Journal ArticleDOI
The Redox Potential of Selenocystine in Unconstrained Cyclic Peptides
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This article is published in Angewandte Chemie.The article was published on 1997-05-02. It has received 122 citations till now. The article focuses on the topics: Redox & Cyclic peptide.read more
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Chemistry of biologically important synthetic organoselenium compounds.
Journal ArticleDOI
Reversible inactivation of the tumor suppressor PTEN by H2O2.
TL;DR: The results suggest that the reversible inactivation of PTEN by H2O2 might be important for the accumulation of 3′-phosphorylated phosphoinositides and that the uncontrolled generation of H 2O2 associated with certain pathological conditions might contribute to cell proliferation by inhibiting PTEN function.
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Selenium metabolism, selenoproteins and mechanisms of cancer prevention: complexities with thioredoxin reductase
TL;DR: A novel chemopreventive mechanism is proposed involving Se catalysis of reversible cysteine/disulfide transformations that occur in a number of redox-regulated proteins, including transcription factors, which would allow normalization of critical cellular processes in the early stages of transformation.
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Why Nature Chose Selenium
Hans J. Reich,Robert J. Hondal +1 more
TL;DR: A point-by-point comparison of the chemistry of selenium with the atom it replaces in biology, sulfur, shows that redox chemistry is the largest chemical difference between the two chalcogens.
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Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence
TL;DR: Mammalian thioredoxin reductases (TrxR) are homodimers, homologous to glutathione reductase (GR), with an essential selenocysteine residue in an extension containing the conserved C-terminal sequence -Gly-Cys-Se Cys-Gly, compatible with known enzyme activities and the effects of inhibitors.