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Development of a New Method for the Absolute Quantification of Selenoproteins in Chicken Serum by Heteroatom-Tagged Proteomics. [PDF]
J Agric Food ChemCallejón-Leblic B +3 more
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Total flavonoids from <i>Abrus cantoniensis</i> alleviate fatty liver hemorrhagic syndrome in laying hens by regulating inflammation, oxidative stress, and cecal metabolites and microbiota. [PDF]
Anim NutrGuo H +7 more
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Adaptive Antioxidant Nanomedicines Inhibit Ferroptosis in Renal Tubular Epithelial Cells to Alleviate Diabetic Kidney Disease. [PDF]
Adv Sci (Weinh)Liu Z +15 more
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EcoSal Plus, 2004
About 50 years ago, research on the biological function of the element selenium was initiated by the report of J. Pinsent that generation of formate dehydrogenase activity by Escherichia coli requires the presence of both selenite and molybdate in the growth medium.
Böck, A. +1 more
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About 50 years ago, research on the biological function of the element selenium was initiated by the report of J. Pinsent that generation of formate dehydrogenase activity by Escherichia coli requires the presence of both selenite and molybdate in the growth medium.
Böck, A. +1 more
openaire +3 more sources
Annual Review of Biochemistry, 1996
Selenocysteine is recognized as the 21st amino acid in ribosome-mediated protein synthesis and its specific incorporation is directed by the UGA codon. Unique tRNAs that have complementary UCA anticodons are aminoacylated with serine, the seryl-tRNA is converted to selenocysteyl-tRNA and the latter binds specifically to a special elongation factor and
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Selenocysteine is recognized as the 21st amino acid in ribosome-mediated protein synthesis and its specific incorporation is directed by the UGA codon. Unique tRNAs that have complementary UCA anticodons are aminoacylated with serine, the seryl-tRNA is converted to selenocysteyl-tRNA and the latter binds specifically to a special elongation factor and
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EcoSal Plus, 2004
Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes.
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Selenocysteine is a naturally occurring analog of cysteine in which the sulfur atom of the latter is replaced with selenium. This seleno-amino acid occurs as a specific component of various selenoproteins and selenium-dependent enzymes.
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Analysis of Selenocysteine‐Containing Proteins
Current Protocols in Protein Science, 2000AbstractRepresentatives of three primary life domains‐‐bacteria, archaea, and eukaryotes‐‐possess specific selenium‐containing proteins. The majority of naturally occurring selenoproteins contain an amino acid, selenocysteine, that is incorporated into protein in response to the code word UGA.
V N, Gladyshev, D L, Hatfield
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Selenocysteine Metabolism in Mammals
1985Publisher Summary This chapter discusses selenocysteine metabolism in mammals. Several microbial and mammalian proteins, particularly enzymes, contain selenium as an essential component. Four of them have been shown to contain a selenocysteine residue in their polypeptide chains: selenoprotein A of glycine reductase complex from Clostridium ...
H, Tanaka, N, Esaki, K, Soda
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Se-ing into selenocysteine biosynthesis
Nature Chemical Biology, 2009A cocrystal structure of the enzyme that synthesizes selenocysteine reveals the elegantly simple recognition mechanism for the tRNA molecule for this '21st amino acid'. The structure resolves some mechanistic questions and allows for comparison of the tRNA-dependent synthesis of cysteine and selenocysteine.
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