메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Functional characterization of a first avian cytochrome P450 of the CYP2d subfamily (CYP2D49)

Author keywords

[No Author keywords available]

Indexed keywords

BUFURALOL; COMPLEMENTARY DNA; CYTOCHROME P450 2D; CYTOCHROME P450 2D49; CYTOCHROME P450 2D6; DEBRISOQUINE; QUINIDINE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ANTISERUM; CYTOCHROME P450; ETHANOLAMINE DERIVATIVE; ISOENZYME;

EID: 84861902895     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0038395     Document Type: Article
Times cited : (12)

References (53)
  • 1
    • 0034973607 scopus 로고    scopus 로고
    • Cytochromes P450 and metabolism of xenobiotics
    • Anzenbacher P, Anzenbacherova E, (2001) Cytochromes P450 and metabolism of xenobiotics. Cell Mol Life Sci 58: 737-747.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 737-747
    • Anzenbacher, P.1    Anzenbacherova, E.2
  • 2
    • 0036548404 scopus 로고    scopus 로고
    • Cytochromes P450 and experimental models of drug metabolism
    • Zuber R, Anzenbacherova E, Anzenbacher P, (2002) Cytochromes P450 and experimental models of drug metabolism. J Cell Mol Med 6: 189-198.
    • (2002) J Cell Mol Med , vol.6 , pp. 189-198
    • Zuber, R.1    Anzenbacherova, E.2    Anzenbacher, P.3
  • 3
    • 79955690297 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 2D6 and variants in terms of drug oxidation rates and substrate inhibition
    • Niwa T, Murayama N, Yamazaki H, (2011) Comparison of cytochrome P450 2D6 and variants in terms of drug oxidation rates and substrate inhibition. Curr Drug Metab 12: 412-435.
    • (2011) Curr Drug Metab , vol.12 , pp. 412-435
    • Niwa, T.1    Murayama, N.2    Yamazaki, H.3
  • 4
    • 70349386728 scopus 로고    scopus 로고
    • Polymorphism of human cytochrome P450 2D6 and its clinical significance: Part I. Clin Pharmacokinet
    • Zhou SF, (2009) Polymorphism of human cytochrome P450 2D6 and its clinical significance: Part I. Clin Pharmacokinet 48: 689-723.
    • (2009) , vol.48 , pp. 689-723
    • Zhou, S.F.1
  • 5
    • 70349386728 scopus 로고    scopus 로고
    • Polymorphism of human cytochrome P450 2D6 and its clinical significance: part II
    • Zhou SF, (2009) Polymorphism of human cytochrome P450 2D6 and its clinical significance: part II. Clin Pharmacokinet 48: 761-804.
    • (2009) Clin Pharmacokinet , vol.48 , pp. 761-804
    • Zhou, S.F.1
  • 6
    • 57349180672 scopus 로고    scopus 로고
    • Functional characterization of 17 CYP2D6 allelic variants (CYP2D6.2, 10, 14A-B, 18, 27, 36, 39, 47-51, 53-55, and 57)
    • Sakuyama K, Sasaki T, Ujiie S, Obata K, Mizugaki M, et al. (2008) Functional characterization of 17 CYP2D6 allelic variants (CYP2D6.2, 10, 14A-B, 18, 27, 36, 39, 47-51, 53-55, and 57). Drug Metab Dispos 36: 2460-2467.
    • (2008) Drug Metab Dispos , vol.36 , pp. 2460-2467
    • Sakuyama, K.1    Sasaki, T.2    Ujiie, S.3    Obata, K.4    Mizugaki, M.5
  • 7
    • 3042515935 scopus 로고    scopus 로고
    • Polymorphic cytochrome P450 2D6: humanized mouse model and endogenous substrates
    • Yu AM, Idle JR, Gonzalez FJ, (2004) Polymorphic cytochrome P450 2D6: humanized mouse model and endogenous substrates. Drug Metab Rev 36: 243-277.
    • (2004) Drug Metab Rev , vol.36 , pp. 243-277
    • Yu, A.M.1    Idle, J.R.2    Gonzalez, F.J.3
  • 10
    • 0023154962 scopus 로고
    • Debrisoquine 4-hydroxylase: characterization of a new P450 gene subfamily, regulation, chromosomal mapping, and molecular analysis of the DA rat polymorphism
    • Gonzalez FJ, Matsunaga T, Nagata K, Meyer UA, Nebert DW, et al. (1987) Debrisoquine 4-hydroxylase: characterization of a new P450 gene subfamily, regulation, chromosomal mapping, and molecular analysis of the DA rat polymorphism. DNA 6: 149-161.
    • (1987) DNA , vol.6 , pp. 149-161
    • Gonzalez, F.J.1    Matsunaga, T.2    Nagata, K.3    Meyer, U.A.4    Nebert, D.W.5
  • 11
    • 0025164996 scopus 로고
    • The rat P450 IID subfamily: complete sequences of four closely linked genes and evidence that gene conversions maintained sequence homogeneity at the heme-binding region of the cytochrome P450 active site
    • Matsunaga E, Umeno M, Gonzalez FJ, (1990) The rat P450 IID subfamily: complete sequences of four closely linked genes and evidence that gene conversions maintained sequence homogeneity at the heme-binding region of the cytochrome P450 active site. J Mol Evol 30: 155-169.
    • (1990) J Mol Evol , vol.30 , pp. 155-169
    • Matsunaga, E.1    Umeno, M.2    Gonzalez, F.J.3
  • 12
    • 0026639457 scopus 로고
    • Purification and characterization of a cytochrome P-450 isozyme catalyzing bunitrolol 4-hydroxylation in liver microsomes of male rats
    • Suzuki T, Narimatsu S, Fujita S, Masubuchi Y, Umeda S, et al. (1992) Purification and characterization of a cytochrome P-450 isozyme catalyzing bunitrolol 4-hydroxylation in liver microsomes of male rats. Drug Metab Dispos 20: 367-373.
    • (1992) Drug Metab Dispos , vol.20 , pp. 367-373
    • Suzuki, T.1    Narimatsu, S.2    Fujita, S.3    Masubuchi, Y.4    Umeda, S.5
  • 13
    • 0036707625 scopus 로고    scopus 로고
    • Catalytic specificity of CYP2D isoforms in rat and human
    • Hiroi T, Chow T, Imaoka S, Funae Y, (2002) Catalytic specificity of CYP2D isoforms in rat and human. Drug Metab Dispos 30: 970-976.
    • (2002) Drug Metab Dispos , vol.30 , pp. 970-976
    • Hiroi, T.1    Chow, T.2    Imaoka, S.3    Funae, Y.4
  • 14
    • 0023621075 scopus 로고
    • Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-450(16) alpha) in mouse liver: cDNA sequences, neonatal imprinting, and reversible regulation by androgen
    • Wong G, Kawajiri K, Negishi M, (1987) Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-450(16) alpha) in mouse liver: cDNA sequences, neonatal imprinting, and reversible regulation by androgen. Biochemistry 26: 8683-8690.
    • (1987) Biochemistry , vol.26 , pp. 8683-8690
    • Wong, G.1    Kawajiri, K.2    Negishi, M.3
  • 15
    • 0024520426 scopus 로고
    • Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-450(16 alpha)) in mice. Organization, differential regulation, and chromosome localization
    • Wong G, Itakura T, Kawajiri K, Skow L, Negishi M, (1989) Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-450(16 alpha)) in mice. Organization, differential regulation, and chromosome localization. J Biol Chem 264: 2920-2927.
    • (1989) J Biol Chem , vol.264 , pp. 2920-2927
    • Wong, G.1    Itakura, T.2    Kawajiri, K.3    Skow, L.4    Negishi, M.5
  • 16
    • 0029068435 scopus 로고
    • Molecular cloning and sequencing of a guinea pig cytochrome P4502D (CYP2D16): high level expression in adrenal microsomes
    • Jiang Q, Voigt JM, Colby HD, (1995) Molecular cloning and sequencing of a guinea pig cytochrome P4502D (CYP2D16): high level expression in adrenal microsomes. Biochem Biophys Res Commun 209: 1149-1156.
    • (1995) Biochem Biophys Res Commun , vol.209 , pp. 1149-1156
    • Jiang, Q.1    Voigt, J.M.2    Colby, H.D.3
  • 17
    • 0029018966 scopus 로고
    • A new cytochrome P450 form belonging to the CYP2D in dog liver microsomes: purification, cDNA cloning, and enzyme characterization
    • Sakamoto K, Kirita S, Baba T, Nakamura Y, Yamazoe Y, et al. (1995) A new cytochrome P450 form belonging to the CYP2D in dog liver microsomes: purification, cDNA cloning, and enzyme characterization. Arch Biochem Biophys 319: 372-382.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 372-382
    • Sakamoto, K.1    Kirita, S.2    Baba, T.3    Nakamura, Y.4    Yamazoe, Y.5
  • 18
    • 0031958789 scopus 로고    scopus 로고
    • Regio- and stereoselectivity in propranolol metabolism by dog liver microsomes and the expressed dog CYP2D15
    • Tasaki T, Iwata H, Kazusaka A, Fujita S, (1998) Regio- and stereoselectivity in propranolol metabolism by dog liver microsomes and the expressed dog CYP2D15. J Biochem 123: 747-751.
    • (1998) J Biochem , vol.123 , pp. 747-751
    • Tasaki, T.1    Iwata, H.2    Kazusaka, A.3    Fujita, S.4
  • 19
    • 0026671134 scopus 로고
    • Characterization of the cytochrome P-450IID subfamily in bovine liver. Nucleotide sequences and microheterogeneity
    • Tsuneoka Y, Matsuo Y, Higuchi R, Ichikawa Y, (1992) Characterization of the cytochrome P-450IID subfamily in bovine liver. Nucleotide sequences and microheterogeneity. Eur J Biochem 208: 739-746.
    • (1992) Eur J Biochem , vol.208 , pp. 739-746
    • Tsuneoka, Y.1    Matsuo, Y.2    Higuchi, R.3    Ichikawa, Y.4
  • 20
    • 0031665302 scopus 로고    scopus 로고
    • Cloning, tissue distribution, and functional expression of two novel rabbit cytochrome P450 isozymes, CYP2D23 and CYP2D24
    • Yamamoto Y, Ishizuka M, Takada A, Fujita S, (1998) Cloning, tissue distribution, and functional expression of two novel rabbit cytochrome P450 isozymes, CYP2D23 and CYP2D24. J Biochem 124: 503-508.
    • (1998) J Biochem , vol.124 , pp. 503-508
    • Yamamoto, Y.1    Ishizuka, M.2    Takada, A.3    Fujita, S.4
  • 21
    • 0036775368 scopus 로고    scopus 로고
    • Complementary DNA cloning and characterization of cytochrome P450 2D29 from Japanese monkey liver
    • Hichiya H, Takemi C, Tsuzuki D, Yamamoto S, Asaoka K, et al. (2002) Complementary DNA cloning and characterization of cytochrome P450 2D29 from Japanese monkey liver. Biochem Pharmacol 64: 1101-1110.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1101-1110
    • Hichiya, H.1    Takemi, C.2    Tsuzuki, D.3    Yamamoto, S.4    Asaoka, K.5
  • 22
    • 2942618689 scopus 로고    scopus 로고
    • Cloning and functional expression of a novel marmoset cytochrome P450 2D enzyme, CYP2D30: comparison with the known marmoset CYP2D19
    • Hichiya H, Kuramoto S, Yamamoto S, Shinoda S, Hanioka N, et al. (2004) Cloning and functional expression of a novel marmoset cytochrome P450 2D enzyme, CYP2D30: comparison with the known marmoset CYP2D19. Biochem Pharmacol 68: 165-175.
    • (2004) Biochem Pharmacol , vol.68 , pp. 165-175
    • Hichiya, H.1    Kuramoto, S.2    Yamamoto, S.3    Shinoda, S.4    Hanioka, N.5
  • 23
    • 84872750285 scopus 로고    scopus 로고
    • Encyclopædia Britannica: Firely Encyclopædia of birds
    • New York, Firefly Books, Ltd
    • Perrins, Christopher B, (2003) Encyclopædia Britannica: Firely Encyclopædia of birds. New York Firefly Books, Ltd.
    • (2003)
    • Perrins1    Christopher, B.2
  • 24
    • 12644271134 scopus 로고    scopus 로고
    • Molecular cloning and expression of two novel avian cytochrome P450 1A enzymes induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Gilday D, Gannon M, Yutzey K, Bader D, Rifkind AB, (1996) Molecular cloning and expression of two novel avian cytochrome P450 1A enzymes induced by 2,3,7,8-tetrachlorodibenzo-p-dioxin. J Biol Chem 271: 33054-33059.
    • (1996) J Biol Chem , vol.271 , pp. 33054-33059
    • Gilday, D.1    Gannon, M.2    Yutzey, K.3    Bader, D.4    Rifkind, A.B.5
  • 25
    • 0034650376 scopus 로고    scopus 로고
    • Cloning and functional expression of a first inducible avian cytochrome P450 of the CYP3A subfamily (CYP3A37)
    • Ourlin JC, Baader M, Fraser D, Halpert JR, Meyer UA, (2000) Cloning and functional expression of a first inducible avian cytochrome P450 of the CYP3A subfamily (CYP3A37). Arch Biochem Biophys 373: 375-384.
    • (2000) Arch Biochem Biophys , vol.373 , pp. 375-384
    • Ourlin, J.C.1    Baader, M.2    Fraser, D.3    Halpert, J.R.4    Meyer, U.A.5
  • 26
    • 0037013291 scopus 로고    scopus 로고
    • Transcriptional activation of cytochrome P450 CYP2C45 by drugs is mediated by the chicken xenobiotic receptor (CXR) interacting with a phenobarbital response enhancer unit
    • Baader M, Gnerre C, Stegeman JJ, Meyer UA, (2002) Transcriptional activation of cytochrome P450 CYP2C45 by drugs is mediated by the chicken xenobiotic receptor (CXR) interacting with a phenobarbital response enhancer unit. J Biol Chem 277: 15647-15653.
    • (2002) J Biol Chem , vol.277 , pp. 15647-15653
    • Baader, M.1    Gnerre, C.2    Stegeman, J.J.3    Meyer, U.A.4
  • 27
    • 0034757667 scopus 로고    scopus 로고
    • In vitro cytochrome P450-mediated hepatic activities for five substrates in specific pathogen free chickens
    • Khalil WF, Saitoh T, Shimoda M, Kokue E, (2001) In vitro cytochrome P450-mediated hepatic activities for five substrates in specific pathogen free chickens. J Vet Pharmacol Ther 24: 343-348.
    • (2001) J Vet Pharmacol Ther , vol.24 , pp. 343-348
    • Khalil, W.F.1    Saitoh, T.2    Shimoda, M.3    Kokue, E.4
  • 28
    • 33745177792 scopus 로고    scopus 로고
    • Cytochrome P450 nomenclature, 2004
    • Nelson DR, (2006) Cytochrome P450 nomenclature, 2004. Methods Mol Biol 320: 1-10.
    • (2006) Methods Mol Biol , vol.320 , pp. 1-10
    • Nelson, D.R.1
  • 29
    • 0022980052 scopus 로고
    • Debrisoquine/sparteine-type polymorphism of drug oxidation. Purification and characterization of two functionally different human liver cytochrome P-450 isozymes involved in impaired hydroxylation of the prototype substrate bufuralol
    • Gut J, Catin T, Dayer P, Kronbach T, Zanger U, et al. (1986) Debrisoquine/sparteine-type polymorphism of drug oxidation. Purification and characterization of two functionally different human liver cytochrome P-450 isozymes involved in impaired hydroxylation of the prototype substrate bufuralol. J Biol Chem 261: 11734-11743.
    • (1986) J Biol Chem , vol.261 , pp. 11734-11743
    • Gut, J.1    Catin, T.2    Dayer, P.3    Kronbach, T.4    Zanger, U.5
  • 30
    • 33845473315 scopus 로고    scopus 로고
    • Species differences between mouse, rat, dog, monkey and human CYP-mediated drug metabolism, inhibition and induction
    • Martignoni M, Groothuis GM, de Kanter R, (2006) Species differences between mouse, rat, dog, monkey and human CYP-mediated drug metabolism, inhibition and induction. Expert Opin Drug Metab Toxicol 2: 875-894.
    • (2006) Expert Opin Drug Metab Toxicol , vol.2 , pp. 875-894
    • Martignoni, M.1    Groothuis, G.M.2    de Kanter, R.3
  • 32
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield NJ, (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1: 2876-2890.
    • (2006) Nat Protoc , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 33
    • 0025978540 scopus 로고
    • NcoI RFLP in the pseudogene (CYP2D8P) of the human debrisoquine 4-hydroxylase locus
    • Mura C, Broyart JP, Jacqz E, Elion J, Krishnamoorthy R, (1991) NcoI RFLP in the pseudogene (CYP2D8P) of the human debrisoquine 4-hydroxylase locus. Nucleic Acids Res 19: 1162.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1162
    • Mura, C.1    Broyart, J.P.2    Jacqz, E.3    Elion, J.4    Krishnamoorthy, R.5
  • 34
    • 0029736710 scopus 로고    scopus 로고
    • Characterization and PCR-based detection of two different hybrid CYP2D7P/CYP2D6 alleles associated with the poor metabolizer phenotype
    • Daly AK, Fairbrother KS, Andreassen OA, London SJ, Idle JR, et al. (1996) Characterization and PCR-based detection of two different hybrid CYP2D7P/CYP2D6 alleles associated with the poor metabolizer phenotype. Pharmacogenetics 6: 319-328.
    • (1996) Pharmacogenetics , vol.6 , pp. 319-328
    • Daly, A.K.1    Fairbrother, K.S.2    Andreassen, O.A.3    London, S.J.4    Idle, J.R.5
  • 35
    • 0842312531 scopus 로고    scopus 로고
    • Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants
    • Nelson DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, et al. (2004) Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14: 1-18.
    • (2004) Pharmacogenetics , vol.14 , pp. 1-18
    • Nelson, D.R.1    Zeldin, D.C.2    Hoffman, S.M.3    Maltais, L.J.4    Wain, H.M.5
  • 36
    • 0034607818 scopus 로고    scopus 로고
    • A conserved nuclear receptor consensus sequence (DR-4) mediates transcriptional activation of the chicken CYP2H1 gene by phenobarbital in a hepatoma cell line
    • Handschin C, Meyer UA, (2000) A conserved nuclear receptor consensus sequence (DR-4) mediates transcriptional activation of the chicken CYP2H1 gene by phenobarbital in a hepatoma cell line. J Biol Chem 275: 13362-13369.
    • (2000) J Biol Chem , vol.275 , pp. 13362-13369
    • Handschin, C.1    Meyer, U.A.2
  • 37
    • 0034838324 scopus 로고    scopus 로고
    • Conservation of signaling pathways of xenobiotic-sensing orphan nuclear receptors, chicken xenobiotic receptor, constitutive androstane receptor, and pregnane X receptor, from birds to humans
    • Handschin C, Podvinec M, Stockli J, Hoffmann K, Meyer UA, (2001) Conservation of signaling pathways of xenobiotic-sensing orphan nuclear receptors, chicken xenobiotic receptor, constitutive androstane receptor, and pregnane X receptor, from birds to humans. Mol Endocrinol 15: 1571-1585.
    • (2001) Mol Endocrinol , vol.15 , pp. 1571-1585
    • Handschin, C.1    Podvinec, M.2    Stockli, J.3    Hoffmann, K.4    Meyer, U.A.5
  • 38
    • 0002030427 scopus 로고
    • Enzyme induction in the cytochrome P450 system
    • In: Kalow W, editors
    • Okey AB, (1992) Enzyme induction in the cytochrome P450 system. In: Kalow W, editors. Pharmacogenetics of Drug Metabolism pp. 594-608.
    • (1992) Pharmacogenetics of Drug Metabolism , pp. 594-608
    • Okey, A.B.1
  • 39
    • 10844274767 scopus 로고    scopus 로고
    • Change in enantioselectivity in bufuralol 1″-hydroxylation by the substitution of phenylalanine-120 by alanine in cytochrome P450 2D6
    • Masuda K, Tamagake K, Okuda Y, Torigoe F, Tsuzuki D, et al. (2005) Change in enantioselectivity in bufuralol 1″-hydroxylation by the substitution of phenylalanine-120 by alanine in cytochrome P450 2D6. Chirality 17: 37-43.
    • (2005) Chirality , vol.17 , pp. 37-43
    • Masuda, K.1    Tamagake, K.2    Okuda, Y.3    Torigoe, F.4    Tsuzuki, D.5
  • 40
    • 0019492928 scopus 로고
    • Animal modelling of human polymorphic drug oxidation-the metabolism of debrisoquine and phenacetin in rat inbred strains
    • Al-Dabbagh SG, Idle JR, Smith RL, (1981) Animal modelling of human polymorphic drug oxidation-the metabolism of debrisoquine and phenacetin in rat inbred strains. J Pharm Pharmacol 33: 161-164.
    • (1981) J Pharm Pharmacol , vol.33 , pp. 161-164
    • Al-Dabbagh, S.G.1    Idle, J.R.2    Smith, R.L.3
  • 41
    • 0034454016 scopus 로고    scopus 로고
    • Determining the best animal model for human cytochrome P450 activities: a comparison of mouse, rat, rabbit, dog, micropig, monkey and man
    • Bogaards JJ, Bertrand M, Jackson P, Oudshoorn MJ, Weaver RJ, et al. (2000) Determining the best animal model for human cytochrome P450 activities: a comparison of mouse, rat, rabbit, dog, micropig, monkey and man. Xenobiotica 30: 1131-1152.
    • (2000) Xenobiotica , vol.30 , pp. 1131-1152
    • Bogaards, J.J.1    Bertrand, M.2    Jackson, P.3    Oudshoorn, M.J.4    Weaver, R.J.5
  • 42
    • 0037423276 scopus 로고    scopus 로고
    • Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6
    • Paine MJ, McLaughlin LA, Flanagan JU, Kemp CA, Sutcliffe MJ, et al. (2003) Residues glutamate 216 and aspartate 301 are key determinants of substrate specificity and product regioselectivity in cytochrome P450 2D6. J Biol Chem 278: 4021-4027.
    • (2003) J Biol Chem , vol.278 , pp. 4021-4027
    • Paine, M.J.1    McLaughlin, L.A.2    Flanagan, J.U.3    Kemp, C.A.4    Sutcliffe, M.J.5
  • 43
    • 0028832796 scopus 로고
    • Evidence that aspartic acid 301 is a critical substrate-contact residue in the active site of cytochrome P450 2D6
    • Ellis SW, Hayhurst GP, Smith G, Lightfoot T, Wong MM, et al. (1995) Evidence that aspartic acid 301 is a critical substrate-contact residue in the active site of cytochrome P450 2D6. J Biol Chem 270: 29055-29058.
    • (1995) J Biol Chem , vol.270 , pp. 29055-29058
    • Ellis, S.W.1    Hayhurst, G.P.2    Smith, G.3    Lightfoot, T.4    Wong, M.M.5
  • 44
    • 7444225179 scopus 로고    scopus 로고
    • Influence of phenylalanine 120 on cytochrome P450 2D6 catalytic selectivity and regiospecificity: crucial role in 7-methoxy-4-(aminomethyl)-coumarin metabolism
    • Keizers PH, Lussenburg BM, de Graaf C, Mentink LM, Vermeulen NP, et al. (2004) Influence of phenylalanine 120 on cytochrome P450 2D6 catalytic selectivity and regiospecificity: crucial role in 7-methoxy-4-(aminomethyl)-coumarin metabolism. Biochem Pharmacol 68: 2263-2271.
    • (2004) Biochem Pharmacol , vol.68 , pp. 2263-2271
    • Keizers, P.H.1    Lussenburg, B.M.2    de Graaf, C.3    Mentink, L.M.4    Vermeulen, N.P.5
  • 45
    • 5044245324 scopus 로고    scopus 로고
    • Phe120 contributes to the regiospecificity of cytochrome P450 2D6: mutation leads to the formation of a novel dextromethorphan metabolite
    • Flanagan JU, Marechal JD, Ward R, Kemp CA, McLaughlin LA, et al. (2004) Phe120 contributes to the regiospecificity of cytochrome P450 2D6: mutation leads to the formation of a novel dextromethorphan metabolite. Biochem J 380: 353-360.
    • (2004) Biochem J , vol.380 , pp. 353-360
    • Flanagan, J.U.1    Marechal, J.D.2    Ward, R.3    Kemp, C.A.4    McLaughlin, L.A.5
  • 46
    • 0035870926 scopus 로고    scopus 로고
    • Influence of phenylalanine-481 substitutions on the catalytic activity of cytochrome P450 2D6
    • Hayhurst GP, Harlow J, Chowdry J, Gross E, Hilton E, et al. (2001) Influence of phenylalanine-481 substitutions on the catalytic activity of cytochrome P450 2D6. Biochem J 355: 373-379.
    • (2001) Biochem J , vol.355 , pp. 373-379
    • Hayhurst, G.P.1    Harlow, J.2    Chowdry, J.3    Gross, E.4    Hilton, E.5
  • 47
    • 0031574143 scopus 로고    scopus 로고
    • Expression of four rat CYP2D isoforms in Saccharomyces cerevisiae and their catalytic specificity
    • Wan J, Imaoka S, Chow T, Hiroi T, Yabusaki Y, et al. (1997) Expression of four rat CYP2D isoforms in Saccharomyces cerevisiae and their catalytic specificity. Arch Biochem Biophys 348: 383-390.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 383-390
    • Wan, J.1    Imaoka, S.2    Chow, T.3    Hiroi, T.4    Yabusaki, Y.5
  • 48
    • 59749096859 scopus 로고    scopus 로고
    • The mechanism causing the difference in kinetic properties between rat CYP2D4 and human CYP2D6 in the oxidation of dextromethorphan and bufuralol
    • Narimatsu S, Kazamori D, Masuda K, Katsu T, Funae Y, et al. (2009) The mechanism causing the difference in kinetic properties between rat CYP2D4 and human CYP2D6 in the oxidation of dextromethorphan and bufuralol. Biochem Pharmacol 77: 920-931.
    • (2009) Biochem Pharmacol , vol.77 , pp. 920-931
    • Narimatsu, S.1    Kazamori, D.2    Masuda, K.3    Katsu, T.4    Funae, Y.5
  • 49
  • 50
    • 0035370360 scopus 로고    scopus 로고
    • Preparation and functional properties of polyclonal and monoclonal antibodies to murine MD-1
    • Hadidi S, Yu K, Chen Z, Gorczynski RM, (2001) Preparation and functional properties of polyclonal and monoclonal antibodies to murine MD-1. Immunol Lett 77: 97-103.
    • (2001) Immunol Lett , vol.77 , pp. 97-103
    • Hadidi, S.1    Yu, K.2    Chen, Z.3    Gorczynski, R.M.4
  • 51
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 53
    • 0016169865 scopus 로고
    • Determination of the helix and beta form of proteins in aqueous solution by circular dichroism
    • Chen YH, Yang JT, Chau KH, (1974) Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. Biochemistry 13: 3350-3359.
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.