Im, S.C.1    Waskell, L.2
  • 34
    • 34548528384 scopus 로고    scopus 로고
    • Global analysis of protein-protein interactions reveals multiple CYP2E1-reductase complexes
    • DOI 10.1021/bi7003476
    • Jamakhandi AP, Kuzmic P, Sanders DE, and Miller GP (2007) Global analysis of protein-protein interactions reveals multiple CYP2E1-reductase complexes. Biochemistry 46:10192-10201. (Pubitemid 47381277)
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 10192-10201
    • Jamakhandi, A.P.1    Kuzmic, P.2    Sanders, D.E.3    Miller, G.P.4
  • 35
    • 84879053714 scopus 로고    scopus 로고
    • Structural diversity of eukaryotic membrane cytochrome p450s
    • Johnson EF and Stout CD (2013) Structural diversity of eukaryotic membrane cytochrome p450s. J Biol Chem 288:17082-17090.
    • (2013) J Biol Chem , vol.288 , pp. 17082-17090
    • Johnson, E.F.1    Stout, C.D.2
  • 36
    • 0036136527 scopus 로고    scopus 로고
    • Computational models for cytochrome P450: A predictive electronic model for aromatic oxidation and hydrogen atom abstraction
    • DOI 10.1124/dmd.30.1.7
    • Jones JP, Mysinger M, and Korzekwa KR (2002) Computational models for cytochrome P450: a predictive electronic model for aromatic oxidation and hydrogen atom abstraction. Drug Metab Dispos 30:7-12. (Pubitemid 34016934)
    • (2002) Drug Metabolism and Disposition , vol.30 , Issue.1 , pp. 7-12
    • Jones, J.P.1    Mysinger, M.2    Korzekwa, K.R.3
  • 37
    • 0032542015 scopus 로고    scopus 로고
    • Identification of amino acid substitutions that confer a high affinity for sulfaphenazole binding and a high catalytic efficiency for warfarin metabolism to P450 2C19
    • DOI 10.1021/bi981704c
    • Jung F, Griffin KJ, Song W, Richardson TH, Yang M, and Johnson EF (1998) Identification of amino acid substitutions that confer a high affinity for sulfaphenazole binding and a high catalytic efficiency for warfarin metabolism to P450 2C19. Biochemistry 37:16270-16279. (Pubitemid 28536263)
    • (1998) Biochemistry , vol.37 , Issue.46 , pp. 16270-16279
    • Jung, F.1    Griffin, K.J.2    Song, W.3    Richardson, T.H.4    Yang, M.5    Johnson, E.F.6
  • 40
    • 0032530108 scopus 로고    scopus 로고
    • Identification of residues 286 and 289 as critical for conferring substrate specificity of human CYP2C9 for diclofenac and ibuprofen
    • DOI 10.1006/abbi.1998.0826
    • Klose TS, Ibeanu GC, Ghanayem BI, Pedersen LG, Li L, Hall SD, and Goldstein JA (1998) Identification of residues 286 and 289 as critical for conferring substrate specificity of human CYP2C9 for diclofenac and ibuprofen. Arch Biochem Biophys 357:240-248. (Pubitemid 28419205)
    • (1998) Archives of Biochemistry and Biophysics , vol.357 , Issue.2 , pp. 240-248
    • Klose, T.S.1    Ibeanu, G.C.2    Ghanayem, B.I.3    Pedersen, L.G.4    Li, L.5    Hall, S.D.6    Goldstein, J.A.7
  • 41
    • 0025150366 scopus 로고
    • Theoretical studies on cytochrome P-450 mediated hydroxylation: A predictive model for hydrogen atom abstractions
    • Korzekwa KR, Jones JP, and Gillette JR (1990) Theoretical studies on cytochrome P-450 mediated hydroxylation: A predictive model for hydrogen atom abstractions. J Am Chem Soc 112: 7042-7046. (Pubitemid 20319136)
    • (1990) Journal of the American Chemical Society , vol.112 , Issue.19 , pp. 7042-7046
    • Korzekwa, K.R.1    Jones, J.P.2    Gillette, J.R.3
  • 43
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • DOI 10.1038/nsb0297-140
    • Li H and Poulos TL (1997) The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat Struct Biol 4:140-146. (Pubitemid 27066389)
    • (1997) Nature Structural Biology , vol.4 , Issue.2 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 44
    • 31044440024 scopus 로고    scopus 로고
    • 5 requires residues E48 and E49 to stimulate the 17,20-lyase activity of cytochrome P450c17
    • DOI 10.1021/bi051623y
    • Naffin-Olivos JL and Auchus RJ (2006) Human cytochrome b5 requires residues E48 and E49 to stimulate the 17, 20-lyase activity of cytochrome P450c17. Biochemistry 45:755-762. (Pubitemid 43122240)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 755-762
    • Naffin-Olivos, J.L.1    Auchus, R.J.2
  • 47
    • 13944268698 scopus 로고    scopus 로고
    • Greater than the sum of its parts: Combining models for useful ADMET prediction
    • DOI 10.1021/jm049254b
    • O'Brien SE and de Groot MJ (2005) Greater than the sum of its parts: combining models for useful ADMET prediction. J Med Chem 48:1287-1291. (Pubitemid 40270476)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.4 , pp. 1287-1291
    • O'Brien, S.E.1    De Groot, M.J.2
  • 48
    • 23944462892 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation analysis of cytochrome P450 2C2, 2E1, and NADPH-cytochrome P450 reductase molecular interactions in living cells
    • DOI 10.1124/dmd.105.005538
    • Ozalp C, Szczesna-Skorupa E, and Kemper B (2005) Bimolecular fluorescence complementation analysis of cytochrome p450 2c2, 2e1, and NADPH-cytochrome p450 reductase molecular interactions in living cells. Drug Metab Dispos 33:1382-1390. (Pubitemid 41196983)
    • (2005) Drug Metabolism and Disposition , vol.33 , Issue.9 , pp. 1382-1390
    • Ozalp, C.1    Szczesna-Skorupa, E.2    Kemper, B.3
  • 49
    • 84872116423 scopus 로고    scopus 로고
    • The action of cytochrome b(5) on CYP2E1 and CYP2C19 activities requires anionic residues D58 and D65
    • Peng HM and Auchus RJ (2013) The action of cytochrome b(5) on CYP2E1 and CYP2C19 activities requires anionic residues D58 and D65. Biochemistry 52:210-220.
    • (2013) Biochemistry , vol.52 , pp. 210-220
    • Peng, H.M.1    Auchus, R.J.2
  • 50
    • 0017112947 scopus 로고
    • Temperature dependence of cytochrome P-450 reduction. A model for NADPH-cytochrome P-450 re-ductase:cytochrome P-450 interaction
    • Peterson JA, Ebel RE, O'Keeffe DH, Matsubara T, and Estabrook RW (1976) Temperature dependence of cytochrome P-450 reduction. A model for NADPH-cytochrome P-450 re-ductase:cytochrome P-450 interaction. J Biol Chem 251:4010-4016.
    • (1976) J Biol Chem , vol.251 , pp. 4010-4016
    • Peterson, J.A.1    Ebel, R.E.2    O'Keeffe, D.H.3    Matsubara, T.4    Estabrook, R.W.5
  • 51
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos TL, Finzel BC, and Howard AJ (1987) High-resolution crystal structure of cytochrome P450cam. J Mol Biol 195:687-700.
    • (1987) J Mol Biol , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 52
    • 0027326717 scopus 로고
    • Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's
    • Ravichandran KG, Boddupalli SS, Hasermann CA, Peterson JA, and Deisenhofer J (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261:731-736. (Pubitemid 23278388)
    • (1993) Science , vol.261 , Issue.5122 , pp. 731-736
    • Ravichandran, K.G.1    Boddupalli, S.S.2    Hasemann, C.A.3    Peterson, J.A.4    Deisenhofer, J.5
  • 53
    • 84856488429 scopus 로고    scopus 로고
    • Formation of P450 · P450 complexes and their effect on P450 function
    • Reed JR and Backes WL (2012) Formation of P450 · P450 complexes and their effect on P450 function. Pharmacol Ther 133:299-310.
    • (2012) Pharmacol Ther , vol.133 , pp. 299-310
    • Reed, J.R.1    Backes, W.L.2
  • 55
    • 77950578788 scopus 로고    scopus 로고
    • Functional interactions between cytochromes P450 1A2 and 2B4 require both enzymes to reside in the same phospholipid vesicle: Evidence for physical complex formation
    • Reed JR, Eyer M, and Backes WL (2010) Functional interactions between cytochromes P450 1A2 and 2B4 require both enzymes to reside in the same phospholipid vesicle: evidence for physical complex formation. J Biol Chem 285:8942-8952.
    • (2010) J Biol Chem , vol.285 , pp. 8942-8952
    • Reed, J.R.1    Eyer, M.2    Backes, W.L.3
  • 56
    • 0036223831 scopus 로고    scopus 로고
    • Summary of information on human CYP enzymes: Human P450 metabolism data
    • DOI 10.1081/DMR-120001392
    • Rendic S (2002) Summary of information on human CYP enzymes: human P450 metabolism data. Drug Metab Rev 34:83-448. (Pubitemid 34311090)
    • (2002) Drug Metabolism Reviews , vol.34 , Issue.1-2 , pp. 83-448
    • Rendic, S.1
  • 57
    • 0030834058 scopus 로고    scopus 로고
    • Human cytochrome P450 enzymes: A status report summarizing their reactions, substrates, inducers, and inhibitors
    • Rendic S and Di Carlo FJ (1997) Human cytochrome P450 enzymes: a status report summarizing their reactions, substrates, inducers, and inhibitors. Drug Metab Rev 29:413-580. (Pubitemid 27293618)
    • (1997) Drug Metabolism Reviews , vol.29 , Issue.1-2 , pp. 413-580
    • Rendic, S.1    Di Carlo, F.J.2
  • 58
    • 84871813154 scopus 로고    scopus 로고
    • Structural characterization of human cytochrome P450 2C19: Active site differences between P450s 2C8, 2C9, and 2C19
    • Reynald RL, Sansen S, Stout CD, and Johnson EF (2012) Structural characterization of human cytochrome P450 2C19: active site differences between P450s 2C8, 2C9, and 2C19. J Biol Chem 287:44581-44591.
    • (2012) J Biol Chem , vol.287 , pp. 44581-44591
    • Reynald, R.L.1    Sansen, S.2    Stout, C.D.3    Johnson, E.F.4
  • 59
    • 78149373621 scopus 로고    scopus 로고
    • Cytochrome P450 compound I: Capture, characterization, and C-H bond activation kinetics
    • Rittle J and Green MT (2010) Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics. Science 330:933-937.
    • (2010) Science , vol.330 , pp. 933-937
    • Rittle, J.1    Green, M.T.2
  • 60
    • 33645451369 scopus 로고    scopus 로고
    • Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hy-droxylase activity
    • Rui L, Pochapsky SS, and Pochapsky TC (2006) Comparison of the complexes formed by cytochrome P450cam with cytochrome b5 and putidaredoxin, two effectors of camphor hy-droxylase activity. Biochemistry 45:3887-3897.
    • (2006) Biochemistry , vol.45 , pp. 3887-3897
    • Rui, L.1    Pochapsky, S.S.2    Pochapsky, T.C.3
  • 61
  • 62
    • 84862876886 scopus 로고    scopus 로고
    • Co-formulated elvitegravir, cobicistat, emtricitabine, and tenofovir versus co-formulated efavirenz, emtricitabine, and tenofovir for initial treatment of HIV-1 infection: A randomised, double-blind, phase 3 trial, analysis of results after 48 weeks
    • GS-US-236-0102 study team
    • Sax PE, DeJesus E, Mills A, Zolopa A, Cohen C, Wohl D, Gallant JE, Liu HC, Zhong L, and Yale K, et al.; GS-US-236-0102 study team (2012) Co-formulated elvitegravir, cobicistat, emtricitabine, and tenofovir versus co-formulated efavirenz, emtricitabine, and tenofovir for initial treatment of HIV-1 infection: a randomised, double-blind, phase 3 trial, analysis of results after 48 weeks. Lancet 379:2439-2448.
    • (2012) Lancet , vol.379 , pp. 2439-2448
    • Sax, P.E.1    Dejesus, E.2    Mills, A.3    Zolopa, A.4    Cohen, C.5    Wohl, D.6    Gallant, J.E.7    Liu, H.C.8    Zhong, L.9    Yale, K.10
  • 63
    • 47749092044 scopus 로고    scopus 로고
    • Determinants of cytochrome P450 2C8 substrate binding: Structures of complexes with montelukast, troglita-zone, felodipine, and 9-cis-retinoic acid
    • Schoch GA, Yano JK, Sansen S, Dansette PM, Stout CD, and Johnson EF (2008) Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglita-zone, felodipine, and 9-cis-retinoic acid. J Biol Chem 283:17227-17237.
    • (2008) J Biol Chem , vol.283 , pp. 17227-17237
    • Schoch, G.A.1    Yano, J.K.2    Sansen, S.3    Dansette, P.M.4    Stout, C.D.5    Johnson, E.F.6
  • 64
    • 1542364450 scopus 로고    scopus 로고
    • Structure of human microsomal cytochrome P450 2C8: Evidence for a peripheral fatty acid binding site
    • DOI 10.1074/jbc.M312516200
    • Schoch GA, Yano JK, Wester MR, Griffin KJ, Stout CD, and Johnson EF (2004) Structure of human microsomal cytochrome P450 2C8. Evidence for a peripheral fatty acid binding site. J Biol Chem 279:9497-9503. (Pubitemid 38296017)
    • (2004) Journal of Biological Chemistry , 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
  • 65
    • 84859353403 scopus 로고    scopus 로고
    • Interaction of human cytochrome P4503A4 with ritonavir analogs
    • Sevrioukova IF and Poulos TL (2012) Interaction of human cytochrome P4503A4 with ritonavir analogs. Arch Biochem Biophys 520:108-116.
    • (2012) Arch Biochem Biophys , vol.520 , pp. 108-116
    • Sevrioukova, I.F.1    Poulos, T.L.2
  • 66
    • 0024518203 scopus 로고
    • Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis
    • Shen AL, Porter TD, Wilson TE, and Kasper CB (1989) Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. J Biol Chem 264:7584-7589. (Pubitemid 19119176)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.13 , pp. 7584-7589
    • Shen, A.L.1    Porter, T.D.2    Wilson, T.E.3    Kasper, C.B.4
  • 67
    • 37849002059 scopus 로고    scopus 로고
    • Broad antiretroviral activity and resistance profile of the novel human immunodeficiency virus integrase inhibitor elvitegravir (JTK-303/GS-9137)
    • Shimura K, Kodama E, Sakagami Y, Matsuzaki Y, Watanabe W, Yamataka K, Watanabe Y, Ohata Y, Doi S, and Sato M, et al. (2008) Broad antiretroviral activity and resistance profile of the novel human immunodeficiency virus integrase inhibitor elvitegravir (JTK-303/GS-9137). J Virol 82:764-774.
    • (2008) J Virol , vol.82 , pp. 764-774
    • Shimura, K.1    Kodama, E.2    Sakagami, Y.3    Matsuzaki, Y.4    Watanabe, W.5    Yamataka, K.6    Watanabe, Y.7    Ohata, Y.8    Doi, S.9    Sato, M.10
  • 69
    • 77957924784 scopus 로고    scopus 로고
    • Prediction and analysis of the modular structure of cytochrome P450 monooxygenases
    • Sirim D, Widmann M, Wagner F, and Pleiss J (2010) Prediction and analysis of the modular structure of cytochrome P450 monooxygenases. BMC Struct Biol 10:34-46.
    • (2010) BMC Struct Biol , vol.10 , pp. 34-46
    • Sirim, D.1    Widmann, M.2    Wagner, F.3    Pleiss, J.4
  • 70
    • 55749115080 scopus 로고    scopus 로고
    • High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands
    • Skinner AL and Laurence JS (2008) High-field solution NMR spectroscopy as a tool for assessing protein interactions with small molecule ligands. J Pharm Sci 97:4670-4695.
    • (2008) J Pharm Sci , vol.97 , pp. 4670-4695
    • Skinner, A.L.1    Laurence, J.S.2
  • 71
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar SG (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15:5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 72
    • 67650809065 scopus 로고    scopus 로고
    • CYP2D6-CYP2C9 protein-protein interactions and isoform-selective effects on substrate binding and catalysis
    • Subramanian M, Low M, Locuson CW, and Tracy TS (2009) CYP2D6-CYP2C9 protein-protein interactions and isoform-selective effects on substrate binding and catalysis. Drug Metab Dispos 37:1682-1689.
    • (2009) Drug Metab Dispos , vol.37 , pp. 1682-1689
    • Subramanian, M.1    Low, M.2    Locuson, C.W.3    Tracy, T.S.4
  • 73
    • 77952304154 scopus 로고    scopus 로고
    • CYP2C9-CYP3A4 protein-protein interactions: Role of the hydrophobic N terminus
    • Subramanian M, Tam H, Zheng H, and Tracy TS (2010) CYP2C9-CYP3A4 protein-protein interactions: role of the hydrophobic N terminus. Drug Metab Dispos 38:1003-1009.
    • (2010) Drug Metab Dispos , vol.38 , pp. 1003-1009
    • Subramanian, M.1    Tam, H.2    Zheng, H.3    Tracy, T.S.4
  • 74
    • 84874798958 scopus 로고    scopus 로고
    • Mapping of interaction between cytochrome P450 2B4 and cytochrome b5: The first evidence of two mutual orientations
    • Sulc M, Jecmen T, Snajdrova R, Novak P, Martinek V, Hodek P, Stiborova M, and Hudecek J (2012) Mapping of interaction between cytochrome P450 2B4 and cytochrome b5: the first evidence of two mutual orientations. Neuroendocrinol Lett 33 (Suppl 3):41-47.
    • (2012) Neuroendocrinol Lett , vol.33 , Issue.SUPPL. 3 , pp. 41-47
    • Sulc, M.1    Jecmen, T.2    Snajdrova, R.3    Novak, P.4    Martinek, V.5    Hodek, P.6    Stiborova, M.7    Hudecek, J.8
  • 75
    • 71449103290 scopus 로고    scopus 로고
    • Structure-based drug metabolism predictions for drug design
    • Sun H and Scott DO (2010) Structure-based drug metabolism predictions for drug design. Chem Biol Drug Des 75:3-17.
    • (2010) Chem Biol Drug des , vol.75 , pp. 3-17
    • Sun, H.1    Scott, D.O.2
  • 76
    • 0034652164 scopus 로고    scopus 로고
    • Cytochromes P450 2C1/2 and P450 2E1 are retained in the endoplasmic reticulum membrane by different mechanisms
    • DOI 10.1006/abbi.1999.1628
    • Szczesna-Skorupa E, Chen CD, and Kemper B (2000) Cytochromes P450 2C1/2 and P450 2E1 are retained in the endoplasmic reticulum membrane by different mechanisms. Arch Biochem Biophys 374:128-136. (Pubitemid 30120245)
    • (2000) Archives of Biochemistry and Biophysics , vol.374 , Issue.2 , pp. 128-136
    • Szczesna-Skorupa, E.1    Chen, C.-D.2    Kemper, B.3
  • 77
    • 84878747590 scopus 로고    scopus 로고
    • Structural basis for effector control and redox partner recognition in cytochrome P450
    • Tripathi S, Li H, and Poulos TL (2013) Structural basis for effector control and redox partner recognition in cytochrome P450. Science 340:1227-1230.
    • (2013) Science , vol.340 , pp. 1227-1230
    • Tripathi, S.1    Li, H.2    Poulos, T.L.3
  • 78
    • 0035916224 scopus 로고    scopus 로고
    • Identification of human CYP2C19 residues that confer S-mephenytoin 4́-hydroxylation activity to CYP2C9
    • DOI 10.1021/bi001678u
    • Tsao CC, Wester MR, Ghanayem B, Coulter SJ, Chanas B, Johnson EF, and Goldstein JA (2001) Identification of human CYP2C19 residues that confer S-mephenytoin 49-hydroxylation activity to CYP2C9. Biochemistry 40:1937-1944. (Pubitemid 32165662)
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 1937-1944
    • Tsao, C.-C.1    Wester, M.R.2    Ghanayem, B.3    Coulter, S.J.4    Chanas, B.5    Johnson, E.F.6    Goldstein, J.A.7
  • 79
    • 84877134071 scopus 로고    scopus 로고
    • Human cytochrome P450 1A1 structure and utility in understanding drug and xenobiotic metabolism
    • Walsh AA, Szklarz GD, and Scott EE (2013) Human cytochrome P450 1A1 structure and utility in understanding drug and xenobiotic metabolism. J Biol Chem 288:12932-12943.
    • (2013) J Biol Chem , vol.288 , pp. 12932-12943
    • Walsh, A.A.1    Szklarz, G.D.2    Scott, E.E.3
  • 80
    • 84859500879 scopus 로고    scopus 로고
    • Crystal structure of human cytochrome P450 2D6 with prinomastat bound
    • Wang A, Savas U, Hsu MH, Stout CD, and Johnson EF (2012) Crystal structure of human cytochrome P450 2D6 with prinomastat bound. J Biol Chem 287:10834-10843.
    • (2012) J Biol Chem , vol.287 , pp. 10834-10843
    • Wang, A.1    Savas, U.2    Hsu, M.H.3    Stout, C.D.4    Johnson, E.F.5
  • 81
    • 79953126762 scopus 로고    scopus 로고
    • Structural characterization of the complex between alpha-naphthoflavone and human cytochrome P450 1B1
    • Wang A, Savas U, Stout CD, and Johnson EF (2011) Structural characterization of the complex between alpha-naphthoflavone and human cytochrome P450 1B1. J Biol Chem 286: 5736-5743.
    • (2011) J Biol Chem , vol.286 , pp. 5736-5743
    • Wang, A.1    Savas, U.2    Stout, C.D.3    Johnson, E.F.4
  • 82
    • 70350044889 scopus 로고    scopus 로고
    • New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme
    • Wang B, Yang LP, Zhang XZ, Huang SQ, Bartlam M, and Zhou SF (2009) New insights into the structural characteristics and functional relevance of the human cytochrome P450 2D6 enzyme. Drug Metab Rev 41:573-643.
    • (2009) Drug Metab Rev , vol.41 , pp. 573-643
    • Wang, B.1    Yang, L.P.2    Zhang, X.Z.3    Huang, S.Q.4    Bartlam, M.5    Zhou, S.F.6
  • 84
    • 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
    • DOI 10.1021/bi034556l
    • Wester MR, Johnson EF, Marques-Soares C, Dijols S, Dansette PM, Mansuy D, and Stout CD (2003) 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: 9335-9345. (Pubitemid 36959241)
    • (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
  • 85
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams PA, Cosme J, Sridhar V, Johnson EF, and McRee DE (2000) Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol Cell 5:121-131. (Pubitemid 30105441)
    • (2000) Molecular 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
  • 89
    • 68649113534 scopus 로고    scopus 로고
    • Pharmacokinetic enhancers for HIV drugs
    • Xu L and Desai MC (2009) Pharmacokinetic enhancers for HIV drugs. Curr Opin Investig Drugs 10:775-786.
    • (2009) Curr Opin Investig Drugs , vol.10 , pp. 775-786
    • Xu, L.1    Desai, M.C.2
  • 92
    • 4644301430 scopus 로고    scopus 로고
    • The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution
    • DOI 10.1074/jbc.C400293200
    • Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, and Johnson EF (2004) The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 279:38091-38094. (Pubitemid 39295952)
    • (2004) Journal of Biological Chemistry , 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
  • 94
    • 84875211310 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes in drug metabolism: Regulation of gene expression, enzyme activities, and impact of genetic variation
    • Zanger UM and Schwab M (2013) Cytochrome P450 enzymes in drug metabolism: regulation of gene expression, enzyme activities, and impact of genetic variation. Pharmacol Ther 138:103-141.
    • (2013) Pharmacol Ther , vol.138 , pp. 103-141
    • Zanger, U.M.1    Schwab, M.2
  • 95
    • 54949144309 scopus 로고    scopus 로고
    • Functional pharmacogenetics/genomics of human cytochromes P450 involved in drug biotransformation
    • Zanger UM, Turpeinen M, Klein K, and Schwab M (2008) Functional pharmacogenetics/genomics of human cytochromes P450 involved in drug biotransformation. Anal Bioanal Chem 392:1093-1108.
    • (2008) Anal Bioanal Chem , vol.392 , pp. 1093-1108
    • Zanger, U.M.1    Turpeinen, M.2    Klein, K.3    Schwab, M.4
  • 96
    • 84870202411 scopus 로고    scopus 로고
    • Cross-linking mass spectrometry and mutagenesis confirm the functional importance of surface interactions between CYP3A4 and holo/apo cytochrome b(5)
    • Zhao C, Gao Q, Roberts AG, Shaffer SA, Doneanu CE, Xue S, Goodlett DR, Nelson SD, and Atkins WM (2012) Cross-linking mass spectrometry and mutagenesis confirm the functional importance of surface interactions between CYP3A4 and holo/apo cytochrome b(5). Biochemistry 51:9488-9500.
    • (2012) Biochemistry , vol.51 , pp. 9488-9500
    • Zhao, C.1    Gao, Q.2    Roberts, A.G.3    Shaffer, S.A.4    Doneanu, C.E.5    Xue, S.6    Goodlett, D.R.7    Nelson, S.D.8    Atkins, W.M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.