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Selenoprotein S ablation-mediated pyroptosis contributes to liver damage resulting from selenium deficiency in chickens. [PDF]
Poult SciZhang H, Chen X, Lu T, Cao Q, Li X.
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Supranutritional Selenomethionine but not Selenite Reduces Malignant Cell Transformation. [PDF]
Biol Trace Elem ResMeyer CE +4 more
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Recent Progress in Selenium Nanomedicines for Ocular Diseases. [PDF]
Int J NanomedicineJiang B +6 more
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Adapt or Perish: Efficient Selenocysteine Insertion Is Critical for Metastasizing Cancer Cells. [PDF]
Cancer ResLee N, Kim D.
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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
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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
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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
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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
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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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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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Antioxidants & Redox Signaling, 2015
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. Among them, membrane-bound selenoproteins play prominent roles in signaling pathways, Ca(2+) regulation ...
Jun, Liu, Sharon, Rozovsky
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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. Among them, membrane-bound selenoproteins play prominent roles in signaling pathways, Ca(2+) regulation ...
Jun, Liu, Sharon, Rozovsky
openaire +2 more sources