Results 131 to 140 of about 7,542 (180)
Some of the next articles are maybe not open access.
Annual Review of Nutrition, 1993
Selenium exerts its biological activity largely through selenoproteins, which contain the element in the form of selenocysteine. Five selenoproteins have been characterized in animal tissues and there is evidence that a number of others exist. Selenoprotein synthesis is a complex process that has been well characterized in prokaryotic systems but ...
R F, Burk, K E, Hill
openaire +3 more sources
Selenium exerts its biological activity largely through selenoproteins, which contain the element in the form of selenocysteine. Five selenoproteins have been characterized in animal tissues and there is evidence that a number of others exist. Selenoprotein synthesis is a complex process that has been well characterized in prokaryotic systems but ...
R F, Burk, K E, Hill
openaire +3 more sources
BioEssays, 1999
Selenoproteins contain selenium in stoichiometric amounts. Most are synthesized by a process that decodes UGA codons as selenocysteine. Twelve animal selenoproteins have been characterized, and biochemical functions have been described for all but three. Two of these "orphan" selenoproteins are discussed in this paper.
R F, Burk, K E, Hill
openaire +2 more sources
Selenoproteins contain selenium in stoichiometric amounts. Most are synthesized by a process that decodes UGA codons as selenocysteine. Twelve animal selenoproteins have been characterized, and biochemical functions have been described for all but three. Two of these "orphan" selenoproteins are discussed in this paper.
R F, Burk, K E, Hill
openaire +2 more sources
Selenoproteins and cardiovascular stress [PDF]
Thrombosis and Haemostasis, 2015 SummaryDietary selenium (Se) is an essential micronutrient that exerts its biological effects through its incorporation into selenoproteins. This family of proteins contains several antioxidant enzymes such as the glutathione peroxidases, redox-regulating enzymes such as thioredoxin reductases, a methionine sulfoxide reductase, and others.
Peter Hoffmann
exaly +3 more sources
Selenoprotein expression and function—Selenoprotein W
Biochimica et Biophysica Acta (BBA) - General Subjects, 2009Selenoprotein 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.
openaire +2 more sources
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.
openaire +2 more sources
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.
openaire +2 more sources
The Deiodinase Family of Selenoproteins
Thyroid, 1997The 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
openaire +2 more sources
Selenoprotein inAspergillus terreus
Biological Trace Element Research, 1988Aspergillus 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
openaire +2 more sources
Human selenoproteins at a glance
Cellular and Molecular Life Sciences CMLS, 2005The 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
openaire +2 more sources
Molecular Biology of Selenoproteins
Annual Review of Nutrition, 1990Article 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).
openaire +2 more sources