F
Franz Oesch
Researcher at University of Mainz
Publications - 580
Citations - 22320
Franz Oesch is an academic researcher from University of Mainz. The author has contributed to research in topics: Epoxide hydrolase & Microsomal epoxide hydrolase. The author has an hindex of 76, co-authored 578 publications receiving 21684 citations. Previous affiliations of Franz Oesch include University of Basel & National Institutes of Health.
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Regio- and stereoselective regulation of monooxygenase activities by isoenzyme-selective phosphorylation of cytochrome P450.
Barbara Bartlomowicz,Thomas Friedberg,Dietmar Utesch,Elvira Molitor,Karl-Ludwig Platt,Franz Oesch +5 more
TL;DR: Isoenzyme-selective phosphorylation of cytochrome P450 leads to a corresponding isoenzyme -selective modulation of monooxygenase activity which holds promise to be especially important as a fast regulation of the control of genotoxic metabolites.
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First evidence of cytochrome P-450 induction in the mouse brain by phenytoin
TL;DR: The cerebellar tissue was shown to be distinguished by a 15-fold enhancement of cytochrome P-450 PB3a activity, that means twice the extent of that found in liver and cerebrum.
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Mutagenicity of structurally related oxiranes derivatives of benzene and its hydrogenated congeners
TL;DR: The mutagenicities of 17 closely related oxiranes were determined in 4 tester strains and the influence of bromo and hydroxyl substitution on oxirane mutagenicity is discussed.
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Detoxification of optically active bay- and fjord-region polycyclic aromatic hydrocarbon dihydrodiol epoxides by human glutathione transferase P1-1 expressed in Chinese hamster V79 cells.
A. Seidel,Thomas Friedberg,Bettina Löllmann,A Schwierzok,Mario Funk,Heinz Frank,Romy Holler,Franz Oesch,Hansruedi Glatt +8 more
TL;DR: This study demonstrates that differences in the caalytic activity seen for purified GST towards individual mutagens do not necessarily reflect the detoxification of DEs by the same enzyme in a living cell and provides further evidence that specific human GSTs play a role in the detoxifying ofDEs of PAHs.
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A fluorometric assay for quantitating phenol sulfotransferase activities in homogenates of cells and tissues.
TL;DR: A comparison to another widely used method is given to point out the advantages provided by the new procedure and results clearly indicate the superiority of the new method.