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Volumn 14, Issue 4, 2001, Pages 338-347

Allosteric behavior in cytochrome P450-dependent in vitro drug-drug interactions: A prospective based on conformational dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE; CYTOCHROME P450; NIFEDIPINE; TESTOSTERONE;

EID: 0035059352     PISSN: 0893228X     EISSN: None     Source Type: Journal    
DOI: 10.1021/tx0002132     Document Type: Review
Times cited : (98)

References (9)
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    • The human hepatic cytochromes P450 involved in drug metabolism
    • Wrighton, S. A., and Stevens, J. C. (1992) The human hepatic cytochromes P450 involved in drug metabolism. Crit. Rev. Toxicol. 22, 1-21.
    • (1992) Crit. Rev. Toxicol. , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 4
    • 0032924934 scopus 로고    scopus 로고
    • Cytochrome P450 3A4: Regulation and role in drug metabolism
    • Guengerich, F. P. (1999) Cytochrome P450 3A4: Regulation and role in drug metabolism. Anna. Rev. Pharmacol. Toxicol. 39, 1-17.
    • (1999) Anna. Rev. Pharmacol. Toxicol. , vol.39 , pp. 1-17
    • Guengerich, F.P.1
  • 5
    • 0028307539 scopus 로고
    • Activation of P4503A4: Evidence for the simultaneous binding of two substrates in a Cytochrome P450 active site
    • Shou, M., Grogan, J., Mancewicz, J. A., Krausz, K. W., Gonzalez, F. J., Gelboin, H. V., and Korzekwa, K. R. (1994) Activation of P4503A4: evidence for the simultaneous binding of two substrates in a Cytochrome P450 active site. Biochemistry 33, 6450.
    • (1994) Biochemistry , vol.33 , pp. 6450
    • Shou, M.1    Grogan, J.2    Mancewicz, J.A.3    Krausz, K.W.4    Gonzalez, F.J.5    Gelboin, H.V.6    Korzekwa, K.R.7
  • 6
    • 0032499691 scopus 로고    scopus 로고
    • Analysis of human Cytochrome P450 3A4 cooperativity: Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics
    • Harlow, G. R., and Halpert, J. R. (1998) Analysis of human Cytochrome P450 3A4 cooperativity: Construction and characterization of a site-directed mutant that displays hyperbolic steroid hydroxylation kinetics. Proc. Natl. Acad. Sci. U.S.A. 95, 6636-6641.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6636-6641
    • Harlow, G.R.1    Halpert, J.R.2
  • 8
    • 0029805701 scopus 로고    scopus 로고
    • Molecular modelling of P4503A4 from an alignment with P450102: Identification of key interactions between putative active site residues and P4503A-specific chemicals
    • Lewis, D. F., Eddershaw, P. J., Goldfarb, P. S., and Tarbet, M. H. (1996) Molecular modelling of P4503A4 from an alignment with P450102: identification of key interactions between putative active site residues and P4503A-specific chemicals. Xenobiotica 26, 1067-1086.
    • (1996) Xenobiotica , vol.26 , pp. 1067-1086
    • Lewis, D.F.1    Eddershaw, P.J.2    Goldfarb, P.S.3    Tarbet, M.H.4
  • 9
    • 0033970047 scopus 로고    scopus 로고
    • Mamalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., and McRee, D. E. (2000) Mamalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol. Cell 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.