• Publications
  • Influence
Ketoconazole: a potent inhibitor of cytochrome P-450-dependent drug metabolism in rat liver.
  • J. Sheets, J. Mason
  • Chemistry, Medicine
  • Drug metabolism and disposition: the biological…
  • 1 September 1984
Ketoconazole, an orally active imidazole antimycotic agent, is shown to be a potent inhibitor of drug N-demethylase activities of liver microsomes from rats pretreated with phenobarbital orExpand
  • 115
  • 2
Imidazole antimycotics: inhibitors of steroid aromatase.
Miconazole and clotrimazole, members of a class of imidazole agents which have broad spectrum antimycotic activity, were shown to be potent inhibitors of steroid aromatase activity of human placentalExpand
  • 129
  • 2
Inhibition of rat liver microsomal cytochrome P-450 steroid hydroxylase reactions by imidazole antimycotic agents.
The imidazole antimycotic agents ketoconazole, miconazole and clotrimazole were tested for their abilities to inhibit the reactions involved in the oxidative metabolism of androst-4-ene-3,17-dione byExpand
  • 98
  • 2
Proximity of the substrate binding site and the heme-iron catalytic site in cytochrome P-450scc.
  • J. Sheets, L. Vickery
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1 October 1982
As an approach to "mapping" the active site of the cytochrome P-450 that catalyzes cholesterol side-chain cleavage, designated cytochrome P-450scc, we have synthesized steroid derivatives with theExpand
  • 23
Active site-directed inhibitors of cytochrome P-450scc. Structural and mechanistic implications of a side chain-substituted series of amino-steroids.
A series of analogues of cholesterol, each having a shortened side chain and a primary amine group, were prepared and tested for their effects on bovine adrenocortical cholesterol side chain cleavageExpand
  • 23
C-22-substituted steroid derivatives as substrate analogues and inhibitors of cytochrome P-450scc.
Spectral and kinetic studies are reported for the effects of C-22-substituted steroids on purified bovine adrenocortical cytochrome P-450scc. The results are consistent with the recent proposal thatExpand
  • 16
Inhibition of Steroidogenesis in Cultured Leydig Tumor Cells by 22-Amino-23,24-Bisnor-5-Cholen-3β-Ol and (20R)20-Phenyl-5-Pregnene-3β,20-Diol
Using the cholesterol side-chain cleavage enzyme purified from bovine adrenals, we have previously shown that 22-amino-23,24-bisnor-5-cholen-3-α-ol (22-ABC) and (20R)20-phenyl-5-pregnene-3α,20 diolExpand
  • 9
Multiple sites of steroid hydroxylation by the liver microsomal cytochrome P-450 system: primary and secondary metabolism of androstenedione.
To investigate the potential interaction of the various pathways of androgen hydroxylation, we have conducted studies to identify the profile of products formed during the time course of metabolismExpand
  • 23
Discriminatory inhibition of adrenocortical 17 alpha-hydroxylase activity by inhibitors of cholesterol side chain cleavage cytochrome P-450.
Two inhibitors of the cholesterol side chain cleavage reaction were tested for their ability to inhibit bovine adrenocortical 17 alpha-hydroxylase and 21-hydroxylase activities. One inhibitor,Expand
  • 10
Amino-steroids as inhibitors and probes of the active site of cytochrome P-450scc. Effects on the enzyme from different sources.
A series of analogues of cholesterol, each having a primary amine attached to a shortened side chain, were tested for their effects on cytochrome P-450scc from several different sources.Expand
  • 10