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Differential selectivity of cytochrome P450 inhibitors against probe substrates in human and rat liver microsomes
British Journal of Clinical Pharmacology · 1998 · Vol. 45(2) · pp. 107–114
Victoria A. Eagling✉(University of Liverpool)John Tjia(University of Liverpool)David Back(University of Liverpool)
Abstract
It is evident that CYP inhibitors do not exhibit the same selectivity in human and rat liver microsomes. This is due to differential selectivity of the inhibitors and/or differences in the CYP isoform responsible for metabolism in the different species.
Pharmacogenetics and Drug MetabolismDrug Transport and Resistance MechanismsDrug-Induced Hepatotoxicity and ProtectionChlorzoxazoneTolbutamideCYP1A2MicrosomePhenacetinChemistryHydroxylationCYP3A4Cytochrome P450CYP2E1
MeSH terms
AnimalsChlorzoxazoneCytochrome P-450 Enzyme SystemDitiocarbEnzyme InhibitorsHumansKetoconazoleKineticsMaleMicrosomes, LiverPhenacetinSubstrate SpecificitySulfaphenazoleTestosteroneTheophylline
Citations
334
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19.97
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38
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100%
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References
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Journal of Biological Chemistry · 1951 · 317,666 citations
Purification and characterization of liver microsomal cytochromes P-450: electrophoretic, spectral, catalytic, and immunochemical properties and inducibility of eight isozymes isolated from rats treated with phenobarbital or .beta.-naphthoflavone
Biochemistry · 1982 · 1,017 citations
Interindividual variations in human liver cytochrome P-450 enzymes involved in the oxidation of drugs, carcinogens and toxic chemicals: studies with liver microsomes of 30 Japanese and 30 Caucasians.
Journal of Pharmacology and Experimental Therapeutics · 1994 · 2,779 citations
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