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Selenoprotein expression and function—Selenoprotein W

Biochimica et Biophysica Acta (BBA) - General Subjects, 2009
Selenoprotein W (SeW) is a small selenoprotein (85 to 88 amino acids) first identified in sheep suffering from selenium deficiency. The levels are highest in muscle, heart (except rodents) spleen and brain. The deduced amino acid sequence has been obtained for mice, rats, monkeys, humans, sheep, pigs, fish and chickens.
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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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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 ...
Norman, Metanis, Donald, Hilvert
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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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Selenoproteins in bladder cancer

Clinica Chimica Acta, 2012
Selenoproteins 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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Mammalian selenoproteins.

Journal of trace elements and electrolytes in health and disease, 1993
Selenium (Se) is an essential trace element for animals and humans. Its biological role was established following the discovery that Se is a structural component of the active center of the enzyme glutathione peroxidase (GSH-Px). During the last decade remarkable progress has been made in the recognition of the structure and function of several ...
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Selenoprotein P

2002
Gavin E, Arteel   +3 more
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Selenoproteins

2006
Dietrich Behne, Antonios Kyriakopoulos
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