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In vitro proguanil activation to cycloguanil by human liver microsomes is mediated by CYP3A isoforms as well as by S‐mephenytoin hydroxylase.

Data up to Jan 2025

Published1994
Citations84
References26

Total Citations Per Year

Abstract

References (26)

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1990 • 169 citations

The activation of the biguanide antimalarial proguanil co‐segregates with the mephenytoin oxidation polymorphism‐a panel study.

1991 • 162 citations

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1990 • 129 citations

Relationship between phenytoin and tolbutamide hydroxylations in human liver microsomes.

1991 • 111 citations

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1992 • 95 citations

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1990 • 85 citations

In vitro metabolism of the biguanide antimalarials in human liver microsomes: evidence for a role of the mephenytoin hydroxylase (P450 MP) enzyme.

1990 • 67 citations

High-performance liquid chromatographic assay for 4-nitrophenol hydroxylation, a putative cytochrome P-4502E1 activity, in human liver microsomes

1993 • 67 citations

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1987 • 63 citations

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1985 • 54 citations

Inter‐subject variability in the metabolism of proguanil to the active metabolite cycloguanil in man.

1989 • 53 citations

Variability in the metabolism of proguanil to the active metabolite cycloguanil in healthy Kenyan adults

1990 • 53 citations

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1991 • 43 citations

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1987 • 38 citations

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1986 • 37 citations

Relation between chloroguanide bioactivation to cycloguanil and the genetically determined metabolism of mephenytoin in humans

1992 • 28 citations

Mephenytoin-type polymorphism of drug oxidation: purification and characterization of a human liver cytochrome P-450 isozyme catalyzing microsomal mephenytoin hydroxylation

1986 • 27 citations

Steady-State Kinetics of Proguanil and Its Active Metabolite, Cycloguanil, in Man

1988 • 18 citations

Deleted Work

1955 • 0 citations

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In vitro proguanil activation to cycloguanil by human liver microsomes is mediated by… (1994) – British Journal of Clinical Pharmacology | Metascience Observatory Explorer