메뉴 건너뛰기
Drug Discovery Today
Volumn 9, Issue 15, 2004, Pages 636-637
The impact of cytochrome P450 allosterism on pharmacokinetics and drug-drug interactions
Author keywords

CYP isoforms; Drug Discovery; effector molecule; in vitro in vivo correlation; new chemical entities; Pharmaceutical Science; substrate
Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 3A4;
EID: 3242789326     PISSN: 13596446     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-6446(04)03132-0     Document Type: Note
Times cited : (9)
References (7)
  • 1
    • 2442626615 scopus 로고    scopus 로고
    • Implications of the allosteric kinetics of cytochrome P450s
    • Atkins W.M. Implications of the allosteric kinetics of cytochrome P450s. Drug Discov. Today. 9:2004;478-484
    • (2004) Drug Discov. Today , vol.9 , pp. 478-484
    • Atkins, W.M.1
  • 2
    • 0000574406 scopus 로고    scopus 로고
    • Evaluation of atypical cytochrome P450 kinetics with two-substrate models: Evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites
    • Korzekwa K.R., et al. Evaluation of atypical cytochrome P450 kinetics with two-substrate models: evidence that multiple substrates can simultaneously bind to cytochrome P450 active sites. Biochemistry. 37:1998;4137-4147
    • (1998) Biochemistry , vol.37 , pp. 4137-4147
    • Korzekwa, K.R.1
  • 3
    • 0035910579 scopus 로고    scopus 로고
    • A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4
    • Shou M., et al. A kinetic model for the metabolic interaction of two substrates at the active site of cytochrome P450 3A4. J. Biol. Chem. 276:2001;2256-2262
    • (2001) J. Biol. Chem. , vol.276 , pp. 2256-2262
    • Shou, M.1
  • 4
    • 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., Halpert J.R. 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. 95:1998;6636-6641
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6636-6641
    • Harlow, G.R.1    Halpert, J.R.2
  • 5
    • 0037031876 scopus 로고    scopus 로고
    • Is there a toxicological advantage for non-hyperbolic kinetics in cytochrome P450 catalysis? Functional allostery from 'distributive catalysis'
    • Atkins W.M., et al. Is there a toxicological advantage for non-hyperbolic kinetics in cytochrome P450 catalysis? Functional allostery from 'distributive catalysis'. J. Biol. Chem. 277:2002;33258-33266
    • (2002) J. Biol. Chem. , vol.277 , pp. 33258-33266
    • Atkins, W.M.1
  • 6
    • 0034105896 scopus 로고    scopus 로고
    • In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model
    • Houston J.B., Kenworthy K.E. In vitro-in vivo scaling of CYP kinetic data not consistent with the classical Michaelis-Menten model. Drug Metab. Dispos. 28:2000;246-254
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 246-254
    • Houston, J.B.1    Kenworthy, K.E.2
  • 7
    • 0034093628 scopus 로고    scopus 로고
    • Human cytochrome P-450 3A4: In vitro drug-drug interaction patterns are substrate-dependent
    • Wang R.W., et al. Human cytochrome P-450 3A4: in vitro drug-drug interaction patterns are substrate-dependent. Drug Metab. Disp. 28:2000;360-366
    • (2000) Drug Metab. Disp. , vol.28 , pp. 360-366
    • Wang, R.W.1

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.