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Selenoprotein P

Cellular and Molecular Life Sciences, 2000
Selenoprotein P (SeP) is an extracellular, monomeric glycoprotein containing up to 10 selenocysteine residues in the polypeptide chain. It is ubiquitously expressed in mammalian tissues, and in human plasma it accounts for at least 40% of the total selenium concentration. SeP binds to heparin and cell membranes, and is associated with endothelial cells.
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The Deiodinase Family of Selenoproteins

Thyroid, 1997
The realization some forty years ago that several iodothyronine compounds are present in the circulation suggested that deiodination occurs in various tissues. Subsequently, deiodination was indeed documented in in vivo studies. Later, using in vitro assay techniques, three deiodinase processes, termed types 1, 2 and 3, were defined that differed in ...
D L, St Germain, V A, Galton
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Selenoprotein inAspergillus terreus

Biological Trace Element Research, 1988
Aspergillus terreus, a moderately selenium-tolerant fungus, metabolized Se-selenite into several protein seleno-amino acids: selenomethionine and selenocysteine, as well as, nonprotein seleno-amino acids, selenocystathionine, and y-glutamyl selenomethyl selenocysteine.
S E, Ramadan, A A, Razak
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Human selenoproteins at a glance

Cellular and Molecular Life Sciences CMLS, 2005
The public perception of selenium has changed significantly over the last decades. Originally mainly known for its high toxicity, it was later recognized as an essential trace element and is now (despite its narrow therapeutic window) almost being marketed as a lifestyle drug.
S, Gromer   +3 more
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Molecular Biology of Selenoproteins

Annual Review of Nutrition, 1990
Article de synthese sur la biologie moleculaire des selenoproteines. Etude du metabolisme du selenium (Se), des quatre classes de selenoproteines, de la glutathion peroxidase (GPX) Se-dependante et non dependante, de la phospholipide hydroperoxide GPX, de la GPX plasmatique, de seleno-proteines de mammiferes (rats).
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Selenoproteins and Cancer Prevention

Annual Review of Nutrition, 2012
The 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, 2014
Once 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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Selenoproteins and the aging brain

Mechanisms of Ageing and Development, 2010
Selenium (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

2004
Selenium 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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Membrane-Bound Selenoproteins

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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