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Selenoproteins and Cancer Prevention
Annual Review of Nutrition, 2012The discovery of multiple selenoproteins has raised tantalizing questions about their role in maintaining normal cellular function. Unfortunately, many of these remain inadequately investigated. While they have a role in maintaining redox balance, other functions are becoming increasingly recognized.
Cindy D, Davis +2 more
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Natural and synthetic selenoproteins
Current Opinion in Chemical Biology, 2014Once considered highly toxic, the element selenium is now recognized as a micronutrient essential for human health. It is inserted co-translationally into many proteins as the non-canonical amino acid selenocysteine, providing the resulting selenoprotein molecules with a range of valuable redox properties; selenocysteine is also increasingly exploited ...
Metanis N, Hilvert D
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Antioxidants & Redox Signaling, 2015
Significance: Selenoproteins employ selenium to supplement the chemistry available through the common 20 amino acids. These powerful enzymes are affiliated with redox biology, often in connection with the detection, management, and signaling of oxidative stress.
Jun, Liu, Sharon, Rozovsky
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Significance: Selenoproteins employ selenium to supplement the chemistry available through the common 20 amino acids. These powerful enzymes are affiliated with redox biology, often in connection with the detection, management, and signaling of oxidative stress.
Jun, Liu, Sharon, Rozovsky
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Selenoproteins and the aging brain
Mechanisms of Ageing and Development, 2010Selenium (Se) is an essential trace mineral mediating its biological function primarily through selenoproteins. Accumulated lines of evidence indicate important roles of selenoproteins in the maintenance of optimal brain functions via redox regulation.
Shu, Zhang +2 more
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Selenocysteine and selenoproteins
2004Selenium occurs normally in living things as a highly specific component of certain enzymes and amino acid transfer nucleic acids (tRNAs). In bacteria, biosynthesis of essential selenoenzymes has been shown to be unaffected by wide variations in sulfur levels.
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Selenoprotein synthesis in archaea
BioFactors, 2001AbstractThe availability of the genome sequences from several archaea has facilitated the identification of the encoded selenoproteins and also of most of the components of the machinery for selenocysteine biosynthesis and insertion. Until now, selenoproteins have been identified solely in species of the genera Methanococcus (M.) and Methanopyrus ...
M, Rother +3 more
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Selenoproteins and maternal nutrition
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2008Selenium (Se) is an essential trace element of fundamental importance to health due to its antioxidant, anti-inflammatory and chemopreventive properties attributed to its presence within at least 25 selenoproteins (Sel). Sel include but not limited to glutathione peroxidases (GPx1-GPx6), thioredoxin reductases (TrxR1-TrxR3), iodothyronine deiodinases ...
A C, Pappas +3 more
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Update on Selenoprotein Biosynthesis
Antioxidants & Redox Signaling, 2015Significance: Selenium is an essential trace element that is incorporated in the small but vital family of proteins, namely the selenoproteins, as the selenocysteine amino acid residue. In humans, 25 selenoprotein genes have been characterized.
Anne-Laure, Bulteau, Laurent, Chavatte
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Selenoproteins in bladder cancer
Clinica Chimica Acta, 2012Selenoproteins with genetically encoded selenium (Se) are very important in response to oxidative stress, redox balance and regulation of various metabolic and developmental processes. Although increased circulating Se has been associated with 33% risk reduction of bladder cancer, there are little data on selenoprotein expression at the protein and ...
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Selenium and Selenoproteins in Health and Disease
Antioxidants & Redox Signaling, 2010The beneficial role of the trace element selenium (Se) in human health has been known for several decades and is attributed both to low-molecular-weight Se compounds and to its presence within 25 selenoproteins in the form of the amino acid selenocysteine (Sec).
Papp, Laura V. +2 more
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