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Titlebook: Biological Reactive Intermediates V; Basic Mechanistic Re Robert Snyder,I. Glenn Sipes,Charlotte M. Witmer Book 1996 The Editor(s) (if appl

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Akrodermatitis atrophicans chronica (,),ene oxides as electrophilic reactive metabolites. Much less was known until very recently about the metabolic oxidative activation of thiophene derivatives (Rance, 1989). A first report on the metabolism of thiophene itself in rats has shown the formation of thiophene-derived mercapturates in urine
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Pathologische Anatomie der Tuberkulose,ymes are also the major ones involved in the oxidation of potential toxicants and carcinogens such as those encountered among pollutants, solvents, and pesticides, as well as many natural products. A proper understanding of the basic mechanisms by which the P450 enzymes oxidize such compounds is imp
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,Acardiacus, Acardius, herzlose Mißgeburt,iety of physiological and pathophysiological processes [22]. Despite of its function in the control of blood pressure, platelet aggregation and neurotransmission, which are mediated via the activation of the soluble guanylate cyclase, ·NO has been shown to be a potent modulator of the cytotoxic acti
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Muskelrelaxation bei alten Menschen,r, and the rearrangement product chloroacetaldehyde give rise to the etheno (ε) DNA adducts. This type of modified DNA bases appears to be the molecular basis for the genotoxic effects of the parent compound, and site specific mutagenesis studies (Basu et al., 1993) show its mutagenicity. There is e
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E. Lüllwitz,U. Dybus,S. Piepenbrockryonic development of all multicellular organisms and also in the adult when various cytokines and hormones exert highly inducer-specific influences on genes. The naturally occurring regulating agents interact with specific receptors: e.g., the retinoids, vitamin D3, thyroid hormones and the steroid
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Muskelrelaxanzien und Leberinsuffizienz,DNA binding activity of Fos and Jun is regulated . by a posttranslational mechanism involving reduction-oxidation. Redox regulation is mediated through a conserved cysteine residue located in the DNA binding domain of both proteins. Oxidation or chemical modification of the cysteine has an inhibitor
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