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Cited by 605

The DOI matches its Crossref record.

Cytochrome P450 inhibitors. Evaluation of specificities in the in vitrometabolism of therapeutic agents by human liver microsomes.

Newton, D J, Wang, R W, Lu, A Y·1995·Drug Metabolism and Disposition
DOI 10.1016/s0090-9556(25)06500-6
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Abstract

Identifying selective inhibitors of cytochrome P450 isoforms is a useful tool in defining the role of individual cytochrome P450s in the metabolism process. In this study, nine chemical inhibitors were selected based on literature data and were examined for their specificity toward cytochrome P450-mediated reactions in human liver microsomes. Furafylline was a potent, mechanism-based inhibitor for CYP1A2-mediated phenacetin O-deethylation. The probes sulfaphenazole (CYP2C9) and quinidine (CYP2D6) selectively inhibited tolbutamide methylhydroxylation and bufuralol 1'-hydroxylation, respectively. Additionally, the CYP2E1-catalyzed chlorzoxazone 6-hydroxylation was significantly inhibited by diethyldithiocarbamate. Of the CYP3A4 inhibitor probes used, troleandomycin proved to be the most specific for testosterone 6 beta-hydroxylation.

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Metadata

Authors
Newton, D. J., Wang, R. W., & Lu, A. Y.
Venue
Drug Metabolism and Disposition
Publisher
Elsevier BV
Published
1995-01
Volume
23
Issue
1
Pages
154-158
ISSN
0090-9556 (ISSN-L)
DOI
10.1016/s0090-9556(25)06500-6
OpenAlex
W1765706822
Cited by
605
References
0
FWCI
38.63
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.