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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Mutagenicity of 43 structurally related heterocyclic compounds and its relationship to their carcinogenicity
TL;DR: It is suggested that the complexity of the metabolism of these heterocyclic compounds may lead to critical differences in metabolism in mouse subcutaneous tissue in vivo and in liver homogenates from rats treated with Aroclor, leading to a higher proportion of metabolism in the liver.
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Endogenous role of epoxide-hydratase. Development of a steroid epoxide-hydratase assay and properties of the enzyme.
TL;DR: A highly sensitive and rapid radiometric assay for the determination of specific epoxide hydratase activity with a steroid epoxide (16α, 17α-epoxy-1,3,5(10)-estratrien-3,16,17-triol, ‘estroxide’) has been developed.
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Glycolaldehyde causes DNA-protein crosslinks: a new aspect of ethylene oxide genotoxicity
TL;DR: DNA crosslinks, for which evidence was found in mononuclear blood cells of humans occupationally exposed to Ethylene oxide, are possibly generated by glycolaldehyde, a putative intermediate in the metabolism of ethylene oxide to glycolic acid.
Endogenous Role of Microsomal Epoxide Hydrolase Ontogenesis, Induction, lnhibition, Tissue Distribution, Immunological Behaviour and Purification of Microsomal Epoxide Hydrolase with 164 7a-Epoxyandrostene-3-one as Substrate
TL;DR: The specific activities of microsomal epoxide hydrolase with androstene oxide as substrate were measured in various metabolically important and in various steroidogenic organs of the male and female rat and compared with the activities of 16 alpha, 17 alpha-epoxyestratrienol (estroxide) and benzo[a]pyrene 4,5-oxide.
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Selective detection of mRNA forms encoding the major phenobarbital inducible cytochromes P450 and other members of the P450IIB family by the RNAse A protection assay
TL;DR: The results strongly support earlier studies on the tissue specific expression of these enzymes, which had used oligomer probes, and detected the constitutive hepatic expression of a P450IIB gene which was distinct from P 450IIB1 and IIB2.