Studies were performed to determine the human enzymes responsible for the biotransformation
of atomoxetine to its major metabolite, 4-hydroxyatomoxetine, and to a minor metabolite,…

Previous studies in this laboratory have determined the lack of specificity of several antibody
and substrate probes of CYP2B6. The goals of the current study were to examine the …

The interaction of competitive type inhibitors with the active site of cytochrome P450 (CYP)
2C9 has been predicted using three- and four-dimensional quantitative structure activity …

The formation of R- andS-norfluoxetine was analyzed in vitro in human liver microsomes.
Low apparent K m values forR-norfluoxetine formation of ≤8 μM andS-norfluoxetine of <0.2 …

The program Catalyst was used to build three-dimensional quantitative structure activity
relationship (3D-QSAR) pharmacophore models of the structural features common to competitive…

To begin to build an understanding of the interactions of CYP2B6 with substrates, two
different 3-dimensional quantitative structure activity relationship (3D-QSAR) models were …

Three-and four-dimensional quantitative structure activity relationship (3D/4D-QSAR)
pharmacophore models of competitive inhibitors of CYP2D6 were constructed using data from our …

In the studies reported here, the ability of atomoxetine hydrochloride (Strattera) to inhibit or
induce the metabolic capabilities of selected human isoforms of cytochrome P450 was …

Precision-cut human liver slices are an important tool for defining the metabolism and
hepatotoxicity of drug candidates early in development. Because of the frequent use of this in …

Studies were performed to determine the cytochromes P450 (P450) responsible for the
biotransformation of (S)-13[(dimethylamino)methyl]-10,11,14,15-tetrahydro-4,9:16,21-dimetheno-…