B
B.K. Park
Researcher at University of Liverpool
Publications - 194
Citations - 9088
B.K. Park is an academic researcher from University of Liverpool. The author has contributed to research in topics: Metabolite & Microsome. The author has an hindex of 55, co-authored 192 publications receiving 8716 citations. Previous affiliations of B.K. Park include University of Bern & Western Infirmary.
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Journal ArticleDOI
Association analysis of drug metabolizing enzyme gene polymorphisms in HIV-positive patients with co-trimoxazole hypersensitivity.
Munir Pirmohamed,Ana Alfirevic,Javier Vilar,Anne C. Stalford,Edmund Wilkins,E. Sim,B.K. Park +6 more
TL;DR: The results show that genetic polymorphisms in drug metabolizing enzymes are unlikely to be major predisposing factors in determining individual susceptibility to co-trimoxazole hypersensitivity in HIV-positive patients.
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Stereoselective interaction between the R enantiomer of warfarin and cimetidine.
TL;DR: The stereoselectivity of the pharmacokinetic interaction between warfarin and cimetidine was investigated in eight healthy volunteers and resulted in elevation of vitamin K1 2,3-epoxide concentrations, which were similar in each case.
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Genetic analysis of microsomal epoxide hydrolase in patients with carbamazepine hypersensitivity
V J Green,Munir Pirmohamed,Neil R. Kitteringham,A Gaedigk,Denis M. Grant,M Boxer,Brian Burchell,B.K. Park +7 more
TL;DR: The results of this study suggest that a single mutation within the coding region of the microsomal epoxide hydrolase gene cannot be the sole determinant of the predisposition to carbamazepine hypersensitivity.
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The effect of enzyme inhibition on the metabolism and activation of tacrine by human liver microsomes
TL;DR: Using cytochrome P450 isoform specific inhibitors CYP1A2 was identified as the major enzyme involved in all routes of THA metabolism and may provide a useful tool for examining the relationship between the metabolism and toxicity of ThA in vivo.
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Dexamethasone metabolism in vitro: Species differences
TL;DR: The inhibition of 6-hydroxylation (CYP3A) by ketoconazole was variable, and indicates that ketconazole cannot be regarded as a selective inhibitor of CYP3A proteins in all species.