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Volumn 397, Issue 4, 2010, Pages 1067-1078

Structural basis of human CYP51 inhibition by antifungal azoles

Author keywords

Antifungal drugs; Human cytochrome P450; Sterol 14alpha demethylase; X ray crystallography

Indexed keywords

1 PHENYLIMIDAZOLE; 4 PHENYLIMIDAZOLE; ANTIFUNGAL AGENT; BIFONAZOLE; CLOTRIMAZOLE; CYPROCONAZOLE; ECONAZOLE; FLUCONAZOLE; KETOCONAZOLE; LANOSTEROL; MICONAZOLE; PROPICONAZOLE; PYRROLE DERIVATIVE; STEROL 14ALPHA DEMETHYLASE; TRIADIMENOL; UNCLASSIFIED DRUG;

EID: 77950023120     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.075     Document Type: Article
Times cited : (235)

References (53)
  • 1
    • 17344368276 scopus 로고    scopus 로고
    • Recent progress in the CYP51 research focusing on its unique evolutionary and functional characteristics as a diversozyme P450
    • Aoyama Y. Recent progress in the CYP51 research focusing on its unique evolutionary and functional characteristics as a diversozyme P450. Front. Biosci. 2005, 10:1546-1557.
    • (2005) Front. Biosci. , vol.10 , pp. 1546-1557
    • Aoyama, Y.1
  • 3
    • 16244416503 scopus 로고    scopus 로고
    • Second-generation azole antifungal agents
    • Kale P., Johnson L.B. Second-generation azole antifungal agents. Drugs Today 2005, 41:91-105.
    • (2005) Drugs Today , vol.41 , pp. 91-105
    • Kale, P.1    Johnson, L.B.2
  • 4
    • 0037327813 scopus 로고    scopus 로고
    • Fatty acid and sterol metabolism: potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa
    • Roberts C.W., McLeod R., Rice D.W., Ginger M., Chance M.L., Goad L.J. Fatty acid and sterol metabolism: potential antimicrobial targets in apicomplexan and trypanosomatid parasitic protozoa. Mol. Biochem. Parasitol. 2003, 126:129-142.
    • (2003) Mol. Biochem. Parasitol. , vol.126 , pp. 129-142
    • Roberts, C.W.1    McLeod, R.2    Rice, D.W.3    Ginger, M.4    Chance, M.L.5    Goad, L.J.6
  • 5
    • 34247579197 scopus 로고    scopus 로고
    • Chemotherapy of leishmaniasis: past, present and future
    • Mishra J., Saxena A., Singh S. Chemotherapy of leishmaniasis: past, present and future. Curr. Med. Chem. 2007, 14:1153-1169.
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1153-1169
    • Mishra, J.1    Saxena, A.2    Singh, S.3
  • 6
    • 0032826408 scopus 로고    scopus 로고
    • Contribution of mutations in the cytochrome P450 14alpha-demethylase (Erg11p, Cyp51p) to azole resistance in Candida albicans
    • Marichal P., Koymans L., Willemsens S., Bellens D., Verhasselt P., Luyten W., et al. Contribution of mutations in the cytochrome P450 14alpha-demethylase (Erg11p, Cyp51p) to azole resistance in Candida albicans. Microbiology 1999, 145(Pt. 10):2701-2713.
    • (1999) Microbiology , vol.145 , Issue.PART. 10 , pp. 2701-2713
    • Marichal, P.1    Koymans, L.2    Willemsens, S.3    Bellens, D.4    Verhasselt, P.5    Luyten, W.6
  • 8
    • 34248654584 scopus 로고    scopus 로고
    • Impact of changes in the target P450 CYP51 enzyme associated with altered triazole-sensitivity in fungal pathogens of cereal crops
    • Cools H.J., Fraaije B.A., Kim S.H., Lucas J.A. Impact of changes in the target P450 CYP51 enzyme associated with altered triazole-sensitivity in fungal pathogens of cereal crops. Biochem. Soc. Trans. 2006, 34:1219-1222.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1219-1222
    • Cools, H.J.1    Fraaije, B.A.2    Kim, S.H.3    Lucas, J.A.4
  • 10
    • 0029135441 scopus 로고
    • Azalanstat (RS-21607), a lanosterol 14 alpha-demethylase inhibitor with cholesterol-lowering activity
    • Burton P.M., Swinney D.C., Heller R., Dunlap B., Chiou M., Malonzo E., et al. Azalanstat (RS-21607), a lanosterol 14 alpha-demethylase inhibitor with cholesterol-lowering activity. Biochem. Pharmacol. 1995, 50:529-544.
    • (1995) Biochem. Pharmacol. , vol.50 , pp. 529-544
    • Burton, P.M.1    Swinney, D.C.2    Heller, R.3    Dunlap, B.4    Chiou, M.5    Malonzo, E.6
  • 11
    • 0025889775 scopus 로고
    • Effects of a novel lanosterol 14 alpha-demethylase inhibitor on the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in Hep G2 cells
    • Mayer R.J., Adams J.L., Bossard M.J., Berkhout T.A. Effects of a novel lanosterol 14 alpha-demethylase inhibitor on the regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in Hep G2 cells. J. Biol. Chem. 1991, 266:20070-20078.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20070-20078
    • Mayer, R.J.1    Adams, J.L.2    Bossard, M.J.3    Berkhout, T.A.4
  • 12
    • 0032940786 scopus 로고    scopus 로고
    • Lanosterol analogs: dual-action inhibitors of cholesterol biosynthesis
    • Frye L.L., Leonard D.A. Lanosterol analogs: dual-action inhibitors of cholesterol biosynthesis. Crit. Rev. Biochem. Mol. Biol. 1999, 34:123-140.
    • (1999) Crit. Rev. Biochem. Mol. Biol. , vol.34 , pp. 123-140
    • Frye, L.L.1    Leonard, D.A.2
  • 13
    • 24144472566 scopus 로고    scopus 로고
    • Dual-action hypoglycemic and hypocholesterolemic agents that inhibit glycogen phosphorylase and lanosterol demethylase
    • Harwood H.J., Petras S.F., Hoover D.J., Mankowski D.C., Soliman V.F., Sugarman E.D., et al. Dual-action hypoglycemic and hypocholesterolemic agents that inhibit glycogen phosphorylase and lanosterol demethylase. J. Lipid Res. 2005, 46:547-563.
    • (2005) J. Lipid Res. , vol.46 , pp. 547-563
    • Harwood, H.J.1    Petras, S.F.2    Hoover, D.J.3    Mankowski, D.C.4    Soliman, V.F.5    Sugarman, E.D.6
  • 15
    • 0030601099 scopus 로고    scopus 로고
    • Sterol 14-demethylase P450 activity expressed in rat gonads: contribution to the formation of mammalian meiosis-activating sterol
    • Yoshida Y., Yamashita C., Noshiro M., Fukuda M., Aoyama Y. Sterol 14-demethylase P450 activity expressed in rat gonads: contribution to the formation of mammalian meiosis-activating sterol. Biochem. Biophys. Res. Commun. 1996, 223:534-538.
    • (1996) Biochem. Biophys. Res. Commun. , vol.223 , pp. 534-538
    • Yoshida, Y.1    Yamashita, C.2    Noshiro, M.3    Fukuda, M.4    Aoyama, Y.5
  • 17
    • 0031763463 scopus 로고    scopus 로고
    • Elevated expression of lanosterol 14alpha-demethylase (CYP51) and the synthesis of oocyte meiosis-activating sterols in postmeiotic germ cells of male rats
    • Stromstedt M., Waterman M.R., Haugen T.B., Tasken K., Parvinen M., Rozman D. Elevated expression of lanosterol 14alpha-demethylase (CYP51) and the synthesis of oocyte meiosis-activating sterols in postmeiotic germ cells of male rats. Endocrinology 1998, 139:2314-2321.
    • (1998) Endocrinology , vol.139 , pp. 2314-2321
    • Stromstedt, M.1    Waterman, M.R.2    Haugen, T.B.3    Tasken, K.4    Parvinen, M.5    Rozman, D.6
  • 18
    • 1942476682 scopus 로고    scopus 로고
    • Meiosis-activating sterol promotes the metaphase I to metaphase II transition and preimplantation developmental competence of mouse oocytes maturing in vitro
    • Marin Bivens C.L., Grondahl C., Murray A., Blume T., Su Y.Q., Eppig J.J. Meiosis-activating sterol promotes the metaphase I to metaphase II transition and preimplantation developmental competence of mouse oocytes maturing in vitro. Biol. Reprod. 2004, 70:1458-1464.
    • (2004) Biol. Reprod. , vol.70 , pp. 1458-1464
    • Marin Bivens, C.L.1    Grondahl, C.2    Murray, A.3    Blume, T.4    Su, Y.Q.5    Eppig, J.J.6
  • 19
    • 18144439446 scopus 로고    scopus 로고
    • Physiology of meiosis-activating sterol: endogenous formation and mode of action
    • Grondahl C., Breinholt J., Wahl P., Murray A., Hansen T.H., Faerge I., et al. Physiology of meiosis-activating sterol: endogenous formation and mode of action. Hum. Reprod. 2003, 18:122-129.
    • (2003) Hum. Reprod. , vol.18 , pp. 122-129
    • Grondahl, C.1    Breinholt, J.2    Wahl, P.3    Murray, A.4    Hansen, T.H.5    Faerge, I.6
  • 20
    • 10744230098 scopus 로고    scopus 로고
    • A functional cytochrome P450 lanosterol 14 alpha-demethylase CYP51 enzyme in the acrosome: transport through the Golgi and synthesis of meiosis-activating sterols
    • Cotman M., Jezek D., Fon Tacer K., Frangez R., Rozman D. A functional cytochrome P450 lanosterol 14 alpha-demethylase CYP51 enzyme in the acrosome: transport through the Golgi and synthesis of meiosis-activating sterols. Endocrinology 2004, 145:1419-1426.
    • (2004) Endocrinology , vol.145 , pp. 1419-1426
    • Cotman, M.1    Jezek, D.2    Fon Tacer, K.3    Frangez, R.4    Rozman, D.5
  • 22
    • 40949139660 scopus 로고    scopus 로고
    • Oocyte maturation. Basic and clinical aspects of in vitro maturation (IVM) with special emphasis of the role of FF-MAS
    • Grondahl C. Oocyte maturation. Basic and clinical aspects of in vitro maturation (IVM) with special emphasis of the role of FF-MAS. Dan. Med. Bull. 2008, 55:1-16.
    • (2008) Dan. Med. Bull. , vol.55 , pp. 1-16
    • Grondahl, C.1
  • 23
    • 0035853108 scopus 로고    scopus 로고
    • Crystal structure of cytochrome P450 14alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors
    • Podust L.M., Poulos T.L., Waterman M.R. Crystal structure of cytochrome P450 14alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors. Proc. Natl Acad. Sci. USA 2001, 98:3068-3073.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3068-3073
    • Podust, L.M.1    Poulos, T.L.2    Waterman, M.R.3
  • 24
    • 0031767825 scopus 로고    scopus 로고
    • CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450 similar to eukaryotic CYP51
    • Aoyama Y., Horiuchi T., Gotoh O., Noshiro M., Yoshida Y. CYP51-like gene of Mycobacterium tuberculosis actually encodes a P450 similar to eukaryotic CYP51. J. Biochem. 1998, 124:694-696.
    • (1998) J. Biochem. , vol.124 , pp. 694-696
    • Aoyama, Y.1    Horiuchi, T.2    Gotoh, O.3    Noshiro, M.4    Yoshida, Y.5
  • 25
    • 34248671409 scopus 로고    scopus 로고
    • CYP121, CYP51 and associated redox systems in Mycobacterium tuberculosis: towards deconvoluting enzymology of P450 systems in a human pathogen
    • McLean K.J., Dunford A.J., Sabri M., Neeli R., Girvan H.M., Balding P.R., et al. CYP121, CYP51 and associated redox systems in Mycobacterium tuberculosis: towards deconvoluting enzymology of P450 systems in a human pathogen. Biochem. Soc. Trans. 2006, 34:1178-1182.
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1178-1182
    • McLean, K.J.1    Dunford, A.J.2    Sabri, M.3    Neeli, R.4    Girvan, H.M.5    Balding, P.R.6
  • 28
    • 0022829026 scopus 로고
    • Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14 alpha-methyl demethylase cytochrome P-450 from hepatic microsomes
    • Trzaskos J., Kawata S., Gaylor J.L. Microsomal enzymes of cholesterol biosynthesis. Purification of lanosterol 14 alpha-methyl demethylase cytochrome P-450 from hepatic microsomes. J. Biol. Chem. 1986, 261:14651-14657.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14651-14657
    • Trzaskos, J.1    Kawata, S.2    Gaylor, J.L.3
  • 29
    • 28044468385 scopus 로고    scopus 로고
    • Molecular identification of adrenal inner zone antigen as a heme-binding protein
    • Min L., Strushkevich N.V., Harnastai I.N., Iwamoto H., Gilep A.A., Takemori H., et al. Molecular identification of adrenal inner zone antigen as a heme-binding protein. FEBS J. 2005, 272:5832-5843.
    • (2005) FEBS J. , vol.272 , pp. 5832-5843
    • Min, L.1    Strushkevich, N.V.2    Harnastai, I.N.3    Iwamoto, H.4    Gilep, A.A.5    Takemori, H.6
  • 30
    • 57749085501 scopus 로고    scopus 로고
    • PGRMC1 (progesterone receptor membrane component 1): a targetable protein with multiple functions in steroid signaling, P450 activation and drug binding
    • Rohe H.J., Ahmed I.S., Twist K.E., Craven R.J. PGRMC1 (progesterone receptor membrane component 1): a targetable protein with multiple functions in steroid signaling, P450 activation and drug binding. Pharmacol. Ther. 2009, 121:14-19.
    • (2009) Pharmacol. Ther. , vol.121 , pp. 14-19
    • Rohe, H.J.1    Ahmed, I.S.2    Twist, K.E.3    Craven, R.J.4
  • 31
    • 47649089787 scopus 로고    scopus 로고
    • Structural biology and biochemistry of cytochrome P450 systems in Mycobacterium tuberculosis
    • McLean K.J., Munro A.W. Structural biology and biochemistry of cytochrome P450 systems in Mycobacterium tuberculosis. Drug Metab. Rev. 2008, 40:427-446.
    • (2008) Drug Metab. Rev. , vol.40 , pp. 427-446
    • McLean, K.J.1    Munro, A.W.2
  • 32
    • 41949110521 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis CYP130: crystal structure, biophysical characterization, and interactions with antifungal azole drugs
    • Ouellet H., Podust L.M., de Montellano P.R. Mycobacterium tuberculosis CYP130: crystal structure, biophysical characterization, and interactions with antifungal azole drugs. J. Biol. Chem. 2008, 283:5069-5080.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5069-5080
    • Ouellet, H.1    Podust, L.M.2    de Montellano, P.R.3
  • 33
    • 0041664878 scopus 로고    scopus 로고
    • Conservation in the CYP51 family. Role of the B′ helix/BC loop and helices F and G in enzymatic function
    • Lepesheva G.I., Virus C., Waterman M.R. Conservation in the CYP51 family. Role of the B′ helix/BC loop and helices F and G in enzymatic function. Biochemistry 2003, 42:9091-9101.
    • (2003) Biochemistry , vol.42 , pp. 9091-9101
    • Lepesheva, G.I.1    Virus, C.2    Waterman, M.R.3
  • 34
    • 15744377346 scopus 로고    scopus 로고
    • Fluconazole binding and sterol demethylation in three CYP51 isoforms indicate differences in active site topology
    • Bellamine A., Lepesheva G.I., Waterman M.R. Fluconazole binding and sterol demethylation in three CYP51 isoforms indicate differences in active site topology. J. Lipid Res. 2004, 45:2000-2007.
    • (2004) J. Lipid Res. , vol.45 , pp. 2000-2007
    • Bellamine, A.1    Lepesheva, G.I.2    Waterman, M.R.3
  • 36
    • 33748802003 scopus 로고    scopus 로고
    • Structural basis for ligand promiscuity in cytochrome P450 3A4
    • Ekroos M., Sjogren T. Structural basis for ligand promiscuity in cytochrome P450 3A4. Proc. Natl Acad Sci. USA 2006, 103:13682-13687.
    • (2006) Proc. Natl Acad Sci. USA , vol.103 , pp. 13682-13687
    • Ekroos, M.1    Sjogren, T.2
  • 37
    • 0035800617 scopus 로고    scopus 로고
    • Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF
    • Cupp-Vickery J.R., Garcia C., Hofacre A., McGee-Estrada K. Ketoconazole-induced conformational changes in the active site of cytochrome P450eryF. J. Mol. Biol. 2001, 311:101-110.
    • (2001) J. Mol. Biol. , vol.311 , pp. 101-110
    • Cupp-Vickery, J.R.1    Garcia, C.2    Hofacre, A.3    McGee-Estrada, K.4
  • 38
    • 33645639221 scopus 로고    scopus 로고
    • CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B′ helix defines substrate preferences of sterol 14alpha-demethylase
    • Lepesheva G.I., Zaitseva N.G., Nes W.D., Zhou W., Arase M., Liu J., et al. CYP51 from Trypanosoma cruzi: a phyla-specific residue in the B′ helix defines substrate preferences of sterol 14alpha-demethylase. J. Biol. Chem. 2006, 281:3577-3585.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3577-3585
    • Lepesheva, G.I.1    Zaitseva, N.G.2    Nes, W.D.3    Zhou, W.4    Arase, M.5    Liu, J.6
  • 39
    • 17144372582 scopus 로고    scopus 로고
    • Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation
    • Powl A.M., East J.M., Lee A.G. Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation. Biochemistry 2005, 44:5873-5883.
    • (2005) Biochemistry , vol.44 , pp. 5873-5883
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 40
    • 67650732710 scopus 로고    scopus 로고
    • Lipid-dependent membrane protein topogenesis
    • Dowhan W., Bogdanov M. Lipid-dependent membrane protein topogenesis. Annu. Rev. Biochem. 2009, 78:515-540.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 515-540
    • Dowhan, W.1    Bogdanov, M.2
  • 41
    • 0025059797 scopus 로고
    • The role of charged amino acids in the localization of secreted and membrane proteins
    • Boyd D., Beckwith J. The role of charged amino acids in the localization of secreted and membrane proteins. Cell 1990, 62:1031-1033.
    • (1990) Cell , vol.62 , pp. 1031-1033
    • Boyd, D.1    Beckwith, J.2
  • 42
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity
    • Williams P.A., Cosme J., Sridhar V., Johnson E.F., McRee D.E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell 2000, 5:121-131.
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 44
    • 47749117627 scopus 로고    scopus 로고
    • Crystal structures of substrate-bound and substrate-free cytochrome P450 46A1, the principal cholesterol hydroxylase in the brain
    • Mast N., White M.A., Bjorkhem I., Johnson E.F., Stout C.D., Pikuleva I.A. Crystal structures of substrate-bound and substrate-free cytochrome P450 46A1, the principal cholesterol hydroxylase in the brain. Proc. Natl Acad Sci. USA 2008, 105:9546-9551.
    • (2008) Proc. Natl Acad Sci. USA , vol.105 , pp. 9546-9551
    • Mast, N.1    White, M.A.2    Bjorkhem, I.3    Johnson, E.F.4    Stout, C.D.5    Pikuleva, I.A.6
  • 45
    • 58149339806 scopus 로고    scopus 로고
    • Structural basis for androgen specificity and oestrogen synthesis in human aromatase
    • Ghosh D., Griswold J., Erman M., Pangborn W. Structural basis for androgen specificity and oestrogen synthesis in human aromatase. Nature 2009, 457:219-223.
    • (2009) Nature , vol.457 , pp. 219-223
    • Ghosh, D.1    Griswold, J.2    Erman, M.3    Pangborn, W.4
  • 46
    • 76249100348 scopus 로고    scopus 로고
    • Crystal structures of Trypanosoma brucei sterol 14 alpha-demethylase and implications for selective treatment of human infections
    • Lepesheva G.I., Park H.W., Hargrove T.Y., Vanhollebeke B., Wawrzak Z., Harp J.M., et al. Crystal structures of Trypanosoma brucei sterol 14 alpha-demethylase and implications for selective treatment of human infections. J. Biol. Chem. 2010, 285:1773-1780.
    • (2010) J. Biol. Chem. , vol.285 , pp. 1773-1780
    • Lepesheva, G.I.1    Park, H.W.2    Hargrove, T.Y.3    Vanhollebeke, B.4    Wawrzak, Z.5    Harp, J.M.6
  • 47
    • 0031106366 scopus 로고    scopus 로고
    • Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus
    • von Wachenfeldt C., Richardson T.H., Cosme J., Johnson E.F. Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus. Arch. Biochem. Biophys. 1997, 339:107-114.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 107-114
    • von Wachenfeldt, C.1    Richardson, T.H.2    Cosme, J.3    Johnson, E.F.4
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collection in oscillation mode
    • Otwinovski Z. Processing of X-ray diffraction data collection in oscillation mode. Methods. Enzymol. 1997, 276:307-326.
    • (1997) Methods. Enzymol. , vol.276 , pp. 307-326
    • Otwinovski, Z.1
  • 49
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 1997, 30:1022-1025.
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 50
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 1991, 47(Pt. 2):110-119.
    • (1991) Acta Crystallogr. A. , vol.47 , Issue.PART. 2 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 52
    • 3242750661 scopus 로고    scopus 로고
    • Quantitation of lanosterol and its major metabolite FF-MAS in an inhibition assay of CYP51 by azoles with atmospheric pressure photoionization based LC-MS/MS
    • Trosken E.R., Straube E., Lutz W.K., Volkel W., Patten C. Quantitation of lanosterol and its major metabolite FF-MAS in an inhibition assay of CYP51 by azoles with atmospheric pressure photoionization based LC-MS/MS. J. Am. Soc. Mass. Spectrom. 2004, 15:1216-1221.
    • (2004) J. Am. Soc. Mass. Spectrom. , vol.15 , pp. 1216-1221
    • Trosken, E.R.1    Straube, E.2    Lutz, W.K.3    Volkel, W.4    Patten, C.5


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